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UniProtKB/Swiss-Prot entry Q04917


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 1433F_HUMAN
Primary accession number Q04917
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 104)
Name and origin of the protein
Protein name 14-3-3 protein eta
Synonym Protein AS1
Gene name
Name: YWHAH
Synonyms: YWHA1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1016/0167-4781(93)90053-G; PubMed=8218406 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1002/jnr.490310403; PubMed=1578511 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1007/BF02740697; PubMed=8561965 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1006/geno.1996.0426; PubMed=8812417 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
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:RESEARCH84.1-RESEARCH84.11(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1006/jmbi.1993.1346; PubMed=8515476 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
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 MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V.;
Submitted (AUG-2005) to UniProtKB.
[12]
INTERACTION WITH AR; ESR1; ESR2; MC2R; NRIP1; NR3C1; PPARBP AND THRA.
DOI=10.1210/me.15.4.501; PubMed=11266503 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
INTERACTION WITH CDKN1B.
DOI=10.1074/jbc.M306614200; PubMed=14504289 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
INTERACTION WITH ABL1, AND MASS SPECTROMETRY.
DOI=10.1038/ncb1228; PubMed=15696159 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[16]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
DOI=10.1073/pnas.0605779103; PubMed=17085597 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L20422; AAA35483.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X80536; CAA56676.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X78138; CAA55017.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X57345; CAA40620.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D78577; BAA11418.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S80794; AAB36036.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456612; CAG30498.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82248; CAB05112.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003047; AAH03047.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00216319; -.
PIR S34756; S34756.
S38509; S38509.
S38532; S38532.
RefSeq NP_003396.1; -.
UniGene Hs.226755
3D structure databases
PDB
2C63; X-ray; 2.15 A; A/B/C/D=1-246.[ExPASy / RCSB / EBI]
2C74; X-ray; 2.70 A; A/B=1-246.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2C63; -.
2C74; -.
ModBase Q04917.
Protein-protein interaction databases
DIP DIP:27566N; -.
IntAct Q04917; 91.
PTM databases
PhosphoSite Q04917; -.
Enzyme and pathway databases
Pathway_Interaction_DB a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
foxopathway; FoxO family signaling.
insulin_glucose_pathway; Insulin-mediated glucose transport.
p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
Organism-specific databases
GeneCards GC22P030665; -.
H-InvDB HIX0016401; -.
HGNC HGNC:12853; YWHAH.
GenAtlas YWHAH.
MIM 113508; gene. [NCBI / EBI]
PharmGKB PA37442; -.
Gene expression databases
ArrayExpress Q04917; -.
Bgee Q04917; -.
CleanEx HS_YWHAH; -.
GermOnline ENSG00000128245; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0019899; Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0035259; Molecular function: glucocorticoid receptor binding (inferred from physical interaction from UniProtKB).
GO:0005159; Molecular function: insulin-like growth factor receptor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0019904; Molecular function: protein domain specific binding (inferred from sequence or structural similarity from UniProtKB).
GO:0016563; Molecular function: transcription activator activity (inferred from direct assay from UniProtKB).
GO:0006713; Biological process: glucocorticoid catabolic process (inferred from direct assay from UniProtKB).
GO:0042921; Biological process: glucocorticoid receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0006886; Biological process: intracellular protein transport (inferred from sequence or structural similarity from UniProtKB).
GO:0050774; Biological process: negative regulation of dendrite morphogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0045941; Biological process: positive regulation of transcription (inferred from direct assay from UniProtKB).
GO:0048167; Biological process: regulation of synaptic plasticity (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000308; 14-3-3.
Graphical view of domain structure.
Gene3D G3DSA:1.20.190.20; 14-3-3; 1.
PANTHER PTHR18860; 14-3-3; 1.
Pfam PF00244; 14-3-3; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000868; 14-3-3; 1.
PRINTS PR00305; 1433ZETA.
ProDom PD000600; 14-3-3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00101; 14_3_3; 1.
SMART graphical view of domain structure.
PROSITE PS00796; 1433_1; 1.
PS00797; 1433_2; 1.
Proteomic databases
PeptideAtlas Q04917; -.
PRIDE Q04917; -.
Genome annotation databases
Ensembl ENSG00000128245; Homo sapiens. [Contig view]
GeneID 7533; -.
KEGG hsa:7533; -.
Phylogenomic databases
HOGENOM Q04917; -.
HOVERGEN Q04917; -.
OMA Q04917; ESSEAAY.
Other
NextBio 29471; -.
SOURCE YWHAH; Homo sapiens.
ProtoNet Q04917.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   246  245     14-3-3 protein eta. PRO_0000058623
SITE   57    57  1     Interaction with phosphoserine on interacting protein. 
SITE   132   132  1     Interaction with phosphoserine on interacting protein. 
MOD_RES   2     2        N-acetylglycine. 
MOD_RES   117   117        Phosphotyrosine (By similarity). 
CONFLICT   144   144        N -> T (in Ref. 9; CAA40620). 
CONFLICT   157   157        A -> G (in Ref. 1; AAA35483). 
CONFLICT   237   237        Q -> L (in Ref. 1; AAA35483). 
HELIX   4    16  13      
HELIX   20    31  12      
HELIX   39    73  35      
HELIX   76   106  31      
TURN   107   111  5      
HELIX   117   137  21      
HELIX   140   164  25      
HELIX   170   185  16      
HELIX   190   206  17      
HELIX   207   210  4      
TURN   213   215  3      
HELIX   216   234  19      
Sequence information
Length: 246 AA [This is the length of the unprocessed precursor] Molecular weight: 28219 Da [This is the MW of the unprocessed precursor] CRC64: D70FBC100C45D6E5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW 

        70         80         90        100        110        120 
RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LSLLDKFLIK NCNDFQYESK 

       130        140        150        160        170        180 
VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEQMQPTHP IRLGLALNFS 

       190        200        210        220        230        240 
VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE 


EAGEGN 

Q04917 in FASTA format

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