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P42232 (STA5B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal transducer and activator of transcription 5B
Gene names
Name:Stat5b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length786 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.12

Subunit structure

Forms a homodimer or a heterodimer with a related family member. Interacts with SOCS7 By similarity. Binds NR3C1 and NCOA1. Interacts (via SH2 domain) with INSR. Ref.9 Ref.10

Subcellular location

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

Tissue specificity

In the virgin, found in most tissues. Particularly abundant in muscle tissue of virgin and lactating females, and of males.

Developmental stage

Detected both in virgin mouse and after mammary gland involution. The level of STAT5A increases constantly during pregnancy, but decreases during lactation.

Post-translational modification

Tyrosine phosphorylated. 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 By similarity. Phosphoryation at Tyr-699 by PTK6 or HCK leads to an increase of its transcriptional activity By similarity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates prolactin signaling pathway. Ref.11 Ref.12 Ref.13 Ref.14

Polymorphism

The polymorphism at position 327 in strain NOD reduces DNA-binding affinity.

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
   DomainSH2 domain
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

JAK-STAT cascade

Inferred from direct assay PubMed 10485657. Source: MGI

JAK-STAT cascade involved in growth hormone signaling pathway

Inferred from direct assay PubMed 8923468. Source: BHF-UCL

Peyer's patch development

Inferred from genetic interaction PubMed 15294943. Source: MGI

T cell differentiation in thymus

Inferred from genetic interaction PubMed 15294943. Source: MGI

T cell homeostasis

Inferred from genetic interaction PubMed 10072077. Source: MGI

acute-phase response

Inferred from electronic annotation. Source: Ensembl

allantoin metabolic process

Inferred from mutant phenotype PubMed 18648510. 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 direct assay PubMed 20639532. Source: UniProtKB

citrate metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

creatine metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

creatinine metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

cytokine-mediated signaling pathway

Inferred from direct assay PubMed 10485657. Source: MGI

development of secondary female sexual characteristics

Inferred from mutant phenotype PubMed 9630227. Source: MGI

development of secondary male sexual characteristics

Inferred from mutant phenotype PubMed 9630227. Source: MGI

fatty acid metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

female pregnancy

Inferred from mutant phenotype PubMed 15471942. Source: MGI

isoleucine metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

lactation

Inferred from mutant phenotype PubMed 11706048PubMed 9630227. Source: MGI

lipid storage

Inferred from genetic interaction PubMed 9630227. Source: MGI

liver development

Inferred from electronic annotation. Source: Ensembl

luteinization

Inferred from genetic interaction PubMed 9630227. Source: MGI

natural killer cell differentiation

Inferred from genetic interaction PubMed 10072077. Source: MGI

negative regulation of apoptotic process

Inferred from genetic interaction PubMed 10652277. Source: MGI

negative regulation of erythrocyte differentiation

Inferred from genetic interaction PubMed 10072077. Source: MGI

oxaloacetate metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

positive regulation of B cell differentiation

Inferred from genetic interaction PubMed 10979977. Source: MGI

positive regulation of activated T cell proliferation

Inferred from mutant phenotype PubMed 9841920. Source: MGI

positive regulation of cell proliferation

Inferred from genetic interaction PubMed 10652277. Source: MGI

positive regulation of cellular component movement

Inferred from electronic annotation. Source: Ensembl

positive regulation of gamma-delta T cell differentiation

Inferred from genetic interaction PubMed 15294943. Source: MGI

positive regulation of inflammatory response

Inferred from genetic interaction PubMed 10652277. Source: MGI

positive regulation of interleukin-2 biosynthetic process

Inferred from genetic interaction PubMed 10072077. Source: MGI

positive regulation of lymphocyte differentiation

Inferred from genetic interaction PubMed 15294943. Source: MGI

positive regulation of mitotic cell cycle

Inferred from genetic interaction PubMed 10072077. Source: MGI

positive regulation of multicellular organism growth

Inferred from mutant phenotype PubMed 9630227. Source: MGI

positive regulation of natural killer cell differentiation

Inferred from mutant phenotype PubMed 9841920. Source: MGI

positive regulation of natural killer cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 9841920. Source: MGI

positive regulation of natural killer cell proliferation

Inferred from mutant phenotype PubMed 9841920. Source: MGI

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20639532PubMed 21106534. Source: UniProtKB

progesterone metabolic process

Inferred from genetic interaction PubMed 15471942. Source: MGI

prolactin signaling pathway

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of cell adhesion

Inferred from mutant phenotype PubMed 11706048. Source: MGI

regulation of epithelial cell differentiation

Inferred from mutant phenotype PubMed 11706048. Source: MGI

regulation of multicellular organism growth

Inferred from direct assay PubMed 18648510. Source: BHF-UCL

regulation of steroid metabolic process

Inferred from genetic interaction PubMed 15471942. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 15294943. Source: MGI

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to interleukin-15

Inferred from mutant phenotype PubMed 9841920. Source: MGI

response to interleukin-2

Inferred from mutant phenotype PubMed 9841920. Source: MGI

response to interleukin-4

Inferred from mutant phenotype PubMed 9841920. Source: MGI

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

sex differentiation

Inferred from mutant phenotype PubMed 17412818. Source: MGI

succinate metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

taurine metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

valine metabolic process

Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 20639532. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 20639532. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 10485657PubMed 12147240PubMed 22801370. Source: MGI

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 19666510. Source: MGI

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

protein dimerization activity

Inferred from direct assay PubMed 20639532. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction Ref.12. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

signal transducer activity

Inferred from genetic interaction PubMed 10485657. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DNAJA3Q96EY13EBI-617454,EBI-356767From a different organism.
DNAJA3Q96EY1-12EBI-617454,EBI-4322330From a different organism.
DNAJA3Q96EY1-22EBI-617454,EBI-3952284From a different organism.
GHRP199416EBI-617454,EBI-7526279From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 786786Signal transducer and activator of transcription 5B
PRO_0000182430

Regions

Domain589 – 68698SH2

Amino acid modifications

Modified residue1281Phosphoserine By similarity
Modified residue6991Phosphotyrosine; by HCK, JAK and PTK6 By similarity

Natural variations

Natural variant3271L → M in strain: NOD. Ref.4

Experimental info

Mutagenesis6841T → A: Fails to interact with INSR. Ref.9
Sequence conflict2101S → P in CAB51862. Ref.8
Sequence conflict4331E → G in AAC52282. Ref.2
Sequence conflict4331E → G in AAL05590. Ref.4
Sequence conflict4331E → G in AAK97791. Ref.4
Sequence conflict4331E → G in AAK97792. Ref.4
Sequence conflict4331E → G in AAK97793. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P42232 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A8FE76405E41B2EF

FASTA78690,002
        10         20         30         40         50         60 
MAMWIQAQQL QGDALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSIDLDN PQENIKATQL 

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

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

       190        200        210        220        230        240 
RIQAQFAQLG QLNPQERMSR ETALQQKQVS LETWLQREAQ 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 TILFDSQFSV GGNELVFQVK TLSLPVVVIV HGSQDNNATA 

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

       550        560        570        580        590        600 
SSNHLEDYNS MSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK 

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

       670        680        690        700        710        720 
GDLNYLIYVF PDRPKDEVYS KYYTPVPCEP ATAKAADGYV KPQIKQVVPE FANASTDAGS 

       730        740        750        760        770        780 
GATYMDQAPS PVVCPQAHYN MYPPNPDSVL DTDGDFDLED TMDVARRVEE LLGRPMDSQW 


IPHAQS 

« Hide

References

« Hide 'large scale' references
[1]"Interleukin-3, granulocyte-macrophage colony stimulating factor and interleukin-5 transduce signals through two STAT5 homologs."
Mui A.L.-F., Wakao H., O'Farrell A.-M., Harada N., Miyajima A.
EMBO J. 14:1166-1175(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X A/J.
Tissue: Liver.
[2]"Cloning and expression of Stat5 and an additional homologue (Stat5b) involved in prolactin signal transduction in mouse mammary tissue."
Liu X., Robinson G.W., Gouilleux F., Groner B., Hennighausen L.
Proc. Natl. Acad. Sci. U.S.A. 92:8831-8835(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[3]"Structure of the mouse Stat 3/5 locus: evolution from Drosophila to zebrafish to mouse."
Miyoshi K., Cui Y., Riedlinger G., Robinson P., Lehoczky J., Zon L., Oka T., Dewar K., Hennighausen L.
Genomics 71:150-155(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129.
[4]"A mutant Stat5b with weaker DNA binding affinity defines a key defective pathway in non-obese diabetic (NOD) mice."
Davoodi-Semiromi A., Laloraya M., Kumar G.P., Purohit S., Jha R.K., She J.-X.
J. Biol. Chem. 279:11553-11561(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-327.
Strain: BALB/c, C3H, C57BL/6, CBA and NOD.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Dendritic cell and Thymus.
[6]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[7]"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].
Strain: FVB/N.
Tissue: Kidney.
[8]"Molecular characterization of STAT5A- and STAT5B-encoding genes reveals extended intragenic sequence homogeneity in cattle and mouse and different degrees of divergent evolution of various domains."
Seyfert H.-M., Pitra C., Meyer L., Brunner R.M., Wheeler T.T., Molenaar A., McCracken J.Y., Herrmann J., Thiesen H.-J., Schwerin M.
J. Mol. Evol. 50:550-561(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-389.
[9]"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: INTERACTION WITH INRS, MUTAGENESIS OF THR-684.
[10]"Characterization of Stat5a and Stat5b homodimers and heterodimers and their association with the glucocortiocoid receptor in mammary cells."
Cella N., Groner B., Hynes N.E.
Mol. Cell. Biol. 18:1783-1792(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR3C1.
[11]"Flt3 mutations from patients with acute myeloid leukemia induce transformation of 32D cells mediated by the Ras and STAT5 pathways."
Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C., Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T., Kienast J., Kanakura Y., Berdel W.E., Serve H.
Blood 96:3907-3914(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
[12]"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.
[13]"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.
[14]"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling."
Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K., Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D., Muller J.P.
J. Biol. Chem. 286:10918-10929(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48539 mRNA. Translation: CAA88420.1.
U21110 mRNA. Translation: AAC52282.1.
AF234171 Genomic DNA. Translation: AAF62911.2.
AY040231 mRNA. Translation: AAK74074.1.
AY042906 mRNA. Translation: AAL05590.1.
AY044901 mRNA. Translation: AAK97791.1.
AY044902 mRNA. Translation: AAK97792.1.
AY044903 mRNA. Translation: AAK97793.1.
AK150098 mRNA. Translation: BAE29305.1.
AK154014 mRNA. Translation: BAE32317.1.
AK154664 mRNA. Translation: BAE32752.1.
AL591466 Genomic DNA. Translation: CAM19465.1.
BC024319 mRNA. Translation: AAH24319.1.
AJ237939 Genomic DNA. Translation: CAB51862.1.
PIRI49274.
RefSeqNP_001107035.1. NM_001113563.1.
NP_035619.3. NM_011489.3.
UniGeneMm.34064.

3D structure databases

ProteinModelPortalP42232.
SMRP42232. Positions 2-686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203526. 6 interactions.
DIPDIP-898N.
IntActP42232. 3 interactions.

PTM databases

PhosphoSiteP42232.

Proteomic databases

PaxDbP42232.
PRIDEP42232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004143; ENSMUSP00000004143; ENSMUSG00000020919.
ENSMUST00000107358; ENSMUSP00000102981; ENSMUSG00000020919.
GeneID20851.
KEGGmmu:20851.
UCSCuc007lmi.2. mouse.

Organism-specific databases

CTD6777.
MGIMGI:103035. Stat5b.

Phylogenomic databases

eggNOGNOG245085.
GeneTreeENSGT00740000115175.
HOVERGENHBG107486.
InParanoidQ9R0X8.
KOK11224.
OMAVREATNS.
OrthoDBEOG73JKTT.
PhylomeDBP42232.
TreeFamTF318648.

Enzyme and pathway databases

ReactomeREACT_169390. Signaling by Leptin.
REACT_188257. Signal Transduction.
REACT_98458. Immune System.

Gene expression databases

ArrayExpressP42232.
BgeeP42232.
GenevestigatorP42232.

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. mouse.
NextBio299639.
PROP42232.
SOURCESearch...

Entry information

Entry nameSTA5B_MOUSE
AccessionPrimary (citable) accession number: P42232
Secondary accession number(s): A2A5D5 expand/collapse secondary AC list , Q541Q5, Q60804, Q8K3Q1, Q9JKM1, Q9R0X8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot