P42232 (STA5B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal transducer and activator of transcription 5B

Gene names

Name:

Stat5b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	786 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
Subunit structure	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. Ref.9 Ref.10
Subcellular location	Cytoplasm. Nucleus. Note: Translocated into the nucleus in response to phosphorylation.
Tissue specificity	In the virgin, found in most tissues. Particularly abundant in muscle tissue of virgin and lactating females, and of males.
Developmental stage	Detected both in virgin mouse and after mammary gland involution. The level of STAT5A increases constantly during pregnancy, but decreases during lactation.
Post-translational modification	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. Ref.11 Ref.12 Ref.13
Polymorphism	The polymorphism at position 327 in strain NOD reduces DNA-binding affinity.
Sequence similarities	Belongs to the transcription factor STAT family. Contains 1 SH2 domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	SH2 domain
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL JAK-STAT cascade involved in growth hormone signaling pathway Inferred from direct assay PubMed 8923468. Source: BHF-UCL Peyer's patch development Inferred from genetic interaction PubMed 15294943. Source: MGI T cell differentiation in thymus Inferred from genetic interaction PubMed 15294943. Source: MGI T cell homeostasis Inferred from genetic interaction PubMed 10072077. Source: MGI acute-phase response Inferred from electronic annotation. Source: Compara allantoin metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL citrate metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL creatine metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL creatinine metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL cytokine-mediated signaling pathway Inferred from direct assay PubMed 10485657. Source: MGI development of secondary female sexual characteristics Inferred from mutant phenotype PubMed 9630227. Source: MGI development of secondary male sexual characteristics Inferred from mutant phenotype PubMed 9630227. Source: MGI fatty acid metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL female pregnancy Inferred from mutant phenotype PubMed 15471942. Source: MGI isoleucine metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL lactation Inferred from mutant phenotype PubMed 11706048PubMed 9630227. Source: MGI lipid storage Inferred from genetic interaction PubMed 9630227. Source: MGI liver development Inferred from electronic annotation. Source: Compara luteinization Inferred from genetic interaction PubMed 9630227. Source: MGI natural killer cell differentiation Inferred from genetic interaction PubMed 10072077. Source: MGI negative regulation of apoptotic process Inferred from genetic interaction PubMed 10652277. Source: MGI negative regulation of erythrocyte differentiation Inferred from genetic interaction PubMed 10072077. Source: MGI oxaloacetate metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL positive regulation of B cell differentiation Inferred from genetic interaction PubMed 10979977. Source: MGI positive regulation of activated T cell proliferation Inferred from mutant phenotype PubMed 9841920. Source: MGI positive regulation of cellular component movement Inferred from electronic annotation. Source: Compara positive regulation of gamma-delta T cell differentiation Inferred from genetic interaction PubMed 15294943. Source: MGI positive regulation of inflammatory response Inferred from genetic interaction PubMed 10652277. Source: MGI positive regulation of interleukin-2 biosynthetic process Inferred from genetic interaction PubMed 10072077. Source: MGI positive regulation of mitotic cell cycle Inferred from genetic interaction PubMed 10072077. Source: MGI positive regulation of multicellular organism growth Inferred from mutant phenotype PubMed 9630227. Source: MGI positive regulation of natural killer cell differentiation Inferred from mutant phenotype PubMed 9841920. Source: MGI positive regulation of natural killer cell mediated cytotoxicity Inferred from mutant phenotype PubMed 9841920. Source: MGI positive regulation of natural killer cell proliferation Inferred from mutant phenotype PubMed 9841920. Source: MGI positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 21106534. Source: UniProtKB progesterone metabolic process Inferred from genetic interaction PubMed 15471942. Source: MGI regulation of cell adhesion Inferred from mutant phenotype PubMed 11706048. Source: MGI regulation of epithelial cell differentiation Inferred from mutant phenotype PubMed 11706048. Source: MGI regulation of steroid metabolic process Inferred from genetic interaction PubMed 15471942. Source: MGI response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to interleukin-15 Inferred from mutant phenotype PubMed 9841920. Source: MGI response to interleukin-2 Inferred from mutant phenotype PubMed 9841920. Source: MGI response to interleukin-4 Inferred from mutant phenotype PubMed 9841920. Source: MGI response to lipopolysaccharide Inferred from electronic annotation. Source: Compara succinate metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL taurine metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara valine metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 12147240. Source: MGI
Molecular_function	RNA polymerase II core promoter sequence-specific DNA binding Inferred from direct assay PubMed 19666510. Source: MGI calcium ion binding Inferred from electronic annotation. Source: InterPro double-stranded DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara signal transducer activity Inferred from genetic interaction PubMed 10485657. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DNAJA3	Q96EY1	3	EBI-617454,EBI-356767	From a different organism.
DNAJA3	Q96EY1-1	2	EBI-617454,EBI-4322330	From a different organism.
DNAJA3	Q96EY1-2	2	EBI-617454,EBI-3952284	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 786	786	Signal transducer and activator of transcription 5B		PRO_0000182430
Regions
	Domain	589 – 686	98	SH2
Amino acid modifications
	Modified residue	128	1	Phosphoserine By similarity
	Modified residue	699	1	Phosphotyrosine; by HCK, JAK and PTK6 By similarity
Natural variations
	Natural variant	327	1	L → M in strain: NOD. Ref.4
Experimental info
	Mutagenesis	684	1	T → A: Fails to interact with INSR. Ref.9
	Sequence conflict	210	1	S → P in CAB51862. Ref.8
	Sequence conflict	433	1	E → G in AAC52282. Ref.2
	Sequence conflict	433	1	E → G in AAL05590. Ref.4
	Sequence conflict	433	1	E → G in AAK97791. Ref.4
	Sequence conflict	433	1	E → G in AAK97792. Ref.4
	Sequence conflict	433	1	E → G in AAK97793. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P42232 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: A8FE76405E41B2EF	FASTA	786	90,002
	10 20 30 40 50 60 MAMWIQAQQL QGDALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSIDLDN PQENIKATQL 70 80 90 100 110 120 LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQSTYDR CPMELVRCIR HILYNEQRLV 130 140 150 160 170 180 REANNGSSPA GSLADAMSQK HLQINQTFEE LRLITQDTEN ELKKLQQTQE YFIIQYQESL 190 200 210 220 230 240 RIQAQFAQLG QLNPQERMSR ETALQQKQVS LETWLQREAQ TLQQYRVELA EKHQKTLQLL 250 260 270 280 290 300 RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC 310 320 330 340 350 360 QQLPIPGPVE EMLAEVNATI TDIISALVTS 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 TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNI 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 KYYTPVPCEP ATAKAADGYV KPQIKQVVPE FANASTDAGS 730 740 750 760 770 780 GATYMDQAPS PVVCPQAHYN MYPPNPDSVL DTDGDFDLED TMDVARRVEE LLGRPMDSQW IPHAQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1995) [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(1995) [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(2001) [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(2004) [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(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Dendritic cell and Thymus.
[6]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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(2004) [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(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-389.
[9]	"Identification of Stat 5B as a substrate of the insulin receptor." Sawka-Verhelle D., Filloux C., Tartare-Deckert S., Mothe I., Van Obberghen E. Eur. J. Biochem. 250:411-417(1997) [PubMed] [Europe PMC] [Abstract] 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(1998) [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(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
[12]	"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.
[13]	"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling." Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K., Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D., Muller J.P. J. Biol. Chem. 286:10918-10929(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00114982.
PIR	I49274.
RefSeq	NP_001107035.1. NM_001113563.1. NP_035619.3. NM_011489.3.
UniGene	Mm.34064.
3D structure databases
ProteinModelPortal	P42232.
SMR	P42232. Positions 2-686.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-898N.
IntAct	P42232. 2 interactions.
PTM databases
PhosphoSite	P42232.
Proteomic databases
PaxDb	P42232.
PRIDE	P42232.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000004143; ENSMUSP00000004143; ENSMUSG00000020919. ENSMUST00000107358; ENSMUSP00000102981; ENSMUSG00000020919.
GeneID	20851.
KEGG	mmu:20851.
UCSC	uc007lmi.2. mouse.
Organism-specific databases
CTD	6777.
MGI	MGI:103035. Stat5b.
Phylogenomic databases
eggNOG	NOG245085.
GeneTree	ENSGT00550000074337.
HOVERGEN	HBG107486.
InParanoid	Q9R0X8.
KO	K11224.
OMA	DLAEKHQ.
OrthoDB	EOG457560.
Enzyme and pathway databases
Reactome	REACT_107772. Immune System.
Gene expression databases
ArrayExpress	P42232.
Bgee	P42232.
Genevestigator	P42232.
GermOnline	ENSMUSG00000020919. Mus musculus.
Family and domain databases
Gene3D	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.
InterPro	IPR011992. EF-hand-like_dom. IPR008967. p53-like_TF_DNA-bd. IPR000980. SH2. IPR013800. STAT_TF_alpha. IPR015988. STAT_TF_coiled-coil. IPR001217. STAT_TF_core. IPR013801. STAT_TF_DNA-bd. IPR012345. STAT_TF_DNA-bd_sub. IPR013799. STAT_TF_prot_interaction. [Graphical view]
PANTHER	PTHR11801. PTHR11801. 1 hit.
Pfam	PF00017. SH2. 1 hit. PF01017. STAT_alpha. 1 hit. PF02864. STAT_bind. 1 hit. PF02865. STAT_int. 1 hit. [Graphical view]
SMART	SM00252. SH2. 1 hit. SM00964. STAT_int. 1 hit. [Graphical view]
SUPFAM	SSF49417. P53_like_DNA_bnd. 1 hit. SSF47655. STAT. 1 hit. SSF48092. STAT. 1 hit.
PROSITE	PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	STAT5B. mouse.
NextBio	299639.
SOURCE	Search...

Entry information

Entry name

STA5B_MOUSE

Accession

Primary (citable) accession number: P42232
Secondary accession number(s): A2A5D5 , Q541Q5, Q60804, Q8K3Q1, Q9JKM1, Q9R0X8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program