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P52632 (STA5B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length786 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Subunit structure

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

Subcellular location

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

Post-translational modification

Tyrosine phosphorylated. Tyrosine phosphorylated in response to signaling via activated FLT3 and KIT, resulting in translocation to the nucleus. 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 By similarity.

Sequence similarities

Belongs to the transcription factor STAT family.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainSH2 domain
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from electronic annotation. Source: Ensembl

JAK-STAT cascade

Inferred from direct assay PubMed 11064147. Source: RGD

JAK-STAT cascade involved in growth hormone signaling pathway

Inferred from electronic annotation. Source: Ensembl

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 direct assay PubMed 17565389. Source: RGD

allantoin metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to epidermal growth factor stimulus

Inferred from direct assay PubMed 20639532. Source: UniProtKB

cellular response to growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

citrate metabolic process

Inferred from electronic annotation. Source: Ensembl

creatine metabolic process

Inferred from electronic annotation. Source: Ensembl

creatinine metabolic process

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

isoleucine metabolic process

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

lipid storage

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from direct assay PubMed 17565389. Source: RGD

luteinization

Inferred from direct assay PubMed 10598581. Source: RGD

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 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 cellular component movement

Inferred from mutant phenotype PubMed 16527988. Source: RGD

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 mutant phenotype PubMed 16527988. Source: RGD

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 steroid metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11562369. Source: RGD

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from expression pattern PubMed 12933671. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 16730240. Source: RGD

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 direct assay PubMed 17327369. Source: RGD

response to peptide hormone

Inferred from direct assay PubMed 9092792. Source: RGD

succinate metabolic process

Inferred from electronic annotation. Source: Ensembl

taurine metabolic process

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11064147. Source: RGD

valine metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 12933671. Source: RGD

nucleus

Inferred from direct assay PubMed 17327369. Source: RGD

   Molecular_functionDNA binding

Inferred from direct assay PubMed 11562369. Source: RGD

RNA 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 direct assay PubMed 20639532. Source: UniProtKB

double-stranded DNA binding

Inferred from direct assay PubMed 11064147. Source: RGD

protein dimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 11064147. Source: RGD

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11064147PubMed 11562369. Source: RGD

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 786786Signal transducer and activator of transcription 5B
PRO_0000182432

Regions

Domain589 – 68698SH2

Amino acid modifications

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

Experimental info

Sequence conflict2961L → A in CAA66141. Ref.2
Sequence conflict3281S → V in CAA66141. Ref.2
Sequence conflict4891R → A in CAA66141. Ref.2
Sequence conflict6901R → P in CAA66141. Ref.2
Sequence conflict7161T → A in CAA66141. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P52632 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 52250DE6ACC8DBE3

FASTA78690,223
        10         20         30         40         50         60 
MAMWIQAQQL QGDALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSIDLDN PQENIKATQL 

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

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

       190        200        210        220        230        240 
RIQAQFAQLA QLNPQERMSR ETALQQKQVS LETWLQREAQ TLQQYRVELA EKHQKTLQLL 

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

       310        320        330        340        350        360 
QQLPIPGPVE EMLAEVNATI TDIISALSTS 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 
TVLWDNAFRE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNS 

       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 KYYTPVPCER ATAKAADGYV KPQIKQVVPE FVNASTDAGS 

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


IPHAQS 

« Hide

References

[1]"Transcription factors Stat3 and Stat5b are present in rat liver nuclei late in an acute phase response and bind interleukin-6 response elements."
Ripperger J.A., Fritz S., Richter K., Hocke G.M., Lottspeich F., Fey G.H.
J. Biol. Chem. 270:29998-30006(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Luo G., Yu-Lee L.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Noble.
Tissue: Lymph node.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91988 mRNA. Translation: CAA63043.1. Different termination.
X91988 mRNA. Translation: CAA63042.1.
X97541 mRNA. Translation: CAA66141.1.
RefSeqNP_071775.1. NM_022380.1.
UniGeneRn.54486.

3D structure databases

ProteinModelPortalP52632.
SMRP52632. Positions 138-686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000026354.

PTM databases

PhosphoSiteP52632.

Proteomic databases

PaxDbP52632.
PRIDEP52632.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026354; ENSRNOP00000026354; ENSRNOG00000019075.
GeneID25126.
KEGGrno:25126.
UCSCRGD:3774. rat.

Organism-specific databases

CTD6777.
RGD3774. Stat5b.

Phylogenomic databases

eggNOGNOG245085.
GeneTreeENSGT00740000115175.
HOGENOMHOG000230988.
HOVERGENHBG107486.
InParanoidP52632.
KOK11224.
OrthoDBEOG73JKTT.
PhylomeDBP52632.
TreeFamTF318648.

Gene expression databases

GenevestigatorP52632.

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

NextBio605525.
PROP52632.

Entry information

Entry nameSTA5B_RAT
AccessionPrimary (citable) accession number: P52632
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 114 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