Reviewed, UniProtKB/Swiss-Prot P42232 (STA5B_MOUSE)

Names and origin

Protein names

Recommended name:
    Signal transducer and activator of transcription 5B

Gene names

Name:

Stat5b

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	786 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Carries out a dual function: signal transduction and activation of transcription. 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.
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.
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
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from mutant phenotype. Source: UniProtKB JAK-STAT cascade involved in growth hormone signaling pathway Inferred from direct assay. Source: UniProtKB Peyer's patch development Inferred from genetic interaction. Source: MGI T cell differentiation in the thymus Inferred from genetic interaction. Source: MGI T cell homeostasis Inferred from genetic interaction. Source: MGI allantoin metabolic process Inferred from mutant phenotype. Source: UniProtKB citrate metabolic process Inferred from mutant phenotype. Source: UniProtKB creatine metabolic process Inferred from mutant phenotype. Source: UniProtKB creatinine metabolic process Inferred from mutant phenotype. Source: UniProtKB cytokine-mediated signaling pathway Inferred from direct assay. Source: MGI development of secondary female sexual characteristics Inferred from mutant phenotype. Source: MGI development of secondary male sexual characteristics Inferred from genetic interaction. Source: MGI fatty acid metabolic process Inferred from mutant phenotype. Source: UniProtKB female pregnancy Inferred from genetic interaction. Source: MGI isoleucine metabolic process Inferred from mutant phenotype. Source: UniProtKB lactation Inferred from mutant phenotype. Source: MGI lipid storage Inferred from genetic interaction. Source: MGI luteinization Inferred from genetic interaction. Source: MGI natural killer cell differentiation Inferred from genetic interaction. Source: MGI negative regulation of erythrocyte differentiation Inferred from genetic interaction. Source: MGI oxaloacetate metabolic process Inferred from mutant phenotype. Source: UniProtKB positive regulation of B cell differentiation Inferred from genetic interaction. Source: MGI positive regulation of activated T cell proliferation Inferred from mutant phenotype. Source: MGI positive regulation of gamma-delta T cell differentiation Inferred from genetic interaction. Source: MGI positive regulation of inflammatory response Inferred from genetic interaction. Source: MGI positive regulation of interleukin-2 biosynthetic process Inferred from genetic interaction. Source: MGI positive regulation of mitotic cell cycle Inferred from genetic interaction. Source: MGI positive regulation of multicellular organism growth Inferred from genetic interaction. Source: MGI positive regulation of natural killer cell differentiation Inferred from mutant phenotype. Source: MGI positive regulation of natural killer cell mediated cytotoxicity Inferred from mutant phenotype. Source: MGI positive regulation of natural killer cell proliferation Inferred from mutant phenotype. Source: MGI positive regulation of survival gene product expression Inferred from genetic interaction. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: MGI progesterone metabolic process Inferred from genetic interaction. Source: MGI regulation of cell adhesion Inferred from mutant phenotype. Source: MGI regulation of epithelial cell differentiation Inferred from mutant phenotype. Source: MGI regulation of steroid metabolic process Inferred from genetic interaction. Source: MGI succinate metabolic process Inferred from mutant phenotype. Source: UniProtKB taurine metabolic process Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW valine metabolic process Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from genetic interaction. Source: MGI transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 JAK By similarity
Natural variations
	Natural variant	327	1	L → M in strain: NOD. Ref.4
Experimental info
	Sequence conflict	210	1	S → P in CAB51862. Ref.7
	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)
	P42232-1 [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: 7720707] [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: 7568026] [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: 11161808] [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: 14701862] [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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Dendritic cell and Thymus.
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
[7]	"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: 10835485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-389.
[8]	"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: 9528750] [Abstract] Cited for: INTERACTION WITH NR3C1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. BC024319 mRNA. Translation: AAH24319.1. AJ237939 Genomic DNA. Translation: CAB51862.1.
IPI	IPI00114982.
PIR	I49274.
RefSeq	NP_001107035.1. NP_035619.3.
UniGene	Mm.34064
3D structure databases
HSSP	HSSP built from PDB template 1BF5 based on UniProtKB P42224.
SMR	P42232. Positions 138-686.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:898N.
IntAct	P42232. 1 interaction.
PTM databases
PhosphoSite	P42232.
Proteomic databases
PRIDE	P42232.
Genome annotation databases
Ensembl	ENSMUSG00000020919. Mus musculus. [Contig view]
GeneID	20851.
KEGG	mmu:20851.
Organism-specific databases
MGI	MGI:103035. Stat5b.
Phylogenomic databases
HOGENOM	P42232.
HOVERGEN	P42232.
OMA	P42232. CEPATAK.
Gene expression databases
ArrayExpress	P42232.
Bgee	P42232.
GermOnline	ENSMUSG00000020919. Mus musculus.
Family and domain databases
InterPro	IPR011992. EF-Hand_type. IPR000980. SH2. IPR013800. STAT_TF_alpha. IPR001217. STAT_TF_core. IPR013801. STAT_TF_DNA-bd. IPR012345. STAT_TF_DNA-bd_sub. IPR013799. STAT_TF_prot_interaction. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:3.30.505.10. SH2. 1 hit. G3DSA:1.20.1050.20. STAT_alpha. 1 hit. G3DSA:2.60.40.630. STAT_DNA_bd_sub. 1 hit. G3DSA:1.10.532.10. STAT_protein_interaction. 1 hit.
PANTHER	PTHR11801. STAT. 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. [Graphical view]
PROSITE	PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	299639.
SOURCE	Search...

Entry information

Entry name

STA5B_MOUSE

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	July 7, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)