P51692 (STA5B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal transducer and activator of transcription 5B

Gene names

Name:

STAT5B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	787 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.9 Ref.13
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. Ref.6 Ref.8 Ref.10 Ref.12 Ref.16 Ref.22
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.14 Ref.23 Ref.24
Sequence similarities	Belongs to the transcription factor STAT family. Contains 1 SH2 domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Dwarfism
Domain	SH2 domain
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL 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: Compara T cell differentiation in thymus Inferred from electronic annotation. Source: Compara T cell homeostasis Inferred from electronic annotation. Source: Compara acute-phase response Inferred from electronic annotation. Source: Compara 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 cytokine-mediated signaling pathway Inferred from electronic annotation. Source: Compara development of secondary female sexual characteristics Inferred from electronic annotation. Source: Compara development of secondary male sexual characteristics Inferred from electronic annotation. Source: Compara fatty acid metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL female pregnancy Inferred from electronic annotation. Source: Compara isoleucine metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL lactation Inferred from electronic annotation. Source: Compara lipid storage Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara luteinization Inferred from electronic annotation. Source: Compara natural killer cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of erythrocyte differentiation Inferred from electronic annotation. Source: Compara oxaloacetate metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of B cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of activated T cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of cellular component movement Inferred from electronic annotation. Source: Compara positive regulation of gamma-delta T cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of inflammatory response Inferred from electronic annotation. Source: Compara positive regulation of interleukin-2 biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara positive regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara positive regulation of natural killer cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of natural killer cell mediated cytotoxicity Inferred from electronic annotation. Source: Compara positive regulation of natural killer cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara 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: Compara regulation of cell adhesion Inferred from electronic annotation. Source: Compara regulation of epithelial cell differentiation Inferred from electronic annotation. Source: Compara regulation of multicellular organism growth Inferred from sequence or structural similarity. Source: BHF-UCL regulation of steroid metabolic process Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from direct assay PubMed 12552091. Source: BHF-UCL response to ethanol Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to interleukin-15 Inferred from electronic annotation. Source: Compara response to interleukin-2 Inferred from electronic annotation. Source: Compara response to interleukin-4 Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara 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: Compara valine metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	RNA polymerase II core promoter sequence-specific DNA binding Inferred from electronic annotation. Source: Compara calcium ion binding Inferred from electronic annotation. Source: InterPro double-stranded DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Traceable author statement Ref.3. Source: ProtInc signal transducer activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DNAJA3	Q96EY1	2	EBI-1186119,EBI-356767
NMI	Q13287	7	EBI-1186119,EBI-372942

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 787	787	Signal transducer and activator of transcription 5B		PRO_0000182429
Regions
	Domain	589 – 686	98	SH2
	Region	232 – 321	90	Required for interaction with NMI
Amino acid modifications
	Modified residue	128	1	Phosphoserine Ref.19
	Modified residue	193	1	Phosphoserine Ref.15 Ref.17 Ref.20
	Modified residue	699	1	Phosphotyrosine; by HCK, JAK and PTK6 Ref.8 Ref.16
Natural variations
	Natural variant	130	1	A → V. Corresponds to variant rs2277619 [ dbSNP | Ensembl ].		VAR_052074
	Natural variant	630	1	A → P in GHII; affects activation by growth hormone or interferon-gamma. Ref.23		VAR_018728
	Natural variant	646	1	F → S in GHII; transcriptionally inactive. Ref.24		VAR_067368
Experimental info
	Mutagenesis	684	1	T → A: Abolishes interaction with INSR. Ref.6
	Mutagenesis	699	1	Y → F: Abolishes phosphorylation by HCK. Ref.8
	Sequence conflict	230	1	A → P in AAC50491. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P51692 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: AA2F1CAB20955ACA	FASTA	787	89,866
	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

References

	« Hide 'large scale' referencesShow '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]	"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.
[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]	"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.
[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]	"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.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"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.
[23]	"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.
[24]	"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.

Web resources

STAT5Bbase

STAT5B mutation db

Wikipedia

STAT5 entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	U48730 mRNA. Translation: AAC50485.2. U47686 mRNA. Translation: AAC50491.1. AJ412888 , AJ412889, AJ412890, AJ412891, AJ412892, AJ412893, AJ412894, AJ412895, AJ412896, AJ412897, AJ412898, AJ412899 Genomic DNA. Translation: CAD19638.1. BC065227 mRNA. Translation: AAH65227.1.
IPI	IPI00103415.
RefSeq	NP_036580.2. NM_012448.3.
UniGene	Hs.731529.
3D structure databases
ProteinModelPortal	P51692.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51692. 10 interactions.
MINT	MINT-132900.
STRING	9606.ENSP00000293328.
PTM databases
PhosphoSite	P51692.
Polymorphism databases
DMDM	41019536.
Proteomic databases
PaxDb	P51692.
PeptideAtlas	P51692.
PRIDE	P51692.
Protocols and materials databases
DNASU	6777.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000293328; ENSP00000293328; ENSG00000173757.
GeneID	6777.
KEGG	hsa:6777.
UCSC	uc002hzh.3. human.
Organism-specific databases
CTD	6777.
GeneCards	GC17M040351.
HGNC	HGNC:11367. STAT5B.
HPA	CAB004298.
MIM	245590. phenotype. 604260. gene.
neXtProt	NX_P51692.
Orphanet	220465. Laron syndrome with immunodeficiency.
PharmGKB	PA36186.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG245085.
HOVERGEN	HBG107486.
InParanoid	P51692.
KO	K11224.
OMA	DLAEKHQ.
OrthoDB	EOG457560.
PhylomeDB	P51692.
Enzyme and pathway databases
Pathway_Interaction_DB	angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling. epopathway. EPO signaling pathway. fgf_pathway. FGF signaling pathway. il2_stat5pathway. IL2 signaling events mediated by STAT5. il2_1pathway. IL2-mediated signaling events. il4_2pathway. IL4-mediated signaling events. pdgfrbpathway. PDGFR-beta signaling pathway. ptp1bpathway. Signaling events mediated by PTP1B.
Reactome	REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P51692.
Bgee	P51692.
CleanEx	HS_STAT5B.
Genevestigator	P51692.
GermOnline	ENSG00000173757. Homo sapiens.
Family and domain databases
Gene3D	1.10.238.10. 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.
InterPro	IPR011992. EF-hand-like_dom. IPR008967. p53-like_TF_DNA-bd. IPR000980. SH2. IPR013800. STAT_TF_alpha. IPR015988. STAT_TF_coiled-coil. IPR001217. STAT_TF_core. IPR013801. STAT_TF_DNA-bd. IPR012345. STAT_TF_DNA-bd_sub. IPR013799. STAT_TF_prot_interaction. [Graphical view]
PANTHER	PTHR11801. PTHR11801. 1 hit.
Pfam	PF00017. SH2. 1 hit. PF01017. STAT_alpha. 1 hit. PF02864. STAT_bind. 1 hit. PF02865. STAT_int. 1 hit. [Graphical view]
SMART	SM00252. SH2. 1 hit. SM00964. STAT_int. 1 hit. [Graphical view]
SUPFAM	SSF49417. P53_like_DNA_bnd. 1 hit. SSF47655. STAT. 1 hit. SSF48092. STAT. 1 hit.
PROSITE	PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P51692.
ChEMBL	CHEMBL5817.
ChiTaRS	STAT5B. human.
DrugBank	DB01254. Dasatinib.
GenomeRNAi	6777.
NextBio	26454.
PMAP-CutDB	P51692.
SOURCE	Search...

Entry information

Entry name

STA5B_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.