ID   1433B_HUMAN             Reviewed;         246 AA.
AC   P31946; A8K9K2; E1P616;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-APR-2013, entry version 151.
DE   RecName: Full=14-3-3 protein beta/alpha;
DE   AltName: Full=Protein 1054;
DE   AltName: Full=Protein kinase C inhibitor protein 1;
DE            Short=KCIP-1;
DE   Contains:
DE     RecName: Full=14-3-3 protein beta/alpha, N-terminally processed;
GN   Name=YWHAB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Keratinocyte;
RX   PubMed=8515476; DOI=10.1006/jmbi.1993.1346;
RA   Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H.,
RA   Walbum E., Vandekerckhove J., Celis J.E.;
RT   "Molecular cloning and expression of the transformation sensitive
RT   epithelial marker stratifin. A member of a protein family that has
RT   been involved in the protein kinase C signalling pathway.";
RL   J. Mol. Biol. 231:982-998(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-11; 14-57; 63-70; 106-117; 130-169 AND 215-246,
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Colon carcinoma;
RA   Bienvenut W.V., Zebisch A., Kolch W.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 3-20.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [8]
RP   INTERACTION WITH AANAT.
RX   PubMed=11427721; DOI=10.1073/pnas.141118798;
RA   Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA   Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA   Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT   "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-
RT   3-3-binding switch in melatonin synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN   [9]
RP   INTERACTION WITH CRTC2.
RX   PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
RA   Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,
RA   Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,
RA   Okamoto M., Montminy M.;
RT   "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
RT   coincidence detector.";
RL   Cell 119:61-74(2004).
RN   [10]
RP   INTERACTION WITH SSH1.
RX   PubMed=15159416; DOI=10.1083/jcb.200401136;
RA   Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
RA   Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
RT   "A pathway of neuregulin-induced activation of cofilin-phosphatase
RT   Slingshot and cofilin in lamellipodia.";
RL   J. Cell Biol. 165:465-471(2004).
RN   [11]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA   Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA   Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA   Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [12]
RP   INTERACTION WITH YAP1.
RX   PubMed=17974916; DOI=10.1101/gad.1602907;
RA   Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J.,
RA   Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G.,
RA   Lai Z.C., Guan K.L.;
RT   "Inactivation of YAP oncoprotein by the Hippo pathway is involved in
RT   cell contact inhibition and tissue growth control.";
RL   Genes Dev. 21:2747-2761(2007).
RN   [13]
RP   INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, AND
RP   MASS SPECTROMETRY.
RX   PubMed=17717073; DOI=10.1210/me.2007-0323;
RA   Liu Y., Ross J.F., Bodine P.V.N., Billiard J.;
RT   "Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-
RT   3(beta) phosphorylation and promotes osteoblast differentiation and
RT   bone formation.";
RL   Mol. Endocrinol. 21:3050-3061(2007).
RN   [14]
RP   INTERACTION WITH GAB2.
RX   PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA   Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA   Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA   Guilhaus M., James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT   the Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH SRPK2.
RX   PubMed=19592491; DOI=10.1074/jbc.M109.026237;
RA   Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.;
RT   "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell
RT   cycle and cell death in neurons.";
RL   J. Biol. Chem. 284:24512-24525(2009).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-117, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, MASS SPECTROMETRY,
RP   INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
RX   PubMed=17085597; DOI=10.1073/pnas.0605779103;
RA   Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
RA   Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
RT   "Structural basis for protein-protein interactions in the 14-3-3
RT   protein family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
RN   [20]
RP   VARIANT ILE-99.
RX   PubMed=21248752; DOI=10.1038/nature09639;
RA   Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
RA   Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA   Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA   Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA   Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA   Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA   Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA   Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA   Futreal P.A.;
RT   "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT   gene PBRM1 in renal carcinoma.";
RL   Nature 469:539-542(2011).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner. Negative
CC       regulator of osteogenesis. Blocks the nuclear translocation of the
CC       phosphorylated form (by AKT1) of SRPK2 and antagonizes its
CC       stimulatory effect on cyclin D1 expression resulting in blockage
CC       of neuronal apoptosis elicited by SRPK2.
CC   -!- SUBUNIT: Homodimer. Interacts with SAMSN1 and KRPCE (By
CC       similarity). Interacts with SSH1 and TORC2/CRTC2. Interacts with
CC       ABL1; the interaction results in cytoplasmic location of ABL1 and
CC       inhibition of cABL-mediated apoptosis. Interacts with ROR2
CC       (dimer); the interaction results in phosphorylation of YWHAB on
CC       tyrosine residues. Interacts with GAB2 and YAP1 (phosphorylated
CC       form). Interacts with the phosphorylated (by AKT1) form of SRPK2.
CC       Interacts with PKA-phosphorylated AANAT.
CC   -!- INTERACTION:
CC       Q76353:- (xeno); NbExp=3; IntAct=EBI-359815, EBI-6248077;
CC       Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359815, EBI-1567267;
CC       O00257:CBX4; NbExp=2; IntAct=EBI-359815, EBI-722425;
CC       P30304:CDC25A; NbExp=8; IntAct=EBI-359815, EBI-747671;
CC       O94921:CDK14; NbExp=5; IntAct=EBI-359815, EBI-1043945;
CC       Q9NYF0:DACT1; NbExp=4; IntAct=EBI-359815, EBI-3951744;
CC       Q13627-2:DYRK1A; NbExp=3; IntAct=EBI-359815, EBI-1053621;
CC       Q11184:let-756 (xeno); NbExp=2; IntAct=EBI-359815, EBI-3843983;
CC       Q5S007:LRRK2; NbExp=3; IntAct=EBI-359815, EBI-5323863;
CC       Q99683:MAP3K5; NbExp=3; IntAct=EBI-359815, EBI-476263;
CC       Q7KZI7:MARK2; NbExp=2; IntAct=EBI-359815, EBI-516560;
CC       P27448:MARK3; NbExp=2; IntAct=EBI-359815, EBI-707595;
CC       P04049:RAF1; NbExp=10; IntAct=EBI-359815, EBI-365996;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by
CC       mass spectrometry in melanosome fractions from stage I to stage
CC       IV.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P31946-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P31946-2; Sequence=VSP_018632;
CC         Note=Contains a N-acetylmethionine at position 1 (By
CC         similarity);
CC   -!- PTM: The alpha, brain-specific form differs from the beta form in
CC       being phosphorylated (By similarity). Phosphorylated on Ser-60 by
CC       protein kinase C delta type catalytic subunit in a sphingosine-
CC       dependent fashion (By similarity).
CC   -!- PTM: Isoform Short contains a N-acetylmethionine at position 1 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; X57346; CAA40621.1; -; mRNA.
DR   EMBL; AK292717; BAF85406.1; -; mRNA.
DR   EMBL; AL008725; CAA15497.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75893.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75894.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75896.1; -; Genomic_DNA.
DR   EMBL; BC001359; AAH01359.1; -; mRNA.
DR   IPI; IPI00216318; -.
DR   IPI; IPI00759832; -.
DR   PIR; S34755; S34755.
DR   RefSeq; NP_003395.1; NM_003404.3.
DR   RefSeq; NP_647539.1; NM_139323.2.
DR   UniGene; Hs.643544; -.
DR   PDB; 2BQ0; X-ray; 2.50 A; A/B=1-239.
DR   PDB; 2C23; X-ray; 2.65 A; A=1-239.
DR   PDB; 4DNK; X-ray; 2.20 A; A/B=1-246.
DR   PDBsum; 2BQ0; -.
DR   PDBsum; 2C23; -.
DR   PDBsum; 4DNK; -.
DR   ProteinModelPortal; P31946; -.
DR   SMR; P31946; 1-234.
DR   DIP; DIP-743N; -.
DR   IntAct; P31946; 53.
DR   MINT; MINT-99570; -.
DR   STRING; 9606.ENSP00000300161; -.
DR   PhosphoSite; P31946; -.
DR   DMDM; 1345590; -.
DR   OGP; P31946; -.
DR   REPRODUCTION-2DPAGE; IPI00216318; -.
DR   PaxDb; P31946; -.
DR   PRIDE; P31946; -.
DR   DNASU; 7529; -.
DR   Ensembl; ENST00000353703; ENSP00000300161; ENSG00000166913.
DR   Ensembl; ENST00000372839; ENSP00000361930; ENSG00000166913.
DR   GeneID; 7529; -.
DR   KEGG; hsa:7529; -.
DR   UCSC; uc002xmt.3; human.
DR   CTD; 7529; -.
DR   GeneCards; GC20P043515; -.
DR   HGNC; HGNC:12849; YWHAB.
DR   HPA; CAB003759; -.
DR   HPA; HPA007925; -.
DR   HPA; HPA011212; -.
DR   MIM; 601289; gene.
DR   neXtProt; NX_P31946; -.
DR   PharmGKB; PA37438; -.
DR   eggNOG; COG5040; -.
DR   HOGENOM; HOG000240379; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P31946; -.
DR   KO; K16197; -.
DR   OMA; CNDVLXT; -.
DR   OrthoDB; EOG4N30PR; -.
DR   PhylomeDB; P31946; -.
DR   Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
DR   Pathway_Interaction_DB; pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
DR   Pathway_Interaction_DB; foxopathway; FoxO family signaling.
DR   Pathway_Interaction_DB; insulin_glucose_pathway; Insulin-mediated glucose transport.
DR   Pathway_Interaction_DB; p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
DR   Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
DR   Pathway_Interaction_DB; hdac_classii_pathway; Signaling events mediated by HDAC Class II.
DR   Pathway_Interaction_DB; pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
DR   Reactome; REACT_111045; Developmental Biology.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_11123; Membrane Trafficking.
DR   Reactome; REACT_116125; Disease.
DR   Reactome; REACT_21257; Metabolism of RNA.
DR   Reactome; REACT_578; Apoptosis.
DR   Reactome; REACT_6900; Immune System.
DR   Reactome; REACT_71; Gene Expression.
DR   ChiTaRS; YWHAB; human.
DR   EvolutionaryTrace; P31946; -.
DR   GenomeRNAi; 7529; -.
DR   NextBio; 29453; -.
DR   ArrayExpress; P31946; -.
DR   Bgee; P31946; -.
DR   CleanEx; HS_YWHAB; -.
DR   Genevestigator; P31946; -.
DR   GermOnline; ENSG00000166913; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0017053; C:transcriptional repressor complex; IEA:Compara.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Compara.
DR   GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
DR   GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0051220; P:cytoplasmic sequestering of protein; IDA:BHF-UCL.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0035329; P:hippo signaling cascade; TAS:Reactome.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR   GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara.
DR   GO; GO:0048011; P:nerve growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0051291; P:protein heterooligomerization; IEA:Compara.
DR   GO; GO:0006605; P:protein targeting; IEA:Compara.
DR   GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; 14-3-3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Phosphoprotein; Polymorphism;
KW   Reference proteome.
FT   CHAIN         1    246       14-3-3 protein beta/alpha.
FT                                /FTId=PRO_0000367900.
FT   INIT_MET      1      1       Removed; alternate.
FT   CHAIN         2    246       14-3-3 protein beta/alpha, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000000003.
FT   SITE         58     58       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        129    129       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine; in 14-3-3 protein
FT                                beta/alpha; alternate.
FT   MOD_RES       2      2       N-acetylthreonine; in 14-3-3 protein
FT                                beta/alpha, N-terminally processed.
FT   MOD_RES      60     60       Phosphoserine (By similarity).
FT   MOD_RES      70     70       N6-acetyllysine.
FT   MOD_RES     117    117       N6-acetyllysine.
FT   MOD_RES     186    186       Phosphoserine (By similarity).
FT   VAR_SEQ       1      2       Missing (in isoform Short).
FT                                /FTId=VSP_018632.
FT   VARIANT      99     99       V -> I (found in a renal cell carcinoma
FT                                sample; somatic mutation).
FT                                /FTId=VAR_064762.
FT   HELIX         5     17
FT   HELIX        21     33
FT   HELIX        40     69
FT   HELIX        75    105
FT   HELIX       107    110
FT   HELIX       114    133
FT   HELIX       139    161
FT   HELIX       167    182
FT   HELIX       187    202
FT   HELIX       203    207
FT   TURN        210    212
FT   HELIX       213    232
SQ   SEQUENCE   246 AA;  28082 MW;  6BE1A9BF97468017 CRC64;
     MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS
     WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY
     LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY
     YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
     AGEGEN
//
ID   1433E_HUMAN             Reviewed;         255 AA.
AC   P62258; B3KY71; D3DTH5; P29360; P42655; Q4VJB6; Q53XZ5; Q63631;
AC   Q7M4R4;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-APR-2013, entry version 109.
DE   RecName: Full=14-3-3 protein epsilon;
DE            Short=14-3-3E;
GN   Name=YWHAE;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=7644510; DOI=10.1073/pnas.92.17.7892;
RA   Conklin D.S., Galaktionov K., Beach D.;
RT   "14-3-3 proteins associate with cdc25 phosphatases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=8858348;
RA   Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.;
RT   "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on
RT   chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome
RT   region.";
RL   Genome Res. 6:735-741(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8684458; DOI=10.1038/382308a0;
RA   Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T.;
RT   "Function of 14-3-3 proteins.";
RL   Nature 382:308-308(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV), AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   PubMed=20417184; DOI=10.1016/j.bbrc.2010.04.104;
RA   Han D., Ye G., Liu T., Chen C., Yang X., Wan B., Pan Y., Yu L.;
RT   "Functional identification of a novel 14-3-3 epsilon splicing variant
RT   suggests dimerization is not necessary for 14-3-3 epsilon to inhibit
RT   UV-induced apoptosis.";
RL   Biochem. Biophys. Res. Commun. 396:401-406(2010).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RA   Luk S.C.W., Lee C.Y., Waye M.M.Y.;
RT   "Sequence determination of human epsilon 14-3-3 protein.";
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tanigami A., Chong S.S., Ledbetter D.H.;
RT   "14-3-3 epsilon genomic sequence.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND SV).
RC   TISSUE=Caudate nucleus, Heart, and Subthalamic nucleus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   PROTEIN SEQUENCE OF 1-19.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [12]
RP   PROTEIN SEQUENCE OF 1-19; 30-50 AND 131-170, ACETYLATION AT MET-1, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (MAY-2005) to UniProtKB.
RN   [13]
RP   PROTEIN SEQUENCE OF 103-108; 120-123; 131-141 AND 143-153.
RC   TISSUE=Histiocytic lymphoma;
RX   PubMed=2026444;
RA   Demeter J., Medzihradszky D., Kha H., Goetzl E.J., Turck C.W.;
RT   "Isolation and partial characterization of the structures of
RT   fibroblast activating factor-related proteins from U937 cells.";
RL   Immunology 72:350-354(1991).
RN   [14]
RP   PROTEIN SEQUENCE OF 131-141 AND 154-190, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [15]
RP   INTERACTION WITH HCV CORE PROTEIN.
RX   PubMed=10644344; DOI=10.1128/JVI.74.4.1736-1741.2000;
RA   Aoki H., Hayashi J., Moriyama M., Arakawa Y., Hino O.;
RT   "Hepatitis C virus core protein interacts with 14-3-3 protein and
RT   activates the kinase Raf-1.";
RL   J. Virol. 74:1736-1741(2000).
RN   [16]
RP   INTERACTION WITH AANAT.
RX   PubMed=11427721; DOI=10.1073/pnas.141118798;
RA   Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA   Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA   Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT   "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-
RT   3-3-binding switch in melatonin synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN   [17]
RP   INTERACTION WITH CDKN1B, AND SUBCELLULAR LOCATION.
RX   PubMed=12042314; DOI=10.1074/jbc.M203668200;
RA   Fujita N., Sato S., Katayama K., Tsuruo T.;
RT   "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3
RT   and cytoplasmic localization.";
RL   J. Biol. Chem. 277:28706-28713(2002).
RN   [18]
RP   INTERACTION WITH GRB10.
RX   PubMed=15722337; DOI=10.1074/jbc.M501477200;
RA   Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
RT   "Phosphorylation of grb10 regulates its interaction with 14-3-3.";
RL   J. Biol. Chem. 280:16987-16993(2005).
RN   [19]
RP   INTERACTION WITH ABL1, AND MASS SPECTROMETRY.
RX   PubMed=15696159; DOI=10.1038/ncb1228;
RA   Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
RT   "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of
RT   c-Abl in the apoptotic response to DNA damage.";
RL   Nat. Cell Biol. 7:278-285(2005).
RN   [20]
RP   INTERACTION WITH YWHAZ.
RX   PubMed=16376338; DOI=10.1016/j.febslet.2005.12.024;
RA   Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.;
RT   "Protein kinase A phosphorylates and regulates dimerization of 14-3-3
RT   epsilon.";
RL   FEBS Lett. 580:305-310(2006).
RN   [21]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA   Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA   Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA   Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [22]
RP   INTERACTION WITH GAB2.
RX   PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA   Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA   Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA   Guilhaus M., James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT   the Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by
RT   enrichment and fractionation of phosphopeptides with strong anion
RT   exchange chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [24]
RP   INTERACTION WITH SRPK2.
RX   PubMed=19592491; DOI=10.1074/jbc.M109.026237;
RA   Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.;
RT   "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell
RT   cycle and cell death in neurons.";
RL   J. Biol. Chem. 284:24512-24525(2009).
RN   [25]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50; LYS-69; LYS-118 AND
RP   LYS-123, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASS
RP   SPECTROMETRY.
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-233, MASS SPECTROMETRY,
RP   INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
RX   PubMed=17085597; DOI=10.1073/pnas.0605779103;
RA   Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
RA   Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
RT   "Structural basis for protein-protein interactions in the 14-3-3
RT   protein family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC   -!- SUBUNIT: Homodimer. Heterodimerizes with YWHAZ. Interacts with
CC       NDEL1, ARHGEF28 and TIAM2 (By similarity). Interacts with HCV core
CC       protein. Interacts with ABL1 (phosphorylated form); the
CC       interaction retains it in the cytoplasm. Weakly interacts with
CC       CDKN1B. Interacts with GAB2. Interacts with phosphorylated GRB10.
CC       Interacts with PKA-phosphorylated AANAT. Interacts with the
CC       phosphorylated (by AKT1) form of SRPK2.
CC   -!- INTERACTION:
CC       O00257-3:CBX4; NbExp=2; IntAct=EBI-356498, EBI-4392727;
CC       O94921:CDK14; NbExp=3; IntAct=EBI-356498, EBI-1043945;
CC       Q9UKT5:FBXO4; NbExp=5; IntAct=EBI-356498, EBI-960409;
CC       Q14678-2:KANK1; NbExp=3; IntAct=EBI-356498, EBI-6173812;
CC       Q5S007:LRRK2; NbExp=3; IntAct=EBI-356498, EBI-5323863;
CC       P61981:YWHAG; NbExp=4; IntAct=EBI-356498, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome.
CC       Note=Identified by mass spectrometry in melanosome fractions from
CC       stage I to stage IV.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P62258-1; Sequence=Displayed;
CC       Name=SV;
CC         IsoId=P62258-2; Sequence=VSP_040621;
CC         Note=Unable to dimerize with YWHAZ;
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; U20972; AAC50175.1; -; mRNA.
DR   EMBL; U54778; AAC50710.1; -; mRNA.
DR   EMBL; U43399; AAC50625.1; -; mRNA.
DR   EMBL; U43430; AAD00026.1; -; mRNA.
DR   EMBL; U28936; AAA75301.1; -; mRNA.
DR   EMBL; AB017103; BAA32538.1; -; Genomic_DNA.
DR   EMBL; AY883089; AAX68683.1; -; mRNA.
DR   EMBL; AK128785; BAG54733.1; -; mRNA.
DR   EMBL; AK295260; BAG58249.1; -; mRNA.
DR   EMBL; AK316185; BAH14556.1; -; mRNA.
DR   EMBL; BT007161; AAP35825.1; -; mRNA.
DR   EMBL; CH471108; EAW90628.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90629.1; -; Genomic_DNA.
DR   EMBL; BC000179; AAH00179.1; -; mRNA.
DR   EMBL; BC001440; AAH01440.1; -; mRNA.
DR   IPI; IPI00000816; -.
DR   IPI; IPI00974544; -.
DR   PIR; A61235; A61235.
DR   PIR; I38947; I38947.
DR   RefSeq; NP_006752.1; NM_006761.4.
DR   UniGene; Hs.513851; -.
DR   PDB; 2BR9; X-ray; 1.75 A; A=1-233.
DR   PDB; 3UAL; X-ray; 1.80 A; A=1-232.
DR   PDB; 3UBW; X-ray; 1.90 A; A=1-234.
DR   PDBsum; 2BR9; -.
DR   PDBsum; 3UAL; -.
DR   PDBsum; 3UBW; -.
DR   ProteinModelPortal; P62258; -.
DR   SMR; P62258; 3-232.
DR   DIP; DIP-36676N; -.
DR   IntAct; P62258; 98.
DR   MINT; MINT-4998623; -.
DR   STRING; 9606.ENSP00000264335; -.
DR   PhosphoSite; P62258; -.
DR   DMDM; 51702210; -.
DR   OGP; P42655; -.
DR   UCD-2DPAGE; P62258; -.
DR   PaxDb; P62258; -.
DR   PeptideAtlas; P62258; -.
DR   PRIDE; P62258; -.
DR   DNASU; 7531; -.
DR   Ensembl; ENST00000264335; ENSP00000264335; ENSG00000108953.
DR   Ensembl; ENST00000571732; ENSP00000461762; ENSG00000108953.
DR   GeneID; 7531; -.
DR   KEGG; hsa:7531; -.
DR   UCSC; uc002fsj.3; human.
DR   CTD; 7531; -.
DR   GeneCards; GC17M001247; -.
DR   H-InvDB; HIX0013751; -.
DR   H-InvDB; HIX0030006; -.
DR   HGNC; HGNC:12851; YWHAE.
DR   HPA; CAB016200; -.
DR   HPA; CAB021109; -.
DR   HPA; CAB047350; -.
DR   HPA; HPA008445; -.
DR   MIM; 605066; gene.
DR   neXtProt; NX_P62258; -.
DR   Orphanet; 217385; 17p13.3 microduplication syndrome.
DR   PharmGKB; PA37440; -.
DR   eggNOG; COG5040; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P62258; -.
DR   KO; K06630; -.
DR   OMA; KESALIM; -.
DR   OrthoDB; EOG4HHP34; -.
DR   PhylomeDB; P62258; -.
DR   Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
DR   Pathway_Interaction_DB; pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
DR   Pathway_Interaction_DB; foxopathway; FoxO family signaling.
DR   Pathway_Interaction_DB; igf1_pathway; IGF1 pathway.
DR   Pathway_Interaction_DB; insulin_glucose_pathway; Insulin-mediated glucose transport.
DR   Pathway_Interaction_DB; lis1pathway; Lissencephaly gene (LIS1) in neuronal migration and development.
DR   Pathway_Interaction_DB; p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
DR   Pathway_Interaction_DB; p75ntrpathway; p75(NTR)-mediated signaling.
DR   Pathway_Interaction_DB; telomerasepathway; Regulation of Telomerase.
DR   Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
DR   Pathway_Interaction_DB; hdac_classii_pathway; Signaling events mediated by HDAC Class II.
DR   Pathway_Interaction_DB; tgfbrpathway; TGF-beta receptor signaling.
DR   Pathway_Interaction_DB; pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_11123; Membrane Trafficking.
DR   Reactome; REACT_115566; Cell Cycle.
DR   ChiTaRS; YWHAE; human.
DR   EvolutionaryTrace; P62258; -.
DR   GenomeRNAi; 7531; -.
DR   NextBio; 29461; -.
DR   PMAP-CutDB; P62258; -.
DR   ArrayExpress; P62258; -.
DR   Bgee; P62258; -.
DR   CleanEx; HS_YWHAE; -.
DR   Genevestigator; P62258; -.
DR   GermOnline; ENSG00000108953; Homo sapiens.
DR   GO; GO:0033267; C:axon part; IEA:Compara.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005871; C:kinesin complex; IEA:Compara.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:Compara.
DR   GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR   GO; GO:0021987; P:cerebral cortex development; IEA:Compara.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0035329; P:hippo signaling cascade; TAS:Reactome.
DR   GO; GO:0021766; P:hippocampus development; IEA:Compara.
DR   GO; GO:0035308; P:negative regulation of protein dephosphorylation; IEA:Compara.
DR   GO; GO:0048011; P:nerve growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0001764; P:neuron migration; IEA:Compara.
DR   GO; GO:0006605; P:protein targeting; IEA:Compara.
DR   GO; GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; 14-3-3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Host-virus interaction;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1    255       14-3-3 protein epsilon.
FT                                /FTId=PRO_0000058618.
FT   SITE         57     57       Interaction with phosphoserine on
FT                                interacting protein.
FT   SITE        130    130       Interaction with phosphoserine on
FT                                interacting protein.
FT   MOD_RES       1      1       N-acetylmethionine.
FT   MOD_RES      50     50       N6-acetyllysine.
FT   MOD_RES      69     69       N6-acetyllysine.
FT   MOD_RES     118    118       N6-acetyllysine.
FT   MOD_RES     123    123       N6-acetyllysine.
FT   MOD_RES     210    210       Phosphoserine.
FT   VAR_SEQ       1     22       Missing (in isoform SV).
FT                                /FTId=VSP_040621.
FT   CONFLICT    106    107       KH -> NY (in Ref. 13; AA sequence).
FT   CONFLICT    143    143       E -> F (in Ref. 13; AA sequence).
FT   CONFLICT    148    148       S -> T (in Ref. 13; AA sequence).
FT   HELIX         4     17
FT   HELIX        20     31
FT   HELIX        39     73
FT   HELIX        76    106
FT   HELIX       108    111
FT   HELIX       115    135
FT   HELIX       138    162
FT   HELIX       168    183
FT   HELIX       188    204
FT   HELIX       205    208
FT   TURN        211    213
FT   HELIX       214    231
SQ   SEQUENCE   255 AA;  29174 MW;  07817CCBD1F75B26 CRC64;
     MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
     RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
     YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
     YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
     EQNKEALQDV EDENQ
//
ID   1433F_HUMAN             Reviewed;         246 AA.
AC   Q04917;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-APR-2013, entry version 146.
DE   RecName: Full=14-3-3 protein eta;
DE   AltName: Full=Protein AS1;
GN   Name=YWHAH; Synonyms=YWHA1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8218406; DOI=10.1016/0167-4781(93)90053-G;
RA   Swanson K.D., Dhar M.S., Joshi J.G.;
RT   "The human and bovine 14-3-3 eta protein mRNAs are highly conserved in
RT   both their translated and untranslated regions.";
RL   Biochim. Biophys. Acta 1216:145-148(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Brain;
RX   PubMed=1578511; DOI=10.1002/jnr.490310403;
RA   Ichimura-Ohshima Y., Morii K., Ichimura T., Araki K., Takahashi Y.,
RA   Isobe T., Minoshima S., Fukuyama R., Shimizu N., Kuwano R.;
RT   "cDNA cloning and chromosome assignment of the gene for human brain
RT   14-3-3 protein eta chain.";
RL   J. Neurosci. Res. 31:600-605(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Leffers H., Tommerup N., Celis J.E.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8561965; DOI=10.1007/BF02740697;
RA   Muratake T., Hayashi S., Ichimura Y., Morii K., Kuwano R.,
RA   Ichikawa T., Kumanishi T., Isobe T., Watanabe M., Kondo H.;
RT   "The effect on methamphetamine on the mRNA level for 14.3.3 eta chain
RT   in the human cultured cells.";
RL   Mol. Neurobiol. 11:223-230(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8812417; DOI=10.1006/geno.1996.0426;
RA   Muratake T., Hayashi S., Ichikawa T., Kumanishi T., Ichimura Y.,
RA   Kuwano R., Isobe T., Wang Y., Minoshima S., Shimizu N., Takahashi Y.;
RT   "Structural organization and chromosomal assignment of the human 14-3-
RT   3 eta chain gene (YWHAH).";
RL   Genomics 36:63-69(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA   Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA   Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA   Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA   Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA   Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA   Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA   Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA   Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA   Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA   Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA   Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA   Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA   Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA   Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA   Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA   Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA   Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA   Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA   Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA   Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA   Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA   Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA   Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA   Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA   Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA   Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA   Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA   Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA   Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA   Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA   Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA   O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA   Khan A.S., Lane L., Tilahun Y., Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 27-225.
RC   TISSUE=Keratinocyte;
RX   PubMed=8515476; DOI=10.1006/jmbi.1993.1346;
RA   Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H.,
RA   Walbum E., Vandekerckhove J., Celis J.E.;
RT   "Molecular cloning and expression of the transformation sensitive
RT   epithelial marker stratifin. A member of a protein family that has
RT   been involved in the protein kinase C signalling pathway.";
RL   J. Mol. Biol. 231:982-998(1993).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-10.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [11]
RP   PROTEIN SEQUENCE OF 2-10; 29-50; 62-69; 126-132; 144-155; 163-172 AND
RP   218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Platelet;
RA   Bienvenut W.V.;
RL   Submitted (AUG-2005) to UniProtKB.
RN   [12]
RP   INTERACTION WITH AR; ESR1; ESR2; MC2R; NRIP1; NR3C1; PPARBP AND THRA.
RX   PubMed=11266503; DOI=10.1210/me.15.4.501;
RA   Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E.,
RA   Gustafsson J.-A.;
RT   "Regulation of glucocorticoid receptor activity by 14-3-3-dependent
RT   intracellular relocalization of the corepressor RIP140.";
RL   Mol. Endocrinol. 15:501-511(2001).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH PDPK1.
RX   PubMed=12177059; DOI=10.1074/jbc.M205141200;
RA   Sato S., Fujita N., Tsuruo T.;
RT   "Regulation of kinase activity of 3-phosphoinositide-dependent protein
RT   kinase-1 by binding to 14-3-3.";
RL   J. Biol. Chem. 277:39360-39367(2002).
RN   [14]
RP   INTERACTION WITH CDKN1B.
RX   PubMed=14504289; DOI=10.1074/jbc.M306614200;
RA   Fujita N., Sato S., Tsuruo T.;
RT   "Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein
RT   S6 kinases promotes its binding to 14-3-3 and cytoplasmic
RT   localization.";
RL   J. Biol. Chem. 278:49254-49260(2003).
RN   [15]
RP   INTERACTION WITH ABL1, AND MASS SPECTROMETRY.
RX   PubMed=15696159; DOI=10.1038/ncb1228;
RA   Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
RT   "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of
RT   c-Abl in the apoptotic response to DNA damage.";
RL   Nat. Cell Biol. 7:278-285(2005).
RN   [16]
RP   INTERACTION WITH GAB2.
RX   PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA   Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA   Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA   Guilhaus M., James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT   the Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), MASS SPECTROMETRY, INTERACTION
RP   WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
RX   PubMed=17085597; DOI=10.1073/pnas.0605779103;
RA   Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
RA   Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
RT   "Structural basis for protein-protein interactions in the 14-3-3
RT   protein family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC       Negatively regulates the kinase activity of PDPK1.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with many nuclear
CC       hormone receptors and cofactors including AR, ESR1, ESR2, MC2R,
CC       NR3C1, NRIP1, PPARBP and THRA. Interacts with ABL1 (phosphorylated
CC       form); the interaction retains it in the cytoplasm. Interacts with
CC       ARHGEF28 and CDK16 (By similarity). Weakly interacts with CDKN1B.
CC       Interacts with GAB2. Interacts with KCNK18 in a phosphorylation-
CC       dependent manner. Interacts with SAMSN1 (By similarity). Interacts
CC       with the 'Ser-241' phosphorylated form of PDPK1.
CC   -!- INTERACTION:
CC       O94921:CDK14; NbExp=3; IntAct=EBI-306940, EBI-1043945;
CC       O60565:GREM1; NbExp=5; IntAct=EBI-306940, EBI-944395;
CC       Q14678-2:KANK1; NbExp=3; IntAct=EBI-306940, EBI-6173812;
CC       Q5S007:LRRK2; NbExp=2; IntAct=EBI-306940, EBI-5323863;
CC       Q7KZI7:MARK2; NbExp=6; IntAct=EBI-306940, EBI-516560;
CC       P27448:MARK3; NbExp=4; IntAct=EBI-306940, EBI-707595;
CC       Q96L34:MARK4; NbExp=6; IntAct=EBI-306940, EBI-302319;
CC       Q8TEW0:PARD3; NbExp=6; IntAct=EBI-306940, EBI-1221123;
CC       Q9NPB6:PARD6A; NbExp=2; IntAct=EBI-306940, EBI-81876;
CC       Q9BYG5:PARD6B; NbExp=2; IntAct=EBI-306940, EBI-295391;
CC       Q9BYG4:PARD6G; NbExp=2; IntAct=EBI-306940, EBI-295417;
CC       P41743:PRKCI; NbExp=3; IntAct=EBI-306940, EBI-286199;
CC       P04049:RAF1; NbExp=2; IntAct=EBI-306940, EBI-365996;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in the brain and present in
CC       other tissues albeit at lower levels.
CC   -!- PTM: Phosphorylated on Ser-59 by protein kinase C delta type
CC       catalytic subunit in a sphingosine-dependent fashion (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; L20422; AAA35483.1; -; mRNA.
DR   EMBL; X80536; CAA56676.1; -; Genomic_DNA.
DR   EMBL; X78138; CAA55017.1; -; mRNA.
DR   EMBL; X57345; CAA40620.1; -; mRNA.
DR   EMBL; D78577; BAA11418.1; -; Genomic_DNA.
DR   EMBL; S80794; AAB36036.1; -; mRNA.
DR   EMBL; CR456612; CAG30498.1; -; mRNA.
DR   EMBL; Z82248; CAB05112.1; -; Genomic_DNA.
DR   EMBL; BC003047; AAH03047.1; -; mRNA.
DR   IPI; IPI00216319; -.
DR   PIR; S34756; S34756.
DR   PIR; S38509; S38509.
DR   PIR; S38532; S38532.
DR   RefSeq; NP_003396.1; NM_003405.3.
DR   UniGene; Hs.226755; -.
DR   PDB; 2C63; X-ray; 2.15 A; A/B/C/D=1-246.
DR   PDB; 2C74; X-ray; 2.70 A; A/B=1-246.
DR   PDBsum; 2C63; -.
DR   PDBsum; 2C74; -.
DR   ProteinModelPortal; Q04917; -.
DR   SMR; Q04917; 3-235.
DR   DIP; DIP-27566N; -.
DR   IntAct; Q04917; 111.
DR   MINT; MINT-124456; -.
DR   STRING; 9606.ENSP00000248975; -.
DR   PhosphoSite; Q04917; -.
DR   DMDM; 1345593; -.
DR   PaxDb; Q04917; -.
DR   PeptideAtlas; Q04917; -.
DR   PRIDE; Q04917; -.
DR   DNASU; 7533; -.
DR   Ensembl; ENST00000248975; ENSP00000248975; ENSG00000128245.
DR   GeneID; 7533; -.
DR   KEGG; hsa:7533; -.
DR   UCSC; uc003alz.3; human.
DR   CTD; 7533; -.
DR   GeneCards; GC22P032340; -.
DR   HGNC; HGNC:12853; YWHAH.
DR   HPA; CAB025918; -.
DR   MIM; 113508; gene.
DR   neXtProt; NX_Q04917; -.
DR   PharmGKB; PA37442; -.
DR   eggNOG; COG5040; -.
DR   HOGENOM; HOG000240379; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; Q04917; -.
DR   KO; K16198; -.
DR   OMA; ESSEAAY; -.
DR   OrthoDB; EOG48PMM0; -.
DR   PhylomeDB; Q04917; -.
DR   Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
DR   Pathway_Interaction_DB; pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
DR   Pathway_Interaction_DB; foxopathway; FoxO family signaling.
DR   Pathway_Interaction_DB; insulin_glucose_pathway; Insulin-mediated glucose transport.
DR   Pathway_Interaction_DB; p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
DR   Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
DR   Pathway_Interaction_DB; pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
DR   Reactome; REACT_11123; Membrane Trafficking.
DR   ChiTaRS; YWHAH; human.
DR   EvolutionaryTrace; Q04917; -.
DR   GenomeRNAi; 7533; -.
DR   NextBio; 29471; -.
DR   ArrayExpress; Q04917; -.
DR   Bgee; Q04917; -.
DR   CleanEx; HS_YWHAH; -.
DR   Genevestigator; Q04917; -.
DR   GermOnline; ENSG00000128245; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0014704; C:intercalated disc; IC:BHF-UCL.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR   GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
DR   GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB.
DR   GO; GO:0017080; F:sodium channel regulator activity; ISS:BHF-UCL.
DR   GO; GO:0006713; P:glucocorticoid catabolic process; IDA:UniProtKB.
DR   GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR   GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; 14-3-3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; Phosphoprotein; Reference proteome.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    246       14-3-3 protein eta.
FT                                /FTId=PRO_0000058623.
FT   SITE         57     57       Interaction with phosphoserine on
FT                                interacting protein.
FT   SITE        132    132       Interaction with phosphoserine on
FT                                interacting protein.
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES      59     59       Phosphoserine (By similarity).
FT   MOD_RES     117    117       Phosphotyrosine (By similarity).
FT   CONFLICT    144    144       N -> T (in Ref. 9; CAA40620).
FT   CONFLICT    157    157       A -> G (in Ref. 1; AAA35483).
FT   CONFLICT    237    237       Q -> L (in Ref. 1; AAA35483).
FT   HELIX         4     16
FT   HELIX        20     31
FT   HELIX        39     73
FT   HELIX        76    106
FT   TURN        107    111
FT   HELIX       117    137
FT   HELIX       140    164
FT   HELIX       170    185
FT   HELIX       190    206
FT   HELIX       207    210
FT   TURN        213    215
FT   HELIX       216    234
SQ   SEQUENCE   246 AA;  28219 MW;  D70FBC100C45D6E5 CRC64;
     MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW
     RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LSLLDKFLIK NCNDFQYESK
     VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEQMQPTHP IRLGLALNFS
     VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE
     EAGEGN
//
ID   1433G_HUMAN             Reviewed;         247 AA.
AC   P61981; O70457; P35214; Q6FH52; Q9UDP2; Q9UN99;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-APR-2013, entry version 107.
DE   RecName: Full=14-3-3 protein gamma;
DE   AltName: Full=Protein kinase C inhibitor protein 1;
DE            Short=KCIP-1;
DE   Contains:
DE     RecName: Full=14-3-3 protein gamma, N-terminally processed;
GN   Name=YWHAG;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND INTERACTION WITH
RP   RAF1.
RC   TISSUE=Vascular smooth muscle;
RX   PubMed=10433554; DOI=10.1089/104454999315105;
RA   Autieri M.V., Carbone C.J.;
RT   "14-3-3gamma interacts with and is phosphorylated by multiple protein
RT   kinase C isoforms in PDGF-stimulated human vascular smooth muscle
RT   cells.";
RL   DNA Cell Biol. 18:555-564(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=10486217; DOI=10.1006/geno.1999.5887;
RA   Horie M., Suzuki M., Takahashi E., Tanigami A.;
RT   "Cloning, expression, and chromosomal mapping of the human 14-3-3gamma
RT   gene (YWHAG) to 7q11.23.";
RL   Genomics 60:241-243(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Endometrial tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-10; 13-56; 62-69; 133-172 AND 199-227, CLEAVAGE
RP   OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2,
RP   PHOSPHORYLATION AT THR-145, AND MASS SPECTROMETRY.
RC   TISSUE=Colon carcinoma, and Hepatoma;
RA   Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 2-12.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-10; 13-19; 29-42; 62-69; 133-143 AND 218-227,
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Platelet;
RA   Bienvenut W.V., Claeys D.;
RL   Submitted (NOV-2005) to UniProtKB.
RN   [9]
RP   PROTEIN SEQUENCE OF 92-110; 199-217 AND 228-247, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [10]
RP   INTERACTION WITH AANAT.
RX   PubMed=11427721; DOI=10.1073/pnas.141118798;
RA   Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA   Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA   Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT   "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-
RT   3-3-binding switch in melatonin synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN   [11]
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND MASS
RP   SPECTROMETRY.
RX   PubMed=14534293; DOI=10.1074/jbc.M309039200;
RA   Towbin H., Bair K.W., DeCaprio J.A., Eck M.J., Kim S., Kinder F.R.,
RA   Morollo A., Mueller D.R., Schindler P., Song H.K., van Oostrum J.,
RA   Versace R.W., Voshol H., Wood J., Zabludoff S., Phillips P.E.;
RT   "Proteomics-based target identification: bengamides as a new class of
RT   methionine aminopeptidase inhibitors.";
RL   J. Biol. Chem. 278:52964-52971(2003).
RN   [12]
RP   INTERACTION WITH CRTC2.
RX   PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
RA   Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,
RA   Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,
RA   Okamoto M., Montminy M.;
RT   "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
RT   coincidence detector.";
RL   Cell 119:61-74(2004).
RN   [13]
RP   INTERACTION WITH SSH1.
RX   PubMed=15159416; DOI=10.1083/jcb.200401136;
RA   Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
RA   Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
RT   "A pathway of neuregulin-induced activation of cofilin-phosphatase
RT   Slingshot and cofilin in lamellipodia.";
RL   J. Cell Biol. 165:465-471(2004).
RN   [14]
RP   INTERACTION WITH ABL1, AND MASS SPECTROMETRY.
RX   PubMed=15696159; DOI=10.1038/ncb1228;
RA   Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
RT   "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of
RT   c-Abl in the apoptotic response to DNA damage.";
RL   Nat. Cell Biol. 7:278-285(2005).
RN   [15]
RP   FUNCTION IN TP53 ACTIVATION, AND INTERACTION WITH MDM4.
RX   PubMed=16511572; DOI=10.1038/sj.emboj.7601010;
RA   Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H.;
RT   "14-3-3gamma binds to MDMX that is phosphorylated by UV-activated
RT   Chk1, resulting in p53 activation.";
RL   EMBO J. 25:1207-1218(2006).
RN   [16]
RP   INTERACTION WITH GAB2.
RX   PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA   Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA   Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA   Guilhaus M., James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT   the Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [19]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), MASS SPECTROMETRY, INTERACTION
RP   WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
RX   PubMed=17085597; DOI=10.1073/pnas.0605779103;
RA   Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
RA   Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
RT   "Structural basis for protein-protein interactions in the 14-3-3
RT   protein family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC   -!- SUBUNIT: Homodimer. Interacts with SAMSN1 (By similarity).
CC       Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1
CC       (phosphorylated form); the interaction retains it in the
CC       cytoplasm. Interacts with GAB2. Interacts with MDM4
CC       (phosphorylated); negatively regulates MDM4 activity toward TP53.
CC       Interacts with PKA-phosphorylated AANAT.
CC   -!- INTERACTION:
CC       Q14678-2:KANK1; NbExp=3; IntAct=EBI-359832, EBI-6173812;
CC       Q5S007:LRRK2; NbExp=2; IntAct=EBI-359832, EBI-5323863;
CC       Q7KZI7:MARK2; NbExp=2; IntAct=EBI-359832, EBI-516560;
CC       P27448:MARK3; NbExp=2; IntAct=EBI-359832, EBI-707595;
CC       P62258:YWHAE; NbExp=4; IntAct=EBI-359832, EBI-356498;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, skeletal muscle,
CC       and heart.
CC   -!- PTM: Phosphorylated by various PKC isozymes.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; AF142498; AAD48408.1; -; mRNA.
DR   EMBL; AB024334; BAA85184.1; -; mRNA.
DR   EMBL; CR541904; CAG46702.1; -; mRNA.
DR   EMBL; CR541925; CAG46723.1; -; mRNA.
DR   EMBL; AC006388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020963; AAH20963.1; -; mRNA.
DR   IPI; IPI00220642; -.
DR   RefSeq; NP_036611.2; NM_012479.3.
DR   UniGene; Hs.706016; -.
DR   PDB; 2B05; X-ray; 2.55 A; A/B/C/D/E/F=2-246.
DR   PDB; 3UZD; X-ray; 1.86 A; A=1-247.
DR   PDB; 4E2E; X-ray; 2.25 A; A=1-247.
DR   PDBsum; 2B05; -.
DR   PDBsum; 3UZD; -.
DR   PDBsum; 4E2E; -.
DR   ProteinModelPortal; P61981; -.
DR   SMR; P61981; 1-235.
DR   IntAct; P61981; 66.
DR   MINT; MINT-248956; -.
DR   STRING; 9606.ENSP00000306330; -.
DR   PhosphoSite; P61981; -.
DR   DMDM; 48428721; -.
DR   REPRODUCTION-2DPAGE; IPI00220642; -.
DR   PaxDb; P61981; -.
DR   PeptideAtlas; P61981; -.
DR   PRIDE; P61981; -.
DR   DNASU; 7532; -.
DR   Ensembl; ENST00000307630; ENSP00000306330; ENSG00000170027.
DR   GeneID; 7532; -.
DR   KEGG; hsa:7532; -.
DR   UCSC; uc011kgj.1; human.
DR   CTD; 7532; -.
DR   GeneCards; GC07M075956; -.
DR   HGNC; HGNC:12852; YWHAG.
DR   HPA; CAB013274; -.
DR   HPA; CAB018389; -.
DR   HPA; HPA026918; -.
DR   MIM; 605356; gene.
DR   neXtProt; NX_P61981; -.
DR   PharmGKB; PA37441; -.
DR   eggNOG; COG5040; -.
DR   HOGENOM; HOG000240379; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P61981; -.
DR   KO; K16198; -.
DR   OMA; CSETQHE; -.
DR   OrthoDB; EOG48PMM0; -.
DR   PhylomeDB; P61981; -.
DR   Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
DR   Pathway_Interaction_DB; pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
DR   Pathway_Interaction_DB; foxopathway; FoxO family signaling.
DR   Pathway_Interaction_DB; insulin_glucose_pathway; Insulin-mediated glucose transport.
DR   Pathway_Interaction_DB; p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
DR   Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
DR   Pathway_Interaction_DB; pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
DR   Reactome; REACT_11123; Membrane Trafficking.
DR   Reactome; REACT_115566; Cell Cycle.
DR   BindingDB; P61981; -.
DR   ChEMBL; CHEMBL1293296; -.
DR   ChiTaRS; YWHAG; human.
DR   EvolutionaryTrace; P61981; -.
DR   GenomeRNAi; 7532; -.
DR   NextBio; 29467; -.
DR   ArrayExpress; P61981; -.
DR   Bgee; P61981; -.
DR   CleanEx; HS_YWHAG; -.
DR   Genevestigator; P61981; -.
DR   GermOnline; ENSG00000170027; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0008426; F:protein kinase C inhibitor activity; NAS:UniProtKB.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0006605; P:protein targeting; IEA:Compara.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IMP:UniProtKB.
DR   GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; 14-3-3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Phosphoprotein; Reference proteome.
FT   CHAIN         1    247       14-3-3 protein gamma.
FT                                /FTId=PRO_0000367907.
FT   INIT_MET      1      1       Removed; alternate.
FT   CHAIN         2    247       14-3-3 protein gamma, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000058606.
FT   SITE         57     57       Interaction with phosphoserine on
FT                                interacting protein.
FT   SITE        132    132       Interaction with phosphoserine on
FT                                interacting protein.
FT   MOD_RES       1      1       N-acetylmethionine; in 14-3-3 protein
FT                                gamma; alternate; partial.
FT   MOD_RES       2      2       N-acetylvaline; in 14-3-3 protein gamma,
FT                                N-terminally processed; partial.
FT   MOD_RES       2      2       N-acetylvaline; partial.
FT   MOD_RES     117    117       Phosphotyrosine (By similarity).
FT   MOD_RES     145    145       Phosphothreonine.
FT   CONFLICT      4      4       R -> P (in Ref. 1; AAD48408).
FT   CONFLICT     19     19       R -> G (in Ref. 1; AAD48408).
FT   CONFLICT     78     78       Missing (in Ref. 1; AAD48408).
FT   CONFLICT     89     89       I -> V (in Ref. 1; AAD48408).
FT   CONFLICT    104    104       L -> V (in Ref. 1; AAD48408).
FT   CONFLICT    109    109       I -> Y (in Ref. 1; AAD48408).
FT   CONFLICT    119    122       SKVF -> RKDL (in Ref. 1; AAD48408).
FT   CONFLICT    144    145       AT -> GD (in Ref. 1; AAD48408).
FT   CONFLICT    157    158       AH -> R (in Ref. 1; AAD48408).
FT   CONFLICT    200    202       AFD -> EFE (in Ref. 1; AAD48408).
FT   CONFLICT    214    214       D -> E (in Ref. 1; AAD48408).
FT   CONFLICT    240    240       D -> DH (in Ref. 1; AAD48408).
FT   HELIX         4     16
FT   HELIX        20     31
FT   HELIX        39     70
FT   HELIX        79    106
FT   HELIX       108    111
FT   HELIX       117    137
FT   HELIX       140    164
FT   HELIX       170    185
FT   HELIX       190    206
FT   HELIX       207    210
FT   TURN        213    215
FT   HELIX       216    233
SQ   SEQUENCE   247 AA;  28303 MW;  B0D16C6DE1F4455D CRC64;
     MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW
     RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK
     VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS
     VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD
     DGGEGNN
//
ID   1433S_HUMAN             Reviewed;         248 AA.
AC   P31947; Q6FH30; Q6FH51; Q96DH0;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-APR-2013, entry version 138.
DE   RecName: Full=14-3-3 protein sigma;
DE   AltName: Full=Epithelial cell marker protein 1;
DE   AltName: Full=Stratifin;
GN   Name=SFN; Synonyms=HME1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Epithelium;
RX   PubMed=1390337;
RA   Prasad G.L., Valverius E.M., McDuffie E., Cooper H.L.;
RT   "Complementary DNA cloning of a novel epithelial cell marker protein,
RT   HME1, that may be down-regulated in neoplastic mammary cells.";
RL   Cell Growth Differ. 3:507-513(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 19-25;
RP   42-49; 118-122; 130-139; 149-159; 161-181; 196-199; 225-229 AND
RP   231-239.
RC   TISSUE=Keratinocyte;
RX   PubMed=8515476; DOI=10.1006/jmbi.1993.1346;
RA   Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H.,
RA   Walbum E., Vandekerckhove J., Celis J.E.;
RT   "Molecular cloning and expression of the transformation sensitive
RT   epithelial marker stratifin. A member of a protein family that has
RT   been involved in the protein kinase C signalling pathway.";
RL   J. Mol. Biol. 231:982-998(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   PubMed=9659898; DOI=10.1016/S1097-2765(00)80002-7;
RA   Hermeking H., Lengauer C., Polyak K., He T.-C., Zhang L.,
RA   Thiagalingam S., Kinzler K.W., Vogelstein B.;
RT   "14-3-3 sigma is a p53-regulated inhibitor of G2/M progression.";
RL   Mol. Cell 1:3-11(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Cervix, Lung, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 42-49 AND 118-122.
RC   TISSUE=Keratinocyte;
RX   PubMed=1286667; DOI=10.1002/elps.11501301199;
RA   Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA   Vandekerckhove J.;
RT   "Microsequences of 145 proteins recorded in the two-dimensional gel
RT   protein database of normal human epidermal keratinocytes.";
RL   Electrophoresis 13:960-969(1992).
RN   [8]
RP   IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS29
RP   AND VPS35.
RX   PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA   Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT   "Exportin 7 defines a novel general nuclear export pathway.";
RL   EMBO J. 23:3227-3236(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [10]
RP   INTERACTION WITH GAB2.
RX   PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA   Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA   Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA   Guilhaus M., James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT   the Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [13]
RP   INTERACTION WITH SRPK2.
RX   PubMed=19592491; DOI=10.1074/jbc.M109.026237;
RA   Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.;
RT   "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell
RT   cycle and cell death in neurons.";
RL   J. Biol. Chem. 284:24512-24525(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-248, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [16]
RP   INTERACTION WITH COPS6 AND RFWD2.
RX   PubMed=21625211; DOI=10.1038/onc.2011.192;
RA   Choi H.H., Gully C., Su C.H., Velazquez-Torres G., Chou P.C.,
RA   Tseng C., Zhao R., Phan L., Shaiken T., Chen J., Yeung S.C., Lee M.H.;
RT   "COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3
RT   ubiquitin ligase for 14-3-3sigma.";
RL   Oncogene 30:4791-4801(2011).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHOSERINE
RP   PEPTIDE.
RX   PubMed=15731107; DOI=10.1074/jbc.M500982200;
RA   Wilker E.W., Grant R.A., Artim S.C., Yaffe M.B.;
RT   "A structural basis for 14-3-3sigma functional specificity.";
RL   J. Biol. Chem. 280:18891-18898(2005).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner. When
CC       bound to KRT17, regulates protein synthesis and epithelial cell
CC       growth by stimulating Akt/mTOR pathway (By similarity).
CC   -!- FUNCTION: p53-regulated inhibitor of G2/M progression.
CC   -!- SUBUNIT: Homodimer. Interacts with KRT17 and SAMSN1 (By
CC       similarity). Found in a complex with XPO7, EIF4A1, ARHGAP1,
CC       VPS26A, VPS29, VPS35 and SFN. Interacts with GAB2. Interacts with
CC       SRPK2. Interacts with COPS6. Interacts with RFWD2; this
CC       interaction leads to proteasomal degradation.
CC   -!- INTERACTION:
CC       P00519:ABL1; NbExp=2; IntAct=EBI-476295, EBI-1550796;
CC       Q7L5N1:COPS6; NbExp=7; IntAct=EBI-476295, EBI-486838;
CC       Q14103-4:HNRNPD; NbExp=7; IntAct=EBI-476295, EBI-432545;
CC       O00444:PLK4; NbExp=2; IntAct=EBI-476295, EBI-746202;
CC       Q8NHY2:RFWD2; NbExp=6; IntAct=EBI-476295, EBI-5280824;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC       Secreted. Note=May be secreted by a non-classical secretory
CC       pathway.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P31947-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P31947-2; Sequence=VSP_021768;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Present mainly in tissues enriched in
CC       stratified squamous keratinizing epithelium.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; M93010; AAA59546.1; -; mRNA.
DR   EMBL; X57348; CAA40623.1; -; mRNA.
DR   EMBL; AF029081; AAC52029.1; -; Genomic_DNA.
DR   EMBL; AF029082; AAC52030.1; -; mRNA.
DR   EMBL; CR541905; CAG46703.1; -; mRNA.
DR   EMBL; CR541926; CAG46724.1; -; mRNA.
DR   EMBL; AL034380; CAB92118.1; -; Genomic_DNA.
DR   EMBL; BC000329; AAH00329.1; -; mRNA.
DR   EMBL; BC000995; AAH00995.1; -; mRNA.
DR   EMBL; BC001550; AAH01550.1; -; mRNA.
DR   EMBL; BC002995; AAH02995.1; -; mRNA.
DR   EMBL; BC023552; AAH23552.1; -; mRNA.
DR   IPI; IPI00013890; -.
DR   IPI; IPI00411765; -.
DR   PIR; S34753; S34753.
DR   PIR; S38956; S38956.
DR   RefSeq; NP_006133.1; NM_006142.3.
DR   UniGene; Hs.523718; -.
DR   PDB; 1YWT; X-ray; 2.40 A; A/B=1-248.
DR   PDB; 1YZ5; X-ray; 2.80 A; A/B=1-248.
DR   PDB; 3IQJ; X-ray; 1.15 A; A=1-231.
DR   PDB; 3IQU; X-ray; 1.05 A; A=1-231.
DR   PDB; 3IQV; X-ray; 1.20 A; A=1-231.
DR   PDB; 3LW1; X-ray; 1.28 A; A=1-248.
DR   PDB; 3MHR; X-ray; 1.15 A; A=1-231.
DR   PDB; 3O8I; X-ray; 2.00 A; A=1-231.
DR   PDB; 3P1N; X-ray; 1.40 A; A=1-231.
DR   PDB; 3P1O; X-ray; 1.90 A; A=1-231.
DR   PDB; 3P1P; X-ray; 1.95 A; A=1-231.
DR   PDB; 3P1Q; X-ray; 1.70 A; A=1-231.
DR   PDB; 3P1R; X-ray; 1.70 A; A=1-231.
DR   PDB; 3P1S; X-ray; 1.65 A; A=1-231.
DR   PDB; 3SMK; X-ray; 2.10 A; A=1-231.
DR   PDB; 3SML; X-ray; 1.90 A; A=1-231.
DR   PDB; 3SMM; X-ray; 2.00 A; A=1-231.
DR   PDB; 3SMN; X-ray; 2.00 A; A=1-231.
DR   PDB; 3SMO; X-ray; 1.80 A; A=1-231.
DR   PDB; 3SPR; X-ray; 1.99 A; A=1-231.
DR   PDB; 3T0L; X-ray; 1.60 A; A=1-231.
DR   PDB; 3T0M; X-ray; 1.62 A; A=1-231.
DR   PDB; 3U9X; X-ray; 1.80 A; A=1-231.
DR   PDB; 3UX0; X-ray; 1.75 A; A=1-231.
DR   PDB; 4DAT; X-ray; 1.40 A; A=1-231.
DR   PDB; 4DAU; X-ray; 2.00 A; A=1-231.
DR   PDBsum; 1YWT; -.
DR   PDBsum; 1YZ5; -.
DR   PDBsum; 3IQJ; -.
DR   PDBsum; 3IQU; -.
DR   PDBsum; 3IQV; -.
DR   PDBsum; 3LW1; -.
DR   PDBsum; 3MHR; -.
DR   PDBsum; 3O8I; -.
DR   PDBsum; 3P1N; -.
DR   PDBsum; 3P1O; -.
DR   PDBsum; 3P1P; -.
DR   PDBsum; 3P1Q; -.
DR   PDBsum; 3P1R; -.
DR   PDBsum; 3P1S; -.
DR   PDBsum; 3SMK; -.
DR   PDBsum; 3SML; -.
DR   PDBsum; 3SMM; -.
DR   PDBsum; 3SMN; -.
DR   PDBsum; 3SMO; -.
DR   PDBsum; 3SPR; -.
DR   PDBsum; 3T0L; -.
DR   PDBsum; 3T0M; -.
DR   PDBsum; 3U9X; -.
DR   PDBsum; 3UX0; -.
DR   PDBsum; 4DAT; -.
DR   PDBsum; 4DAU; -.
DR   ProteinModelPortal; P31947; -.
DR   SMR; P31947; 1-231.
DR   DIP; DIP-29861N; -.
DR   IntAct; P31947; 24.
DR   MINT; MINT-108060; -.
DR   STRING; 9606.ENSP00000340989; -.
DR   PhosphoSite; P31947; -.
DR   DMDM; 398953; -.
DR   OGP; P31947; -.
DR   SWISS-2DPAGE; P31947; -.
DR   PaxDb; P31947; -.
DR   PeptideAtlas; P31947; -.
DR   PRIDE; P31947; -.
DR   DNASU; 2810; -.
DR   Ensembl; ENST00000339276; ENSP00000340989; ENSG00000175793.
DR   GeneID; 2810; -.
DR   KEGG; hsa:2810; -.
DR   UCSC; uc001bnc.1; human.
DR   CTD; 2810; -.
DR   GeneCards; GC01P027189; -.
DR   HGNC; HGNC:10773; SFN.
DR   HPA; CAB006268; -.
DR   HPA; CAB040552; -.
DR   HPA; HPA011105; -.
DR   MIM; 601290; gene.
DR   neXtProt; NX_P31947; -.
DR   PharmGKB; PA177; -.
DR   eggNOG; COG5040; -.
DR   HOGENOM; HOG000240379; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P31947; -.
DR   KO; K06644; -.
DR   OMA; AFMKSAV; -.
DR   OrthoDB; EOG4XH00X; -.
DR   PhylomeDB; P31947; -.
DR   Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
DR   Pathway_Interaction_DB; pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
DR   Pathway_Interaction_DB; foxopathway; FoxO family signaling.
DR   Pathway_Interaction_DB; insulin_glucose_pathway; Insulin-mediated glucose transport.
DR   Pathway_Interaction_DB; p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
DR   Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
DR   Pathway_Interaction_DB; pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
DR   Reactome; REACT_11123; Membrane Trafficking.
DR   BindingDB; P31947; -.
DR   ChEMBL; CHEMBL1909482; -.
DR   EvolutionaryTrace; P31947; -.
DR   GenomeRNAi; 2810; -.
DR   NextBio; 11071; -.
DR   Bgee; P31947; -.
DR   CleanEx; HS_SFN; -.
DR   Genevestigator; P31947; -.
DR   GermOnline; ENSG00000175793; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008426; F:protein kinase C inhibitor activity; TAS:ProtInc.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:HGNC.
DR   GO; GO:0030216; P:keratinocyte differentiation; IEA:Compara.
DR   GO; GO:0043616; P:keratinocyte proliferation; IEA:Compara.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Compara.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Compara.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein kinase activity; IEA:Compara.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC.
DR   GO; GO:0043588; P:skin development; IEA:Compara.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; 14-3-3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Secreted.
FT   CHAIN         1    248       14-3-3 protein sigma.
FT                                /FTId=PRO_0000058643.
FT   SITE         56     56       Interaction with phosphoserine on
FT                                interacting protein.
FT   SITE        129    129       Interaction with phosphoserine on
FT                                interacting protein.
FT   MOD_RES       5      5       Phosphoserine.
FT   MOD_RES      64     64       Phosphoserine (By similarity).
FT   MOD_RES     216    216       Phosphoserine (By similarity).
FT   MOD_RES     248    248       Phosphoserine.
FT   VAR_SEQ      85    116       Missing (in isoform 2).
FT                                /FTId=VSP_021768.
FT   VARIANT     155    155       M -> I (in dbSNP:rs11542705).
FT                                /FTId=VAR_048095.
FT   CONFLICT     77     77       K -> M (in Ref. 4; CAG46703).
FT   CONFLICT    120    120       Y -> H (in Ref. 2; AAA59546).
FT   CONFLICT    242    242       A -> V (in Ref. 2; AAA59546).
FT   HELIX         3     15
FT   HELIX        19     31
FT   HELIX        38     69
FT   HELIX        80    104
FT   HELIX       107    110
FT   HELIX       114    134
FT   STRAND      137    139
FT   HELIX       140    161
FT   HELIX       167    182
FT   HELIX       187    204
FT   HELIX       205    207
FT   HELIX       210    230
SQ   SEQUENCE   248 AA;  27774 MW;  7F4B44E3AA59ECE6 CRC64;
     MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR
     VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY
     LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH
     YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG
     EAPQEPQS
//
ID   1433T_HUMAN             Reviewed;         245 AA.
AC   P27348; D6W4Z5; Q567U5; Q5TZU8; Q9UP48;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-APR-2013, entry version 143.
DE   RecName: Full=14-3-3 protein theta;
DE   AltName: Full=14-3-3 protein T-cell;
DE   AltName: Full=14-3-3 protein tau;
DE   AltName: Full=Protein HS1;
GN   Name=YWHAQ;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=T-cell;
RX   PubMed=2015305; DOI=10.1016/0167-4781(91)90136-A;
RA   Nielsen P.J.;
RT   "Primary structure of a human protein kinase regulator protein.";
RL   Biochim. Biophys. Acta 1088:425-428(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Keratinocyte;
RX   PubMed=8515476; DOI=10.1006/jmbi.1993.1346;
RA   Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H.,
RA   Walbum E., Vandekerckhove J., Celis J.E.;
RT   "Molecular cloning and expression of the transformation sensitive
RT   epithelial marker stratifin. A member of a protein family that has
RT   been involved in the protein kinase C signalling pathway.";
RL   J. Mol. Biol. 231:982-998(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta, Skin, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-18.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-9; 28-49; 61-68; 104-115; 139-167 AND 213-222,
RP   ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma, and Hepatoma;
RA   Bienvenut W.V., Dhillon A.S., Kolch W.;
RL   Submitted (FEB-2008) to UniProtKB.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-245.
RC   TISSUE=Brain;
RA   Yu W., Gibbs R.A.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION AT SER-232, AND MASS SPECTROMETRY.
RX   PubMed=9360956; DOI=10.1074/jbc.272.46.28882;
RA   Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y.,
RA   Morrice N., Moelling K., Aitken A.;
RT   "14-3-3 is phosphorylated by casein kinase I on residue 233.
RT   Phosphorylation at this site in vivo regulates Raf/14-3-3
RT   interaction.";
RL   J. Biol. Chem. 272:28882-28888(1997).
RN   [10]
RP   TISSUE SPECIFICITY.
RX   PubMed=11080204; DOI=10.1046/j.1471-4159.2000.0752511.x;
RA   Malaspina A., Kaushik N., de Belleroche J.;
RT   "A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal
RT   cord.";
RL   J. Neurochem. 75:2511-2520(2000).
RN   [11]
RP   INTERACTION WITH CDKN1B.
RX   PubMed=12042314; DOI=10.1074/jbc.M203668200;
RA   Fujita N., Sato S., Katayama K., Tsuruo T.;
RT   "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3
RT   and cytoplasmic localization.";
RL   J. Biol. Chem. 277:28706-28713(2002).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH PDPK1.
RX   PubMed=12177059; DOI=10.1074/jbc.M205141200;
RA   Sato S., Fujita N., Tsuruo T.;
RT   "Regulation of kinase activity of 3-phosphoinositide-dependent protein
RT   kinase-1 by binding to 14-3-3.";
RL   J. Biol. Chem. 277:39360-39367(2002).
RN   [13]
RP   INTERACTION WITH SSH1.
RX   PubMed=15159416; DOI=10.1083/jcb.200401136;
RA   Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
RA   Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
RT   "A pathway of neuregulin-induced activation of cofilin-phosphatase
RT   Slingshot and cofilin in lamellipodia.";
RL   J. Cell Biol. 165:465-471(2004).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [15]
RP   INTERACTION WITH GAB2.
RX   PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA   Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA   Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA   Guilhaus M., James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT   the Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3; LYS-49; LYS-68 AND
RP   LYS-115, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=7603573; DOI=10.1038/376188a0;
RA   Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A.,
RA   Gamblin S.J.;
RT   "Structure of a 14-3-3 protein and implications for coordination of
RT   multiple signalling pathways.";
RL   Nature 376:188-191(1995).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234, MASS SPECTROMETRY,
RP   INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
RX   PubMed=17085597; DOI=10.1073/pnas.0605779103;
RA   Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
RA   Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
RT   "Structural basis for protein-protein interactions in the 14-3-3
RT   protein family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC       Negatively regulates the kinase activity of PDPK1.
CC   -!- SUBUNIT: Homodimer. Interacts with CDK16 (By similarity).
CC       Interacts with SSH1. Interacts with CDKN1B ('Thr-198'
CC       phosphorylated form); the interaction translocates CDKN1B to the
CC       cytoplasm. Interacts with GAB2. Interacts with the 'Ser-241'
CC       phosphorylated form of PDPK1.
CC   -!- INTERACTION:
CC       Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359854, EBI-1567267;
CC       P49407:ARRB1; NbExp=3; IntAct=EBI-359854, EBI-2561130;
CC       P32121:ARRB2; NbExp=3; IntAct=EBI-359854, EBI-714559;
CC       O94921:CDK14; NbExp=3; IntAct=EBI-359854, EBI-1043945;
CC       P00533:EGFR; NbExp=4; IntAct=EBI-359854, EBI-297353;
CC       P23945:FSHR; NbExp=3; IntAct=EBI-359854, EBI-848267;
CC       Q14678:KANK1; NbExp=2; IntAct=EBI-359854, EBI-2556221;
CC       Q14678-2:KANK1; NbExp=3; IntAct=EBI-359854, EBI-6173812;
CC       Q5S007:LRRK2; NbExp=3; IntAct=EBI-359854, EBI-5323863;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, axonally
CC       transported to the nerve terminals.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in brain, heart and
CC       pancreas, and at lower levels in kidney and placenta. Up-regulated
CC       in the lumbar spinal cord from patients with sporadic amyotrophic
CC       lateral sclerosis (ALS) compared with controls, with highest
CC       levels of expression in individuals with predominant lower motor
CC       neuron involvement.
CC   -!- PTM: Ser-232 is probably phosphorylated by CK1.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; X56468; CAA39840.1; -; mRNA.
DR   EMBL; X57347; CAA40622.1; -; mRNA.
DR   EMBL; BT020014; AAV38817.1; -; mRNA.
DR   EMBL; CH471053; EAX00977.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00979.1; -; Genomic_DNA.
DR   EMBL; BC050601; AAH50601.1; -; mRNA.
DR   EMBL; BC056867; AAH56867.1; -; mRNA.
DR   EMBL; BC093019; AAH93019.1; -; mRNA.
DR   EMBL; AF070556; AAC28640.1; -; mRNA.
DR   IPI; IPI00018146; -.
DR   PIR; S15076; S15076.
DR   RefSeq; NP_006817.1; NM_006826.2.
DR   UniGene; Hs.74405; -.
DR   PDB; 2BTP; X-ray; 2.80 A; A/B=1-234.
DR   PDBsum; 2BTP; -.
DR   ProteinModelPortal; P27348; -.
DR   SMR; P27348; 1-230.
DR   DIP; DIP-27584N; -.
DR   IntAct; P27348; 40.
DR   MINT; MINT-121282; -.
DR   STRING; 9606.ENSP00000238081; -.
DR   PhosphoSite; P27348; -.
DR   DMDM; 112690; -.
DR   OGP; P27348; -.
DR   REPRODUCTION-2DPAGE; IPI00018146; -.
DR   PaxDb; P27348; -.
DR   PeptideAtlas; P27348; -.
DR   PRIDE; P27348; -.
DR   DNASU; 10971; -.
DR   Ensembl; ENST00000238081; ENSP00000238081; ENSG00000134308.
DR   Ensembl; ENST00000381844; ENSP00000371267; ENSG00000134308.
DR   GeneID; 10971; -.
DR   KEGG; hsa:10971; -.
DR   UCSC; uc002qzx.3; human.
DR   CTD; 10971; -.
DR   GeneCards; GC02M009724; -.
DR   H-InvDB; HIX0077146; -.
DR   HGNC; HGNC:12854; YWHAQ.
DR   HPA; CAB010286; -.
DR   HPA; HPA007925; -.
DR   MIM; 609009; gene.
DR   neXtProt; NX_P27348; -.
DR   PharmGKB; PA37443; -.
DR   eggNOG; COG5040; -.
DR   HOGENOM; HOG000240379; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P27348; -.
DR   KO; K16197; -.
DR   OMA; AMEKTEL; -.
DR   OrthoDB; EOG480HXJ; -.
DR   PhylomeDB; P27348; -.
DR   Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
DR   Pathway_Interaction_DB; pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
DR   Pathway_Interaction_DB; foxopathway; FoxO family signaling.
DR   Pathway_Interaction_DB; insulin_glucose_pathway; Insulin-mediated glucose transport.
DR   Pathway_Interaction_DB; p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
DR   Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
DR   Pathway_Interaction_DB; pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
DR   Reactome; REACT_11123; Membrane Trafficking.
DR   ChiTaRS; YWHAQ; human.
DR   EvolutionaryTrace; P27348; -.
DR   GenomeRNAi; 10971; -.
DR   NextBio; 41686; -.
DR   PMAP-CutDB; P27348; -.
DR   ArrayExpress; P27348; -.
DR   Bgee; P27348; -.
DR   CleanEx; HS_YWHAQ; -.
DR   Genevestigator; P27348; -.
DR   GermOnline; ENSG00000134308; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:BHF-UCL.
DR   GO; GO:0006605; P:protein targeting; IEA:Compara.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Compara.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; 14-3-3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Phosphoprotein; Reference proteome.
FT   CHAIN         1    245       14-3-3 protein theta.
FT                                /FTId=PRO_0000058636.
FT   SITE         56     56       Interaction with phosphoserine on
FT                                interacting protein.
FT   SITE        127    127       Interaction with phosphoserine on
FT                                interacting protein.
FT   MOD_RES       1      1       N-acetylmethionine.
FT   MOD_RES       3      3       N6-acetyllysine.
FT   MOD_RES      49     49       N6-acetyllysine.
FT   MOD_RES      68     68       N6-acetyllysine.
FT   MOD_RES     115    115       N6-acetyllysine.
FT   MOD_RES     232    232       Phosphoserine.
FT   CONFLICT    136    136       D -> N (in Ref. 3; AAV38817).
FT   HELIX         3     15
FT   HELIX        19     31
FT   HELIX        38     68
FT   HELIX        75    103
FT   TURN        104    108
FT   HELIX       112    132
FT   HELIX       135    159
FT   HELIX       165    180
FT   HELIX       185    201
FT   TURN        202    205
FT   HELIX       208    227
SQ   SEQUENCE   245 AA;  27764 MW;  175534325E9E37C4 CRC64;
     MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR
     VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK
     MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE
     ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA
     EGAEN
//
ID   1433Z_HUMAN             Reviewed;         245 AA.
AC   P63104; A8K1N0; P29213; P29312; Q32P43; Q5XJ08; Q6GPI2; Q6IN74;
AC   Q6NUR9; Q6P3U9; Q86V33;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-APR-2013, entry version 114.
DE   RecName: Full=14-3-3 protein zeta/delta;
DE   AltName: Full=Protein kinase C inhibitor protein 1;
DE            Short=KCIP-1;
GN   Name=YWHAZ;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=1577711;
RA   Zupan L.A., Steffens D.L., Berry C.A., Landt M.L., Gross R.W.;
RT   "Cloning and expression of a human 14-3-3 protein mediating
RT   phospholipolysis. Identification of an arachidonoyl-enzyme
RT   intermediate during catalysis.";
RL   J. Biol. Chem. 267:8707-8710(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=9512661; DOI=10.1016/S0167-4781(97)00171-1;
RA   Seluja G.A., Pietromonaco S.F., Elias L.;
RT   "Two unique 5' untranslated regions in mRNAs encoding human 14-3-3
RT   zeta: differential expression in hemopoietic cells.";
RL   Biochim. Biophys. Acta 1395:281-287(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Colon, Eye, Melanoma, PNS, Skin, Testis, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-18.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-9; 12-18; 28-49; 61-68; 86-91; 128-158 AND
RP   213-222, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma, and Platelet;
RA   Bienvenut W.V., Potts A., Barblan J., Claeys D., Quadroni M.;
RL   Submitted (NOV-2005) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 92-103; 140-157; 194-212 AND 223-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [9]
RP   PHOSPHORYLATION AT THR-232, INTERACTION WITH RAF1, AND FUNCTION.
RX   PubMed=9360956; DOI=10.1074/jbc.272.46.28882;
RA   Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y.,
RA   Morrice N., Moelling K., Aitken A.;
RT   "14-3-3 is phosphorylated by casein kinase I on residue 233.
RT   Phosphorylation at this site in vivo regulates Raf/14-3-3
RT   interaction.";
RL   J. Biol. Chem. 272:28882-28888(1997).
RN   [10]
RP   INTERACTION WITH TLK2.
RX   PubMed=10455159; DOI=10.1074/jbc.274.35.24865;
RA   Zhang S., Xing H., Muslin A.J.;
RT   "Nuclear localization of protein kinase U-alpha is regulated by 14-3-
RT   3.";
RL   J. Biol. Chem. 274:24865-24872(1999).
RN   [11]
RP   INTERACTION WITH AANAT.
RX   PubMed=11427721; DOI=10.1073/pnas.141118798;
RA   Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA   Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA   Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT   "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-
RT   3-3-binding switch in melatonin synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN   [12]
RP   PHOSPHORYLATION AT SER-58, AND INTERACTION WITH AKT1.
RX   PubMed=11956222; DOI=10.1074/jbc.M203167200;
RA   Powell D.W., Rane M.J., Chen Q., Singh S., McLeish K.R.;
RT   "Identification of 14-3-3zeta as a protein kinase B/Akt substrate.";
RL   J. Biol. Chem. 277:21639-21642(2002).
RN   [13]
RP   PHOSPHORYLATION AT SER-58, AND DIMERIZATION.
RX   PubMed=12865427; DOI=10.1074/jbc.M304689200;
RA   Woodcock J.M., Murphy J., Stomski F.C., Berndt M.C., Lopez A.F.;
RT   "The dimeric versus monomeric status of 14-3-3zeta is controlled by
RT   phosphorylation of Ser58 at the dimer interface.";
RL   J. Biol. Chem. 278:36323-36327(2003).
RN   [14]
RP   INTERACTION WITH AANAT, AND FUNCTION.
RX   PubMed=14578935; DOI=10.1038/nsb1005;
RA   Zheng W., Zhang Z., Ganguly S., Weller J.L., Klein D.C., Cole P.A.;
RT   "Cellular stabilization of the melatonin rhythm enzyme induced by
RT   nonhydrolyzable phosphonate incorporation.";
RL   Nat. Struct. Biol. 10:1054-1057(2003).
RN   [15]
RP   PHOSPHORYLATION AT SER-184, INTERACTION WITH BAX, FUNCTION, AND
RP   MUTAGENESIS OF SER-184.
RX   PubMed=15071501; DOI=10.1038/sj.emboj.7600194;
RA   Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S.,
RA   Tsujimoto Y., Yoshioka K., Masuyama N., Gotoh Y.;
RT   "JNK promotes Bax translocation to mitochondria through
RT   phosphorylation of 14-3-3 proteins.";
RL   EMBO J. 23:1889-1899(2004).
RN   [16]
RP   INTERACTION WITH SSH1.
RX   PubMed=15159416; DOI=10.1083/jcb.200401136;
RA   Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
RA   Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
RT   "A pathway of neuregulin-induced activation of cofilin-phosphatase
RT   Slingshot and cofilin in lamellipodia.";
RL   J. Cell Biol. 165:465-471(2004).
RN   [17]
RP   INTERACTION WITH MLLT7.
RX   PubMed=16114898; DOI=10.1021/bi050618r;
RA   Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J.,
RA   Boura E., Obsil T.;
RT   "14-3-3 protein interacts with nuclear localization sequence of
RT   forkhead transcription factor FoxO4.";
RL   Biochemistry 44:11608-11617(2005).
RN   [18]
RP   INTERACTION WITH SSH1.
RX   PubMed=15660133; DOI=10.1038/sj.emboj.7600543;
RA   Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N.,
RA   Sarcevic B., Sampath R., Bamburg J.R., Bernard O.;
RT   "Interplay between components of a novel LIM kinase-slingshot
RT   phosphatase complex regulates cofilin.";
RL   EMBO J. 24:473-486(2005).
RN   [19]
RP   PHOSPHORYLATION AT SER-58, AND MUTAGENESIS OF SER-58.
RX   PubMed=15883165; DOI=10.1074/jbc.M409081200;
RA   Ma Y., Pitson S., Hercus T., Murphy J., Lopez A., Woodcock J.;
RT   "Sphingosine activates protein kinase A type II by a novel cAMP-
RT   independent mechanism.";
RL   J. Biol. Chem. 280:26011-26017(2005).
RN   [20]
RP   INTERACTION WITH ABL1, MASS SPECTROMETRY, PHOSPHORYLATION AT SER-184,
RP   AND MUTAGENESIS OF SER-184.
RX   PubMed=15696159; DOI=10.1038/ncb1228;
RA   Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
RT   "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of
RT   c-Abl in the apoptotic response to DNA damage.";
RL   Nat. Cell Biol. 7:278-285(2005).
RN   [21]
RP   INTERACTION WITH AANAT, AND FUNCTION.
RX   PubMed=15644438; DOI=10.1073/pnas.0406871102;
RA   Ganguly S., Weller J.L., Ho A., Chemineau P., Malpaux B., Klein D.C.;
RT   "Melatonin synthesis: 14-3-3-dependent activation and inhibition of
RT   arylalkylamine N-acetyltransferase mediated by phosphoserine-205.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:1222-1227(2005).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [23]
RP   PHOSPHORYLATION AT SER-58, DIMERIZATION, INTERACTION WITH TP53 AND
RP   YWHAE, FUNCTION, AND MUTAGENESIS OF SER-58.
RX   PubMed=16376338; DOI=10.1016/j.febslet.2005.12.024;
RA   Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.;
RT   "Protein kinase A phosphorylates and regulates dimerization of 14-3-3
RT   epsilon.";
RL   FEBS Lett. 580:305-310(2006).
RN   [24]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA   Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA   Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA   Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [25]
RP   INTERACTION WITH NOXA1, AND MUTAGENESIS OF LYS-49.
RX   PubMed=17913709; DOI=10.1074/jbc.M704754200;
RA   Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.;
RT   "Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1
RT   and 14-3-3 binding.";
RL   J. Biol. Chem. 282:34787-34800(2007).
RN   [26]
RP   INTERACTION WITH ARHGEF2.
RX   PubMed=14970201; DOI=10.1074/jbc.M400084200;
RA   Zenke F.T., Krendel M., DerMardirossian C., King C.C., Bohl B.P.,
RA   Bokoch G.M.;
RT   "p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to
RT   GEF-H1, a microtubule-localized Rho exchange factor.";
RL   J. Biol. Chem. 279:18392-18400(2004).
RN   [27]
RP   INTERACTION WITH GAB2.
RX   PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA   Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA   Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA   Guilhaus M., James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT   the Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [30]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3 AND LYS-68, AND
RP   MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [31]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND THR-232, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [32]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [33]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=10488331; DOI=10.1016/S1097-2765(00)80363-9;
RA   Rittinger K., Budman J., Xu J., Volinia S., Cantley L.C.,
RA   Smerdon S.J., Gamblin S.J., Yaffe M.B.;
RT   "Structural analysis of 14-3-3 phosphopeptide complexes identifies a
RT   dual role for the nuclear export signal of 14-3-3 in ligand binding.";
RL   Mol. Cell 4:153-166(1999).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AANAT.
RX   PubMed=11336675; DOI=10.1016/S0092-8674(01)00316-6;
RA   Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F.;
RT   "Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase
RT   complex. a role for scaffolding in enzyme regulation.";
RL   Cell 105:257-267(2001).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HISTONE H3
RP   PHOSPHOPEPTIDE.
RX   PubMed=16246723; DOI=10.1016/j.molcel.2005.08.032;
RA   Macdonald N., Welburn J.P.I., Noble M.E.M., Nguyen A., Yaffe M.B.,
RA   Clynes D., Moggs J.G., Orphanides G., Thomson S., Edmunds J.W.,
RA   Clayton A.L., Endicott J.A., Mahadevan L.C.;
RT   "Molecular basis for the recognition of phosphorylated and
RT   phosphoacetylated histone h3 by 14-3-3.";
RL   Mol. Cell 20:199-211(2005).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-230 IN COMPLEX WITH
RP   PSEUDOMONAS AERUGINOSA EXOS.
RX   PubMed=17235285; DOI=10.1038/sj.emboj.7601530;
RA   Ottmann C., Yasmin L., Weyand M., Veesenmeyer J.L., Diaz M.H.,
RA   Palmer R.H., Francis M.S., Hauser A.R., Wittinghofer A., Hallberg B.;
RT   "Phosphorylation-independent interaction between 14-3-3 and exoenzyme
RT   S: from structure to pathogenesis.";
RL   EMBO J. 26:902-913(2007).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC   -!- SUBUNIT: Interacts with CDK16 and BSPRY (By similarity). Interacts
CC       with WEE1 (C-terminal). Interacts with SAMSN1 (By similarity).
CC       Interacts with MLF1 (phosphorylated form); the interaction retains
CC       it in the cytoplasm (By similarity). Interacts with Thr-
CC       phosphorylated ITGB2 (By similarity). Interacts with BCL2L11 (By
CC       similarity). Homodimer. Heterodimerizes with YWHAE. Homo- and
CC       hetero-dimerization is inhibited by phosphorylation on Ser-58.
CC       Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. Interacts with
CC       Pseudomonas aeruginosa exoS (unphosphorylated form). Interacts
CC       with BAX; the interaction occurs in the cytoplasm. Under stress
CC       conditions, MAPK8-mediated phosphorylation releases BAX to
CC       mitochondria. Interacts with phosphorylated RAF1; the interaction
CC       is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts
CC       with TP53; the interaction enhances p53 transcriptional activity.
CC       The Ser-58 phosphorylated form inhibits this interaction and p53
CC       transcriptional activity. Interacts with ABL1 (phosphorylated
CC       form); the interaction retains ABL1 in the cytoplasm. Interacts
CC       with PKA-phosphorylated AANAT; the interaction modulates AANAT
CC       enzymatic activity by increasing affinity for arylalkylamines and
CC       acetyl-CoA and protecting the enzyme from dephosphorylation and
CC       proteasomal degradation. It may also prevent thiol-dependent
CC       inactivation. Interacts with AKT1; the interaction phosphorylates
CC       YWHAZ and modulates dimerization. Interacts with GAB2 and TLK2.
CC   -!- INTERACTION:
CC       Q29495:AANAT (xeno); NbExp=3; IntAct=EBI-347088, EBI-446413;
CC       P00519:ABL1; NbExp=2; IntAct=EBI-347088, EBI-1550796;
CC       Q9P0K1-3:ADAM22; NbExp=3; IntAct=EBI-347088, EBI-1567267;
CC       O00257-3:CBX4; NbExp=2; IntAct=EBI-347088, EBI-4392727;
CC       P23528:CFL1; NbExp=2; IntAct=EBI-347088, EBI-352733;
CC       P00533:EGFR; NbExp=4; IntAct=EBI-347088, EBI-297353;
CC       P30793:GCH1; NbExp=4; IntAct=EBI-347088, EBI-958183;
CC       Q5S007:LRRK2; NbExp=3; IntAct=EBI-347088, EBI-5323863;
CC       Q99683:MAP3K5; NbExp=2; IntAct=EBI-347088, EBI-476263;
CC       Q7KZI7:MARK2; NbExp=3; IntAct=EBI-347088, EBI-516560;
CC       P27448:MARK3; NbExp=6; IntAct=EBI-347088, EBI-707595;
CC       Q9NYL2:MLTK; NbExp=4; IntAct=EBI-347088, EBI-1058916;
CC       Q8TEW0:PARD3; NbExp=3; IntAct=EBI-347088, EBI-1221123;
CC       P04049:RAF1; NbExp=3; IntAct=EBI-347088, EBI-365996;
CC       P57059:SIK1; NbExp=4; IntAct=EBI-347088, EBI-1181640;
CC       Q9Y2K2:SIK3; NbExp=5; IntAct=EBI-347088, EBI-1384133;
CC       O00506:STK25; NbExp=2; IntAct=EBI-347088, EBI-5773834;
CC       P36897:TGFBR1; NbExp=4; IntAct=EBI-347088, EBI-1027557;
CC       P84198:VIM (xeno); NbExp=5; IntAct=EBI-347088, EBI-457639;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage
CC       I to stage IV melanosomes.
CC   -!- PTM: The delta, brain-specific form differs from the zeta form in
CC       being phosphorylated (By similarity). Phosphorylation on Ser-184
CC       by MAPK8; promotes dissociation of BAX and translocation of BAX to
CC       mitochondria. Phosphorylation on Thr-232; inhibits binding of
CC       RAF1. Phosphorylated on Ser-58 by PKA and protein kinase C delta
CC       type catalytic subunit in a sphingosine-dependent fashion.
CC       Phosphorylation on Ser-58 by PKA; disrupts homodimerization and
CC       heterodimerization with YHAE and TP53.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
CC   -!- CAUTION: Was originally (PubMed:1577711) thought to have
CC       phospholipase A2 activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH51814.1; Type=Erroneous initiation;
CC       Sequence=AAH73141.1; Type=Erroneous initiation;
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DR   EMBL; M86400; AAA36446.1; -; mRNA.
DR   EMBL; U28964; AAC52052.1; -; mRNA.
DR   EMBL; AK289945; BAF82634.1; -; mRNA.
DR   EMBL; CH471060; EAW91823.1; -; Genomic_DNA.
DR   EMBL; BC003623; AAH03623.3; -; mRNA.
DR   EMBL; BC051814; AAH51814.1; ALT_INIT; mRNA.
DR   EMBL; BC063824; AAH63824.2; -; mRNA.
DR   EMBL; BC068456; AAH68456.2; -; mRNA.
DR   EMBL; BC072426; AAH72426.2; -; mRNA.
DR   EMBL; BC073141; AAH73141.1; ALT_INIT; mRNA.
DR   EMBL; BC083508; AAH83508.2; -; mRNA.
DR   EMBL; BC099904; AAH99904.1; -; mRNA.
DR   EMBL; BC101483; AAI01484.1; -; mRNA.
DR   EMBL; BC108281; AAI08282.1; -; mRNA.
DR   EMBL; BC111951; AAI11952.1; -; mRNA.
DR   IPI; IPI00021263; -.
DR   PIR; A38246; PSHUAM.
DR   RefSeq; NP_001129171.1; NM_001135699.1.
DR   RefSeq; NP_001129172.1; NM_001135700.1.
DR   RefSeq; NP_001129173.1; NM_001135701.1.
DR   RefSeq; NP_001129174.1; NM_001135702.1.
DR   RefSeq; NP_003397.1; NM_003406.3.
DR   RefSeq; NP_663723.1; NM_145690.2.
DR   UniGene; Hs.492407; -.
DR   PDB; 1IB1; X-ray; 2.70 A; A/B/C/D=1-245.
DR   PDB; 1QJA; X-ray; 2.00 A; A/B=1-245.
DR   PDB; 1QJB; X-ray; 2.00 A; A/B=1-245.
DR   PDB; 2C1J; X-ray; 2.60 A; A/B=1-245.
DR   PDB; 2C1N; X-ray; 2.00 A; A/B=1-245.
DR   PDB; 2O02; X-ray; 1.50 A; A/B=1-230.
DR   PDB; 2WH0; X-ray; 2.25 A; A/B/C/D=1-245.
DR   PDB; 3CU8; X-ray; 2.40 A; A/B=1-245.
DR   PDB; 3NKX; X-ray; 2.40 A; A/B=1-245.
DR   PDB; 3RDH; X-ray; 2.39 A; A/B/C/D=1-245.
DR   PDB; 4FJ3; X-ray; 1.95 A; A/B=1-230.
DR   PDBsum; 1IB1; -.
DR   PDBsum; 1QJA; -.
DR   PDBsum; 1QJB; -.
DR   PDBsum; 2C1J; -.
DR   PDBsum; 2C1N; -.
DR   PDBsum; 2O02; -.
DR   PDBsum; 2WH0; -.
DR   PDBsum; 3CU8; -.
DR   PDBsum; 3NKX; -.
DR   PDBsum; 3RDH; -.
DR   PDBsum; 4FJ3; -.
DR   ProteinModelPortal; P63104; -.
DR   SMR; P63104; 1-230.
DR   DIP; DIP-563N; -.
DR   IntAct; P63104; 156.
DR   MINT; MINT-89071; -.
DR   PhosphoSite; P63104; -.
DR   DMDM; 52000887; -.
DR   DOSAC-COBS-2DPAGE; P63104; -.
DR   OGP; P63104; -.
DR   UCD-2DPAGE; P63104; -.
DR   PaxDb; P63104; -.
DR   PRIDE; P63104; -.
DR   DNASU; 7534; -.
DR   Ensembl; ENST00000353245; ENSP00000309503; ENSG00000164924.
DR   Ensembl; ENST00000395951; ENSP00000379281; ENSG00000164924.
DR   Ensembl; ENST00000395953; ENSP00000379283; ENSG00000164924.
DR   Ensembl; ENST00000395956; ENSP00000379286; ENSG00000164924.
DR   Ensembl; ENST00000395957; ENSP00000379287; ENSG00000164924.
DR   Ensembl; ENST00000395958; ENSP00000379288; ENSG00000164924.
DR   Ensembl; ENST00000419477; ENSP00000395114; ENSG00000164924.
DR   Ensembl; ENST00000457309; ENSP00000398599; ENSG00000164924.
DR   GeneID; 7534; -.
DR   KEGG; hsa:7534; -.
DR   UCSC; uc003yjv.2; human.
DR   CTD; 7534; -.
DR   GeneCards; GC08M101930; -.
DR   HGNC; HGNC:12855; YWHAZ.
DR   HPA; CAB005065; -.
DR   MIM; 601288; gene.
DR   neXtProt; NX_P63104; -.
DR   PharmGKB; PA37444; -.
DR   eggNOG; COG5040; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P63104; -.
DR   KO; K16197; -.
DR   OrthoDB; EOG4N30PR; -.
DR   PhylomeDB; P63104; -.
DR   Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
DR   Pathway_Interaction_DB; pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
DR   Pathway_Interaction_DB; foxopathway; FoxO family signaling.
DR   Pathway_Interaction_DB; igf1_pathway; IGF1 pathway.
DR   Pathway_Interaction_DB; insulin_glucose_pathway; Insulin-mediated glucose transport.
DR   Pathway_Interaction_DB; p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
DR   Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
DR   Pathway_Interaction_DB; pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
DR   Reactome; REACT_11123; Membrane Trafficking.
DR   Reactome; REACT_21257; Metabolism of RNA.
DR   Reactome; REACT_604; Hemostasis.
DR   Reactome; REACT_6900; Immune System.
DR   Reactome; REACT_71; Gene Expression.
DR   ChiTaRS; YWHAZ; human.
DR   DrugBank; DB01381; Ginkgo biloba.
DR   EvolutionaryTrace; P63104; -.
DR   GenomeRNAi; 7534; -.
DR   NextBio; 29475; -.
DR   ArrayExpress; P63104; -.
DR   Bgee; P63104; -.
DR   Genevestigator; P63104; -.
DR   GermOnline; ENSG00000164924; Homo sapiens.
DR   GO; GO:0031252; C:cell leading edge; IEA:Compara.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:Compara.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Compara.
DR   GO; GO:0043234; C:protein complex; IEA:Compara.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0002553; P:histamine secretion by mast cell; IEA:Compara.
DR   GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; IEA:Compara.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; 14-3-3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Phosphoprotein; Reference proteome.
FT   CHAIN         1    245       14-3-3 protein zeta/delta.
FT                                /FTId=PRO_0000058627.
FT   SITE         56     56       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        127    127       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine.
FT   MOD_RES       3      3       N6-acetyllysine.
FT   MOD_RES      58     58       Phosphoserine; by PKA and PKB/AKT1.
FT   MOD_RES      68     68       N6-acetyllysine.
FT   MOD_RES     184    184       Phosphoserine; by MAPK8.
FT   MOD_RES     207    207       Phosphoserine.
FT   MOD_RES     232    232       Phosphothreonine; by CK1.
FT   MUTAGEN      49     49       K->E: Loss of interaction with NOXA1.
FT   MUTAGEN      58     58       S->A: Loss of sphingosine-activated PKA
FT                                phosphorylation. Promotes
FT                                homodimerization and heterodimerization
FT                                with YWHAE. Enhanced transcriptional
FT                                activity of P53.
FT   MUTAGEN      58     58       S->E: Loss of homodimerization. Reduced
FT                                dimerization with YWHAE. Significantly
FT                                reduced interaction with P53. No
FT                                enhancement of P53 transcriptional
FT                                activity.
FT   MUTAGEN     184    184       S->A: On DNA damage, loss of MAPK8-
FT                                mediated phosphorylation. Loss of binding
FT                                ABL1. Attenuates ABL1-mediated apoptosis.
FT                                No loss of interaction with BAX under
FT                                stress conditions. Inhibits translocation
FT                                of BAX to mitochondria.
FT   CONFLICT     22     22       M -> V (in Ref. 5; AAH68456).
FT   HELIX         3     15
FT   HELIX        19     31
FT   HELIX        38     67
FT   TURN         69     71
FT   HELIX        76    103
FT   HELIX       105    108
FT   HELIX       112    131
FT   HELIX       135    159
FT   HELIX       165    180
FT   HELIX       185    200
FT   HELIX       201    205
FT   TURN        208    210
FT   HELIX       211    228
SQ   SEQUENCE   245 AA;  27745 MW;  D464DF2286BBFE60 CRC64;
     MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR
     VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK
     MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE
     ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG
     EGGEN
//
ID   1A01_HUMAN              Reviewed;         365 AA.
AC   P30443; O77964; O78171; Q9MYA3; Q9TP25; Q9TQP5;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-APR-2013, entry version 121.
DE   RecName: Full=HLA class I histocompatibility antigen, A-1 alpha chain;
DE   AltName: Full=MHC class I antigen A*1;
DE   Flags: Precursor;
GN   Name=HLA-A; Synonyms=HLAA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*01:01).
RX   PubMed=3375250; DOI=10.1073/pnas.85.11.4005;
RA   Parham P., Lomen C.E., Lawlor D.A., Ways J.P., Holmes N., Coppin H.L.,
RA   Salter R.D., Wan A.M., Ennis P.D.;
RT   "Nature of polymorphism in HLA-A, -B, and -C molecules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:4005-4009(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*01:01).
RX   PubMed=2715640;
RA   Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.;
RT   "Diversity and diversification of HLA-A,B,C alleles.";
RL   J. Immunol. 142:3937-3950(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*01:01).
RA   Warren E.;
RL   Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01).
RX   PubMed=2251137; DOI=10.1093/nar/18.22.6701;
RA   Girdlestone J.;
RT   "Nucleotide sequence of an HLA-A1 gene.";
RL   Nucleic Acids Res. 18:6701-6701(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01).
RX   PubMed=9349617; DOI=10.1111/j.1399-0039.1997.tb02885.x;
RA   Laforet M., Froelich N., Parissiadis A., Pfeiffer B., Schell A.,
RA   Faller B., Woehl-Jaegle M.L., Cazenave J.-P., Tongio M.M.;
RT   "A nucleotide insertion in exon 4 is responsible for the absence of
RT   expression of an HLA-A*01 allele.";
RL   Tissue Antigens 50:347-350(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*01:01).
RA   Waller M.J., Robinson J., Marsh S.G.E.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE A*01:01).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*01:02).
RX   PubMed=7761977; DOI=10.1111/j.1399-0039.1995.tb02437.x;
RA   Browning M.J., Madrigal J.A., Krausa P., Kowalski H., Allsopp C.E.,
RA   Little A.-M., Turner S., Adams E.J., Arnett K.L., Bodmer W.F.,
RA   Parham P.;
RT   "The HLA-A,B,C genotype of the class I negative cell line Daudi
RT   reveals novel HLA-A and -B alleles.";
RL   Tissue Antigens 45:177-187(1995).
RN   [9]
RP   NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*01:03).
RX   PubMed=9438203; DOI=10.1016/S0198-8859(97)00204-8;
RA   Sitha S., Scheltinga S.A., Johnston-Dow L.A., White C.B.,
RA   der van Zwan A.W., Bakema J.E., Rozemuller E.H., van der Tweel J.G.,
RA   Kronink M.N., Tilanus M.G.J.;
RT   "A generic sequencing based typing approach for the identification of
RT   HLA-A diversity.";
RL   Hum. Immunol. 57:120-128(1997).
RN   [10]
RP   NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*01:03).
RC   TISSUE=Blood;
RX   PubMed=11182232; DOI=10.1016/S0198-8859(00)00238-X;
RA   Poland G.A., Sohni Y., Domanico M., Kroning C.M., DeGoey S.R.,
RA   Jimale M., Jacobson R.M., Moore S.B.;
RT   "High frequency of HLA-A*0103 allele in a Somali population.";
RL   Hum. Immunol. 62:197-200(2001).
RN   [11]
RP   NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*01:06).
RX   PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x;
RA   Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R.,
RA   Ng J., Hartzman R.J., Hurley C.K.;
RT   "Seventeen more novel HLA-A locus alleles.";
RL   Tissue Antigens 55:369-373(2000).
RN   [12]
RP   NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*01:07).
RA   Tamouza R., Fortier C., Mahfoudh N., Schaeffer V., Poirier J.C.,
RA   Marzais F., Gautreau C., Charron D.;
RT   "A new HLA-A*01 allele.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   SULFATION.
RX   PubMed=3121736;
RA   Sant A.J., Zacheis M., Rumbarger T., Giacoletto K.S., Schwartz B.D.;
RT   "Human Ia alpha- and beta-chains are sulfated.";
RL   J. Immunol. 140:155-160(1988).
RN   [14]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 25-298 IN COMPLEX WITH MAGE
RP   ANTIGENIC PEPTIDE AND ANTIBODY, AND DISULFIDE BONDS.
RX   PubMed=15537658; DOI=10.1074/jbc.M411323200;
RA   Hulsmeyer M., Chames P., Hillig R.C., Stanfield R.L., Held G.,
RA   Coulie P.G., Alings C., Wille G., Saenger W., Uchanska-Ziegler B.,
RA   Hoogenboom H.R., Ziegler A.;
RT   "A major histocompatibility complex-peptide-restricted antibody and t
RT   cell receptor molecules recognize their target by distinct binding
RT   modes: crystal structure of human leukocyte antigen (HLA)-A1-MAGE-A1
RT   in complex with FAB-HYB3.";
RL   J. Biol. Chem. 280:2972-2980(2005).
RN   [16]
RP   VARIANT [LARGE SCALE ANALYSIS] LYS-151, VARIANT [LARGE SCALE ANALYSIS]
RP   THR-166, AND MASS SPECTROMETRY.
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC       immune system.
CC   -!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2-
CC       microglobulin). Interacts with human herpesvirus 8 MIR1 protein
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Sulfated.
CC   -!- PTM: Polyubiquitinated in a post ER compartment through
CC       interaction with human herpesvirus 8 MIR1 protein. This targets
CC       the protein for rapid degradation via the ubiquitin system (By
CC       similarity).
CC   -!- POLYMORPHISM: The following alleles of A-1 are known: A*01:01,
CC       A*01:02, A*01:03, A*01:06 and A*01:07. The sequence shown is that
CC       of A*01:01.
CC   -!- SIMILARITY: Belongs to the MHC class I family.
CC   -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like)
CC       domain.
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DR   EMBL; M24043; AAA59652.1; -; Genomic_DNA.
DR   EMBL; X55710; CAA39243.1; -; Genomic_DNA.
DR   EMBL; Z93949; CAB07989.1; -; Genomic_DNA.
DR   EMBL; AJ278305; CAB93537.1; -; Genomic_DNA.
DR   EMBL; BC003069; AAH03069.1; -; mRNA.
DR   EMBL; U07161; AAA80569.1; -; mRNA.
DR   EMBL; Y12469; CAA73072.1; -; Genomic_DNA.
DR   EMBL; Y12470; CAA73073.1; -; Genomic_DNA.
DR   EMBL; AH008863; AAF19525.1; -; Genomic_DNA.
DR   EMBL; AH007762; AAD33894.1; -; Genomic_DNA.
DR   EMBL; AH009407; AAF73862.1; -; Genomic_DNA.
DR   IPI; IPI00026569; -.
DR   PIR; I38518; I38518.
DR   PIR; I61856; I61856.
DR   RefSeq; NP_001229687.1; NM_001242758.1.
DR   UniGene; Hs.181244; -.
DR   UniGene; Hs.713441; -.
DR   PDB; 1W72; X-ray; 2.15 A; A/D=25-298.
DR   PDB; 3BO8; X-ray; 1.80 A; A=25-298.
DR   PDBsum; 1W72; -.
DR   PDBsum; 3BO8; -.
DR   ProteinModelPortal; P30443; -.
DR   SMR; P30443; 25-298.
DR   MINT; MINT-4655826; -.
DR   DMDM; 231347; -.
DR   PaxDb; P30443; -.
DR   PRIDE; P30443; -.
DR   DNASU; 3105; -.
DR   Ensembl; ENST00000431930; ENSP00000406366; ENSG00000229215.
DR   Ensembl; ENST00000443552; ENSP00000404678; ENSG00000224320.
DR   Ensembl; ENST00000549869; ENSP00000447635; ENSG00000224320.
DR   Ensembl; ENST00000552193; ENSP00000447614; ENSG00000229215.
DR   GeneID; 3105; -.
DR   KEGG; hsa:3105; -.
DR   UCSC; uc011ejp.2; human.
DR   CTD; 3105; -.
DR   GeneCards; GC06P029933; -.
DR   HGNC; HGNC:4931; HLA-A.
DR   MIM; 142800; gene.
DR   neXtProt; NX_P30443; -.
DR   eggNOG; NOG42056; -.
DR   HOVERGEN; HBG016709; -.
DR   KO; K06751; -.
DR   OrthoDB; EOG4F4SBG; -.
DR   Reactome; REACT_6900; Immune System.
DR   ChiTaRS; HLA-A; human.
DR   EvolutionaryTrace; P30443; -.
DR   GenomeRNAi; 3105; -.
DR   NextBio; 12319; -.
DR   ArrayExpress; P30443; -.
DR   CleanEx; HS_HLA-A; -.
DR   Genevestigator; P30443; -.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
DR   GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   GO; GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.500.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR011161; MHC_I-like_Ag-recog.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   InterPro; IPR001039; MHC_I_a_a1/a2.
DR   InterPro; IPR010579; MHC_I_a_C.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00129; MHC_I; 1.
DR   Pfam; PF06623; MHC_I_C; 1.
DR   PRINTS; PR01638; MHCCLASSI.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF54452; MHC_I/II-like_Ag-recog; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
KW   Host-virus interaction; Immunity; Immunoglobulin domain; Membrane;
KW   MHC I; Polymorphism; Reference proteome; Signal; Sulfation;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     24
FT   CHAIN        25    365       HLA class I histocompatibility antigen,
FT                                A-1 alpha chain.
FT                                /FTId=PRO_0000018813.
FT   TOPO_DOM     25    308       Extracellular (Potential).
FT   TRANSMEM    309    332       Helical; (Potential).
FT   TOPO_DOM    333    365       Cytoplasmic (Potential).
FT   DOMAIN      209    295       Ig-like C1-type.
FT   REGION       25    114       Alpha-1.
FT   REGION      115    206       Alpha-2.
FT   REGION      207    298       Alpha-3.
FT   REGION      299    308       Connecting peptide.
FT   MOD_RES      83     83       Sulfotyrosine (Potential).
FT   CARBOHYD    110    110       N-linked (GlcNAc...).
FT   DISULFID    125    188
FT   DISULFID    227    283
FT   VARIANT      33     33       F -> S (in allele A*01:02;
FT                                dbSNP:rs2075684).
FT                                /FTId=VAR_004332.
FT   VARIANT      41     41       R -> S (in allele A*01:02).
FT                                /FTId=VAR_004333.
FT   VARIANT      80     80       G -> R (in allele A*01:07).
FT                                /FTId=VAR_016719.
FT   VARIANT      89     89       R -> G (in dbSNP:rs1059459).
FT                                /FTId=VAR_056247.
FT   VARIANT      91     91       M -> V (in allele A*01:07).
FT                                /FTId=VAR_016720.
FT   VARIANT     100    100       A -> E (in allele A*01:07).
FT                                /FTId=VAR_016721.
FT   VARIANT     114    114       D -> A (in allele A*01:07).
FT                                /FTId=VAR_016722.
FT   VARIANT     121    121       I -> M (in allele A*01:03).
FT                                /FTId=VAR_016723.
FT   VARIANT     131    131       G -> W (in dbSNP:rs1136702).
FT                                /FTId=VAR_056248.
FT   VARIANT     133    133       F -> L (in dbSNP:rs1059488).
FT                                /FTId=VAR_056249.
FT   VARIANT     151    151       N -> K (in dbSNP:rs1059509).
FT                                /FTId=VAR_056250.
FT   VARIANT     166    166       I -> T (in dbSNP:rs1059516).
FT                                /FTId=VAR_056251.
FT   VARIANT     169    169       R -> H (in dbSNP:rs1059520).
FT                                /FTId=VAR_056252.
FT   VARIANT     180    180       R -> L (in allele A*01:06).
FT                                /FTId=VAR_016724.
FT   VARIANT     182    182       V -> A (in allele A*01:06).
FT                                /FTId=VAR_016725.
FT   VARIANT     205    205       R -> H (in dbSNP:rs17185861).
FT                                /FTId=VAR_056253.
FT   STRAND       27     36
FT   STRAND       41     43
FT   STRAND       45     52
FT   STRAND       55     61
FT   STRAND       64     66
FT   STRAND       70     73
FT   HELIX        74     76
FT   HELIX        81    109
FT   STRAND      113    115
FT   STRAND      118    127
FT   STRAND      133    142
FT   STRAND      145    150
FT   STRAND      157    159
FT   HELIX       162    173
FT   HELIX       176    185
FT   HELIX       187    198
FT   HELIX       200    203
FT   STRAND      210    217
FT   STRAND      219    235
FT   STRAND      238    243
FT   HELIX       249    251
FT   STRAND      261    263
FT   STRAND      265    274
FT   HELIX       278    280
FT   STRAND      281    286
FT   STRAND      294    296
SQ   SEQUENCE   365 AA;  40846 MW;  8667AFF3F06C4932 CRC64;
     MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF
     DSDAASQKME PRAPWIEQEG PEYWDQETRN MKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ
     IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAVHAAEQR
     RVYLEGRCVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT
     WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL
     SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL
     TACKV
//
ID   1A02_HUMAN              Reviewed;         365 AA.
AC   P01892; O19619; P06338; P10313; P30444; P30445; P30446; P30514;
AC   Q29680; Q29837; Q29899; Q95352; Q95380; Q9TPX8; Q9TPX9; Q9TPY0;
AC   Q9TQH5; Q9TQI3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-APR-2013, entry version 154.
DE   RecName: Full=HLA class I histocompatibility antigen, A-2 alpha chain;
DE   AltName: Full=MHC class I antigen A*2;
DE   Flags: Precursor;
GN   Name=HLA-A; Synonyms=HLAA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
RX   PubMed=2982951;
RA   Koller B.H., Orr H.T.;
RT   "Cloning and complete sequence of an HLA-A2 gene: analysis of two HLA-
RT   A alleles at the nucleotide level.";
RL   J. Immunol. 134:2727-2733(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*02:01).
RX   PubMed=2914713; DOI=10.1007/BF00395855;
RA   Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., Boccoli G.,
RA   Giannella G., Peschle C., Boncinelli E.;
RT   "Three new class I HLA alleles: structure of mRNAs and alternative
RT   mechanisms of processing.";
RL   Immunogenetics 29:80-91(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*02:01).
RX   PubMed=2320591; DOI=10.1073/pnas.87.7.2833;
RA   Ennis P.D., Zemmour J., Salter R.D., Parham P.;
RT   "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction:
RT   frequency and nature of errors produced in amplification.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 91-365.
RX   PubMed=3863816;
RA   Davidson W.F., Kress M., Khoury G., Jay G.;
RT   "Comparison of HLA class I gene sequences. Derivation of locus-
RT   specific oligonucleotide probes specific for HLA-A, HLA-B, and HLA-C
RT   genes.";
RL   J. Biol. Chem. 260:13414-13423(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE (ALLELES A*02:01; A*02:11 AND A*02:12).
RX   PubMed=1317015; DOI=10.1038/357326a0;
RA   Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J.,
RA   Williams R.C., Luz R., Petzl-Erler M.L., Parham P.;
RT   "Unusual HLA-B alleles in two tribes of Brazilian Indians.";
RL   Nature 357:326-329(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 39-365 (ALLELE A*02:01).
RX   PubMed=3874058;
RA   Krangel M.S.;
RT   "Unusual RNA splicing generates a secreted form of HLA-A2 in a
RT   mutagenized B lymphoblastoid cell line.";
RL   EMBO J. 4:1205-1210(1985).
RN   [7]
RP   PROTEIN SEQUENCE OF 25-295 (ALLELE A*02:01).
RX   PubMed=92029; DOI=10.1073/pnas.76.9.4395;
RA   Orr H.T., Lopez de Castro J.A., Parham P., Ploegh H.L.,
RA   Strominger J.L.;
RT   "Comparison of amino acid sequences of two human histocompatibility
RT   antigens, HLA-A2 and HLA-B7: location of putative alloantigenic
RT   sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 76:4395-4399(1979).
RN   [8]
RP   SEQUENCE REVISION (ALLELE A*02:01).
RX   PubMed=6179086; DOI=10.1073/pnas.79.12.3813;
RA   Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.;
RT   "Structure of crossreactive human histocompatibility antigens HLA-A28
RT   and HLA-A2: possible implications for the generation of HLA
RT   polymorphism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
RC   TISSUE=Blood;
RX   PubMed=7836067; DOI=10.1016/0198-8859(94)90087-6;
RA   Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.;
RT   "HLA class I allele (HLA-A2) expression defect associated with a
RT   mutation in its enhancer B inverted CAT box in two families.";
RL   Hum. Immunol. 41:69-73(1994).
RN   [10]
RP   SEQUENCE REVISION.
RA   Balas A.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*02:01).
RA   Cox S.T.;
RT   "Confirmation of HLA-A*0201.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELES A*02:02 AND
RP   A*02:03).
RX   PubMed=3497874; DOI=10.1007/BF00365911;
RA   Mattson D.H., Handy D.E., Bradley D.A., Coligan J.E., Cowan E.P.,
RA   Biddison W.E.;
RT   "DNA sequences of the genes that encode the CTL-defined HLA-A2
RT   variants M7 and DK1.";
RL   Immunogenetics 26:190-192(1987).
RN   [13]
RP   NUCLEOTIDE SEQUENCE (ALLELES A*02:03 AND A*02:05).
RX   PubMed=3496393;
RA   Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.;
RT   "Multiple genetic mechanisms have contributed to the generation of the
RT   HLA-A2/A28 family of class I MHC molecules.";
RL   J. Immunol. 139:936-941(1987).
RN   [14]
RP   NUCLEOTIDE SEQUENCE (ALLELES A*02:03 AND A*02:05).
RA   Domena J.D.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:04).
RX   PubMed=1937577; DOI=10.1007/BF00211991;
RA   Castano A.R., Lopez de Castro J.A.;
RT   "Structure of the HLA-A*0204 antigen, found in South American Indians.
RT   Spatial clustering of HLA-A2 subtype polymorphism.";
RL   Immunogenetics 34:281-285(1991).
RN   [16]
RP   NUCLEOTIDE SEQUENCE OF 9-365 (ALLELE A*02:04).
RX   PubMed=1589035; DOI=10.1038/357329a0;
RA   Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L.,
RA   Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H.,
RA   Troup G.M., Hughes A.L., Letvin N.L.;
RT   "New recombinant HLA-B alleles in a tribe of South American
RT   Amerindians indicate rapid evolution of MHC class I loci.";
RL   Nature 357:329-333(1992).
RN   [17]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*02:06).
RX   PubMed=2715640;
RA   Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.;
RT   "Diversity and diversification of HLA-A,B,C alleles.";
RL   J. Immunol. 142:3937-3950(1989).
RN   [18]
RP   PARTIAL PROTEIN SEQUENCE (ALLELE A*02:06).
RX   PubMed=3489037;
RA   Ezquerra A., Domenech N., van der Poel J., Strominger J.L., Vega M.A.,
RA   Lopez de Castro J.A.;
RT   "Molecular analysis of an HLA-A2 functional variant CLA defined by
RT   cytolytic T lymphocytes.";
RL   J. Immunol. 137:1642-1649(1986).
RN   [19]
RP   PARTIAL PROTEIN SEQUENCE (ALLELE A*02:07).
RX   PubMed=2448239; DOI=10.1007/BF00346586;
RA   Domenech N., Ezquerra A., Castano R., Lopez de Castro J.A.;
RT   "Structural analysis of HLA-A2.4 functional variant KNE. Implications
RT   for the mapping of HLA-A2-specific T-cell epitopes.";
RL   Immunogenetics 27:196-202(1988).
RN   [20]
RP   PARTIAL PROTEIN SEQUENCE (ALLELE A*02:08).
RX   PubMed=2457548; DOI=10.1007/BF00375853;
RA   Domenech N., Castano R., Goulmy E., Lopez de Castro J.A.;
RT   "Molecular analysis of HLA-A2.4 functional variant KLO: close
RT   structural and evolutionary relatedness to the HLA-A2.2 subtype.";
RL   Immunogenetics 28:143-152(1988).
RN   [21]
RP   PARTIAL PROTEIN SEQUENCE (ALLELE A*02:09).
RX   PubMed=3258580; DOI=10.1007/BF00395130;
RA   Castano R., Ezquerra A., Domenech N., Lopez de Castro J.A.;
RT   "An HLA-A2 population variant with structural polymorphism in the
RT   alpha 3 region.";
RL   Immunogenetics 27:345-355(1988).
RN   [22]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*02:10).
RX   PubMed=2783680; DOI=10.1007/BF00395859;
RA   Epstein H., Kennedy L., Holmes N.;
RT   "An Oriental HLA-A2 subtype is closely related to a subset of
RT   Caucasoid HLA-A2 alleles.";
RL   Immunogenetics 29:112-116(1989).
RN   [23]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:11).
RX   PubMed=1559719; DOI=10.1007/BF00189898;
RA   Castano A.R., Lopez de Castro J.A.;
RT   "Structure of the HLA-A*0211 (A2.5) subtype: further evidence for
RT   selection-driven diversification of HLA-A2 antigens.";
RL   Immunogenetics 35:344-346(1992).
RN   [24]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:13).
RX   PubMed=8168863; DOI=10.1007/BF00189243;
RA   Barber D.F., Fernandez J.M., Lopez de Castro J.A.;
RT   "Primary structure of a new HLA-A2 subtype: HLA-A*0213.";
RL   Immunogenetics 39:378-378(1994).
RN   [25]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:16).
RX   PubMed=7759139; DOI=10.1007/BF00164000;
RA   Barouch D., Krausa P., Bodmer J., Browning M.J., McMichael A.J.;
RT   "Identification of a novel HLA-A2 subtype, HLA-A*0216.";
RL   Immunogenetics 41:388-388(1995).
RN   [26]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:17).
RC   TISSUE=Blood;
RX   PubMed=7652742; DOI=10.1111/j.1399-0039.1995.tb02464.x;
RA   Selvakumar A., Granja C.B., Salazar M., Alosco S.M., Yunis E.J.,
RA   Dupont B.;
RT   "A novel subtype of A2 (A*0217) isolated from the South American
RT   Indian B-cell line AMALA.";
RL   Tissue Antigens 45:343-347(1995).
RN   [27]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*02:18).
RC   TISSUE=Blood;
RA   Kashiwase K., Tokunaga K., Ishikawa Y., Oohashi H., Hashimoto M.,
RA   Akaza T., Tadokoro K., Juji T.;
RT   "A new A2 sequence HLA-A2K from Japanese.";
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [28]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:20).
RC   TISSUE=Blood;
RX   PubMed=9008310; DOI=10.1111/j.1399-0039.1996.tb02691.x;
RA   Fleischhauer K., Zino E., Mazzi B., Severini G.M., Benazzi E.,
RA   Bordignon C.;
RT   "HLA-A*02 subtype distribution in Caucasians from northern Italy:
RT   identification of A*0220.";
RL   Tissue Antigens 48:673-679(1996).
RN   [29]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*02:21).
RC   TISSUE=Blood;
RA   Szmania S., Baxter-Lowe L.A.;
RT   "Nucleotide sequence of a novel HLA-A2 gene.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [30]
RP   NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*02:31).
RX   PubMed=10689125; DOI=10.1016/S0198-8859(99)00155-X;
RA   Ellis J.M., Henson V., Slack R., Ng J., Hartzman R.J., Hurley C.K.;
RT   "Frequencies of HLA-A2 alleles in five U.S. population groups.
RT   Predominance Of A*02011 and identification of HLA-A*0231.";
RL   Hum. Immunol. 61:334-340(2000).
RN   [31]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELE A*02:34).
RX   PubMed=10746792; DOI=10.1034/j.1399-0039.2000.550212.x;
RA   Moses J.H., Greville W.D., Downes J., McClenahan W., Kennedy A.,
RA   Dunckley H.;
RT   "A new HLA-A*02 allele, A*0234, detected by polymerase chain reaction
RT   using sequence-specific primers (PCR-SSP).";
RL   Tissue Antigens 55:175-177(2000).
RN   [32]
RP   NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*02:35; A*02:36 AND A*02:37).
RX   PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x;
RA   Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R.,
RA   Ng J., Hartzman R.J., Hurley C.K.;
RT   "Seventeen more novel HLA-A locus alleles.";
RL   Tissue Antigens 55:369-373(2000).
RN   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [34]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF A*02:01.
RX   PubMed=3309677; DOI=10.1038/329506a0;
RA   Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L.,
RA   Wiley D.C.;
RT   "Structure of the human class I histocompatibility antigen, HLA-A2.";
RL   Nature 329:506-512(1987).
RN   [36]
RP   INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
RX   PubMed=11390610; DOI=10.1128/JVI.75.13.6086-6094.2001;
RA   Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L.,
RA   Mulloy J.C., Jacobson S., Franchini G.;
RT   "Free major histocompatibility complex class I heavy chain is
RT   preferentially targeted for degradation by human T-cell
RT   leukemia/lymphotropic virus type 1 p12(I) protein.";
RL   J. Virol. 75:6086-6094(2001).
RN   [37]
RP   INTERACTION WITH HUMAN HERPESVIRUS 8 MIR1 PROTEIN, AND UBIQUITINATION.
RX   PubMed=12006494; DOI=10.1093/emboj/21.10.2418;
RA   Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G.,
RA   Lehner P.J.;
RT   "Ubiquitylation of MHC class I by the K3 viral protein signals
RT   internalization and TSG101-dependent degradation.";
RL   EMBO J. 21:2418-2429(2002).
RN   [38]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 25-300 OF HLA-A/B2M
RP   HETERODIMER IN COMPLEX WITH TRAC AND TRBC1, AND DISULFIDE BONDS.
RX   PubMed=12796775; DOI=10.1038/ni942;
RA   Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I.,
RA   Jones E.Y.;
RT   "A structural basis for immunodominant human T cell receptor
RT   recognition.";
RL   Nat. Immunol. 4:657-663(2003).
RN   [39]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF A*02:01.
RX   PubMed=2038058; DOI=10.1016/0022-2836(91)90567-P;
RA   Saper M.A., Bjorkman P.J., Wiley D.C.;
RT   "Refined structure of the human histocompatibility antigen HLA-A2 at
RT   2.6-A resolution.";
RL   J. Mol. Biol. 219:277-319(1991).
RN   [40]
RP   VARIANT [LARGE SCALE ANALYSIS] GLU-176, VARIANT [LARGE SCALE ANALYSIS]
RP   TRP-180, AND MASS SPECTROMETRY.
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC       immune system.
CC   -!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2-
CC       microglobulin). Interacts with human herpesvirus 8 MIR1 protein.
CC       Interacts with HTLV-1 accessory protein p12I.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Polyubiquitinated in a post ER compartment through
CC       interaction with human herpesvirus 8 MIR1 protein. This targets
CC       the protein for rapid degradation via the ubiquitin system.
CC   -!- POLYMORPHISM: The following alleles of A-2 are known: A*02:01,
CC       A*02:02, A*02:03, A*02:04, A*02:05, A*02:06 (A2.4A), A*02:07,
CC       A*02:08, A*02:09, A*02:10, A*02:11 (A2.5), A*02:12, A*02:13
CC       (A*02SLU), A*02:16, A*02:17, A*02:18 (A2K), A*02:19, A*02:20,
CC       A*02:21, A*02:31, A*02:34 (A*AAT), A*02:35, A*02:36 and A*02:37.
CC       The sequence shown is that of A*02:01.
CC   -!- SIMILARITY: Belongs to the MHC class I family.
CC   -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like)
CC       domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA41022.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown extensively;
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DR   EMBL; K02883; AAA98727.1; -; Genomic_DNA.
DR   EMBL; M84379; AAA59606.1; -; mRNA.
DR   EMBL; X02457; CAA26297.1; -; mRNA.
DR   EMBL; M11887; AAA52656.1; -; mRNA.
DR   EMBL; M19670; AAA03683.2; -; Genomic_DNA.
DR   EMBL; AH003586; AAB02120.1; -; Genomic_DNA.
DR   EMBL; U03863; AAA03604.1; -; mRNA.
DR   EMBL; M86404; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X57954; CAA41022.1; ALT_SEQ; mRNA.
DR   EMBL; U02935; AAA76608.2; -; Genomic_DNA.
DR   EMBL; AJ555412; CAD87771.1; -; Genomic_DNA.
DR   EMBL; U03862; AAA03603.1; -; mRNA.
DR   EMBL; M24042; AAA59653.1; -; mRNA.
DR   EMBL; Z23071; CAA80612.1; -; mRNA.
DR   EMBL; M84377; AAA59603.1; -; mRNA.
DR   EMBL; X60764; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M84378; AAA59604.1; -; mRNA.
DR   EMBL; Z27120; CAA81644.1; -; mRNA.
DR   EMBL; Z46633; CAA86602.1; -; mRNA.
DR   EMBL; U18930; AAA87076.1; -; mRNA.
DR   EMBL; D83515; BAA11935.1; -; mRNA.
DR   EMBL; X96724; CAA65501.1; -; mRNA.
DR   EMBL; U56825; AAB17465.1; -; mRNA.
DR   EMBL; AH007560; AAD23437.1; -; Genomic_DNA.
DR   EMBL; AH007704; AAD30272.1; -; Genomic_DNA.
DR   EMBL; AH008013; AAD45690.1; -; Genomic_DNA.
DR   EMBL; AH008012; AAD45689.1; -; Genomic_DNA.
DR   EMBL; AH008007; AAD45324.1; -; Genomic_DNA.
DR   IPI; IPI00876963; -.
DR   PIR; B24512; HLHU10.
DR   PIR; I37470; I37470.
DR   PIR; I37542; I37542.
DR   PIR; I38418; I38418.
DR   PIR; I38442; I38442.
DR   PIR; I38443; I38443.
DR   PIR; I55948; HLHUA2.
DR   PIR; I61857; I61857.
DR   PIR; I61902; I61902.
DR   PIR; I84448; I84448.
DR   UniGene; Hs.181244; -.
DR   UniGene; Hs.713441; -.
DR   PDB; 1AKJ; X-ray; 2.65 A; A=25-300.
DR   PDB; 1AO7; X-ray; 2.60 A; A=25-299.
DR   PDB; 1AQD; X-ray; 2.45 A; C/F/I/L=127-141.
DR   PDB; 1B0G; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 1B0R; X-ray; 2.90 A; A=25-299.
DR   PDB; 1BD2; X-ray; 2.50 A; A=25-299.
DR   PDB; 1DUY; X-ray; 2.15 A; A/D=25-299.
DR   PDB; 1DUZ; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 1EEY; X-ray; 2.25 A; A/D=25-299.
DR   PDB; 1EEZ; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 1HHG; X-ray; 2.60 A; A/D=25-299.
DR   PDB; 1HHH; X-ray; 3.00 A; A=25-299.
DR   PDB; 1HHI; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 1HHJ; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 1HHK; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 1HLA; X-ray; 3.50 A; A=25-294.
DR   PDB; 1I1F; X-ray; 2.80 A; A/D=25-299.
DR   PDB; 1I1Y; X-ray; 2.20 A; A/D=25-299.
DR   PDB; 1I4F; X-ray; 1.40 A; A=25-299.
DR   PDB; 1I7R; X-ray; 2.20 A; A/D=25-299.
DR   PDB; 1I7T; X-ray; 2.80 A; A/D=25-299.
DR   PDB; 1I7U; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 1IM3; X-ray; 2.20 A; A/E/I/M=25-299.
DR   PDB; 1JF1; X-ray; 1.85 A; A=25-299.
DR   PDB; 1JHT; X-ray; 2.15 A; A=25-299.
DR   PDB; 1LP9; X-ray; 2.00 A; A/H=25-299.
DR   PDB; 1OGA; X-ray; 1.40 A; A=25-300.
DR   PDB; 1P7Q; X-ray; 3.40 A; A=25-300.
DR   PDB; 1QEW; X-ray; 2.20 A; A=25-299.
DR   PDB; 1QR1; X-ray; 2.40 A; A/D=25-299.
DR   PDB; 1QRN; X-ray; 2.80 A; A=25-298.
DR   PDB; 1QSE; X-ray; 2.80 A; A=25-298.
DR   PDB; 1QSF; X-ray; 2.80 A; A=25-298.
DR   PDB; 1S8D; X-ray; 2.20 A; A=25-299.
DR   PDB; 1S9W; X-ray; 2.20 A; A=25-298.
DR   PDB; 1S9X; X-ray; 2.50 A; A=25-298.
DR   PDB; 1S9Y; X-ray; 2.30 A; A=25-298.
DR   PDB; 1T1W; X-ray; 2.20 A; A=25-299.
DR   PDB; 1T1X; X-ray; 2.20 A; A=25-299.
DR   PDB; 1T1Y; X-ray; 2.00 A; A=25-299.
DR   PDB; 1T1Z; X-ray; 1.90 A; A=25-299.
DR   PDB; 1T20; X-ray; 2.20 A; A=25-299.
DR   PDB; 1T21; X-ray; 2.19 A; A=25-299.
DR   PDB; 1T22; X-ray; 2.20 A; A=25-299.
DR   PDB; 1TVB; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 1TVH; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 1UR7; Model; -; A=25-299.
DR   PDB; 2AV1; X-ray; 1.95 A; A/D=25-299.
DR   PDB; 2AV7; X-ray; 2.05 A; A/D=25-299.
DR   PDB; 2BNQ; X-ray; 1.70 A; A=25-300.
DR   PDB; 2BNR; X-ray; 1.90 A; A=25-300.
DR   PDB; 2C7U; X-ray; 2.38 A; A/D=25-300.
DR   PDB; 2CLR; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 2F53; X-ray; 2.10 A; A=25-299.
DR   PDB; 2F54; X-ray; 2.70 A; A/F=25-298.
DR   PDB; 2GIT; X-ray; 1.70 A; A/D=25-299.
DR   PDB; 2GJ6; X-ray; 2.56 A; A=25-299.
DR   PDB; 2GT9; X-ray; 1.75 A; A/D=25-299.
DR   PDB; 2GTW; X-ray; 1.55 A; A/D=25-299.
DR   PDB; 2GTZ; X-ray; 1.70 A; A/D=25-299.
DR   PDB; 2GUO; X-ray; 1.90 A; A/D=25-299.
DR   PDB; 2J8U; X-ray; 2.88 A; A/H=25-299.
DR   PDB; 2JCC; X-ray; 2.50 A; A/H=25-299.
DR   PDB; 2P5E; X-ray; 1.89 A; A=25-300.
DR   PDB; 2P5W; X-ray; 2.20 A; A=25-300.
DR   PDB; 2PYE; X-ray; 2.30 A; A=25-300.
DR   PDB; 2UWE; X-ray; 2.40 A; A/H=25-299.
DR   PDB; 2V2W; X-ray; 1.60 A; A/D=25-300.
DR   PDB; 2V2X; X-ray; 1.60 A; A/D=25-300.
DR   PDB; 2VLJ; X-ray; 2.40 A; A=25-300.
DR   PDB; 2VLK; X-ray; 2.50 A; A=25-300.
DR   PDB; 2VLL; X-ray; 1.60 A; A/D=25-300.
DR   PDB; 2VLR; X-ray; 2.30 A; A/F=25-300.
DR   PDB; 2X4N; X-ray; 2.34 A; A/D=25-299.
DR   PDB; 2X4O; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 2X4P; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 2X4Q; X-ray; 1.90 A; A/D=25-299.
DR   PDB; 2X4R; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 2X4S; X-ray; 2.55 A; A/D=25-299.
DR   PDB; 2X4T; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 2X4U; X-ray; 2.10 A; A/D=25-299.
DR   PDB; 2X70; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 3BGM; X-ray; 1.60 A; A=25-298.
DR   PDB; 3BH8; X-ray; 1.65 A; A=25-298.
DR   PDB; 3BH9; X-ray; 1.70 A; A=25-299.
DR   PDB; 3BHB; X-ray; 2.20 A; A=25-298.
DR   PDB; 3D25; X-ray; 1.30 A; A=25-298.
DR   PDB; 3D39; X-ray; 2.81 A; A=25-299.
DR   PDB; 3D3V; X-ray; 2.80 A; A=25-299.
DR   PDB; 3FQN; X-ray; 1.65 A; A=25-299.
DR   PDB; 3FQR; X-ray; 1.70 A; A=25-299.
DR   PDB; 3FQT; X-ray; 1.80 A; A=25-299.
DR   PDB; 3FQU; X-ray; 1.80 A; A=25-299.
DR   PDB; 3FQW; X-ray; 1.93 A; A=25-299.
DR   PDB; 3FQX; X-ray; 1.70 A; A=25-299.
DR   PDB; 3FT2; X-ray; 1.80 A; A=25-299.
DR   PDB; 3FT3; X-ray; 1.95 A; A=25-299.
DR   PDB; 3FT4; X-ray; 1.90 A; A=25-299.
DR   PDB; 3GIV; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 3GJF; X-ray; 1.90 A; A/D=25-300.
DR   PDB; 3GSN; X-ray; 2.80 A; H=25-298.
DR   PDB; 3GSO; X-ray; 1.60 A; A=25-298.
DR   PDB; 3GSQ; X-ray; 2.12 A; A=25-298.
DR   PDB; 3GSR; X-ray; 1.95 A; A=25-298.
DR   PDB; 3GSU; X-ray; 1.80 A; A=25-299.
DR   PDB; 3GSV; X-ray; 1.90 A; A=25-299.
DR   PDB; 3GSW; X-ray; 1.81 A; A=25-298.
DR   PDB; 3GSX; X-ray; 2.10 A; A=25-298.
DR   PDB; 3H7B; X-ray; 1.88 A; A/D=25-299.
DR   PDB; 3H9H; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 3H9S; X-ray; 2.70 A; A=25-299.
DR   PDB; 3HAE; X-ray; 2.90 A; A/D/J/P=25-300.
DR   PDB; 3HG1; X-ray; 3.00 A; A=25-300.
DR   PDB; 3HLA; X-ray; 2.60 A; A=25-294.
DR   PDB; 3HPJ; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 3I6G; X-ray; 2.20 A; A/D=25-299.
DR   PDB; 3I6K; X-ray; 2.80 A; A/E=25-299.
DR   PDB; 3IXA; X-ray; 2.10 A; A/D=25-299.
DR   PDB; 3KLA; X-ray; 1.65 A; A/D=25-299.
DR   PDB; 3MGO; X-ray; 2.30 A; A/D/G/J=25-299.
DR   PDB; 3MGT; X-ray; 2.20 A; A/D/G/J=25-299.
DR   PDB; 3MR9; X-ray; 1.93 A; A=25-300.
DR   PDB; 3MRB; X-ray; 1.40 A; A=25-300.
DR   PDB; 3MRC; X-ray; 1.80 A; A=25-300.
DR   PDB; 3MRD; X-ray; 1.70 A; A=25-300.
DR   PDB; 3MRE; X-ray; 1.10 A; A=25-300.
DR   PDB; 3MRF; X-ray; 2.30 A; A=25-300.
DR   PDB; 3MRG; X-ray; 1.30 A; A=25-300.
DR   PDB; 3MRH; X-ray; 2.40 A; A=25-300.
DR   PDB; 3MRI; X-ray; 2.10 A; A=25-300.
DR   PDB; 3MRJ; X-ray; 1.87 A; A=25-300.
DR   PDB; 3MRK; X-ray; 1.40 A; A=25-300.
DR   PDB; 3MRL; X-ray; 2.41 A; A=25-300.
DR   PDB; 3MRM; X-ray; 1.90 A; A=25-300.
DR   PDB; 3MRN; X-ray; 2.30 A; A=25-300.
DR   PDB; 3MRO; X-ray; 2.35 A; A=25-300.
DR   PDB; 3MRP; X-ray; 2.10 A; A=25-300.
DR   PDB; 3MRQ; X-ray; 2.20 A; A=25-300.
DR   PDB; 3MRR; X-ray; 1.60 A; A=25-300.
DR   PDB; 3MYJ; X-ray; 1.89 A; A/D=25-299.
DR   PDB; 3O3A; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 3O3B; X-ray; 1.90 A; A/D=25-299.
DR   PDB; 3O3D; X-ray; 1.70 A; A/D=25-299.
DR   PDB; 3O3E; X-ray; 1.85 A; A/D=25-299.
DR   PDB; 3O4L; X-ray; 2.54 A; A=25-300.
DR   PDB; 3PWJ; X-ray; 1.70 A; A/D=25-299.
DR   PDB; 3PWL; X-ray; 1.65 A; A/D=25-299.
DR   PDB; 3PWN; X-ray; 1.60 A; A/D=25-299.
DR   PDB; 3PWP; X-ray; 2.69 A; A=25-299.
DR   PDB; 3QDG; X-ray; 2.69 A; A=25-299.
DR   PDB; 3QDJ; X-ray; 2.30 A; A=25-299.
DR   PDB; 3QDM; X-ray; 2.80 A; A=25-299.
DR   PDB; 3QEQ; X-ray; 2.59 A; A=25-299.
DR   PDB; 3QFD; X-ray; 1.68 A; A/D=25-299.
DR   PDB; 3QFJ; X-ray; 2.29 A; A=25-299.
DR   PDB; 3REW; X-ray; 1.90 A; A/D=25-299.
DR   PDB; 3TO2; X-ray; 2.60 A; A=25-299.
DR   PDB; 3UTQ; X-ray; 1.67 A; A=25-300.
DR   PDB; 3UTS; X-ray; 2.71 A; A/F=25-300.
DR   PDB; 3UTT; X-ray; 2.60 A; A/F=25-299.
DR   PDB; 3V5D; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 3V5H; X-ray; 1.63 A; A/D=25-299.
DR   PDB; 3V5K; X-ray; 2.31 A; A/D=25-299.
DR   PDB; 4E5X; X-ray; 1.95 A; A/D=25-299.
DR   PDB; 4EMZ; X-ray; 2.90 A; D/E=338-365.
DR   PDB; 4EN2; X-ray; 2.58 A; D/E=338-365.
DR   PDB; 4GKN; X-ray; 2.75 A; A/D=25-300.
DR   PDB; 4GKS; X-ray; 2.35 A; A/D=25-300.
DR   PDB; 4I4W; X-ray; 1.77 A; A=25-300.
DR   PDBsum; 1AKJ; -.
DR   PDBsum; 1AO7; -.
DR   PDBsum; 1AQD; -.
DR   PDBsum; 1B0G; -.
DR   PDBsum; 1B0R; -.
DR   PDBsum; 1BD2; -.
DR   PDBsum; 1DUY; -.
DR   PDBsum; 1DUZ; -.
DR   PDBsum; 1EEY; -.
DR   PDBsum; 1EEZ; -.
DR   PDBsum; 1HHG; -.
DR   PDBsum; 1HHH; -.
DR   PDBsum; 1HHI; -.
DR   PDBsum; 1HHJ; -.
DR   PDBsum; 1HHK; -.
DR   PDBsum; 1HLA; -.
DR   PDBsum; 1I1F; -.
DR   PDBsum; 1I1Y; -.
DR   PDBsum; 1I4F; -.
DR   PDBsum; 1I7R; -.
DR   PDBsum; 1I7T; -.
DR   PDBsum; 1I7U; -.
DR   PDBsum; 1IM3; -.
DR   PDBsum; 1JF1; -.
DR   PDBsum; 1JHT; -.
DR   PDBsum; 1LP9; -.
DR   PDBsum; 1OGA; -.
DR   PDBsum; 1P7Q; -.
DR   PDBsum; 1QEW; -.
DR   PDBsum; 1QR1; -.
DR   PDBsum; 1QRN; -.
DR   PDBsum; 1QSE; -.
DR   PDBsum; 1QSF; -.
DR   PDBsum; 1S8D; -.
DR   PDBsum; 1S9W; -.
DR   PDBsum; 1S9X; -.
DR   PDBsum; 1S9Y; -.
DR   PDBsum; 1T1W; -.
DR   PDBsum; 1T1X; -.
DR   PDBsum; 1T1Y; -.
DR   PDBsum; 1T1Z; -.
DR   PDBsum; 1T20; -.
DR   PDBsum; 1T21; -.
DR   PDBsum; 1T22; -.
DR   PDBsum; 1TVB; -.
DR   PDBsum; 1TVH; -.
DR   PDBsum; 1UR7; -.
DR   PDBsum; 2AV1; -.
DR   PDBsum; 2AV7; -.
DR   PDBsum; 2BNQ; -.
DR   PDBsum; 2BNR; -.
DR   PDBsum; 2C7U; -.
DR   PDBsum; 2CLR; -.
DR   PDBsum; 2F53; -.
DR   PDBsum; 2F54; -.
DR   PDBsum; 2GIT; -.
DR   PDBsum; 2GJ6; -.
DR   PDBsum; 2GT9; -.
DR   PDBsum; 2GTW; -.
DR   PDBsum; 2GTZ; -.
DR   PDBsum; 2GUO; -.
DR   PDBsum; 2J8U; -.
DR   PDBsum; 2JCC; -.
DR   PDBsum; 2P5E; -.
DR   PDBsum; 2P5W; -.
DR   PDBsum; 2PYE; -.
DR   PDBsum; 2UWE; -.
DR   PDBsum; 2V2W; -.
DR   PDBsum; 2V2X; -.
DR   PDBsum; 2VLJ; -.
DR   PDBsum; 2VLK; -.
DR   PDBsum; 2VLL; -.
DR   PDBsum; 2VLR; -.
DR   PDBsum; 2X4N; -.
DR   PDBsum; 2X4O; -.
DR   PDBsum; 2X4P; -.
DR   PDBsum; 2X4Q; -.
DR   PDBsum; 2X4R; -.
DR   PDBsum; 2X4S; -.
DR   PDBsum; 2X4T; -.
DR   PDBsum; 2X4U; -.
DR   PDBsum; 2X70; -.
DR   PDBsum; 3BGM; -.
DR   PDBsum; 3BH8; -.
DR   PDBsum; 3BH9; -.
DR   PDBsum; 3BHB; -.
DR   PDBsum; 3D25; -.
DR   PDBsum; 3D39; -.
DR   PDBsum; 3D3V; -.
DR   PDBsum; 3FQN; -.
DR   PDBsum; 3FQR; -.
DR   PDBsum; 3FQT; -.
DR   PDBsum; 3FQU; -.
DR   PDBsum; 3FQW; -.
DR   PDBsum; 3FQX; -.
DR   PDBsum; 3FT2; -.
DR   PDBsum; 3FT3; -.
DR   PDBsum; 3FT4; -.
DR   PDBsum; 3GIV; -.
DR   PDBsum; 3GJF; -.
DR   PDBsum; 3GSN; -.
DR   PDBsum; 3GSO; -.
DR   PDBsum; 3GSQ; -.
DR   PDBsum; 3GSR; -.
DR   PDBsum; 3GSU; -.
DR   PDBsum; 3GSV; -.
DR   PDBsum; 3GSW; -.
DR   PDBsum; 3GSX; -.
DR   PDBsum; 3H7B; -.
DR   PDBsum; 3H9H; -.
DR   PDBsum; 3H9S; -.
DR   PDBsum; 3HAE; -.
DR   PDBsum; 3HG1; -.
DR   PDBsum; 3HLA; -.
DR   PDBsum; 3HPJ; -.
DR   PDBsum; 3I6G; -.
DR   PDBsum; 3I6K; -.
DR   PDBsum; 3IXA; -.
DR   PDBsum; 3KLA; -.
DR   PDBsum; 3MGO; -.
DR   PDBsum; 3MGT; -.
DR   PDBsum; 3MR9; -.
DR   PDBsum; 3MRB; -.
DR   PDBsum; 3MRC; -.
DR   PDBsum; 3MRD; -.
DR   PDBsum; 3MRE; -.
DR   PDBsum; 3MRF; -.
DR   PDBsum; 3MRG; -.
DR   PDBsum; 3MRH; -.
DR   PDBsum; 3MRI; -.
DR   PDBsum; 3MRJ; -.
DR   PDBsum; 3MRK; -.
DR   PDBsum; 3MRL; -.
DR   PDBsum; 3MRM; -.
DR   PDBsum; 3MRN; -.
DR   PDBsum; 3MRO; -.
DR   PDBsum; 3MRP; -.
DR   PDBsum; 3MRQ; -.
DR   PDBsum; 3MRR; -.
DR   PDBsum; 3MYJ; -.
DR   PDBsum; 3O3A; -.
DR   PDBsum; 3O3B; -.
DR   PDBsum; 3O3D; -.
DR   PDBsum; 3O3E; -.
DR   PDBsum; 3O4L; -.
DR   PDBsum; 3PWJ; -.
DR   PDBsum; 3PWL; -.
DR   PDBsum; 3PWN; -.
DR   PDBsum; 3PWP; -.
DR   PDBsum; 3QDG; -.
DR   PDBsum; 3QDJ; -.
DR   PDBsum; 3QDM; -.
DR   PDBsum; 3QEQ; -.
DR   PDBsum; 3QFD; -.
DR   PDBsum; 3QFJ; -.
DR   PDBsum; 3REW; -.
DR   PDBsum; 3TO2; -.
DR   PDBsum; 3UTQ; -.
DR   PDBsum; 3UTS; -.
DR   PDBsum; 3UTT; -.
DR   PDBsum; 3V5D; -.
DR   PDBsum; 3V5H; -.
DR   PDBsum; 3V5K; -.
DR   PDBsum; 4E5X; -.
DR   PDBsum; 4EMZ; -.
DR   PDBsum; 4EN2; -.
DR   PDBsum; 4GKN; -.
DR   PDBsum; 4GKS; -.
DR   PDBsum; 4I4W; -.
DR   ProteinModelPortal; P01892; -.
DR   SMR; P01892; 25-298.
DR   DIP; DIP-6085N; -.
DR   IntAct; P01892; 6.
DR   MINT; MINT-5000859; -.
DR   PhosphoSite; P01892; -.
DR   DMDM; 122138; -.
DR   PaxDb; P01892; -.
DR   PRIDE; P01892; -.
DR   Ensembl; ENST00000457879; ENSP00000403575; ENSG00000235657.
DR   Ensembl; ENST00000547271; ENSP00000447962; ENSG00000235657.
DR   GeneCards; GC06P029933; -.
DR   GeneCards; GC06Pk29899; -.
DR   HGNC; HGNC:4931; HLA-A.
DR   MIM; 142800; gene.
DR   neXtProt; NX_P01892; -.
DR   eggNOG; NOG42056; -.
DR   HOVERGEN; HBG016709; -.
DR   OrthoDB; EOG4F4SBG; -.
DR   Reactome; REACT_116125; Disease.
DR   Reactome; REACT_6900; Immune System.
DR   ChiTaRS; HLA-A; human.
DR   EvolutionaryTrace; P01892; -.
DR   ArrayExpress; P01892; -.
DR   CleanEx; HS_HLA-A; -.
DR   Genevestigator; P01892; -.
DR   GermOnline; ENSG00000204632; Homo sapiens.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   GO; GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0016032; P:viral reproduction; TAS:Reactome.
DR   GO; GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.500.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR011161; MHC_I-like_Ag-recog.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   InterPro; IPR001039; MHC_I_a_a1/a2.
DR   InterPro; IPR010579; MHC_I_a_C.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00129; MHC_I; 1.
DR   Pfam; PF06623; MHC_I_C; 1.
DR   PRINTS; PR01638; MHCCLASSI.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF54452; MHC_I/II-like_Ag-recog; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Host-virus interaction; Immunity;
KW   Membrane; MHC I; Phosphoprotein; Polymorphism; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     24
FT   CHAIN        25    365       HLA class I histocompatibility antigen,
FT                                A-2 alpha chain.
FT                                /FTId=PRO_0000018814.
FT   TOPO_DOM     25    308       Extracellular (Potential).
FT   TRANSMEM    309    332       Helical; (Potential).
FT   TOPO_DOM    333    365       Cytoplasmic (Potential).
FT   DOMAIN      209    295       Ig-like C1-type.
FT   REGION       25    114       Alpha-1.
FT   REGION      115    206       Alpha-2.
FT   REGION      207    298       Alpha-3.
FT   REGION      299    308       Connecting peptide.
FT   MOD_RES     356    356       Phosphoserine.
FT   CARBOHYD    110    110       N-linked (GlcNAc...).
FT   DISULFID    125    188
FT   DISULFID    227    283
FT   VARIANT      33     33       F -> Y (in allele A*02:05, allele
FT                                A*02:06, allele A*02:08, allele A*02:10
FT                                and allele A*02:21).
FT                                /FTId=VAR_004334.
FT   VARIANT      54     54       D -> N (in allele A*02:21).
FT                                /FTId=VAR_004335.
FT   VARIANT      65     65       A -> G (in allele A*02:31).
FT                                /FTId=VAR_016726.
FT   VARIANT      67     67       Q -> R (in allele A*02:02, allele A*02:05
FT                                and allele A*02:08).
FT                                /FTId=VAR_004336.
FT   VARIANT      90     90       K -> N (in allele A*02:08 and allele
FT                                A*02:20).
FT                                /FTId=VAR_004337.
FT   VARIANT      94     94       H -> Q (in allele A*02:34 and allele
FT                                A*02:35).
FT                                /FTId=VAR_016727.
FT   VARIANT      97     97       T -> I (in allele A*02:11).
FT                                /FTId=VAR_004338.
FT   VARIANT      98     98       H -> D (in allele A*02:11 and allele
FT                                A*02:35).
FT                                /FTId=VAR_016728.
FT   VARIANT     119    119       V -> L (in allele A*02:02, allele
FT                                A*02:05, allele A*02:08 and allele
FT                                A*02:17).
FT                                /FTId=VAR_004339.
FT   VARIANT     121    121       R -> M (in allele A*02:04 and allele
FT                                A*02:17).
FT                                /FTId=VAR_004340.
FT   VARIANT     123    123       Y -> C (in allele A*02:07 and allele
FT                                A*02:18).
FT                                /FTId=VAR_004341.
FT   VARIANT     123    123       Y -> F (in allele A*02:10 and allele
FT                                A*02:17).
FT                                /FTId=VAR_004342.
FT   VARIANT     131    131       W -> G (in allele A*02:10).
FT                                /FTId=VAR_004343.
FT   VARIANT     162    162       M -> K (in allele A*02:18).
FT                                /FTId=VAR_004344.
FT   VARIANT     173    173       A -> T (in allele A*02:03).
FT                                /FTId=VAR_004345.
FT   VARIANT     176    176       V -> E (in allele A*02:03 and allele
FT                                A*02:13).
FT                                /FTId=VAR_004346.
FT   VARIANT     180    180       L -> Q (in allele A*02:12, allele A*02:13
FT                                and allele A*02:37).
FT                                /FTId=VAR_004348.
FT   VARIANT     180    180       L -> W (in allele A*02:02, allele
FT                                A*02:03, allele A*02:05 and allele
FT                                A*02:08).
FT                                /FTId=VAR_004347.
FT   VARIANT     187    187       T -> E (in allele A*02:16; requires 2
FT                                nucleotide substitutions).
FT                                /FTId=VAR_004349.
FT   VARIANT     190    190       E -> D (in allele A*02:36 and allele
FT                                A*02:37).
FT                                /FTId=VAR_016729.
FT   VARIANT     191    191       W -> G (in allele A*02:36 and allele
FT                                A*02:37).
FT                                /FTId=VAR_016730.
FT   VARIANT     260    260       A -> E (in allele A*02:09).
FT                                /FTId=VAR_004350.
FT   CONFLICT    115    115       G -> V (in Ref. 4; AAA52656).
FT   CONFLICT    140    140       Y -> V (in Ref. 4; AAA52656).
FT   CONFLICT    277    277       Q -> E (in Ref. 4; AAA52656).
FT   CONFLICT    318    318       F -> L (in Ref. 4; AAA52656).
FT   STRAND       27     36
FT   STRAND       41     43
FT   STRAND       45     52
FT   STRAND       55     61
FT   STRAND       64     66
FT   STRAND       70     73
FT   HELIX        74     78
FT   HELIX        81    108
FT   STRAND      113    115
FT   STRAND      118    127
FT   STRAND      131    142
FT   STRAND      145    150
FT   STRAND      157    159
FT   HELIX       162    173
FT   HELIX       176    184
FT   HELIX       187    198
FT   HELIX       200    203
FT   STRAND      210    235
FT   STRAND      238    243
FT   STRAND      246    248
FT   HELIX       249    251
FT   STRAND      252    254
FT   STRAND      261    263
FT   STRAND      265    274
FT   HELIX       278    280
FT   STRAND      281    286
FT   STRAND      290    292
FT   STRAND      294    297
FT   STRAND      348    350
SQ   SEQUENCE   365 AA;  40922 MW;  B54A97B24B337C08 CRC64;
     MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF
     DSDAASQRME PRAPWIEQEG PEYWDGETRK VKAHSQTHRV DLGTLRGYYN QSEAGSHTVQ
     RMYGCDVGSD WRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL
     RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT
     WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP
     SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL
     TACKV
//
ID   1A03_HUMAN              Reviewed;         365 AA.
AC   P04439; O19546; O19756; Q65A82; Q9GJE6; Q9GJE7; Q9GJE8; Q9MYE6;
AC   Q9MYG4; Q9TPR8;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   03-APR-2013, entry version 127.
DE   RecName: Full=HLA class I histocompatibility antigen, A-3 alpha chain;
DE   AltName: Full=MHC class I antigen A*3;
DE   Flags: Precursor;
GN   Name=HLA-A; Synonyms=HLAA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*03:01).
RX   PubMed=6609814;
RA   Strachan T., Sodoyer R., Damotte M., Jordan B.R.;
RT   "Complete nucleotide sequence of a functional class I HLA gene, HLA-
RT   A3: implications for the evolution of HLA genes.";
RL   EMBO J. 3:887-894(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*03:01).
RA   Ellexson M.E., Hildebrand W.H.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE A*03:01).
RA   Shiina S., Tamiya G., Oka A., Inoko H.;
RT   "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*03:02).
RX   PubMed=2993417;
RA   Cowan E.P., Jordan B.E., Coligan J.E.;
RT   "Molecular cloning and DNA sequence analysis of genes encoding
RT   cytotoxic T lymphocyte-defined HLA-A3 subtypes: the E1 subtype.";
RL   J. Immunol. 135:2835-2841(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE (ALLELE A*03:02).
RA   Bettinotti M.P., Hadzikadic L., Adams S., Marincola F.M.;
RT   "Complete coding sequence of HLA-A*0302.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mayor N.P.;
RT   "Full length sequence of an HLA-A*0301 intron 2 variant.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-341 (ALLELE A*03:04).
RX   PubMed=10079303; DOI=10.1007/s002510050506;
RA   Santos S., Balas A., Garcia-Sanchez F., Lillo R., Merino J.L.,
RA   Vicario J.L.;
RT   "Complete cDNA coding sequence of a new HLA-A3 subtype (A*0304) with a
RT   new HLA polymorphism at exon 3.";
RL   Immunogenetics 49:360-361(1999).
RN   [9]
RP   NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*03:05).
RA   Becher M.P., Wu J., Williams T.;
RT   "Novel human HLA-A alleles identified in potential bone marrow
RT   donors.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE OF 26-298 (ALLELE A*03:05).
RC   TISSUE=Blood;
RA   Poli F., Frison S., Crespiatico L., Longhi E.;
RT   "Identification of a HLA-A*03 new variant.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*03:06).
RX   PubMed=12135434; DOI=10.1034/j.1399-0039.2002.590413.x;
RA   Bradshaw D., Gans C.P., Jones P., Rizzuto G., Steiner N., Mitton W.,
RA   Ng J., Koester R., Hartzman R.J., Hurley C.K.;
RT   "Novel HLA-A locus alleles including A*01012, A*0306, A*0308, A*2616,
RT   A*2617, A*3009, A*3206, A*3403, A*3602 and A*6604.";
RL   Tissue Antigens 59:325-327(2002).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-298 (ALLELE A*03:01) IN
RP   COMPLEX WITH PLP1 ANTIGENIC PEPTIDE, AND DISULFIDE BONDS.
RX   PubMed=21543847; DOI=10.1107/S0907444911007888;
RA   McMahon R.M., Friis L., Siebold C., Friese M.A., Fugger L.,
RA   Jones E.Y.;
RT   "Structure of HLA-A*0301 in complex with a peptide of proteolipid
RT   protein: insights into the role of HLA-A alleles in susceptibility to
RT   multiple sclerosis.";
RL   Acta Crystallogr. D 67:447-454(2011).
CC   -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC       immune system.
CC   -!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2-
CC       microglobulin). Interacts with human herpesvirus 8 MIR1 protein
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Polyubiquitinated in a post ER compartment by interaction
CC       with human herpesvirus 8 MIR1 protein. This targets the protein
CC       for rapid degradation via the ubiquitin system (By similarity).
CC   -!- POLYMORPHISM: The following alleles of A-3 are known: A*03:01 (A-
CC       3.1), A*03:02, A*03:04, A*03:05 and A*03:06. The sequence shown is
CC       that of A*03:01.
CC   -!- SIMILARITY: Belongs to the MHC class I family.
CC   -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like)
CC       domain.
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DR   EMBL; X00492; CAA25162.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U32184; AAB63980.1; -; mRNA.
DR   EMBL; BA000025; BAB63400.1; -; Genomic_DNA.
DR   EMBL; AF217561; AAF28734.1; -; mRNA.
DR   EMBL; AF015930; AAB66582.1; -; mRNA.
DR   EMBL; AH008295; AAF03243.1; -; Genomic_DNA.
DR   EMBL; AJ401085; CAC06086.1; -; Genomic_DNA.
DR   EMBL; AJ401086; CAC06087.1; -; Genomic_DNA.
DR   EMBL; AJ401087; CAC06088.1; -; Genomic_DNA.
DR   EMBL; AJ748743; CAG38621.1; -; Genomic_DNA.
DR   EMBL; AL671277; CAI18372.1; -; Genomic_DNA.
DR   EMBL; AH009116; AAF29557.1; -; Genomic_DNA.
DR   IPI; IPI00647634; -.
DR   PIR; A02192; HLHUA3.
DR   RefSeq; NP_002107.3; NM_002116.7.
DR   UniGene; Hs.181244; -.
DR   UniGene; Hs.713441; -.
DR   PDB; 2XPG; X-ray; 2.60 A; A=25-298.
DR   PDB; 3RL2; X-ray; 2.39 A; A=25-298.
DR   PDBsum; 2XPG; -.
DR   PDBsum; 3RL2; -.
DR   ProteinModelPortal; P04439; -.
DR   SMR; P04439; 25-298.
DR   IntAct; P04439; 3.
DR   DMDM; 34223717; -.
DR   PaxDb; P04439; -.
DR   PRIDE; P04439; -.
DR   DNASU; 3105; -.
DR   Ensembl; ENST00000376809; ENSP00000366005; ENSG00000206503.
DR   Ensembl; ENST00000396634; ENSP00000379873; ENSG00000206503.
DR   GeneID; 3105; -.
DR   KEGG; hsa:3105; -.
DR   UCSC; uc003nok.3; human.
DR   CTD; 3105; -.
DR   GeneCards; GC06P029933; -.
DR   HGNC; HGNC:4931; HLA-A.
DR   MIM; 142800; gene.
DR   neXtProt; NX_P04439; -.
DR   PharmGKB; PA35055; -.
DR   eggNOG; NOG42056; -.
DR   HOVERGEN; HBG016709; -.
DR   KO; K06751; -.
DR   OrthoDB; EOG4F4SBG; -.
DR   Pathway_Interaction_DB; cd8tcrdownstreampathway; Downstream signaling in naive CD8+ T cells.
DR   Pathway_Interaction_DB; il12_2pathway; IL12-mediated signaling events.
DR   Pathway_Interaction_DB; cd8tcrpathway; TCR signaling in naive CD8+ T cells.
DR   Reactome; REACT_6900; Immune System.
DR   ChEMBL; CHEMBL2632; -.
DR   ChiTaRS; HLA-A; human.
DR   GenomeRNAi; 3105; -.
DR   NextBio; 12319; -.
DR   PMAP-CutDB; P04439; -.
DR   ArrayExpress; P04439; -.
DR   Bgee; P04439; -.
DR   CleanEx; HS_HLA-A; -.
DR   Genevestigator; P04439; -.
DR   GermOnline; ENSG00000204632; Homo sapiens.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   GO; GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.500.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR011161; MHC_I-like_Ag-recog.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   InterPro; IPR001039; MHC_I_a_a1/a2.
DR   InterPro; IPR010579; MHC_I_a_C.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00129; MHC_I; 1.
DR   Pfam; PF06623; MHC_I_C; 1.
DR   PRINTS; PR01638; MHCCLASSI.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF54452; MHC_I/II-like_Ag-recog; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
KW   Host-virus interaction; Immunity; Membrane; MHC I; Polymorphism;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   SIGNAL        1     24
FT   CHAIN        25    365       HLA class I histocompatibility antigen,
FT                                A-3 alpha chain.
FT                                /FTId=PRO_0000018815.
FT   TOPO_DOM     25    308       Extracellular (Potential).
FT   TRANSMEM    309    332       Helical; (Potential).
FT   TOPO_DOM    333    365       Cytoplasmic (Potential).
FT   DOMAIN      209    295       Ig-like C1-type.
FT   REGION       25    114       Alpha-1.
FT   REGION      115    206       Alpha-2.
FT   REGION      207    298       Alpha-3.
FT   REGION      299    308       Connecting peptide.
FT   CARBOHYD    110    110       N-linked (GlcNAc...) (By similarity).
FT   DISULFID    125    188
FT   DISULFID    227    283
FT   VARIANT      89     89       R -> G (in dbSNP:rs1059459).
FT                                /FTId=VAR_050310.
FT   VARIANT      94     94       Q -> H (in dbSNP:rs1059463).
FT                                /FTId=VAR_050311.
FT   VARIANT     101    101       D -> N (in dbSNP:rs1136688).
FT                                /FTId=VAR_050312.
FT   VARIANT     121    121       I -> M (in dbSNP:rs1136695).
FT                                /FTId=VAR_050313.
FT   VARIANT     129    129       S -> P (in dbSNP:rs1136700).
FT                                /FTId=VAR_050314.
FT   VARIANT     131    131       G -> W (in dbSNP:rs1136702).
FT                                /FTId=VAR_050315.
FT   VARIANT     133    133       F -> L (in dbSNP:rs1059488).
FT                                /FTId=VAR_050316.
FT   VARIANT     151    151       N -> K (in dbSNP:rs1059509).
FT                                /FTId=VAR_050317.
FT   VARIANT     166    166       I -> T (in dbSNP:rs1059516).
FT                                /FTId=VAR_050318.
FT   VARIANT     169    169       R -> H (in dbSNP:rs1059520).
FT                                /FTId=VAR_050319.
FT   VARIANT     176    176       E -> V (in allele A*03:02).
FT                                /FTId=VAR_004351.
FT   VARIANT     180    180       L -> Q (in allele A*03:02).
FT                                /FTId=VAR_004352.
FT   VARIANT     185    185       D -> E (in allele A*03:05;
FT                                dbSNP:rs1059542).
FT                                /FTId=VAR_016604.
FT   VARIANT     186    186       G -> A (in allele A*03:06).
FT                                /FTId=VAR_033149.
FT   VARIANT     199    199       G -> R (in allele A*03:04).
FT                                /FTId=VAR_016605.
FT   VARIANT     205    205       R -> H (in dbSNP:rs17185861).
FT                                /FTId=VAR_050320.
FT   CONFLICT    319    319       G -> A (in Ref. 8; AAB66582).
FT   STRAND       27     36
FT   TURN         39     41
FT   STRAND       45     52
FT   STRAND       55     61
FT   STRAND       64     66
FT   TURN         74     78
FT   HELIX        81    109
FT   STRAND      113    115
FT   STRAND      118    127
FT   STRAND      133    150
FT   STRAND      157    161
FT   HELIX       162    173
FT   HELIX       176    185
FT   HELIX       187    198
FT   TURN        199    202
FT   STRAND      210    221
FT   STRAND      223    235
FT   STRAND      238    246
FT   STRAND      251    254
FT   STRAND      261    263
FT   STRAND      265    273
FT   HELIX       278    280
FT   STRAND      281    286
FT   STRAND      290    292
FT   STRAND      294    296
SQ   SEQUENCE   365 AA;  40841 MW;  DEDFCEC4450E0580 CRC64;
     MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF
     DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ
     IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHEAEQL
     RAYLDGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT
     WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL
     SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL
     TACKV
//
