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Protein

Signal transducer and activator of transcription 5A

Gene

Stat5a

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. 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.2 Publications

GO - Molecular functioni

  • DNA binding Source: MGI
  • protein phosphatase binding Source: UniProtKB
  • RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  • signal transducer activity Source: MGI
  • transcription factor activity, sequence-specific DNA binding Source: InterPro

GO - Biological processi

  • 2-oxoglutarate metabolic process Source: BHF-UCL
  • allantoin metabolic process Source: BHF-UCL
  • cellular response to cytokine stimulus Source: MGI
  • cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: MGI
  • cellular response to organic cyclic compound Source: MGI
  • citrate metabolic process Source: BHF-UCL
  • creatine metabolic process Source: BHF-UCL
  • creatinine metabolic process Source: BHF-UCL
  • cytokine-mediated signaling pathway Source: MGI
  • development of secondary female sexual characteristics Source: MGI
  • development of secondary male sexual characteristics Source: MGI
  • epithelial cell differentiation involved in prostate gland development Source: MGI
  • fatty acid metabolic process Source: BHF-UCL
  • female pregnancy Source: MGI
  • isoleucine metabolic process Source: BHF-UCL
  • JAK-STAT cascade Source: MGI
  • JAK-STAT cascade involved in growth hormone signaling pathway Source: BHF-UCL
  • lactation Source: MGI
  • lipid storage Source: MGI
  • luteinization Source: MGI
  • mammary gland development Source: MGI
  • mammary gland epithelium development Source: MGI
  • natural killer cell differentiation Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of erythrocyte differentiation Source: MGI
  • negative regulation of mast cell apoptotic process Source: MGI
  • oxaloacetate metabolic process Source: BHF-UCL
  • peptidyl-tyrosine phosphorylation Source: MGI
  • Peyer's patch development Source: MGI
  • positive regulation of activated T cell proliferation Source: MGI
  • positive regulation of B cell differentiation Source: MGI
  • positive regulation of blood vessel endothelial cell migration Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of endothelial cell proliferation Source: MGI
  • positive regulation of gamma-delta T cell differentiation Source: MGI
  • positive regulation of inflammatory response Source: MGI
  • positive regulation of interleukin-2 biosynthetic process Source: MGI
  • positive regulation of lymphocyte differentiation Source: MGI
  • positive regulation of mast cell differentiation Source: MGI
  • positive regulation of mast cell proliferation Source: MGI
  • positive regulation of mitotic cell cycle Source: MGI
  • positive regulation of multicellular organism growth Source: MGI
  • positive regulation of natural killer cell differentiation Source: MGI
  • positive regulation of natural killer cell mediated cytotoxicity Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • prolactin signaling pathway Source: UniProtKB
  • prostate gland epithelium morphogenesis Source: MGI
  • regulation of cell adhesion Source: MGI
  • regulation of epithelial cell differentiation Source: MGI
  • regulation of multicellular organism growth Source: BHF-UCL
  • regulation of steroid metabolic process Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • response to peptide hormone Source: MGI
  • succinate metabolic process Source: BHF-UCL
  • taurine metabolic process Source: BHF-UCL
  • T cell differentiation in thymus Source: MGI
  • T cell homeostasis Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
  • valine metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Lactation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1251985. Nuclear signaling by ERBB4.
R-MMU-1266695. Interleukin-7 signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-186763. Downstream signal transduction.
R-MMU-2586551. Signaling by Leptin.
R-MMU-2586552. Signaling by Leptin.
R-MMU-451927. Interleukin-2 signaling.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-982772. Growth hormone receptor signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription 5A
Alternative name(s):
Mammary gland factor
Gene namesi
Name:Stat5a
Synonyms:Mgf, Mpf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:103036. Stat5a.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5513.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001824241 – 793Signal transducer and activator of transcription 5AAdd BLAST793

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei90PhosphotyrosineBy similarity1
Modified residuei128PhosphoserineBy similarity1
Modified residuei682PhosphotyrosineBy similarity1
Modified residuei694PhosphotyrosineCombined sources1
Modified residuei779PhosphoserineBy similarity1

Post-translational modificationi

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. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates prolactin signaling pathway (By similarity).By similarity
ISGylated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP42230.
PaxDbiP42230.
PeptideAtlasiP42230.
PRIDEiP42230.

PTM databases

iPTMnetiP42230.
PhosphoSitePlusiP42230.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiENSMUSG00000004043.
ExpressionAtlasiP42230. baseline and differential.
GenevisibleiP42230. MM.

Interactioni

Subunit structurei

Forms a homodimer or a heterodimer with a related family member. Interacts with NCOA1 and SOCS7 (By similarity). Binds NR3C1. Interacts with ERBB4.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGAP2Q99490-22EBI-617434,EBI-7737644From a different organism.
GHRP199413EBI-617434,EBI-7526279From a different organism.

GO - Molecular functioni

  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi203525. 13 interactors.
DIPiDIP-897N.
IntActiP42230. 7 interactors.
MINTiMINT-2576471.
STRINGi10090.ENSMUSP00000102980.

Structurei

Secondary structure

1793
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi144 – 181Combined sources38
Turni182 – 190Combined sources9
Turni196 – 198Combined sources3
Helixi199 – 249Combined sources51
Helixi251 – 262Combined sources12
Turni263 – 265Combined sources3
Helixi273 – 300Combined sources28
Helixi309 – 330Combined sources22
Beta strandi332 – 336Combined sources5
Beta strandi340 – 345Combined sources6
Beta strandi348 – 355Combined sources8
Turni356 – 361Combined sources6
Beta strandi368 – 375Combined sources8
Helixi376 – 383Combined sources8
Beta strandi404 – 406Combined sources3
Turni407 – 410Combined sources4
Beta strandi411 – 413Combined sources3
Beta strandi415 – 419Combined sources5
Helixi435 – 437Combined sources3
Beta strandi439 – 449Combined sources11
Beta strandi451 – 454Combined sources4
Beta strandi456 – 462Combined sources7
Beta strandi466 – 469Combined sources4
Helixi475 – 488Combined sources14
Beta strandi500 – 503Combined sources4
Helixi504 – 519Combined sources16
Helixi527 – 538Combined sources12
Helixi545 – 550Combined sources6
Beta strandi552 – 554Combined sources3
Helixi555 – 559Combined sources5
Beta strandi566 – 569Combined sources4
Helixi570 – 584Combined sources15
Helixi586 – 591Combined sources6
Helixi600 – 608Combined sources9
Beta strandi615 – 620Combined sources6
Beta strandi626 – 631Combined sources6
Beta strandi641 – 646Combined sources6
Helixi648 – 653Combined sources6
Helixi656 – 662Combined sources7
Helixi675 – 679Combined sources5
Turni680 – 682Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y1UX-ray3.21A/B/C128-712[»]
ProteinModelPortaliP42230.
SMRiP42230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42230.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini589 – 686SH2PROSITE-ProRule annotationAdd BLAST98

Sequence similaritiesi

Belongs to the transcription factor STAT family.Curated
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiKOG3667. Eukaryota.
ENOG410XPN8. LUCA.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000230988.
HOVERGENiHBG107486.
InParanoidiP42230.
KOiK11223.
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. 2 hits.
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.

P42230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN
60 70 80 90 100
PQDRGQATQL LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR
110 120 130 140 150
CPMELVRCIR HILYNEQRLV REANNCSSPA GVLVDAMSQK HLQINQRFEE
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 ECSGEILNNC
410 420 430 440 450
CVMEYHQATG TLSAHFRNMS LKRIKRADRR GAESVTEEKF TVLFESQFSV
460 470 480 490 500
GSNELVFQVK TLSLPVVVIV HGSQDHNATA TVLWDNAFAE PGRVPFAVPD
510 520 530 540 550
KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNI SSNHLEDYNS
560 570 580 590 600
MSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK
610 620 630 640 650
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPDRNL WNLKPFTTRD
660 670 680 690 700
FSIRSLADRL GDLNYLIYVF PDRPKDEVFA KYYTPVLAKA VDGYVKPQIK
710 720 730 740 750
QVVPEFVNAS TDAGASATYM DQAPSPVVCP QPHYNMYPPN PDPVLDQDGE
760 770 780 790
FDLDESMDVA RHVEELLRRP MDSLDARLSP PAGLFTSARS SLS
Length:793
Mass (Da):90,831
Last modified:November 1, 1995 - v1
Checksum:i7C66E435C37624DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48538 mRNA. Translation: CAA88419.1.
U21103 mRNA. Translation: AAA80590.1.
U36502 mRNA. Translation: AAA78945.1.
CCDSiCCDS25439.1.
PIRiS54772.
RefSeqiNP_035618.1. NM_011488.3.
XP_006532784.1. XM_006532721.1.
XP_006532785.1. XM_006532722.1.
XP_017169891.1. XM_017314402.1.
UniGeneiMm.277403.

Genome annotation databases

EnsembliENSMUST00000004145; ENSMUSP00000004145; ENSMUSG00000004043.
ENSMUST00000107356; ENSMUSP00000102979; ENSMUSG00000004043.
GeneIDi20850.
KEGGimmu:20850.
UCSCiuc007lml.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48538 mRNA. Translation: CAA88419.1.
U21103 mRNA. Translation: AAA80590.1.
U36502 mRNA. Translation: AAA78945.1.
CCDSiCCDS25439.1.
PIRiS54772.
RefSeqiNP_035618.1. NM_011488.3.
XP_006532784.1. XM_006532721.1.
XP_006532785.1. XM_006532722.1.
XP_017169891.1. XM_017314402.1.
UniGeneiMm.277403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y1UX-ray3.21A/B/C128-712[»]
ProteinModelPortaliP42230.
SMRiP42230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203525. 13 interactors.
DIPiDIP-897N.
IntActiP42230. 7 interactors.
MINTiMINT-2576471.
STRINGi10090.ENSMUSP00000102980.

Chemistry databases

ChEMBLiCHEMBL5513.

PTM databases

iPTMnetiP42230.
PhosphoSitePlusiP42230.

Proteomic databases

EPDiP42230.
PaxDbiP42230.
PeptideAtlasiP42230.
PRIDEiP42230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004145; ENSMUSP00000004145; ENSMUSG00000004043.
ENSMUST00000107356; ENSMUSP00000102979; ENSMUSG00000004043.
GeneIDi20850.
KEGGimmu:20850.
UCSCiuc007lml.2. mouse.

Organism-specific databases

CTDi6776.
MGIiMGI:103036. Stat5a.

Phylogenomic databases

eggNOGiKOG3667. Eukaryota.
ENOG410XPN8. LUCA.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000230988.
HOVERGENiHBG107486.
InParanoidiP42230.
KOiK11223.
TreeFamiTF318648.

Enzyme and pathway databases

ReactomeiR-MMU-1251985. Nuclear signaling by ERBB4.
R-MMU-1266695. Interleukin-7 signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-186763. Downstream signal transduction.
R-MMU-2586551. Signaling by Leptin.
R-MMU-2586552. Signaling by Leptin.
R-MMU-451927. Interleukin-2 signaling.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-982772. Growth hormone receptor signaling.

Miscellaneous databases

EvolutionaryTraceiP42230.
PROiP42230.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004043.
ExpressionAtlasiP42230. baseline and differential.
GenevisibleiP42230. MM.

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. 2 hits.
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...

Entry informationi

Entry nameiSTA5A_MOUSE
AccessioniPrimary (citable) accession number: P42230
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 169 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.