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14-3-3 protein eta (Protein AS1)

 1433F_HUMAN             Reviewed;         246 AA.
Q04917;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 195.
RecName: Full=14-3-3 protein eta;
AltName: Full=Protein AS1;
Name=YWHAH; Synonyms=YWHA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8218406; DOI=10.1016/0167-4781(93)90053-G;
Swanson K.D., Dhar M.S., Joshi J.G.;
"The human and bovine 14-3-3 eta protein mRNAs are highly conserved in
both their translated and untranslated regions.";
Biochim. Biophys. Acta 1216:145-148(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=1578511; DOI=10.1002/jnr.490310403;
Ichimura-Ohshima Y., Morii K., Ichimura T., Araki K., Takahashi Y.,
Isobe T., Minoshima S., Fukuyama R., Shimizu N., Kuwano R.;
"cDNA cloning and chromosome assignment of the gene for human brain
14-3-3 protein eta chain.";
J. Neurosci. Res. 31:600-605(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Leffers H., Tommerup N., Celis J.E.;
Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8561965; DOI=10.1007/BF02740697;
Muratake T., Hayashi S., Ichimura Y., Morii K., Kuwano R.,
Ichikawa T., Kumanishi T., Isobe T., Watanabe M., Kondo H.;
"The effect on methamphetamine on the mRNA level for 14.3.3 eta chain
in the human cultured cells.";
Mol. Neurobiol. 11:223-230(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8812417; DOI=10.1006/geno.1996.0426;
Muratake T., Hayashi S., Ichikawa T., Kumanishi T., Ichimura Y.,
Kuwano R., Isobe T., Wang Y., Minoshima S., Shimizu N., Takahashi Y.;
"Structural organization and chromosomal assignment of the human 14-3-
3 eta chain gene (YWHAH).";
Genomics 36:63-69(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-225.
TISSUE=Keratinocyte;
PubMed=8515476; DOI=10.1006/jmbi.1993.1346;
Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H.,
Walbum E., Vandekerckhove J., Celis J.E.;
"Molecular cloning and expression of the transformation sensitive
epithelial marker stratifin. A member of a protein family that has
been involved in the protein kinase C signalling pathway.";
J. Mol. Biol. 231:982-998(1993).
[10]
PROTEIN SEQUENCE OF 2-10.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[11]
PROTEIN SEQUENCE OF 2-10; 29-50; 62-69; 126-132; 144-155; 163-172 AND
218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V.;
Submitted (AUG-2005) to UniProtKB.
[12]
PROTEIN SEQUENCE OF 1-10; 13-50; 62-78; 111-120 AND 133-162,
INTERACTION WITH PI4KB; TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=23572552; DOI=10.1128/mBio.00098-13;
Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L.,
DeRisi J.L.;
"ACBD3 interaction with TBC1 domain 22 protein is differentially
affected by enteroviral and kobuviral 3A protein binding.";
MBio 4:E00098-E00098(2013).
[13]
INTERACTION WITH AR; ESR1; ESR2; MC2R; NRIP1; NR3C1; PPARBP AND THRA.
PubMed=11266503; DOI=10.1210/mend.15.4.0624;
Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E.,
Gustafsson J.-A.;
"Regulation of glucocorticoid receptor activity by 14-3-3-dependent
intracellular relocalization of the corepressor RIP140.";
Mol. Endocrinol. 15:501-511(2001).
[14]
FUNCTION, AND INTERACTION WITH PDPK1.
PubMed=12177059; DOI=10.1074/jbc.M205141200;
Sato S., Fujita N., Tsuruo T.;
"Regulation of kinase activity of 3-phosphoinositide-dependent protein
kinase-1 by binding to 14-3-3.";
J. Biol. Chem. 277:39360-39367(2002).
[15]
INTERACTION WITH CDKN1B.
PubMed=14504289; DOI=10.1074/jbc.M306614200;
Fujita N., Sato S., Tsuruo T.;
"Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein
S6 kinases promotes its binding to 14-3-3 and cytoplasmic
localization.";
J. Biol. Chem. 278:49254-49260(2003).
[16]
INTERACTION WITH ABL1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15696159; DOI=10.1038/ncb1228;
Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of
c-Abl in the apoptotic response to DNA damage.";
Nat. Cell Biol. 7:278-285(2005).
[17]
INTERACTION WITH GAB2.
PubMed=19172738; DOI=10.1038/emboj.2008.159;
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
Guilhaus M., James D.E., Daly R.J.;
"Phosphorylation-dependent binding of 14-3-3 terminates signalling by
the Gab2 docking protein.";
EMBO J. 27:2305-2316(2008).
[18]
INTERACTION WITH SLITRK1.
PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
Kajiwara Y., Buxbaum J.D., Grice D.E.;
"SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a
phosphorylation-dependent manner.";
Biol. Psychiatry 66:918-925(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
INTERACTION WITH DAPK2.
PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
"Suppression of death-associated protein kinase 2 by interaction with
14-3-3 proteins.";
Biochem. Biophys. Res. Commun. 464:70-75(2015).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), IDENTIFICATION BY MASS
SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
PubMed=17085597; DOI=10.1073/pnas.0605779103;
Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
"Structural basis for protein-protein interactions in the 14-3-3
protein family.";
Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
-!- FUNCTION: Adapter protein implicated in the regulation of a large
spectrum of both general and specialized signaling pathways. Binds
to a large number of partners, usually by recognition of a
phosphoserine or phosphothreonine motif. Binding generally results
in the modulation of the activity of the binding partner.
Negatively regulates the kinase activity of PDPK1.
{ECO:0000269|PubMed:12177059}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with many nuclear
hormone receptors and cofactors including AR, ESR1, ESR2, MC2R,
NR3C1, NRIP1, PPARBP and THRA. Interacts with ABL1 (phosphorylated
form); the interaction retains it in the cytoplasm. Interacts with
ARHGEF28 and CDK16 (By similarity). Weakly interacts with CDKN1B.
Interacts with GAB2. Interacts with KCNK18 in a phosphorylation-
dependent manner. Interacts with SAMSN1 (By similarity). Interacts
with the 'Ser-241' phosphorylated form of PDPK1. Interacts with
the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703).
Interacts with PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552).
Interacts with SLITRK1 (PubMed:19640509). {ECO:0000250,
ECO:0000269|PubMed:11266503, ECO:0000269|PubMed:12177059,
ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:15696159,
ECO:0000269|PubMed:17085597, ECO:0000269|PubMed:19172738,
ECO:0000269|PubMed:19640509, ECO:0000269|PubMed:23572552,
ECO:0000269|PubMed:26047703}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-306940, EBI-306940;
Q96B36:AKT1S1; NbExp=3; IntAct=EBI-306940, EBI-720593;
Q8N5S9:CAMKK1; NbExp=5; IntAct=EBI-306940, EBI-6424030;
P30305:CDC25B; NbExp=4; IntAct=EBI-306940, EBI-1051746;
O94921:CDK14; NbExp=3; IntAct=EBI-306940, EBI-1043945;
P67828:CSNK1A1 (xeno); NbExp=8; IntAct=EBI-306940, EBI-7540603;
O60565:GREM1; NbExp=5; IntAct=EBI-306940, EBI-944395;
P56524:HDAC4; NbExp=4; IntAct=EBI-306940, EBI-308629;
Q14678-2:KANK1; NbExp=3; IntAct=EBI-306940, EBI-6173812;
Q5S007:LRRK2; NbExp=3; IntAct=EBI-306940, EBI-5323863;
Q7KZI7:MARK2; NbExp=8; IntAct=EBI-306940, EBI-516560;
P27448:MARK3; NbExp=4; IntAct=EBI-306940, EBI-707595;
Q96L34:MARK4; NbExp=6; IntAct=EBI-306940, EBI-302319;
Q8TEW0:PARD3; NbExp=6; IntAct=EBI-306940, EBI-81968;
Q9NPB6:PARD6A; NbExp=2; IntAct=EBI-306940, EBI-81876;
Q9BYG5:PARD6B; NbExp=3; IntAct=EBI-306940, EBI-295391;
Q9BYG4:PARD6G; NbExp=2; IntAct=EBI-306940, EBI-295417;
P41743:PRKCI; NbExp=3; IntAct=EBI-306940, EBI-286199;
P04049:RAF1; NbExp=6; IntAct=EBI-306940, EBI-365996;
P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-306940, EBI-6930266;
P37840-1:SNCA; NbExp=9; IntAct=EBI-306940, EBI-9684465;
-!- TISSUE SPECIFICITY: Expressed mainly in the brain and present in
other tissues albeit at lower levels.
-!- PTM: Phosphorylated on Ser-59 by protein kinase C delta type
catalytic subunit in a sphingosine-dependent fashion.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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EMBL; L20422; AAA35483.1; -; mRNA.
EMBL; X80536; CAA56676.1; -; Genomic_DNA.
EMBL; X78138; CAA55017.1; -; mRNA.
EMBL; X57345; CAA40620.1; -; mRNA.
EMBL; D78577; BAA11418.1; -; Genomic_DNA.
EMBL; S80794; AAB36036.1; -; mRNA.
EMBL; CR456612; CAG30498.1; -; mRNA.
EMBL; Z82248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003047; AAH03047.1; -; mRNA.
CCDS; CCDS13901.1; -.
PIR; S34756; S34756.
PIR; S38509; S38509.
PIR; S38532; S38532.
RefSeq; NP_003396.1; NM_003405.3.
UniGene; Hs.226755; -.
PDB; 2C63; X-ray; 2.15 A; A/B/C/D=2-246.
PDB; 2C74; X-ray; 2.70 A; A/B=2-246.
PDBsum; 2C63; -.
PDBsum; 2C74; -.
ProteinModelPortal; Q04917; -.
SMR; Q04917; -.
BioGrid; 113365; 217.
CORUM; Q04917; -.
DIP; DIP-27566N; -.
ELM; Q04917; -.
IntAct; Q04917; 215.
MINT; MINT-124456; -.
STRING; 9606.ENSP00000248975; -.
ChEMBL; CHEMBL3708585; -.
iPTMnet; Q04917; -.
PhosphoSitePlus; Q04917; -.
SwissPalm; Q04917; -.
BioMuta; YWHAH; -.
DMDM; 1345593; -.
EPD; Q04917; -.
MaxQB; Q04917; -.
PaxDb; Q04917; -.
PeptideAtlas; Q04917; -.
PRIDE; Q04917; -.
TopDownProteomics; Q04917; -.
DNASU; 7533; -.
Ensembl; ENST00000248975; ENSP00000248975; ENSG00000128245.
GeneID; 7533; -.
KEGG; hsa:7533; -.
UCSC; uc003alz.4; human.
CTD; 7533; -.
DisGeNET; 7533; -.
EuPathDB; HostDB:ENSG00000128245.14; -.
GeneCards; YWHAH; -.
HGNC; HGNC:12853; YWHAH.
HPA; CAB025918; -.
MIM; 113508; gene.
neXtProt; NX_Q04917; -.
OpenTargets; ENSG00000128245; -.
PharmGKB; PA37442; -.
eggNOG; KOG0841; Eukaryota.
eggNOG; COG5040; LUCA.
GeneTree; ENSGT00760000119116; -.
HOGENOM; HOG000240379; -.
HOVERGEN; HBG050423; -.
InParanoid; Q04917; -.
KO; K16198; -.
OMA; CERYEDM; -.
OrthoDB; EOG091G0VKY; -.
PhylomeDB; Q04917; -.
TreeFam; TF102003; -.
Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLink; Q04917; -.
SIGNOR; Q04917; -.
ChiTaRS; YWHAH; human.
EvolutionaryTrace; Q04917; -.
GeneWiki; YWHAH; -.
GenomeRNAi; 7533; -.
PRO; PR:Q04917; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000128245; -.
CleanEx; HS_YWHAH; -.
ExpressionAtlas; Q04917; baseline and differential.
Genevisible; Q04917; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0014704; C:intercalated disc; IC:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0003779; F:actin binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0035259; F:glucocorticoid receptor binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL.
GO; GO:0006713; P:glucocorticoid catabolic process; IDA:UniProtKB.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
GO; GO:0086010; P:membrane depolarization during action potential; IDA:BHF-UCL.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS:UniProtKB.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0002028; P:regulation of sodium ion transport; IDA:BHF-UCL.
GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
Gene3D; 1.20.190.20; -; 1.
InterPro; IPR000308; 14-3-3.
InterPro; IPR023409; 14-3-3_CS.
InterPro; IPR036815; 14-3-3_dom_sf.
InterPro; IPR023410; 14-3-3_domain.
PANTHER; PTHR18860; PTHR18860; 1.
Pfam; PF00244; 14-3-3; 1.
PIRSF; PIRSF000868; 14-3-3; 1.
PRINTS; PR00305; 1433ZETA.
SMART; SM00101; 14_3_3; 1.
SUPFAM; SSF48445; SSF48445; 1.
PROSITE; PS00796; 1433_1; 1.
PROSITE; PS00797; 1433_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Isopeptide bond; Nitration; Phosphoprotein;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.11}.
CHAIN 2 246 14-3-3 protein eta.
/FTId=PRO_0000058623.
SITE 57 57 Interaction with phosphoserine on
interacting protein.
SITE 132 132 Interaction with phosphoserine on
interacting protein.
MOD_RES 2 2 N-acetylglycine. {ECO:0000269|Ref.11}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 50 50 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P27348}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000250|UniProtKB:P68510}.
MOD_RES 69 69 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27348}.
MOD_RES 85 85 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q9CQV8}.
MOD_RES 120 120 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27348}.
CROSSLNK 50 50 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P27348}.
CONFLICT 144 144 N -> T (in Ref. 9; CAA40620).
{ECO:0000305}.
CONFLICT 157 157 A -> G (in Ref. 1; AAA35483).
{ECO:0000305}.
CONFLICT 237 237 Q -> L (in Ref. 1; AAA35483).
{ECO:0000305}.
HELIX 4 16 {ECO:0000244|PDB:2C63}.
HELIX 20 31 {ECO:0000244|PDB:2C63}.
HELIX 39 73 {ECO:0000244|PDB:2C63}.
HELIX 76 106 {ECO:0000244|PDB:2C63}.
TURN 107 111 {ECO:0000244|PDB:2C63}.
HELIX 117 137 {ECO:0000244|PDB:2C63}.
HELIX 140 164 {ECO:0000244|PDB:2C63}.
HELIX 170 185 {ECO:0000244|PDB:2C63}.
HELIX 190 206 {ECO:0000244|PDB:2C63}.
HELIX 207 210 {ECO:0000244|PDB:2C63}.
TURN 213 215 {ECO:0000244|PDB:2C63}.
HELIX 216 234 {ECO:0000244|PDB:2C63}.
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


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