Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Signal transducer and activator of transcription 5B

Gene

STAT5B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

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 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Growth hormone insensitivity with immunodeficiency (GHII)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:245590
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.

Chemistry

DrugBankiDB01254. Dasatinib.

Polymorphism and mutation databases

BioMutaiSTAT5B.
DMDMi41019536.

PTM / Processingi

Molecule processing

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

BgeeiP51692.
CleanExiHS_STAT5B.
ExpressionAtlasiP51692. baseline and differential.
GenevisibleiP51692. HS.

Organism-specific databases

HPAiCAB004298.
HPA042128.
HPA049883.
HPA051156.

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.By similarity4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112654. 39 interactions.
IntActiP51692. 16 interactions.
MINTiMINT-132900.
STRINGi9606.ENSP00000293328.

Structurei

3D structure databases

ProteinModelPortaliP51692.
SMRiP51692. Positions 4-686.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni232 – 32190Required for interaction with NMIAdd
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.
HOVERGENiHBG107486.
InParanoidiP51692.
KOiK11224.
OMAiTIWQNRQ.
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

        10         20         30         40         50
MAVWIQAQQL QGEALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSVDLDN
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
LRLVTQDTEN ELKKLQQTQE YFIIQYQESL RIQAQFGPLA QLSPQERLSR
210 220 230 240 250
ETALQQKQVS LEAWLQREAQ TLQQYRVELA EKHQKTLQLL RKQQTIILDD
260 270 280 290 300
ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
310 320 330 340 350
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA
360 370 380 390 400
TVRLLVGGKL NVHMNPPQVK ATIISEQQAK SLLKNENTRN DYSGEILNNC
410 420 430 440 450
CVMEYHQATG TLSAHFRNMS LKRIKRSDRR GAESVTEEKF TILFESQFSV
460 470 480 490 500
GGNELVFQVK TLSLPVVVIV HGSQDNNATA TVLWDNAFAE PGRVPFAVPD
510 520 530 540 550
KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNN SSSHLEDYSG
560 570 580 590 600
LSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK
610 620 630 640 650
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSQERMF WNLMPFTTRD
660 670 680 690 700
FSIRSLADRL GDLNYLIYVF PDRPKDEVYS KYYTPVPCES ATAKAVDGYV
710 720 730 740 750
KPQIKQVVPE FVNASADAGG GSATYMDQAP SPAVCPQAHY NMYPQNPDSV
760 770 780
LDTDGDFDLE DTMDVARRVE ELLGRPMDSQ WIPHAQS
Length:787
Mass (Da):89,866
Last modified:January 16, 2004 - v2
Checksum:iAA2F1CAB20955ACA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301A → P in AAC50491 (Ref. 2) Curated

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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP51692.
SMRiP51692. Positions 4-686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112654. 39 interactions.
IntActiP51692. 16 interactions.
MINTiMINT-132900.
STRINGi9606.ENSP00000293328.

Chemistry

BindingDBiP51692.
ChEMBLiCHEMBL5817.
DrugBankiDB01254. Dasatinib.

PTM databases

PhosphoSiteiP51692.

Polymorphism and mutation databases

BioMutaiSTAT5B.
DMDMi41019536.

Proteomic databases

MaxQBiP51692.
PaxDbiP51692.
PeptideAtlasiP51692.
PRIDEiP51692.

Protocols and materials databases

DNASUi6777.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6777.
GeneCardsiGC17M040351.
HGNCiHGNC:11367. STAT5B.
HPAiCAB004298.
HPA042128.
HPA049883.
HPA051156.
MIMi245590. phenotype.
604260. gene.
neXtProtiNX_P51692.
Orphaneti520. Acute promyelocytic leukemia.
220465. Laron syndrome with immunodeficiency.
PharmGKBiPA36186.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG245085.
GeneTreeiENSGT00760000119236.
HOVERGENiHBG107486.
InParanoidiP51692.
KOiK11224.
OMAiTIWQNRQ.
OrthoDBiEOG73JKTT.
PhylomeDBiP51692.
TreeFamiTF318648.

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.

Miscellaneous databases

ChiTaRSiSTAT5B. human.
GeneWikiiSTAT5B.
GenomeRNAii6777.
NextBioi26454.
PMAP-CutDBP51692.
PROiP51692.
SOURCEiSearch...

Gene expression databases

BgeeiP51692.
CleanExiHS_STAT5B.
ExpressionAtlasiP51692. baseline and differential.
GenevisibleiP51692. HS.

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

« 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: July 22, 2015
This is version 157 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

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.