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UniProtKB/Swiss-Prot entry P42229


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

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Entry information
Entry name STA5A_HUMAN
Primary accession number P42229
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 93)
Name and origin of the protein
Protein name Signal transducer and activator of transcription 5A
Synonyms None
Gene name
Name: STAT5A
Synonyms: STAT5
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].
DOI=10.1016/1074-7613(95)90140-X; PubMed=7719937 [NCBI, ExPASy, EBI, Israel, Japan]
Hou J., Schindler U., Henzel W.J., Wong S.C., McKnight S.L.;
"Identification and purification of human Stat proteins activated in response to interleukin-2.";
Immunity 2:321-329(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Lin J.X., Mietz J., Modi W.S., John S., Leonard W.J.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix;
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).
[4]
INTERACTION WITH NCOA1.
DOI=10.1074/jbc.M303644200; PubMed=12954634 [NCBI, ExPASy, EBI, Israel, Japan]
Litterst C.M., Kliem S., Marilley D., Pfitzner E.;
"NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the FDL motif in the alpha-helical region of the STAT5 transactivation domain.";
J. Biol. Chem. 278:45340-45351(2003).
[5]
INTERACTION WITH SOCS7.
DOI=10.1074/jbc.M411596200; PubMed=15677474 [NCBI, ExPASy, EBI, Israel, Japan]
Martens N., Uzan G., Wery M., Hooghe R., Hooghe-Peters E.L., Gertler A.;
"Suppressor of cytokine signaling 7 inhibits prolactin, growth hormone, and leptin signaling by interacting with STAT5 or STAT3 and attenuating their nuclear translocation.";
J. Biol. Chem. 280:13817-13823(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-694, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-694, AND MASS SPECTROMETRY.
TISSUE=Lung;
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-372 AND SER-375, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, 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).
[10]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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
L41142; AAA73962.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U43185; AAB06589.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027036; AAH27036.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00030783; -.
PIR G02317; G02317.
RefSeq NP_003143.2; -.
UniGene Hs.437058
3D structure databases
HSSP P42227; 1BG1. [HSSP ENTRY / PDB]
SMR P42229; 138-690.
ModBase P42229.
Protein-protein interaction databases
DIP DIP:396N; -.
IntAct P42229; 4.
PTM databases
PhosphoSite P42229; -.
Enzyme and pathway databases
Pathway_Interaction_DB angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
epopathway; EPO signaling pathway.
il12_2pathway; IL12-mediated signaling events.
il2_stat5pathway; IL2 signaling events mediated by STAT5.
il2_1pathway; IL2-mediated signaling events.
il23pathway; IL23-mediated signaling events.
il27pathway; IL27-mediated signaling events.
il4_2pathway; IL4-mediated signaling events.
pdgfrbpathway; PDGFR-beta signaling pathway.
ptp1bpathway; Signaling events mediated by PTP1B.
kitpathway; Signaling events mediated by Stem cell factor receptor (c-Kit).
pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
Organism-specific databases
GeneCards GC17P037694; -.
H-InvDB HIX0013838; -.
HGNC HGNC:11366; STAT5A.
GenAtlas STAT5A.
HPA CAB003860; -.
MIM 601511; gene. [NCBI / EBI]
PharmGKB PA338; -.
Gene expression databases
Bgee P42229; -.
CleanEx HS_STAT5A; -.
GermOnline ENSG00000126561; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0042301; Molecular function: phosphate binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0003700; Molecular function: transcription factor activity (traceable author statement from ProtInc).
GO:0006103; Biological process: 2-oxoglutarate metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0000255; Biological process: allantoin metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006101; Biological process: citrate metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006600; Biological process: creatine metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0046449; Biological process: creatinine metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006631; Biological process: fatty acid metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006549; Biological process: isoleucine metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006107; Biological process: oxaloacetate metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006105; Biological process: succinate metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0019530; Biological process: taurine metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
GO:0006573; Biological process: valine metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011992; EF-Hand_type.
IPR000980; SH2.
IPR013800; STAT_TF_alpha.
IPR001217; STAT_TF_core.
IPR013801; STAT_TF_DNA-bd.
IPR012345; STAT_TF_DNA-bd_sub.
IPR013799; STAT_TF_prot_interaction.
Graphical view of domain structure.
Gene3D G3DSA:1.10.238.10; EF-Hand_type; 1.
G3DSA:3.30.505.10; SH2; 1.
G3DSA:1.20.1050.20; STAT_alpha; 1.
G3DSA:2.60.40.630; STAT_DNA_bd_sub; 1.
G3DSA:1.10.532.10; STAT_protein_interaction; 1.
PANTHER PTHR11801; STAT; 1.
Pfam PF00017; SH2; 1.
PF01017; STAT_alpha; 1.
PF02864; STAT_bind; 1.
PF02865; STAT_int; 1.
Pfam graphical view of domain structure.
SMART SM00252; SH2; 1.
SMART graphical view of domain structure.
PROSITE PS50001; SH2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P42229; -.
PRIDE P42229; -.
Genome annotation databases
Ensembl ENSG00000126561; Homo sapiens. [Contig view]
GeneID 6776; -.
KEGG hsa:6776; -.
Phylogenomic databases
HOGENOM P42229; -.
HOVERGEN P42229; -.
OMA P42229; DSPERNL.
Other
NextBio 26450; -.
SOURCE STAT5A; Homo sapiens.
ProtoNet P42229.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; SH2 domain; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   794  794     Signal transducer and activator of transcription 5A. PRO_0000182423
DOMAIN   589   686  98     SH2. 
MOD_RES   193   193        Phosphoserine. 
MOD_RES   372   372        Phosphothreonine. 
MOD_RES   375   375        Phosphoserine. 
MOD_RES   694   694        Phosphotyrosine; by JAK. 
MOD_RES   780   780        Phosphoserine (By similarity). 
VARIANT   389   389  1     R -> H (in dbSNP:rs2230134 [NCBI]). VAR_052073 
CONFLICT   88    88        G -> R (in Ref. 2; AAB06589). 
Sequence information
Length: 794 AA [This is the length of the unprocessed precursor] Molecular weight: 90647 Da [This is the MW of the unprocessed precursor] CRC64: C64237295F88CFBE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN PQDRAQATQL 

        70         80         90        100        110        120 
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQKTYDR CPLELVRCIR HILYNEQRLV 

       130        140        150        160        170        180 
REANNCSSPA GILVDAMSQK HLQINQTFEE LRLVTQDTEN ELKKLQQTQE YFIIQYQESL 

       190        200        210        220        230        240 
RIQAQFAQLA QLSPQERLSR ETALQQKQVS LEAWLQREAQ TLQQYRVELA EKHQKTLQLL 

       250        260        270        280        290        300 
RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC 

       310        320        330        340        350        360 
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL 

       370        380        390        400        410        420 
NVHMNPPQVK ATIISEQQAK SLLKNENTRN ECSGEILNNC CVMEYHQATG TLSAHFRNMS 

       430        440        450        460        470        480 
LKRIKRADRR GAESVTEEKF TVLFESQFSV GSNELVFQVK TLSLPVVVIV HGSQDHNATA 

       490        500        510        520        530        540 
TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNN 

       550        560        570        580        590        600 
SSSHLEDYSG LSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK 

       610        620        630        640        650        660 
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPERNL WNLKPFTTRD FSIRSLADRL 

       670        680        690        700        710        720 
GDLSYLIYVF PDRPKDEVFS KYYTPVLAKA VDGYVKPQIK QVVPEFVNAS ADAGGSSATY 

       730        740        750        760        770        780 
MDQAPSPAVC PQAPYNMYPQ NPDHVLDQDG EFDLDETMDV ARHVEELLRR PMDSLDSRLS 

       790 
PPAGLFTSAR GSLS 

P42229 in FASTA format

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