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P51692 (STA5B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal transducer and activator of transcription 5B
Gene names
Name:STAT5B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length787 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. Binds to the GAS element and activates PRL-induced transcription. Ref.9

Subunit structure

Forms a homodimer or a heterodimer with a related family member. Binds NR3C1 By similarity. Interacts with NCOA1, NMI and SOCS7. Interacts (via SH2 domain) with INSR. Ref.6 Ref.7 Ref.10 Ref.14

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Translocated into the nucleus in response to phosphorylation By similarity.

Post-translational modification

Tyrosine phosphorylated in response to signaling via activated KIT, resulting in translocation to the nucleus. 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. Phosphoryation at Tyr-699 by PTK6 or HCK leads to an increase of its transcriptional activity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates prolactin signaling pathway. Ref.6 Ref.8 Ref.9 Ref.11 Ref.13 Ref.17 Ref.23

Involvement in disease

Growth hormone insensitivity with immunodeficiency (GHII) [MIM:245590]: A disease characterized by short stature, growth hormone deficiency in the presence of normal to elevated circulating concentrations of growth hormone, resistance to hexogeneous growth hormone therapy, and recurrent infections.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.24 Ref.25

Sequence similarities

Belongs to the transcription factor STAT family.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Dwarfism
   DomainSH2 domain
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   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.3. Source: ProtInc

JAK-STAT cascade involved in growth hormone signaling pathway

Inferred from direct assay PubMed 12552091. Source: BHF-UCL

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

acute-phase response

Inferred from electronic annotation. Source: Ensembl

allantoin metabolic process

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

cellular response to epidermal growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hormone stimulus

Inferred from direct assay PubMed 12552091. 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

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: Ensembl

lipid storage

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

luteinization

Inferred from electronic annotation. Source: Ensembl

natural killer cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

oxaloacetate metabolic process

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

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 cellular component movement

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 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 natural killer cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

progesterone metabolic process

Inferred from electronic annotation. Source: Ensembl

prolactin signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

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 Ref.3. Source: ProtInc

response to estradiol

Inferred from direct assay PubMed 12552091. Source: BHF-UCL

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to interleukin-15

Inferred from electronic annotation. Source: Ensembl

response to interleukin-2

Inferred from electronic annotation. Source: Ensembl

response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

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 from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

valine metabolic process

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

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   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

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

glucocorticoid receptor binding

Inferred from physical interaction PubMed 12552091. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 21106534. Source: UniProtKB

protein dimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.3. Source: ProtInc

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 787787Signal transducer and activator of transcription 5B
PRO_0000182429

Regions

Domain589 – 68698SH2
Region232 – 32190Required for interaction with NMI

Amino acid modifications

Modified residue1281Phosphoserine Ref.20
Modified residue1931Phosphoserine Ref.16 Ref.18 Ref.21
Modified residue6991Phosphotyrosine; by HCK, JAK and PTK6 Ref.8 Ref.17

Natural variations

Natural variant1301A → V.
Corresponds to variant rs2277619 [ dbSNP | Ensembl ].
VAR_052074
Natural variant6301A → P in GHII; affects activation by growth hormone or interferon-gamma. Ref.24
VAR_018728
Natural variant6461F → S in GHII; transcriptionally inactive. Ref.25
VAR_067368

Experimental info

Mutagenesis6841T → A: Abolishes interaction with INSR. Ref.6
Mutagenesis6991Y → F: Abolishes phosphorylation by HCK. Ref.8
Sequence conflict2301A → P in AAC50491. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P51692 [UniParc].

Last modified January 16, 2004. Version 2.
Checksum: AA2F1CAB20955ACA

FASTA78789,866
        10         20         30         40         50         60 
MAVWIQAQQL QGEALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSVDLDN PQENIKATQL 

        70         80         90        100        110        120 
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV 

       130        140        150        160        170        180 
REANNGSSPA GSLADAMSQK HLQINQTFEE LRLVTQDTEN ELKKLQQTQE YFIIQYQESL 

       190        200        210        220        230        240 
RIQAQFGPLA 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 DYSGEILNNC CVMEYHQATG TLSAHFRNMS 

       430        440        450        460        470        480 
LKRIKRSDRR GAESVTEEKF TILFESQFSV GGNELVFQVK TLSLPVVVIV HGSQDNNATA 

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

       550        560        570        580        590        600 
SSSHLEDYSG LSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK 

       610        620        630        640        650        660 
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSQERMF WNLMPFTTRD FSIRSLADRL 

       670        680        690        700        710        720 
GDLNYLIYVF PDRPKDEVYS KYYTPVPCES ATAKAVDGYV KPQIKQVVPE FVNASADAGG 

       730        740        750        760        770        780 
GSATYMDQAP SPAVCPQAHY NMYPQNPDSV LDTDGDFDLE DTMDVARRVE ELLGRPMDSQ 


WIPHAQS 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and cloning of STAT5 from IM-9 cells and its activation by growth hormone."
Silva C.M., Lu H., Day R.N.
Mol. Endocrinol. 10:508-518(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Silva C.M., Lu H.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 628; 717 AND 720.
[3]"Cloning of human Stat5B. Reconstitution of interleukin-2-induced Stat5A and Stat5B DNA binding activity in COS-7 cells."
Lin J.-X., Mietz J., Modi W.S., John S., Leonard W.J.
J. Biol. Chem. 271:10738-10744(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The structure of human STAT5A and B genes reveals two regions of nearly identical sequence and an alternative tissue specific STAT5B promoter."
Ambrosio R., Fimiani G., Monfregola J., Sanzari E., De Felice N., Salerno M.C., Pignata C., D'Urso M., Ursini M.V.
Gene 285:311-318(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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].
Tissue: Lymph.
[6]"Identification of Stat 5B as a substrate of the insulin receptor."
Sawka-Verhelle D., Filloux C., Tartare-Deckert S., Mothe I., Van Obberghen E.
Eur. J. Biochem. 250:411-417(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY INSR, INTERACTION WITH INSR, MUTAGENESIS OF THR-684.
[7]"Functional association of Nmi with Stat5 and Stat1 in IL-2- and IFNgamma-mediated signaling."
Zhu M.-H., John S., Berg M., Leonard W.J.
Cell 96:121-130(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NMI.
[8]"The Src family kinase Hck couples BCR/ABL to STAT5 activation in myeloid leukemia cells."
Klejman A., Schreiner S.J., Nieborowska-Skorska M., Slupianek A., Wilson M., Smithgall T.E., Skorski T.
EMBO J. 21:5766-5774(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-699, MUTAGENESIS OF TYR-699.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-B beta."
Kurzer J.H., Argetsinger L.S., Zhou Y.J., Kouadio J.L., O'Shea J.J., Carter-Su C.
Mol. Cell. Biol. 24:4557-4570(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY JAK2.
[14]"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.
[15]"Severe growth hormone insensitivity resulting from total absence of signal transducer and activator of transcription 5b."
Hwa V., Little B., Adiyaman P., Kofoed E.M., Pratt K.L., Ocal G., Berberoglu M., Rosenfeld R.G.
J. Clin. Endocrinol. Metab. 90:4260-4266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GHII.
[16]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Signal transducer and activator of transcription 5b: a new target of breast tumor kinase/protein tyrosine kinase 6."
Weaver A.M., Silva C.M.
Breast Cancer Res. 9:R79-R79(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-699 BY PTK6.
[18]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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.
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"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.
[22]"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].
[23]"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 IN RESPONSE TO KIT SIGNALING.
[24]"Growth hormone insensitivity associated with a STAT5b mutation."
Kofoed E.M., Hwa V., Little B., Woods K.A., Buckway C.K., Tsubaki J., Pratt K.L., Bezrodnik L., Jasper H., Tepper A., Heinrich J.J., Rosenfeld R.G.
N. Engl. J. Med. 349:1139-1147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GHII PRO-630.
[25]"A Novel Missense Mutation in the SH2 Domain of the STAT5B Gene Results in a transcriptionally inactive STAT5b associated with severe IGF-I deficiency, immune dysfunction, and lack of pulmonary disease."
Scaglia P.A., Martinez A.S., Feigerlova E., Bezrodnik L., Gaillard M.I., Di Giovanni D., Ballerini M.G., Jasper H.G., Heinrich J.J., Fang P., Domene H.M., Rosenfeld R.G., Hwa V.
J. Clin. Endocrinol. Metab. 97:E830-839(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GHII SER-646, CHARACTERIZATION OF VARIANT GHII SER-646.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U48730 mRNA. Translation: AAC50485.2.
U47686 mRNA. Translation: AAC50491.1.
AJ412888 expand/collapse EMBL AC list , AJ412889, AJ412890, AJ412891, AJ412892, AJ412893, AJ412894, AJ412895, AJ412896, AJ412897, AJ412898, AJ412899 Genomic DNA. Translation: CAD19638.1.
BC065227 mRNA. Translation: AAH65227.1.
CCDSCCDS11423.1.
RefSeqNP_036580.2. NM_012448.3.
UniGeneHs.595276.

3D structure databases

ProteinModelPortalP51692.
SMRP51692. Positions 4-686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112654. 40 interactions.
IntActP51692. 13 interactions.
MINTMINT-132900.
STRING9606.ENSP00000293328.

Chemistry

BindingDBP51692.
ChEMBLCHEMBL5817.
DrugBankDB01254. Dasatinib.

PTM databases

PhosphoSiteP51692.

Polymorphism databases

DMDM41019536.

Proteomic databases

MaxQBP51692.
PaxDbP51692.
PeptideAtlasP51692.
PRIDEP51692.

Protocols and materials databases

DNASU6777.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000293328; ENSP00000293328; ENSG00000173757.
GeneID6777.
KEGGhsa:6777.
UCSCuc002hzh.3. human.

Organism-specific databases

CTD6777.
GeneCardsGC17M040351.
HGNCHGNC:11367. STAT5B.
HPACAB004298.
MIM245590. phenotype.
604260. gene.
neXtProtNX_P51692.
Orphanet520. Acute promyelocytic leukemia.
220465. Laron syndrome with immunodeficiency.
PharmGKBPA36186.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245085.
HOVERGENHBG107486.
InParanoidP51692.
KOK11224.
OMAVREATNS.
OrthoDBEOG73JKTT.
PhylomeDBP51692.
TreeFamTF318648.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP51692.

Gene expression databases

ArrayExpressP51692.
BgeeP51692.
CleanExHS_STAT5B.
GenevestigatorP51692.

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

ChiTaRSSTAT5B. human.
GeneWikiSTAT5B.
GenomeRNAi6777.
NextBio26454.
PMAP-CutDBP51692.
PROP51692.
SOURCESearch...

Entry information

Entry nameSTA5B_HUMAN
AccessionPrimary (citable) accession number: P51692
Secondary accession number(s): Q8WWS8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 16, 2004
Last modified: July 9, 2014
This is version 149 of the entry and version 2 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