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UniProtKB/Swiss-Prot entry P27348

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

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Entry information
Entry name 1433T_HUMAN
Primary accession number P27348
Secondary accession numbers Q567U5 Q5TZU8 Q9UP48
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name 14-3-3 protein theta
Synonyms 14-3-3 protein tau
14-3-3 protein T-cell
Protein HS1
Gene name
Name: YWHAQ
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=T-cell;
DOI=10.1016/0167-4781(91)90136-A; PubMed=2015305 [NCBI, ExPASy, EBI, Israel, Japan]
Nielsen P.J.;
"Primary structure of a human protein kinase regulator protein.";
Biochim. Biophys. Acta 1088:425-428(1991).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
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).
[3]
 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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, Skin, and Uterus;
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).
[5]
 PROTEIN SEQUENCE OF 1-18.
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).
[6]
 PROTEIN SEQUENCE OF 1-9; 28-49; 61-68; 104-115; 139-167 AND 213-222, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma, and Hepatoma;
Bienvenut W.V., Dhillon A.S., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-245.
TISSUE=Brain;
Yu W., Gibbs R.A.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[8]
 PHOSPHORYLATION AT SER-232, AND MASS SPECTROMETRY.
DOI=10.1074/jbc.272.46.28882; PubMed=9360956 [NCBI, ExPASy, EBI, Israel, Japan]
Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., Morrice N., Moelling K., Aitken A.;
"14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction.";
J. Biol. Chem. 272:28882-28888(1997).
[9]
 TISSUE SPECIFICITY.
DOI=10.1046/j.1471-4159.2000.0752511.x; PubMed=11080204 [NCBI, ExPASy, EBI, Israel, Japan]
Malaspina A., Kaushik N., de Belleroche J.;
"A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal cord.";
J. Neurochem. 75:2511-2520(2000).
[10]
 INTERACTION WITH CDKN1B.
DOI=10.1074/jbc.M203668200; PubMed=12042314 [NCBI, ExPASy, EBI, Israel, Japan]
Fujita N., Sato S., Katayama K., Tsuruo T.;
"Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization.";
J. Biol. Chem. 277:28706-28713(2002).
[11]
 INTERACTION WITH SSH1.
DOI=10.1083/jcb.200401136; PubMed=15159416 [NCBI, ExPASy, EBI, Israel, Japan]
Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
"A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia.";
J. Cell Biol. 165:465-471(2004).
[12]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
 IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[15]
 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1038/376188a0; PubMed=7603573 [NCBI, ExPASy, EBI, Israel, Japan]
Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A., Gamblin S.J.;
"Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways.";
Nature 376:188-191(1995).
[16]
 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234, 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
X56468; CAA39840.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X57347; CAA40622.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020014; AAV38817.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001197; AAH01197.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050601; AAH50601.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC056867; AAH56867.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093019; AAH93019.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF070556; AAC28640.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00018146; -.
PIR S15076; S15076.
RefSeq NP_006817.1; -.
UniGene Hs.74405
3D structure databases
PDB
2BTP; X-ray; 2.80 A; A/B=1-234.[ExPASy / RCSB / EBI]
PDBsum 2BTP; -.
ModBase P27348.
Protein-protein interaction databases
DIP DIP:27584N; -.
IntAct P27348; 68.
PTM databases
PhosphoSite P27348; -.
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.
2D gel databases
Cornea-2DPAGE P27348; -.
OGP P27348; -.
REPRODUCTION-2DPAGE IPI00018146; -.
Organism-specific databases
GeneCards GC02M009674; -.
H-InvDB HIX0029798; -.
HIX0057400; -.
HGNC HGNC:12854; YWHAQ.
GenAtlas YWHAQ.
HPA CAB010286; -.
HPA007925; -.
MIM 609009; gene. [NCBI / EBI]
PharmGKB PA37443; -.
Gene expression databases
ArrayExpress P27348; -.
Bgee P27348; -.
CleanEx HS_YWHAQ; -.
GermOnline ENSG00000134308; Homo sapiens.
Ontologies
GO
GO:0005813; Cellular component: centrosome (inferred from direct assay from HPA).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0019904; Molecular function: protein domain specific binding (inferred from electronic annotation from InterPro).
GO:0047485; Molecular function: protein N-terminus binding (inferred from physical interaction from UniProtKB).
GO:0045892; Biological process: negative regulation of transcription, DNA-dependent (inferred from direct assay 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 P27348; -.
PRIDE P27348; -.
Genome annotation databases
Ensembl ENSG00000134308; Homo sapiens. [Contig view]
GeneID 10971; -.
KEGG hsa:10971; -.
Phylogenomic databases
HOGENOM P27348; -.
HOVERGEN P27348; -.
OMA P27348; DTSDKKM.
Other
NextBio 41686; -.
PMAP-CutDB P27348; -.
SOURCE YWHAQ; Homo sapiens.
ProtoNet P27348.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   245  245     14-3-3 protein theta. PRO_0000058636
SITE   56    56  1     Interaction with phosphoserine on interacting protein. 
SITE   127   127  1     Interaction with phosphoserine on interacting protein. 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   232   232        Phosphoserine; by CK1 (Probable). 
CONFLICT   136   136        D -> N (in Ref. 3; AAV38817). 
HELIX   3    15  13      
HELIX   19    31  13      
HELIX   38    68  31      
HELIX   75   103  29      
TURN   104   108  5      
HELIX   112   132  21      
HELIX   135   159  25      
HELIX   165   180  16      
HELIX   185   201  17      
TURN   202   205  4      
HELIX   208   227  20      
Sequence information
Length: 245 AA [This is the length of the unprocessed precursor] Molecular weight: 27764 Da [This is the MW of the unprocessed precursor] CRC64: 175534325E9E37C4 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR 

        70         80         90        100        110        120 
VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK 

       130        140        150        160        170        180 
MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE 

       190        200        210        220        230        240 
ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA 


EGAEN
P27348 in FASTA format

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