[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. DOI=10.1073/pnas.89.16.7840; PubMed=1502204 [NCBI, ExPASy, EBI, Israel, Japan] Fu X.-Y., Schindler C., Improta T., Aebersold R., Darnell J.E. Jr.; "The proteins of ISGF-3, the interferon alpha-induced transcriptional activator, define a gene family involved in signal transduction."; Proc. Natl. Acad. Sci. U.S.A. 89:7840-7843(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/23.3.459; PubMed=7885841 [NCBI, ExPASy, EBI, Israel, Japan] Yan R., Qureshi S., Zhong Z., Wen Z., Darnell J.E. Jr.; "The genomic structure of the STAT genes: multiple exons in coincident sites in Stat1 and Stat2."; Nucleic Acids Res. 23:459-463(1995).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-448; VAL-464; ILE-594 AND HIS-826. NIEHS SNPs program; Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	ALTERNATIVE SPLICING. DOI=10.1016/0014-5793(96)00121-4; PubMed=8601453 [NCBI, ExPASy, EBI, Israel, Japan] Sugiyama T., Nishio Y., Kishimoto T., Akira S.; "Identification of alternative splicing form of Stat2."; FEBS Lett. 381:191-194(1996).
[6]	CHARACTERIZATION. DOI=10.1074/jbc.272.7.4600; PubMed=9020188 [NCBI, ExPASy, EBI, Israel, Japan] Bluyssen H.A., Levy D.E.; "Stat2 is a transcriptional activator that requires sequence-specific contacts provided by stat1 and p48 for stable interaction with DNA."; J. Biol. Chem. 272:4600-4605(1997).
[7]	REVIEW. DOI=10.1159/000053968; PubMed=10702714 [NCBI, ExPASy, EBI, Israel, Japan] Cebulla C.M., Miller D.M., Sedmak D.D.; "Viral inhibition of interferon signal transduction."; Intervirology 42:325-330(1999).
[8]	SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-374; LYS-375; ARG-409 AND LYS-415. DOI=10.1074/jbc.M008821200; PubMed=11150296 [NCBI, ExPASy, EBI, Israel, Japan] Melen K., Kinnunen L., Julkunen I.; "Arginine/lysine-rich structural element is involved in interferon-induced nuclear import of STATs."; J. Biol. Chem. 276:16447-16455(2001).
[9]	INTERACTION WITH CRSP2 AND CRSP6. DOI=10.1128/MCB.23.2.620-628.2003; PubMed=12509459 [NCBI, ExPASy, EBI, Israel, Japan] Lau J.F., Nusinzon I., Burakov D., Freedman L.P., Horvath C.M.; "Role of metazoan mediator proteins in interferon-responsive transcription."; Mol. Cell. Biol. 23:620-628(2003).
[10]	INTERACTION WITH SIMIAN VIRUS 5 PROTEIN V. DOI=10.1128/JVI.79.21.13434-13441.2005; PubMed=16227264 [NCBI, ExPASy, EBI, Israel, Japan] Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S., Randall R.E.; "Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1."; J. Virol. 79:13434-13441(2005).
[11]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

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 ISGF3G/IRF-9 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.
SUBUNIT: Interacts with ISGF3G/IRF-9 in the cytoplasm. Heterodimer with STAT1 upon IFN-alpha/beta induced phosphorylation. Interacts with CRSP2 and CRSP6. Interacts with Simian virus 5 protein V and rabies virus phosphoprotein (By similarity).
INTERACTION:
P48551:IFNAR2; NbExp=2; IntAct=EBI-1546963, EBI-958408;
Q00978:IRF9; NbExp=3; IntAct=EBI-1546963, EBI-626526;
P42224:STAT1; NbExp=3; IntAct=EBI-1546963, EBI-1057697;
P40763:STAT3; NbExp=1; IntAct=EBI-1546963, EBI-518675;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the nucleus upon activation by IFN-alpha/beta.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	Long
Isoform ID	P52630-1
This is the isoform sequence displayed in this entry.

Name	Short
Isoform ID	P52630-2
Features which should be applied to build the isoform sequence: VSP_006283, VSP_006284.

PTM: Tyrosine phosphorylated in response to IFN-alpha.
SIMILARITY: Belongs to the transcription factor STAT family.
SIMILARITY: Contains 1 SH2 domain.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/stat2/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M97934; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]
U18671; AAA98760.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S81491; AAB36226.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S81491; AAB36227.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY525126; AAS00091.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC051284; AAH51284.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00004312; -.
IPI00219076; -.

A46160; A46160.

NP_005410.1; -.

3D structure databases

PDB

2KA4; NMR; -; B=786-838.

[ExPASy / RCSB / EBI]

PDBsum

2KA4; -.

ModBase

P52630.

Protein-protein interaction databases

IntAct

P52630; 4.

PTM databases

PhosphoSite

P52630; -.

Enzyme and pathway databases

Pathway_Interaction_DB

il27pathway; IL27-mediated signaling events.

Organism-specific databases

GC12M055021; -.

HIX0022259; -.

HGNC:11363; STAT2.

CAB003858; -.

600556; gene. [NCBI / EBI]

PharmGKB

PA36184; -.

Gene expression databases

P52630; -.

P52630; -.

HS_STAT2; -.

ENSG00000170581; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0005062;	Molecular function: hematopoietin/interferon-class (D200-domain) cytokine receptor signal transducer activity (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003700;	Molecular function: transcription factor activity (inferred from electronic annotation from InterPro).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0007259;	Biological process: JAK-STAT cascade (traceable author statement from ProtInc).
GO:0006357;	Biological process: regulation of transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
GO:0009615;	Biological process: response to virus (inferred from electronic annotation from UniProtKB-KW).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:1.10.238.10; EF-Hand_type; 1.
G3DSA:3.30.505.10; SH2; 1.
G3DSA:1.20.1050.20; STAT_alpha; 1.
G3DSA:2.60.40.630; STAT_DNA_bd_sub; 1.
G3DSA:1.10.532.10; STAT_protein_interaction; 1.

PANTHER

PTHR11801; STAT; 1.

Pfam

PF00017; SH2; 1.
PF01017; STAT_alpha; 1.
PF02864; STAT_bind; 1.
PF02865; STAT_int; 1.
Pfam graphical view of domain structure.

ProDom

PD000093; SH2; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00252; SH2; 1.
SMART graphical view of domain structure.

PROSITE

PS50001; SH2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

P52630; -.

PRIDE

P52630; -.

Genome annotation databases

Ensembl

ENSG00000170581; Homo sapiens. [Contig view]

GeneID

6773; -.

KEGG

hsa:6773; -.

Phylogenomic databases

HOGENOM

P52630; -.

HOVERGEN

P52630; -.

OMA

P52630; PFQDQLH.

Other

26434; -.

STAT2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Activator; Alternative splicing; Antiviral defense; Cytoplasm; Direct protein sequencing; DNA-binding; Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism; SH2 domain; Transcription; Transcription regulation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 851`	`851`	`Signal transducer and activator of transcription 2.`	`PRO_0000182413`
`DOMAIN`	`572 667`	`96`	`SH2.`
`MOD_RES`	`690 690`		`Phosphotyrosine; by JAK (By similarity).`
`VAR_SEQ`	`621 652`		`DKVLIYSVQPYTKEVLQSLPLTEIIRHYQLLT -> GQLLCPAIPTASPFCLAPLLPLCLPLASLALN (in isoform Short).`	`VSP_006283`
`VAR_SEQ`	`653 851`		`Missing (in isoform Short).`	`VSP_006284`
`VARIANT`	`66 66`	`1`	`Q -> H (in dbSNP:rs2066816 [NCBI]).`	`VAR_014896`
`VARIANT`	`220 220`	`1`	`L -> P (in dbSNP:rs2066817 [NCBI]).`	`VAR_014897`
`VARIANT`	`246 246`	`1`	`C -> S (in dbSNP:rs2228259 [NCBI]).`	`VAR_052072`
`VARIANT`	`448 448`	`1`	`T -> M (in dbSNP:rs2066815 [NCBI]).`	`VAR_014898`
`VARIANT`	`464 464`	`1`	`I -> V (in dbSNP:rs2066811 [NCBI]).`	`VAR_014899`
`VARIANT`	`501 501`	`1`	`S -> I (in dbSNP:rs2066809 [NCBI]).`	`VAR_014900`
`VARIANT`	`594 594`	`1`	`M -> I (in dbSNP:rs2066807 [NCBI]).`	`VAR_014901`
`VARIANT`	`826 826`	`1`	`Q -> H (in dbSNP:rs2229363 [NCBI]).`	`VAR_019213`
`MUTAGEN`	`374 374`		`R->A: Prevents the nuclear import; when associated with A-375.`
`MUTAGEN`	`375 375`		`K->A: Prevents the nuclear import; when associated with A-374.`
`MUTAGEN`	`409 409`		`R->A: Prevents the nuclear import; when associated with A-415.`
`MUTAGEN`	`415 415`		`K->A: Prevents the nuclear import; when associated with A-409.`

Sequence information

Length: 851 AA [This is the length of the unprocessed precursor]

Molecular weight: 97916 Da [This is the MW of the unprocessed precursor]

CRC64: E4C74674CB7A3215 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQWEMLQNL DSPFQDQLHQ LYSHSLLPVD IRQYLAVWIE DQNWQEAALG SDDSKATMLF 

        70         80         90        100        110        120 
FHFLDQLNYE CGRCSQDPES LLLQHNLRKF CRDIQPFSQD PTQLAEMIFN LLLEEKRILI 

       130        140        150        160        170        180 
QAQRAQLEQG EPVLETPVES QQHEIESRIL DLRAMMEKLV KSISQLKDQQ DVFCFRYKIQ 

       190        200        210        220        230        240 
AKGKTPSLDP HQTKEQKILQ ETLNELDKRR KEVLDASKAL LGRLTTLIEL LLPKLEEWKA 

       250        260        270        280        290        300 
QQQKACIRAP IDHGLEQLET WFTAGAKLLF HLRQLLKELK GLSCLVSYQD DPLTKGVDLR 

       310        320        330        340        350        360 
NAQVTELLQR LLHRAFVVET QPCMPQTPHR PLILKTGSKF TVRTRLLVRL QEGNESLTVE 

       370        380        390        400        410        420 
VSIDRNPPQL QGFRKFNILT SNQKTLTPEK GQSQGLIWDF GYLTLVEQRS GGSGKGSNKG 

       430        440        450        460        470        480 
PLGVTEELHI ISFTVKYTYQ GLKQELKTDT LPVVIISNMN QLSIAWASVL WFNLLSPNLQ 

       490        500        510        520        530        540 
NQQFFSNPPK APWSLLGPAL SWQFSSYVGR GLNSDQLSML RNKLFGQNCR TEDPLLSWAD 

       550        560        570        580        590        600 
FTKRESPPGK LPFWTWLDKI LELVHDHLKD LWNDGRIMGF VSRSQERRLL KKTMSGTFLL 

       610        620        630        640        650        660 
RFSESSEGGI TCSWVEHQDD DKVLIYSVQP YTKEVLQSLP LTEIIRHYQL LTEENIPENP 

       670        680        690        700        710        720 
LRFLYPRIPR DEAFGCYYQE KVNLQERRKY LKHRLIVVSN RQVDELQQPL ELKPEPELES 

       730        740        750        760        770        780 
LELELGLVPE PELSLDLEPL LKAGLDLGPE LESVLESTLE PVIEPTLCMV SQTVPEPDQG 

       790        800        810        820        830        840 
PVSQPVPEPD LPCDLRHLNT EPMEIFRNCV KIEEIMPNGD PLLAGQNTVD EVYVSRPSHF 

       850 
YTDGPLMPSD F

P52630 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools