1433F_HUMAN
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-AUG-2022, entry version 228.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 both
RT 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 14-3-3
RT 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., Ichikawa T.,
RA Kumanishi T., Isobe T., Watanabe M., Kondo H.;
RT "The effect on methamphetamine on the mRNA level for 14.3.3 eta chain in
RT 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., Kuwano R.,
RA Isobe T., Wang Y., Minoshima S., Shimizu N., Takahashi Y.;
RT "Structural organization and chromosomal assignment of the human 14-3-3 eta
RT 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., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., 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., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., 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., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA 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 project:
RT 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., Walbum E.,
RA 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 been
RT 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., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT 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 IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [12]
RP PROTEIN SEQUENCE OF 1-10; 13-50; 62-78; 111-120 AND 133-162, INTERACTION
RP WITH PI4KB; TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT by enteroviral and kobuviral 3A protein binding.";
RL MBio 4:E00098-E00098(2013).
RN [13]
RP INTERACTION WITH AR; ESR1; ESR2; MC2R; NRIP1; NR3C1; PPARBP AND THRA.
RX PubMed=11266503; DOI=10.1210/mend.15.4.0624;
RA Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., 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 [14]
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 [15]
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 S6
RT kinases promotes its binding to 14-3-3 and cytoplasmic localization.";
RL J. Biol. Chem. 278:49254-49260(2003).
RN [16]
RP INTERACTION WITH ABL1, AND IDENTIFICATION BY 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 c-
RT Abl in the apoptotic response to DNA damage.";
RL Nat. Cell Biol. 7:278-285(2005).
RN [17]
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., Guilhaus M.,
RA James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the
RT Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [18]
RP INTERACTION WITH SLITRK1.
RX PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
RA Kajiwara Y., Buxbaum J.D., Grice D.E.;
RT "SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a phosphorylation-
RT dependent manner.";
RL Biol. Psychiatry 66:918-925(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP 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 [20]
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., Buerckstuemmer T.,
RA 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP INTERACTION WITH DAPK2.
RX PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
RA Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
RT "Suppression of death-associated protein kinase 2 by interaction with 14-3-
RT 3 proteins.";
RL Biochem. Biophys. Res. Commun. 464:70-75(2015).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP INTERACTION WITH MEFV.
RX PubMed=27030597; DOI=10.1126/scitranslmed.aaf1471;
RA Masters S.L., Lagou V., Jeru I., Baker P.J., Van Eyck L., Parry D.A.,
RA Lawless D., De Nardo D., Garcia-Perez J.E., Dagley L.F., Holley C.L.,
RA Dooley J., Moghaddas F., Pasciuto E., Jeandel P.Y., Sciot R., Lyras D.,
RA Webb A.I., Nicholson S.E., De Somer L., van Nieuwenhove E., Ruuth-Praz J.,
RA Copin B., Cochet E., Medlej-Hashim M., Megarbane A., Schroder K., Savic S.,
RA Goris A., Amselem S., Wouters C., Liston A.;
RT "Familial autoinflammation with neutrophilic dermatosis reveals a
RT regulatory mechanism of pyrin activation.";
RL Sci. Transl. Med. 8:332ra45-332ra45(2016).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), IDENTIFICATION BY MASS
RP SPECTROMETRY, 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 protein
RT 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 to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner. Negatively regulates the kinase
CC activity of PDPK1. {ECO:0000269|PubMed:12177059}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with many nuclear hormone
CC receptors and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1,
CC PPARBP and THRA. Interacts with ABL1 (phosphorylated form); the
CC interaction retains it in the cytoplasm. Interacts with ARHGEF28 and
CC CDK16 (By similarity). Weakly interacts with CDKN1B. Interacts with
CC GAB2. Interacts with KCNK18 in a phosphorylation-dependent manner.
CC Interacts with SAMSN1 (By similarity). Interacts with the 'Ser-241'
CC phosphorylated form of PDPK1. Interacts with the 'Thr-369'
CC phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB,
CC TBC1D22A and TBC1D22B (PubMed:23572552). Interacts with SLITRK1
CC (PubMed:19640509). Interacts with MEFV (PubMed:27030597). {ECO:0000250,
CC ECO:0000269|PubMed:11266503, ECO:0000269|PubMed:12177059,
CC ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:15696159,
CC ECO:0000269|PubMed:17085597, ECO:0000269|PubMed:19172738,
CC ECO:0000269|PubMed:19640509, ECO:0000269|PubMed:23572552,
CC ECO:0000269|PubMed:26047703, ECO:0000269|PubMed:27030597}.
CC -!- INTERACTION:
CC Q04917; Q96B36: AKT1S1; NbExp=4; IntAct=EBI-306940, EBI-720593;
CC Q04917; P54253: ATXN1; NbExp=8; IntAct=EBI-306940, EBI-930964;
CC Q04917; Q92934: BAD; NbExp=5; IntAct=EBI-306940, EBI-700771;
CC Q04917; Q8N5S9: CAMKK1; NbExp=6; IntAct=EBI-306940, EBI-6424030;
CC Q04917; P22681: CBL; NbExp=3; IntAct=EBI-306940, EBI-518228;
CC Q04917; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-306940, EBI-11977221;
CC Q04917; P30305: CDC25B; NbExp=5; IntAct=EBI-306940, EBI-1051746;
CC Q04917; O94921: CDK14; NbExp=4; IntAct=EBI-306940, EBI-1043945;
CC Q04917; O60565: GREM1; NbExp=5; IntAct=EBI-306940, EBI-944395;
CC Q04917; P56524: HDAC4; NbExp=5; IntAct=EBI-306940, EBI-308629;
CC Q04917; Q14678-2: KANK1; NbExp=3; IntAct=EBI-306940, EBI-6173812;
CC Q04917; Q5S007: LRRK2; NbExp=4; IntAct=EBI-306940, EBI-5323863;
CC Q04917; Q99759: MAP3K3; NbExp=3; IntAct=EBI-306940, EBI-307281;
CC Q04917; Q99683: MAP3K5; NbExp=3; IntAct=EBI-306940, EBI-476263;
CC Q04917; Q7KZI7: MARK2; NbExp=10; IntAct=EBI-306940, EBI-516560;
CC Q04917; P27448: MARK3; NbExp=6; IntAct=EBI-306940, EBI-707595;
CC Q04917; Q96L34: MARK4; NbExp=6; IntAct=EBI-306940, EBI-302319;
CC Q04917; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-306940, EBI-2859639;
CC Q04917; Q8TEW0: PARD3; NbExp=7; IntAct=EBI-306940, EBI-81968;
CC Q04917; Q9NPB6: PARD6A; NbExp=2; IntAct=EBI-306940, EBI-81876;
CC Q04917; Q9BYG5: PARD6B; NbExp=3; IntAct=EBI-306940, EBI-295391;
CC Q04917; Q9BYG4: PARD6G; NbExp=2; IntAct=EBI-306940, EBI-295417;
CC Q04917; P41743: PRKCI; NbExp=3; IntAct=EBI-306940, EBI-286199;
CC Q04917; Q9BZL6: PRKD2; NbExp=2; IntAct=EBI-306940, EBI-1384325;
CC Q04917; O60260-5: PRKN; NbExp=6; IntAct=EBI-306940, EBI-21251460;
CC Q04917; P04049: RAF1; NbExp=10; IntAct=EBI-306940, EBI-365996;
CC Q04917; P37840: SNCA; NbExp=4; IntAct=EBI-306940, EBI-985879;
CC Q04917; P37840-1: SNCA; NbExp=9; IntAct=EBI-306940, EBI-9684465;
CC Q04917; P62258: YWHAE; NbExp=5; IntAct=EBI-306940, EBI-356498;
CC Q04917; Q04917: YWHAH; NbExp=5; IntAct=EBI-306940, EBI-306940;
CC Q04917; P67828: CSNK1A1; Xeno; NbExp=8; IntAct=EBI-306940, EBI-7540603;
CC Q04917; P61588: Rnd3; Xeno; NbExp=2; IntAct=EBI-306940, EBI-6930266;
CC -!- TISSUE SPECIFICITY: Expressed mainly in the brain and present in other
CC tissues albeit at lower levels.
CC -!- PTM: Phosphorylated on Ser-59 by protein kinase C delta type catalytic
CC subunit in a sphingosine-dependent fashion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003047; AAH03047.1; -; mRNA.
DR CCDS; CCDS13901.1; -.
DR PIR; S34756; S34756.
DR PIR; S38509; S38509.
DR PIR; S38532; S38532.
DR RefSeq; NP_003396.1; NM_003405.3.
DR PDB; 2C63; X-ray; 2.15 A; A/B/C/D=2-246.
DR PDB; 2C74; X-ray; 2.70 A; A/B=2-246.
DR PDB; 7NMZ; X-ray; 2.30 A; AA/BA=1-234.
DR PDBsum; 2C63; -.
DR PDBsum; 2C74; -.
DR PDBsum; 7NMZ; -.
DR AlphaFoldDB; Q04917; -.
DR SMR; Q04917; -.
DR BioGRID; 113365; 619.
DR CORUM; Q04917; -.
DR DIP; DIP-27566N; -.
DR ELM; Q04917; -.
DR IntAct; Q04917; 505.
DR MINT; Q04917; -.
DR STRING; 9606.ENSP00000248975; -.
DR BindingDB; Q04917; -.
DR ChEMBL; CHEMBL3708585; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; Q04917; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q04917; -.
DR MetOSite; Q04917; -.
DR PhosphoSitePlus; Q04917; -.
DR SwissPalm; Q04917; -.
DR BioMuta; YWHAH; -.
DR DMDM; 1345593; -.
DR EPD; Q04917; -.
DR jPOST; Q04917; -.
DR MassIVE; Q04917; -.
DR MaxQB; Q04917; -.
DR PaxDb; Q04917; -.
DR PeptideAtlas; Q04917; -.
DR PRIDE; Q04917; -.
DR ProteomicsDB; 58300; -.
DR TopDownProteomics; Q04917; -.
DR Antibodypedia; 11204; 317 antibodies from 37 providers.
DR DNASU; 7533; -.
DR Ensembl; ENST00000248975.6; ENSP00000248975.5; ENSG00000128245.15.
DR GeneID; 7533; -.
DR KEGG; hsa:7533; -.
DR MANE-Select; ENST00000248975.6; ENSP00000248975.5; NM_003405.4; NP_003396.1.
DR UCSC; uc003alz.4; human.
DR CTD; 7533; -.
DR DisGeNET; 7533; -.
DR GeneCards; YWHAH; -.
DR HGNC; HGNC:12853; YWHAH.
DR HPA; ENSG00000128245; Tissue enhanced (brain).
DR MIM; 113508; gene.
DR neXtProt; NX_Q04917; -.
DR OpenTargets; ENSG00000128245; -.
DR PharmGKB; PA37442; -.
DR VEuPathDB; HostDB:ENSG00000128245; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; Q04917; -.
DR OMA; IKNCDES; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; Q04917; -.
DR TreeFam; TF102003; -.
DR PathwayCommons; Q04917; -.
DR Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-HSA-9755779; SARS-CoV-2 targets host intracellular signalling and regulatory pathways.
DR SignaLink; Q04917; -.
DR SIGNOR; Q04917; -.
DR BioGRID-ORCS; 7533; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; YWHAH; human.
DR EvolutionaryTrace; Q04917; -.
DR GeneWiki; YWHAH; -.
DR GenomeRNAi; 7533; -.
DR Pharos; Q04917; Tchem.
DR PRO; PR:Q04917; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q04917; protein.
DR Bgee; ENSG00000128245; Expressed in frontal pole and 194 other tissues.
DR ExpressionAtlas; Q04917; baseline and differential.
DR Genevisible; Q04917; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IC:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI: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:0086010; P:membrane depolarization during action potential; IDA:BHF-UCL.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; IDA:BHF-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
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; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.11"
FT CHAIN 2..246
FT /note="14-3-3 protein eta"
FT /id="PRO_0000058623"
FT SITE 57
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT SITE 132
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|Ref.11"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68510"
FT CONFLICT 144
FT /note="N -> T (in Ref. 9; CAA40620)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="A -> G (in Ref. 1; AAA35483)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="Q -> L (in Ref. 1; AAA35483)"
FT /evidence="ECO:0000305"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:2C63"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:2C63"
FT HELIX 39..73
FT /evidence="ECO:0007829|PDB:2C63"
FT HELIX 76..106
FT /evidence="ECO:0007829|PDB:2C63"
FT TURN 107..111
FT /evidence="ECO:0007829|PDB:2C63"
FT HELIX 117..137
FT /evidence="ECO:0007829|PDB:2C63"
FT HELIX 140..164
FT /evidence="ECO:0007829|PDB:2C63"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:2C63"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:2C63"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2C63"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2C63"
FT HELIX 216..234
FT /evidence="ECO:0007829|PDB:2C63"
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
