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P51692

- STA5B_HUMAN

UniProt

P51692 - STA5B_HUMAN

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Protein
Signal transducer and activator of transcription 5B
Gene
STAT5B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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.1 Publication

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_111133. Growth hormone receptor signaling.
REACT_115529. Interleukin-7 signaling.
REACT_115697. Prolactin receptor signaling.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_169118. Signaling by Leptin.
REACT_17025. Downstream signal transduction.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_27283. Interleukin-2 signaling.
SignaLinkiP51692.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription 5B
Gene namesi
Name:STAT5B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:11367. 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: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti630 – 6301A → P in GHII; affects activation by growth hormone or interferon-gamma. 1 Publication
VAR_018728
Natural varianti646 – 6461F → S in GHII; transcriptionally inactive. 1 Publication
VAR_067368

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi684 – 6841T → A: Abolishes interaction with INSR. 1 Publication
Mutagenesisi699 – 6991Y → F: Abolishes phosphorylation by HCK. 1 Publication

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi245590. phenotype.
Orphaneti520. Acute promyelocytic leukemia.
220465. Laron syndrome with immunodeficiency.
PharmGKBiPA36186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 787787Signal transducer and activator of transcription 5B
PRO_0000182429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281Phosphoserine1 Publication
Modified residuei193 – 1931Phosphoserine3 Publications
Modified residuei699 – 6991Phosphotyrosine; by HCK, JAK and PTK62 Publications

Post-translational modificationi

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.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP51692.
PaxDbiP51692.
PeptideAtlasiP51692.
PRIDEiP51692.

PTM databases

PhosphoSiteiP51692.

Miscellaneous databases

PMAP-CutDBP51692.

Expressioni

Gene expression databases

ArrayExpressiP51692.
BgeeiP51692.
CleanExiHS_STAT5B.
GenevestigatoriP51692.

Organism-specific databases

HPAiCAB004298.

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DNAJA3Q96EY12EBI-1186119,EBI-356767
NMIQ132877EBI-1186119,EBI-372942

Protein-protein interaction databases

BioGridi112654. 40 interactions.
IntActiP51692. 13 interactions.
MINTiMINT-132900.
STRINGi9606.ENSP00000293328.

Structurei

3D structure databases

ProteinModelPortaliP51692.
SMRiP51692. Positions 4-686.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini589 – 68698SH2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni232 – 32190Required for interaction with NMI
Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG245085.
HOVERGENiHBG107486.
InParanoidiP51692.
KOiK11224.
OMAiVREATNS.
OrthoDBiEOG73JKTT.
PhylomeDBiP51692.
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.

P51692-1 [UniParc]FASTAAdd to Basket

« Hide

MAVWIQAQQL QGEALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSVDLDN    50
PQENIKATQL LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR 100
CPMELVRCIR HILYNEQRLV REANNGSSPA GSLADAMSQK HLQINQTFEE 150
LRLVTQDTEN ELKKLQQTQE YFIIQYQESL RIQAQFGPLA QLSPQERLSR 200
ETALQQKQVS LEAWLQREAQ TLQQYRVELA EKHQKTLQLL RKQQTIILDD 250
ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC 300
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA 350
TVRLLVGGKL NVHMNPPQVK ATIISEQQAK SLLKNENTRN DYSGEILNNC 400
CVMEYHQATG TLSAHFRNMS LKRIKRSDRR GAESVTEEKF TILFESQFSV 450
GGNELVFQVK TLSLPVVVIV HGSQDNNATA TVLWDNAFAE PGRVPFAVPD 500
KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNN SSSHLEDYSG 550
LSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK 600
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSQERMF WNLMPFTTRD 650
FSIRSLADRL GDLNYLIYVF PDRPKDEVYS KYYTPVPCES ATAKAVDGYV 700
KPQIKQVVPE FVNASADAGG GSATYMDQAP SPAVCPQAHY NMYPQNPDSV 750
LDTDGDFDLE DTMDVARRVE ELLGRPMDSQ WIPHAQS 787
Length:787
Mass (Da):89,866
Last modified:January 16, 2004 - v2
Checksum:iAA2F1CAB20955ACA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti130 – 1301A → V.
Corresponds to variant rs2277619 [ dbSNP | Ensembl ].
VAR_052074
Natural varianti630 – 6301A → P in GHII; affects activation by growth hormone or interferon-gamma. 1 Publication
VAR_018728
Natural varianti646 – 6461F → S in GHII; transcriptionally inactive. 1 Publication
VAR_067368

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301A → P in AAC50491. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11423.1.
RefSeqiNP_036580.2. NM_012448.3.
UniGeneiHs.595276.

Genome annotation databases

EnsembliENST00000293328; ENSP00000293328; ENSG00000173757.
GeneIDi6777.
KEGGihsa:6777.
UCSCiuc002hzh.3. human.

Polymorphism databases

DMDMi41019536.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

STAT5Bbase

STAT5B mutation db

Wikipedia

STAT5 entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11423.1.
RefSeqi NP_036580.2. NM_012448.3.
UniGenei Hs.595276.

3D structure databases

ProteinModelPortali P51692.
SMRi P51692. Positions 4-686.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112654. 40 interactions.
IntActi P51692. 13 interactions.
MINTi MINT-132900.
STRINGi 9606.ENSP00000293328.

Chemistry

BindingDBi P51692.
ChEMBLi CHEMBL5817.
DrugBanki DB01254. Dasatinib.

PTM databases

PhosphoSitei P51692.

Polymorphism databases

DMDMi 41019536.

Proteomic databases

MaxQBi P51692.
PaxDbi P51692.
PeptideAtlasi P51692.
PRIDEi P51692.

Protocols and materials databases

DNASUi 6777.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000293328 ; ENSP00000293328 ; ENSG00000173757 .
GeneIDi 6777.
KEGGi hsa:6777.
UCSCi uc002hzh.3. human.

Organism-specific databases

CTDi 6777.
GeneCardsi GC17M040351.
HGNCi HGNC:11367. STAT5B.
HPAi CAB004298.
MIMi 245590. phenotype.
604260. gene.
neXtProti NX_P51692.
Orphaneti 520. Acute promyelocytic leukemia.
220465. Laron syndrome with immunodeficiency.
PharmGKBi PA36186.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG245085.
HOVERGENi HBG107486.
InParanoidi P51692.
KOi K11224.
OMAi VREATNS.
OrthoDBi EOG73JKTT.
PhylomeDBi P51692.
TreeFami TF318648.

Enzyme and pathway databases

Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_111133. Growth hormone receptor signaling.
REACT_115529. Interleukin-7 signaling.
REACT_115697. Prolactin receptor signaling.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_169118. Signaling by Leptin.
REACT_17025. Downstream signal transduction.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_27283. Interleukin-2 signaling.
SignaLinki P51692.

Miscellaneous databases

ChiTaRSi STAT5B. human.
GeneWikii STAT5B.
GenomeRNAii 6777.
NextBioi 26454.
PMAP-CutDB P51692.
PROi P51692.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51692.
Bgeei P51692.
CleanExi HS_STAT5B.
Genevestigatori P51692.

Family and domain databases

Gene3Di 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.
InterProi IPR011992. 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 ]
PANTHERi PTHR11801. PTHR11801. 1 hit.
Pfami PF00017. SH2. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view ]
SMARTi SM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view ]
SUPFAMi SSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.

Entry informationi

Entry nameiSTA5B_HUMAN
AccessioniPrimary (citable) accession number: P51692
Secondary accession number(s): Q8WWS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 16, 2004
Last modified: September 3, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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