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Protein

Signal transducer and activator of transcription 5B

Gene

Stat5b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. chromatin binding Source: UniProtKB
  3. DNA binding Source: RGD
  4. double-stranded DNA binding Source: RGD
  5. protein dimerization activity Source: UniProtKB
  6. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  7. sequence-specific DNA binding Source: RGD
  8. sequence-specific DNA binding transcription factor activity Source: RGD
  9. signal transducer activity Source: Ensembl

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: Ensembl
  2. acute-phase response Source: RGD
  3. allantoin metabolic process Source: Ensembl
  4. cellular response to epidermal growth factor stimulus Source: UniProtKB
  5. cellular response to growth factor stimulus Source: UniProtKB
  6. citrate metabolic process Source: Ensembl
  7. creatine metabolic process Source: Ensembl
  8. creatinine metabolic process Source: Ensembl
  9. development of secondary female sexual characteristics Source: Ensembl
  10. development of secondary male sexual characteristics Source: Ensembl
  11. fatty acid metabolic process Source: Ensembl
  12. female pregnancy Source: Ensembl
  13. isoleucine metabolic process Source: Ensembl
  14. JAK-STAT cascade Source: RGD
  15. JAK-STAT cascade involved in growth hormone signaling pathway Source: Ensembl
  16. lactation Source: Ensembl
  17. lipid storage Source: Ensembl
  18. liver development Source: RGD
  19. luteinization Source: RGD
  20. natural killer cell differentiation Source: Ensembl
  21. negative regulation of apoptotic process Source: Ensembl
  22. negative regulation of erythrocyte differentiation Source: Ensembl
  23. oxaloacetate metabolic process Source: Ensembl
  24. Peyer's patch development Source: Ensembl
  25. positive regulation of activated T cell proliferation Source: Ensembl
  26. positive regulation of B cell differentiation Source: Ensembl
  27. positive regulation of cellular component movement Source: RGD
  28. positive regulation of gamma-delta T cell differentiation Source: Ensembl
  29. positive regulation of inflammatory response Source: Ensembl
  30. positive regulation of interleukin-2 biosynthetic process Source: Ensembl
  31. positive regulation of mitotic cell cycle Source: Ensembl
  32. positive regulation of multicellular organism growth Source: Ensembl
  33. positive regulation of natural killer cell differentiation Source: Ensembl
  34. positive regulation of natural killer cell mediated cytotoxicity Source: Ensembl
  35. positive regulation of natural killer cell proliferation Source: Ensembl
  36. positive regulation of smooth muscle cell proliferation Source: RGD
  37. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  38. progesterone metabolic process Source: Ensembl
  39. prolactin signaling pathway Source: UniProtKB
  40. regulation of cell adhesion Source: Ensembl
  41. regulation of epithelial cell differentiation Source: Ensembl
  42. regulation of steroid metabolic process Source: Ensembl
  43. regulation of transcription, DNA-templated Source: RGD
  44. response to estradiol Source: Ensembl
  45. response to ethanol Source: RGD
  46. response to hypoxia Source: RGD
  47. response to interleukin-15 Source: Ensembl
  48. response to interleukin-2 Source: Ensembl
  49. response to interleukin-4 Source: Ensembl
  50. response to lipopolysaccharide Source: RGD
  51. response to peptide hormone Source: RGD
  52. succinate metabolic process Source: Ensembl
  53. taurine metabolic process Source: Ensembl
  54. T cell differentiation in thymus Source: Ensembl
  55. T cell homeostasis Source: Ensembl
  56. transcription from RNA polymerase II promoter Source: RGD
  57. valine metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_195025. Signaling by SCF-KIT.
REACT_195204. Signaling by Leptin.
REACT_196376. Interleukin-7 signaling.
REACT_196425. Growth hormone receptor signaling.
REACT_198628. Signaling by FGFR1 fusion mutants.
REACT_199232. Prolactin receptor signaling.
REACT_206819. Downstream signal transduction.
REACT_235800. Interleukin-2 signaling.
REACT_244635. Interleukin-3, 5 and GM-CSF signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription 5B
Gene namesi
Name:Stat5b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi3774. Stat5b.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RGD
  3. nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 786786Signal transducer and activator of transcription 5BPRO_0000182432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei699 – 6991Phosphotyrosine; by HCK, JAK and PTK6By similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP52632.
PRIDEiP52632.

PTM databases

PhosphoSiteiP52632.

Expressioni

Gene expression databases

GenevestigatoriP52632.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

DIPiDIP-60986N.
STRINGi10116.ENSRNOP00000026354.

Structurei

3D structure databases

ProteinModelPortaliP52632.
SMRiP52632. Positions 138-686.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini589 – 68698SH2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the transcription factor STAT family.Curated
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG245085.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000230988.
HOVERGENiHBG107486.
InParanoidiP52632.
KOiK11224.
OrthoDBiEOG73JKTT.
PhylomeDBiP52632.
TreeFamiTF318648.

Family and domain databases

Gene3Di1.10.238.10. 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.
InterProiIPR011992. 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]
PANTHERiPTHR11801. PTHR11801. 1 hit.
PfamiPF00017. SH2. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]
SUPFAMiSSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52632-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAMWIQAQQL QGDALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSIDLDN
60 70 80 90 100
PQENIKATQL LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR
110 120 130 140 150
CPMELVRCIR HILYNEQRLV REANNGSSPA GSLADAMSQK HLQINQTFEE
160 170 180 190 200
LRLITQDTES ELKKLQQTQE YFIIQYQESL RIQAQFAQLA QLNPQERMSR
210 220 230 240 250
ETALQQKQVS LETWLQREAQ TLQQYRVELA EKHQKTLQLL RKQQTIILDD
260 270 280 290 300
ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRLEHLC
310 320 330 340 350
QQLPIPGPVE EMLAEVNATI TDIISALSTS TFIIEKQPPQ VLKTQTKFAA
360 370 380 390 400
TVRLLVGGKL NVHMNPPQVK ATIISEQQAK SLLKNENTRN DYSGEILNNC
410 420 430 440 450
CVMEYHQATG TLSAHFRNMS LKRIKRSDRR GAESVTEEKF TILFDSQFSV
460 470 480 490 500
GGNELVFQVK TLSLPVVVIV HGSQDNNATA TVLWDNAFRE PGRVPFAVPD
510 520 530 540 550
KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNS SSNHLEDYNS
560 570 580 590 600
MSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK
610 620 630 640 650
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSQERMF WNLMPFTTRD
660 670 680 690 700
FSIRSLADRL GDLNYLIYVF PDRPKDEVYS KYYTPVPCER ATAKAADGYV
710 720 730 740 750
KPQIKQVVPE FVNASTDAGS GATYMDQAPS PVVCPQAHYN MYPQNPDSVL
760 770 780
DTDGDFDLED TMDVARRVEE LLGRPMDSQW IPHAQS
Length:786
Mass (Da):90,223
Last modified:October 1, 1996 - v1
Checksum:i52250DE6ACC8DBE3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti296 – 2961L → A in CAA66141. 1 PublicationCurated
Sequence conflicti328 – 3281S → V in CAA66141. 1 PublicationCurated
Sequence conflicti489 – 4891R → A in CAA66141. 1 PublicationCurated
Sequence conflicti690 – 6901R → P in CAA66141. 1 PublicationCurated
Sequence conflicti716 – 7161T → A in CAA66141. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91988 mRNA. Translation: CAA63043.1. Different termination.
X91988 mRNA. Translation: CAA63042.1.
X97541 mRNA. Translation: CAA66141.1.
RefSeqiNP_071775.1. NM_022380.1.
UniGeneiRn.54486.

Genome annotation databases

EnsembliENSRNOT00000026354; ENSRNOP00000026354; ENSRNOG00000019075.
GeneIDi25126.
KEGGirno:25126.
UCSCiRGD:3774. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91988 mRNA. Translation: CAA63043.1. Different termination.
X91988 mRNA. Translation: CAA63042.1.
X97541 mRNA. Translation: CAA66141.1.
RefSeqiNP_071775.1. NM_022380.1.
UniGeneiRn.54486.

3D structure databases

ProteinModelPortaliP52632.
SMRiP52632. Positions 138-686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60986N.
STRINGi10116.ENSRNOP00000026354.

PTM databases

PhosphoSiteiP52632.

Proteomic databases

PaxDbiP52632.
PRIDEiP52632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026354; ENSRNOP00000026354; ENSRNOG00000019075.
GeneIDi25126.
KEGGirno:25126.
UCSCiRGD:3774. rat.

Organism-specific databases

CTDi6777.
RGDi3774. Stat5b.

Phylogenomic databases

eggNOGiNOG245085.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000230988.
HOVERGENiHBG107486.
InParanoidiP52632.
KOiK11224.
OrthoDBiEOG73JKTT.
PhylomeDBiP52632.
TreeFamiTF318648.

Enzyme and pathway databases

ReactomeiREACT_195025. Signaling by SCF-KIT.
REACT_195204. Signaling by Leptin.
REACT_196376. Interleukin-7 signaling.
REACT_196425. Growth hormone receptor signaling.
REACT_198628. Signaling by FGFR1 fusion mutants.
REACT_199232. Prolactin receptor signaling.
REACT_206819. Downstream signal transduction.
REACT_235800. Interleukin-2 signaling.
REACT_244635. Interleukin-3, 5 and GM-CSF signaling.

Miscellaneous databases

NextBioi605525.
PROiP52632.

Gene expression databases

GenevestigatoriP52632.

Family and domain databases

Gene3Di1.10.238.10. 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.
InterProiIPR011992. 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]
PANTHERiPTHR11801. PTHR11801. 1 hit.
PfamiPF00017. SH2. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]
SUPFAMiSSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiSTA5B_RAT
AccessioniPrimary (citable) accession number: P52632
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.