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P42229 (STA5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal transducer and activator of transcription 5A
Gene names
Name:STAT5A
Synonyms:STAT5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length794 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Mediates cellular responses to ERBB4. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation. Ref.7 Ref.12

Subunit structure

Forms a homodimer or a heterodimer with a related family member. Binds NR3C1 By similarity. Interacts with NCOA1 and SOCS7. Interacts with ERBB4. Ref.8 Ref.12 Ref.13

Subcellular location

Cytoplasm. Nucleus. Note: Translocated into the nucleus in response to phosphorylation. Ref.12

Post-translational modification

Tyrosine phosphorylated in response to KITLG/SCF, IL2, IL3, IL7, IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylation is required for DNA-binding activity and dimerization. Serine phosphorylation is also required for maximal transcriptional activity By similarity. Tyrosine phosphorylated in response to signaling via activated FLT3; wild-type FLT3 results in much weaker phosphorylation than constitutively activated mutant FLT3. Alternatively, can be phosphorylated by JAK2 at Tyr-694. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates prolactin signaling pathway. Ref.7 Ref.9 Ref.10 Ref.17

ISGylated By similarity.

Sequence similarities

Belongs to the transcription factor STAT family.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processLactation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH2 domain
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

JAK-STAT cascade

Traceable author statement Ref.1. Source: ProtInc

JAK-STAT cascade involved in growth hormone signaling pathway

Traceable author statement. Source: Reactome

Peyer's patch development

Inferred from electronic annotation. Source: Ensembl

T cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

T cell homeostasis

Inferred from electronic annotation. Source: Ensembl

allantoin metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

citrate metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

creatine metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

creatinine metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

development of secondary female sexual characteristics

Inferred from electronic annotation. Source: Ensembl

development of secondary male sexual characteristics

Inferred from electronic annotation. Source: Ensembl

epithelial cell differentiation involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

female pregnancy

Inferred from electronic annotation. Source: Ensembl

isoleucine metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

lactation

Inferred from electronic annotation. Source: UniProtKB-KW

lipid storage

Inferred from electronic annotation. Source: Ensembl

luteinization

Inferred from electronic annotation. Source: Ensembl

mammary gland epithelium development

Inferred from electronic annotation. Source: Ensembl

natural killer cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of mast cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

oxaloacetate metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of B cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gamma-delta T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-2 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mast cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mast cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of natural killer cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of natural killer cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

prolactin signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

prostate gland epithelium morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of multicellular organism growth

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of steroid metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 8631883. Source: ProtInc

succinate metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

taurine metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

valine metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA polymerase II core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 16819511. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1PubMed 8631883. Source: ProtInc

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P42229-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P42229-2)

The sequence of this isoform differs from the canonical sequence as follows:
     96-125: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 794794Signal transducer and activator of transcription 5A
PRO_0000182423

Regions

Domain589 – 68698SH2

Amino acid modifications

Modified residue1281Phosphoserine By similarity
Modified residue1931Phosphoserine Ref.15
Modified residue6941Phosphotyrosine; by JAK2 Ref.9 Ref.17

Natural variations

Alternative sequence96 – 12530Missing in isoform 2.
VSP_053332
Natural variant3891R → H.
Corresponds to variant rs2230134 [ dbSNP | Ensembl ].
VAR_052073

Experimental info

Sequence conflict881G → R in AAB06589. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C64237295F88CFBE

FASTA79490,647
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 20FC15C3CDFA26FE
Show »

FASTA76486,949

References

« Hide 'large scale' references
[1]"Identification and purification of human Stat proteins activated in response to interleukin-2."
Hou J., Schindler U., Henzel W.J., Wong S.C., McKnight S.L.
Immunity 2:321-329(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Lin J.X., Mietz J., Modi W.S., John S., Leonard W.J.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Cloning and characterization of a variant of human stat5a, missing a portion of the n-terminal region, with dominant negative effects on the growth of breast cancer cells and [beta]-casein gene expression."
Tan D., Deng C., Luben R.A., Walker A.M.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Synovium.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cervix.
[7]"A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus."
Aoki N., Matsuda T.
Mol. Endocrinol. 16:58-69(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROLACTIN SIGNALING PATHWAY, PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
[8]"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."
Litterst C.M., Kliem S., Marilley D., Pfitzner E.
J. Biol. Chem. 278:45340-45351(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA1.
[9]"STAT5a activation mediates the epithelial to mesenchymal transition induced by oncogenic RhoA."
Benitah S.A., Valeron P.F., Rui H., Lacal J.C.
Mol. Biol. Cell 14:40-53(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-694 BY JAK2.
[10]"FLT3 mutations in the activation loop of tyrosine kinase domain are frequently found in infant ALL with MLL rearrangements and pediatric ALL with hyperdiploidy."
Taketani T., Taki T., Sugita K., Furuichi Y., Ishii E., Hanada R., Tsuchida M., Sugita K., Ida K., Hayashi Y.
Blood 103:1085-1088(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
[11]"Signal transduction via the stem cell factor receptor/c-Kit."
Ronnstrand L.
Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[12]"The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone."
Williams C.C., Allison J.G., Vidal G.A., Burow M.E., Beckman B.S., Marrero L., Jones F.E.
J. Cell Biol. 167:469-478(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4, SUBCELLULAR LOCATION, FUNCTION.
[13]"Suppressor of cytokine signaling 7 inhibits prolactin, growth hormone, and leptin signaling by interacting with STAT5 or STAT3 and attenuating their nuclear translocation."
Martens N., Uzan G., Wery M., Hooghe R., Hooghe-Peters E.L., Gertler A.
J. Biol. Chem. 280:13817-13823(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SOCS7.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Mechanisms of STAT protein activation by oncogenic KIT mutants in neoplastic mast cells."
Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.
J. Biol. Chem. 286:5956-5966(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-694 IN RESPONSE TO KIT SIGNALING.
+Additional computationally mapped references.

Web resources

Wikipedia

STAT5 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L41142 mRNA. Translation: AAA73962.1.
U43185 mRNA. Translation: AAB06589.1.
DQ471288 mRNA. Translation: ABF17939.1.
AK301457 mRNA. Translation: BAH13486.1.
AC087691 Genomic DNA. No translation available.
AC099811 Genomic DNA. No translation available.
BC027036 mRNA. Translation: AAH27036.1.
CCDSCCDS11424.1. [P42229-1]
PIRG02317.
RefSeqNP_001275647.1. NM_001288718.1. [P42229-1]
NP_001275648.1. NM_001288719.1. [P42229-2]
NP_001275649.1. NM_001288720.1.
NP_003143.2. NM_003152.3. [P42229-1]
UniGeneHs.437058.

3D structure databases

ProteinModelPortalP42229.
SMRP42229. Positions 138-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112653. 55 interactions.
DIPDIP-396N.
IntActP42229. 27 interactions.
MINTMINT-223002.
STRING9606.ENSP00000341208.

Chemistry

BindingDBP42229.
ChEMBLCHEMBL5403.

PTM databases

PhosphoSiteP42229.

Polymorphism databases

DMDM1174462.

Proteomic databases

MaxQBP42229.
PaxDbP42229.
PeptideAtlasP42229.
PRIDEP42229.

Protocols and materials databases

DNASU6776.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345506; ENSP00000341208; ENSG00000126561. [P42229-1]
ENST00000546010; ENSP00000443107; ENSG00000126561. [P42229-2]
ENST00000590949; ENSP00000468749; ENSG00000126561. [P42229-1]
GeneID6776.
KEGGhsa:6776.
UCSCuc002hzj.2. human. [P42229-1]

Organism-specific databases

CTD6776.
GeneCardsGC17P040439.
HGNCHGNC:11366. STAT5A.
HPACAB003860.
HPA027873.
MIM601511. gene.
neXtProtNX_P42229.
PharmGKBPA338.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245085.
HOGENOMHOG000230988.
HOVERGENHBG107486.
InParanoidP42229.
KOK11223.
OMAPQNPDHV.
OrthoDBEOG73JKTT.
PhylomeDBP42229.
TreeFamTF318648.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP42229.

Gene expression databases

ArrayExpressP42229.
BgeeP42229.
CleanExHS_STAT5A.
GenevestigatorP42229.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.532.10. 1 hit.
1.20.1050.20. 1 hit.
2.60.40.630. 1 hit.
3.30.505.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR001217. STAT.
IPR013800. STAT_TF_alpha.
IPR015988. STAT_TF_coiled-coil.
IPR013801. STAT_TF_DNA-bd.
IPR012345. STAT_TF_DNA-bd_sub.
IPR013799. STAT_TF_prot_interaction.
[Graphical view]
PANTHERPTHR11801. PTHR11801. 1 hit.
PfamPF00017. SH2. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view]
SMARTSM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]
SUPFAMSSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTAT5A. human.
GeneWikiSTAT5A.
GenomeRNAi6776.
NextBio26450.
PROP42229.
SOURCESearch...

Entry information

Entry nameSTA5A_HUMAN
AccessionPrimary (citable) accession number: P42229
Secondary accession number(s): Q1KLZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM