Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O02799 (STAT2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal transducer and activator of transcription 2
Gene names
Name:STAT2
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length864 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Signal transducer and activator of transcription that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state By similarity.

Subunit structure

Heterodimer with STAT1 upon IFN-alpha/beta induced phosphorylation. The heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9; interacts with IRF9 in the cytoplasm. Interacts with CRSP2 and CRSP6. Can form a homodimer upon IFN-alpha induced phosphorylation. Interacts with IFNAR1; the interaction requires the phosphorylation of IFNAR1 at 'Tyr-467'. Interacts with IFNAR2. Interacts with ARL2BP By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Translocated into the nucleus upon activation by IFN-alpha/beta By similarity.

Post-translational modification

Tyrosine phosphorylated in response to IFN-alpha By similarity.

Sequence similarities

Belongs to the transcription factor STAT family.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainSH2 domain
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtranscription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 864864Signal transducer and activator of transcription 2
PRO_0000182415

Regions

Domain572 – 66796SH2

Amino acid modifications

Modified residue2831Phosphoserine By similarity
Modified residue6901Phosphotyrosine; by JAK By similarity

Sequences

Sequence LengthMass (Da)Tools
O02799 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 2F8CC95569FB5B20

FASTA86499,061
        10         20         30         40         50         60 
MAQWEMLQNL DSPFQDQLHQ LYSESLLPVD VRQYLAVWIE DQNWQEAALG NDDSKANMLF 

        70         80         90        100        110        120 
FHFLDQLNYD CGRCGQDPEC LLLQHNLRKF YRDIQAIPQG PTRLAEMIFN LLLEEKRILI 

       130        140        150        160        170        180 
QAQRAQLEQQ EPALEAPGEN QQHEIESRIL ELRAMMEKLV KSISQLKDQQ DIFCFRYKIK 

       190        200        210        220        230        240 
ASAKTHSLDP HRTRQEQVLQ ETLNELDKRR KEVLDASKAL LGRLTTLIEL LLPKLEEWKV 

       250        260        270        280        290        300 
QQQKACIGAP MDGELEQLEK WFTAEAKLLF HLRQLLKELK GLSSVVKYDE DLLFKGVDLL 

       310        320        330        340        350        360 
KAQVTELLQR LLHRAFIVET QPCMPQTPHR PLILKTGSKF TVRTRLLVRL QEGNESLTAE 

       370        380        390        400        410        420 
VSIDRNPPKS QGFRKFNILT SNRKTLTPEK GQSQGLIWDF GYLTLMEQRS GGAGKGNNKG 

       430        440        450        460        470        480 
PLGVTEELHI ISFTVKYTYQ GLKQELTTDT LPVVIISNMN QLSIAWASIL WFNLLSSDPQ 

       490        500        510        520        530        540 
NQQFFSSPPK APWNLLGPAL SWQFSSHVGQ GLNSDQLGML RDKLFGQNSS TEGLSLSWVD 

       550        560        570        580        590        600 
FIKRESPPGK LPFWTWLDKI LDLVHDHLKD LWKDGHIMGF VSRSEERRLL KKTISGTFLL 

       610        620        630        640        650        660 
RFSETLEGGI TCSWVEHQDD DKVLIYSLQP FTKEVLQSLP LTKIISQYQL LTEENIPENP 

       670        680        690        700        710        720 
LRFLYPRIPR DEAFGCYNQE KANLQERKKY LKHKLIVVSN RQVDELQQPP ELKLEPDLES 

       730        740        750        760        770        780 
LELDLGLAPG PEPGVGLDLE PLLEAGLDLG PELEPMLQST LEPVLEPILD EVLQGVPEPN 

       790        800        810        820        830        840 
LGPELKLEPI LEPVSQPVPE PDLPHDLRHL NTDEMQIFRN SMRIEEIMPN GDPLLASQNT 

       850        860 
NVDEACVFHR SHFYTDGPLI PSDY 

« Hide

References

[1]Ito Y., Mikawa S., Kobayashi E., Wada Y., Minezawa M.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB004061 mRNA. Translation: BAA20332.1.
RefSeqNP_999054.1. NM_213889.1.
UniGeneSsc.14520.

3D structure databases

ProteinModelPortalO02799.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000000422.

Proteomic databases

PaxDbO02799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396923.
KEGGssc:396923.

Organism-specific databases

CTD6773.

Phylogenomic databases

eggNOGNOG303257.
HOGENOMHOG000220792.
HOVERGENHBG055669.
KOK11221.

Family and domain databases

Gene3D1.10.238.10. 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.
InterProIPR011992. EF-hand-dom_pair.
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR001217. STAT.
IPR022756. STAT2_C.
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]
PANTHERPTHR11801. PTHR11801. 1 hit.
PfamPF00017. SH2. 1 hit.
PF12188. STAT2_C. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view]
SMARTSM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]
SUPFAMSSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSTAT2_PIG
AccessionPrimary (citable) accession number: O02799
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families