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Protein

Signal transducer and activator of transcription 5B

Gene

Stat5b

Organism
Mus musculus (Mouse)
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

  1. chromatin binding Source: UniProtKB
  2. DNA binding Source: MGI
  3. double-stranded DNA binding Source: Ensembl
  4. glucocorticoid receptor binding Source: MGI
  5. protein dimerization activity Source: UniProtKB
  6. protein phosphatase binding Source: UniProtKB
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  8. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  9. signal transducer activity Source: MGI

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: BHF-UCL
  2. acute-phase response Source: Ensembl
  3. allantoin metabolic process Source: BHF-UCL
  4. cellular response to epidermal growth factor stimulus Source: UniProtKB
  5. cellular response to growth factor stimulus Source: UniProtKB
  6. cellular response to hormone stimulus Source: MGI
  7. citrate metabolic process Source: BHF-UCL
  8. creatine metabolic process Source: BHF-UCL
  9. creatinine metabolic process Source: BHF-UCL
  10. cytokine-mediated signaling pathway Source: MGI
  11. development of secondary female sexual characteristics Source: MGI
  12. development of secondary male sexual characteristics Source: MGI
  13. fatty acid metabolic process Source: BHF-UCL
  14. female pregnancy Source: MGI
  15. isoleucine metabolic process Source: BHF-UCL
  16. JAK-STAT cascade Source: MGI
  17. JAK-STAT cascade involved in growth hormone signaling pathway Source: BHF-UCL
  18. lactation Source: MGI
  19. lipid storage Source: MGI
  20. liver development Source: Ensembl
  21. luteinization Source: MGI
  22. natural killer cell differentiation Source: MGI
  23. negative regulation of apoptotic process Source: MGI
  24. negative regulation of erythrocyte differentiation Source: MGI
  25. oxaloacetate metabolic process Source: BHF-UCL
  26. Peyer's patch development Source: MGI
  27. positive regulation of activated T cell proliferation Source: MGI
  28. positive regulation of B cell differentiation Source: MGI
  29. positive regulation of cell proliferation Source: MGI
  30. positive regulation of cellular component movement Source: Ensembl
  31. positive regulation of gamma-delta T cell differentiation Source: MGI
  32. positive regulation of inflammatory response Source: MGI
  33. positive regulation of interleukin-2 biosynthetic process Source: MGI
  34. positive regulation of lymphocyte differentiation Source: MGI
  35. positive regulation of mitotic cell cycle Source: MGI
  36. positive regulation of multicellular organism growth Source: MGI
  37. positive regulation of natural killer cell differentiation Source: MGI
  38. positive regulation of natural killer cell mediated cytotoxicity Source: MGI
  39. positive regulation of natural killer cell proliferation Source: MGI
  40. positive regulation of smooth muscle cell proliferation Source: Ensembl
  41. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  42. progesterone metabolic process Source: MGI
  43. prolactin signaling pathway Source: UniProtKB
  44. regulation of cell adhesion Source: MGI
  45. regulation of epithelial cell differentiation Source: MGI
  46. regulation of multicellular organism growth Source: BHF-UCL
  47. regulation of steroid metabolic process Source: MGI
  48. regulation of transcription from RNA polymerase II promoter Source: MGI
  49. response to estradiol Source: MGI
  50. response to ethanol Source: Ensembl
  51. response to hypoxia Source: Ensembl
  52. response to interleukin-15 Source: MGI
  53. response to interleukin-2 Source: MGI
  54. response to interleukin-4 Source: MGI
  55. response to lipopolysaccharide Source: Ensembl
  56. sex differentiation Source: MGI
  57. succinate metabolic process Source: BHF-UCL
  58. taurine metabolic process Source: BHF-UCL
  59. T cell differentiation in thymus Source: MGI
  60. T cell homeostasis Source: MGI
  61. 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_169390. Signaling by Leptin.
REACT_273845. Interleukin-2 signaling.
REACT_276590. Interleukin-7 signaling.
REACT_278498. Downstream signal transduction.
REACT_289947. Prolactin receptor signaling.
REACT_294984. Interleukin-3, 5 and GM-CSF signaling.
REACT_317434. Growth hormone receptor signaling.
REACT_323806. Signaling by Leptin.
REACT_324118. Signaling by FGFR1 fusion mutants.
REACT_327841. Signaling by SCF-KIT.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription 5B
Gene namesi
Name:Stat5b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:103035. Stat5b.

Subcellular locationi

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

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi684 – 6841T → A: Fails to interact with INSR. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 786786Signal transducer and activator of transcription 5BPRO_0000182430Add
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 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.By similarity4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP42232.
PaxDbiP42232.
PRIDEiP42232.

PTM databases

PhosphoSiteiP42232.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiP42232.
ExpressionAtlasiP42232. baseline and differential.
GenevestigatoriP42232.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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.

Protein-protein interaction databases

BioGridi203526. 6 interactions.
DIPiDIP-898N.
IntActiP42232. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP42232.
SMRiP42232. Positions 2-686.
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.
HOVERGENiHBG107486.
InParanoidiP42232.
KOiK11224.
OMAiYPPNPDS.
OrthoDBiEOG73JKTT.
PhylomeDBiP42232.
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.

P42232-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMWIQAQQL QGDALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSIDLDN
60 70 80 90 100
PQENIKATQL LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQSTYDR
110 120 130 140 150
CPMELVRCIR HILYNEQRLV REANNGSSPA GSLADAMSQK HLQINQTFEE
160 170 180 190 200
LRLITQDTEN ELKKLQQTQE YFIIQYQESL RIQAQFAQLG QLNPQERMSR
210 220 230 240 250
ETALQQKQVS LETWLQREAQ 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 TILFDSQFSV
460 470 480 490 500
GGNELVFQVK TLSLPVVVIV HGSQDNNATA TVLWDNAFAE PGRVPFAVPD
510 520 530 540 550
KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNI 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 KYYTPVPCEP ATAKAADGYV
710 720 730 740 750
KPQIKQVVPE FANASTDAGS GATYMDQAPS PVVCPQAHYN MYPPNPDSVL
760 770 780
DTDGDFDLED TMDVARRVEE LLGRPMDSQW IPHAQS
Length:786
Mass (Da):90,002
Last modified:November 1, 1995 - v1
Checksum:iA8FE76405E41B2EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101S → P in CAB51862 (PubMed:10835485).Curated
Sequence conflicti433 – 4331E → G in AAC52282 (PubMed:7568026).Curated
Sequence conflicti433 – 4331E → G in AAL05590 (PubMed:14701862).Curated
Sequence conflicti433 – 4331E → G in AAK97791 (PubMed:14701862).Curated
Sequence conflicti433 – 4331E → G in AAK97792 (PubMed:14701862).Curated
Sequence conflicti433 – 4331E → G in AAK97793 (PubMed:14701862).Curated

Polymorphismi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti327 – 3271L → M in strain: NOD. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25438.1.
PIRiI49274.
RefSeqiNP_001107035.1. NM_001113563.1.
NP_035619.3. NM_011489.3.
UniGeneiMm.34064.

Genome annotation databases

EnsembliENSMUST00000004143; ENSMUSP00000004143; ENSMUSG00000020919.
ENSMUST00000107358; ENSMUSP00000102981; ENSMUSG00000020919.
GeneIDi20851.
KEGGimmu:20851.
UCSCiuc007lmi.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25438.1.
PIRiI49274.
RefSeqiNP_001107035.1. NM_001113563.1.
NP_035619.3. NM_011489.3.
UniGeneiMm.34064.

3D structure databases

ProteinModelPortaliP42232.
SMRiP42232. Positions 2-686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203526. 6 interactions.
DIPiDIP-898N.
IntActiP42232. 3 interactions.

PTM databases

PhosphoSiteiP42232.

Proteomic databases

MaxQBiP42232.
PaxDbiP42232.
PRIDEiP42232.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004143; ENSMUSP00000004143; ENSMUSG00000020919.
ENSMUST00000107358; ENSMUSP00000102981; ENSMUSG00000020919.
GeneIDi20851.
KEGGimmu:20851.
UCSCiuc007lmi.2. mouse.

Organism-specific databases

CTDi6777.
MGIiMGI:103035. Stat5b.

Phylogenomic databases

eggNOGiNOG245085.
GeneTreeiENSGT00760000119236.
HOVERGENiHBG107486.
InParanoidiP42232.
KOiK11224.
OMAiYPPNPDS.
OrthoDBiEOG73JKTT.
PhylomeDBiP42232.
TreeFamiTF318648.

Enzyme and pathway databases

ReactomeiREACT_169390. Signaling by Leptin.
REACT_273845. Interleukin-2 signaling.
REACT_276590. Interleukin-7 signaling.
REACT_278498. Downstream signal transduction.
REACT_289947. Prolactin receptor signaling.
REACT_294984. Interleukin-3, 5 and GM-CSF signaling.
REACT_317434. Growth hormone receptor signaling.
REACT_323806. Signaling by Leptin.
REACT_324118. Signaling by FGFR1 fusion mutants.
REACT_327841. Signaling by SCF-KIT.

Miscellaneous databases

ChiTaRSiStat5b. mouse.
NextBioi299639.
PROiP42232.
SOURCEiSearch...

Gene expression databases

BgeeiP42232.
ExpressionAtlasiP42232. baseline and differential.
GenevestigatoriP42232.

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. "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(1994) [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(1994) [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(2000) [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(2003) [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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Dendritic cell and Thymus.
  6. 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(2003) [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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-389.
  9. 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(1997) [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(1999) [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(2001) [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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION IN RESPONSE TO KIT SIGNALING.
  14. Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.

Entry informationi

Entry nameiSTA5B_MOUSE
AccessioniPrimary (citable) accession number: P42232
Secondary accession number(s): A2A5D5
, Q541Q5, Q60804, Q8K3Q1, Q9JKM1, Q9R0X8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 156 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.