Signal transducer and activator of transcription 5A

Contribute

Send feedback

Read comments (?) or add your own

P42230 (STA5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 133. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Signal transducer and activator of transcription 5A

Alternative name(s):
Mammary gland factor

Gene names

Name:	Stat5a
Synonyms:	Mgf, Mpf

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	793 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. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation. Ref.5 Ref.7
Subunit structure	Forms a homodimer or a heterodimer with a related family member. Interacts with NCOA1 and SOCS7 By similarity. Binds NR3C1. Interacts with ERBB4. Ref.4 Ref.5 Ref.7
Subcellular location	Cytoplasm. Nucleus. Note: Translocated into the nucleus in response to phosphorylation. Ref.7
Tissue specificity	In the virgin, found in most tissues except brain and muscle. During lactation, abundantly found in mammary tissue, as well as in other secretory organs such as salivary gland and seminal vesicle.
Post-translational modification	Tyrosine phosphorylated in response to IL2, IL3, IL7, IL15, KITLG/SCF, CSF2/GMCSF, GH1, PRL, EPO and THPO. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. 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 at Tyr-694. Tyrosine phosphorylation is required for DNA-binding activity and dimerization. Serine phosphorylation is also required for maximal transcriptional activity By similarity. Ref.6 Ref.7 Ref.8 Ref.9
Sequence similarities	Belongs to the transcription factor STAT family. Contains 1 SH2 domain.

Ontologies

Keywords
Biological process	Lactation Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	SH2 domain
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure 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 8702683. 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 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 epithelial cell differentiation involved in prostate gland development Inferred from mutant phenotype PubMed 10908145. Source: MGI fatty acid metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL female pregnancy Inferred from genetic interaction PubMed 15471942. Source: MGI isoleucine metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL lactation Inferred from mutant phenotype PubMed 11706048 PubMed 9630227. Source: MGI lipid storage Inferred from genetic interaction PubMed 9630227. Source: MGI luteinization Inferred from genetic interaction PubMed 9630227. Source: MGI mammary gland epithelium development Inferred from mutant phenotype PubMed 12040017. Source: MGI natural killer cell differentiation Inferred from genetic interaction PubMed 10072077. Source: MGI negative regulation of erythrocyte differentiation Inferred from genetic interaction PubMed 10072077. Source: MGI negative regulation of mast cell apoptotic process Inferred from mutant phenotype PubMed 15947484. Source: MGI oxaloacetate metabolic process Inferred from mutant phenotype PubMed 18648510. Source: BHF-UCL peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 12388746. Source: MGI positive regulation of B cell differentiation Inferred from genetic interaction PubMed 10979977. Source: MGI positive regulation of activated T cell proliferation Inferred from direct assay PubMed 10072077. Source: MGI 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 mast cell differentiation Inferred from mutant phenotype PubMed 15947484. Source: MGI positive regulation of mast cell proliferation Inferred from mutant phenotype PubMed 15947484. Source: MGI positive regulation of mitotic cell cycle Inferred from genetic interaction PubMed 10072077. Source: MGI positive regulation of multicellular organism growth Inferred from genetic interaction 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 transcription from RNA polymerase II promoter Inferred from direct assay PubMed 19666510. Source: MGI prostate gland epithelium morphogenesis Inferred from mutant phenotype PubMed 10908145. 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 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, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW 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 12456807. Source: UniProtKB
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 sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from genetic interaction PubMed 10485657. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 793

793

Signal transducer and activator of transcription 5A

PRO_0000182424

Regions

Domain

589 – 686

SH2

Amino acid modifications

Modified residue

694

Phosphotyrosine; by JAK2 By similarity

Secondary structure

793

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P42230 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7C66E435C37624DD
Show »

FASTA

793

90,831

        10         20         30         40         50         60 
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN PQDRGQATQL 

        70         80         90        100        110        120 
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV 

       130        140        150        160        170        180 
REANNCSSPA GVLVDAMSQK HLQINQRFEE 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 ECSGEILNNC CVMEYHQATG TLSAHFRNMS 

       430        440        450        460        470        480 
LKRIKRADRR GAESVTEEKF TVLFESQFSV GSNELVFQVK TLSLPVVVIV HGSQDHNATA 

       490        500        510        520        530        540 
TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNI 

       550        560        570        580        590        600 
SSNHLEDYNS MSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK 

       610        620        630        640        650        660 
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPDRNL WNLKPFTTRD FSIRSLADRL 

       670        680        690        700        710        720 
GDLNYLIYVF PDRPKDEVFA KYYTPVLAKA VDGYVKPQIK QVVPEFVNAS TDAGASATYM 

       730        740        750        760        770        780 
DQAPSPVVCP QPHYNMYPPN PDPVLDQDGE FDLDESMDVA RHVEELLRRP MDSLDARLSP 

       790 
PAGLFTSARS SLS

« Hide

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]	Zhou L.X., Moore R.C., Oka T. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H/HeN. Tissue: Mammary gland.
[4]	"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.
[5]	"ErbB4 signaling in the mammary gland is required for lobuloalveolar development and Stat5 activation during lactation." Jones F.E., Welte T., Fu X.Y., Stern D.F. J. Cell Biol. 147:77-88(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ERBB4.
[6]	"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.
[7]	"The intracellular domain of ErbB4 induces differentiation of mammary epithelial cells." Muraoka-Cook R.S., Sandahl M., Husted C., Hunter D., Miraglia L., Feng S.M., Elenius K., Earp H.S. III Mol. Biol. Cell 17:4118-4129(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH ERBB4.
[8]	"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.
[9]	"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.
[10]	"Structure of the unphosphorylated STAT5a dimer." Neculai D., Neculai A.M., Verrier S., Straub K., Klumpp K., Pfitzner E., Becker S. J. Biol. Chem. 280:40782-40787(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 128-712.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z48538 mRNA. Translation: CAA88419.1.
U21103 mRNA. Translation: AAA80590.1.
U36502 mRNA. Translation: AAA78945.1.

IPI

IPI00114979.

PIR

S54772.

RefSeq

NP_035618.1. NM_011488.3.

UniGene

Mm.277403.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y1U	X-ray	3.21	A/B/C	128-712	[»]

ProteinModelPortal

P42230.

SMR

P42230. Positions 138-690.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-897N.

IntAct

P42230. 1 interaction.

MINT

MINT-2576471.

PTM databases

PhosphoSite

P42230.

Proteomic databases

PaxDb

P42230.

PRIDE

P42230.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000004145; ENSMUSP00000004145; ENSMUSG00000004043.
ENSMUST00000107356; ENSMUSP00000102979; ENSMUSG00000004043.

GeneID

20850.

KEGG

mmu:20850.

Organism-specific databases

CTD

6776.

MGI

MGI:103036. Stat5a.

Phylogenomic databases

eggNOG

NOG245085.

HOGENOM

HOG000230988.

HOVERGEN

HBG107486.

InParanoid

P42230.

K11223.

OrthoDB

EOG457560.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.

Gene expression databases

ArrayExpress

P42230.

Bgee

P42230.

Genevestigator

P42230.

GermOnline

ENSMUSG00000004043. 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

ChEMBL

CHEMBL5513.

EvolutionaryTrace

P42230.

NextBio

299635.

SOURCE

Search...

Entry information

Entry name

STA5A_MOUSE

Accession

Primary (citable) accession number: P42230

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents