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UniProtKB/Swiss-Prot entry P62258


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

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Entry information
Entry name 1433E_HUMAN
Primary accession number P62258
Secondary accession numbers P29360 P42655 Q53XZ5 Q63631 Q7M4R4
Integrated into Swiss-Prot on July 5, 2004
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 55)
Name and origin of the protein
Protein name 14-3-3 protein epsilon
Synonym 14-3-3E
Gene name
Name: YWHAE
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].
PubMed=7644510 [NCBI, ExPASy, EBI, Israel, Japan]
Conklin D.S., Galaktionov K., Beach D.;
"14-3-3 proteins associate with cdc25 phosphatases.";
Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8858348 [NCBI, ExPASy, EBI, Israel, Japan]
Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.;
"14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region.";
Genome Res. 6:735-741(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/382308a0; PubMed=8684458 [NCBI, ExPASy, EBI, Israel, Japan]
Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T.;
"Function of 14-3-3 proteins.";
Nature 382:308-308(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
Luk S.C.W., Lee C.Y., Waye M.M.Y.;
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tanigami A., Chong S.S., Ledbetter D.H.;
"14-3-3 epsilon genomic sequence.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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]
PROTEIN SEQUENCE OF 1-19.
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).
[10]
PROTEIN SEQUENCE OF 1-19; 30-50 AND 131-170, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAY-2005) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 103-108; 120-123; 131-141 AND 143-153.
TISSUE=Histiocytic lymphoma;
PubMed=2026444 [NCBI, ExPASy, EBI, Israel, Japan]
Demeter J., Medzihradszky D., Kha H., Goetzl E.J., Turck C.W.;
"Isolation and partial characterization of the structures of fibroblast activating factor-related proteins from U937 cells.";
Immunology 72:350-354(1991).
[12]
PROTEIN SEQUENCE OF 131-141 AND 154-190, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[13]
INTERACTION WITH HCV CORE PROTEIN.
DOI=10.1128/JVI.74.4.1736-1741.2000; PubMed=10644344 [NCBI, ExPASy, EBI, Israel, Japan]
Aoki H., Hayashi J., Moriyama M., Arakawa Y., Hino O.;
"Hepatitis C virus core protein interacts with 14-3-3 protein and activates the kinase Raf-1.";
J. Virol. 74:1736-1741(2000).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
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
U20972; AAC50175.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U54778; AAC50710.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U43399; AAC50625.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U43430; AAD00026.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28936; AAA75301.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB017103; BAA32538.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007161; AAP35825.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471108; EAW90628.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000179; AAH00179.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001440; AAH01440.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A61235; A61235.
I38947; I38947.
RefSeq NP_006752.1; -.
UniGene Hs.513851
3D structure databases
PDB
2BR9; X-ray; 1.75 A; A=1-233.[ExPASy / RCSB / EBI]
PDBsum 2BR9; -.
ModBase P62258.
Protein-protein interaction databases
IntAct P62258; -.
2D gel databases
OGP P42655; -.
Organism-specific databases
H-InvDB HIX0013397; -.
HIX0013751; -.
HIX0030006; -.
HGNC HGNC:12851; YWHAE.
GenAtlas YWHAE.
HPA CAB016200; -.
HPA008445; -.
MIM 605066; gene. [NCBI / EBI]
PharmGKB PA37440; -.
GeneCards P62258.
Gene expression databases
ArrayExpress P62258; -.
CleanEx HS_YWHAE; -.
GermOnline ENSG00000108953; Homo sapiens.
Ontologies
GO
GO:0019899; Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0007242; Biological process: intracellular signaling cascade (traceable author statement from ProtInc).
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.
BLOCKS P62258.
Proteomic databases
PeptideAtlas P62258; -.
Genome annotation databases
Ensembl ENSG00000108953; Homo sapiens. [Contig view]
GeneID 7531; -.
KEGG hsa:7531; -.
Phylogenomic databases
HOGENOM P62258; -.
HOVERGEN P62258; -.
Other
LinkHub P62258; -.
SOURCE YWHAE; Homo sapiens.
ProtoNet P62258.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Host-virus interaction; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   255  255     14-3-3 protein epsilon. PRO_0000058618
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   210   210        Phosphoserine. 
CONFLICT   106   107        KH -> NY (in Ref. 11; AA sequence). 
CONFLICT   143   143        E -> F (in Ref. 11; AA sequence). 
CONFLICT   148   148        S -> T (in Ref. 11; AA sequence). 
HELIX   4    17  14      
HELIX   20    31  12      
HELIX   39    73  35      
HELIX   76   106  31      
HELIX   108   111  4      
HELIX   115   135  21      
HELIX   138   162  25      
HELIX   168   183  16      
HELIX   188   204  17      
HELIX   205   208  4      
TURN   211   213  3      
HELIX   214   231  18      
Sequence information
Length: 255 AA [This is the length of the unprocessed precursor] Molecular weight: 29174 Da [This is the MW of the unprocessed precursor] CRC64: 07817CCBD1F75B26 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW 

        70         80         90        100        110        120 
RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF 

       130        140        150        160        170        180 
YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF 

       190        200        210        220        230        240 
YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE 

       250 
EQNKEALQDV EDENQ 

P62258 in FASTA format

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