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

P52630 (STAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal transducer and activator of transcription 2
Alternative name(s):
p113
Gene names
Name:STAT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length851 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.10

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-466'. Interacts with IFNAR2. Interacts with ARL2BP. Interacts with dengue virus NS5; this interaction inhibits the phosphorylation of STAT2, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation. Interacts with human cytomegalovirus/HHV-5 protein UL123; this interaction promotes viral growth. Interacts with Simian virus 5 protein V and rabies virus phosphoprotein. Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Cytoplasm. Nucleus. Note: Translocated into the nucleus upon activation by IFN-alpha/beta. Ref.13 Ref.20

Post-translational modification

Tyrosine phosphorylated in response to IFN-alpha. Phosphorylation at Ser-287 negatively regulates the transcriptional response. Ref.7 Ref.8 Ref.11 Ref.20

Sequence similarities

Belongs to the transcription factor STAT family.

Contains 1 SH2 domain.

Sequence caution

The sequence AAB36226.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAB36227.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processAntiviral defense
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH2 domain
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Traceable author statement Ref.10. Source: ProtInc

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.10. Source: ProtInc

regulation of type I interferon-mediated signaling pathway

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

type I interferon signaling pathway

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: InterPro

identical protein binding

Inferred from physical interaction PubMed 8605877. Source: IntAct

protein binding

Inferred from physical interaction PubMed 12220192PubMed 15825084Ref.15PubMed 17923090PubMed 18579593PubMed 21903422PubMed 24065129PubMed 8605876PubMed 8605877PubMed 9677371. Source: IntAct

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

signal transducer activity

Traceable author statement Ref.10. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P52630-3)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P52630-4)

The sequence of this isoform differs from the canonical sequence as follows:
     96-99: Missing.
Note: No experimental confirmation available. May be due to competing acceptor splice site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 851851Signal transducer and activator of transcription 2
PRO_0000182413

Regions

Domain572 – 66796SH2

Amino acid modifications

Modified residue2831Phosphoserine Ref.20
Modified residue2871Phosphoserine Ref.20
Modified residue2941Phosphothreonine Ref.20
Modified residue6901Phosphotyrosine; by JAK Ref.8 Ref.11

Natural variations

Alternative sequence96 – 994Missing in isoform 2.
VSP_046705
Natural variant661Q → H.
Corresponds to variant rs2066816 [ dbSNP | Ensembl ].
VAR_014896
Natural variant2201L → P.
Corresponds to variant rs2066817 [ dbSNP | Ensembl ].
VAR_014897
Natural variant2461C → S.
Corresponds to variant rs2228259 [ dbSNP | Ensembl ].
VAR_052072
Natural variant4481T → M. Ref.3
Corresponds to variant rs2066815 [ dbSNP | Ensembl ].
VAR_014898
Natural variant4641I → V. Ref.3
Corresponds to variant rs2066811 [ dbSNP | Ensembl ].
VAR_014899
Natural variant5011S → I.
Corresponds to variant rs2066809 [ dbSNP | Ensembl ].
VAR_014900
Natural variant5941M → I. Ref.3
Corresponds to variant rs2066807 [ dbSNP | Ensembl ].
VAR_014901
Natural variant8261Q → H. Ref.3
Corresponds to variant rs2229363 [ dbSNP | Ensembl ].
VAR_019213

Experimental info

Mutagenesis3741R → A: Prevents the nuclear import; when associated with A-375. Ref.13
Mutagenesis3751K → A: Prevents the nuclear import; when associated with A-374. Ref.13
Mutagenesis4091R → A: Prevents the nuclear import; when associated with A-415. Ref.13
Mutagenesis4151K → A: Prevents the nuclear import; when associated with A-409. Ref.13
Mutagenesis6901Y → F: Reduces phosphorylation of STAT1 in response to IFN-ALPHA. Ref.8
Sequence conflict2401A → T in BAG59489. Ref.4

Secondary structure

........... 851
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E4C74674CB7A3215

FASTA85197,916
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 3587443D40AF5E5B
Show »

FASTA84797,457

References

« Hide 'large scale' references
[1]"The proteins of ISGF-3, the interferon alpha-induced transcriptional activator, define a gene family involved in signal transduction."
Fu X.-Y., Schindler C., Improta T., Aebersold R., Darnell J.E. Jr.
Proc. Natl. Acad. Sci. U.S.A. 89:7840-7843(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]"The genomic structure of the STAT genes: multiple exons in coincident sites in Stat1 and Stat2."
Yan R., Qureshi S., Zhong Z., Wen Z., Darnell J.E. Jr.
Nucleic Acids Res. 23:459-463(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]NIEHS SNPs program
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-448; VAL-464; ILE-594 AND HIS-826.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Tongue.
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[7]"A transcription factor with SH2 and SH3 domains is directly activated by an interferon alpha-induced cytoplasmic protein tyrosine kinase(s)."
Fu X.Y.
Cell 70:323-335(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION IN RESPONSE TO IFN-ALPHA.
[8]"Role of STAT2 in the alpha interferon signaling pathway."
Leung S., Qureshi S.A., Kerr I.M., Darnell J.E. Jr., Stark G.R.
Mol. Cell. Biol. 15:1312-1317(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-690, MUTAGENESIS OF TYR-690.
[9]"Identification of alternative splicing form of Stat2."
Sugiyama T., Nishio Y., Kishimoto T., Akira S.
FEBS Lett. 381:191-194(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL ALTERNATIVE SPLICING.
[10]"Stat2 is a transcriptional activator that requires sequence-specific contacts provided by stat1 and p48 for stable interaction with DNA."
Bluyssen H.A., Levy D.E.
J. Biol. Chem. 272:4600-4605(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[11]"Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling."
Li X., Leung S., Kerr I.M., Stark G.R.
Mol. Cell. Biol. 17:2048-2056(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IFNAR1 AND IFNAR2, PHOSPHORYLATION AT TYR-690.
[12]"Viral inhibition of interferon signal transduction."
Cebulla C.M., Miller D.M., Sedmak D.D.
Intervirology 42:325-330(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Arginine/lysine-rich structural element is involved in interferon-induced nuclear import of STATs."
Melen K., Kinnunen L., Julkunen I.
J. Biol. Chem. 276:16447-16455(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-374; LYS-375; ARG-409 AND LYS-415.
[14]"Role of metazoan mediator proteins in interferon-responsive transcription."
Lau J.F., Nusinzon I., Burakov D., Freedman L.P., Horvath C.M.
Mol. Cell. Biol. 23:620-628(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRSP2 AND CRSP6.
[15]"Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1."
Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S., Randall R.E.
J. Virol. 79:13434-13441(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIMIAN VIRUS 5 PROTEIN V.
[16]"Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO."
Huh Y.H., Kim Y.E., Kim E.T., Park J.J., Song M.J., Zhu H., Hayward G.S., Ahn J.H.
J. Virol. 82:10444-10454(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 PROTEIN UL123.
[17]"NS5 of dengue virus mediates STAT2 binding and degradation."
Ashour J., Laurent-Rolle M., Shi P.Y., Garcia-Sastre A.
J. Virol. 83:5408-5418(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DENGUE VIRUS NS5.
[18]"Dengue virus NS5 inhibits interferon-alpha signaling by blocking signal transducer and activator of transcription 2 phosphorylation."
Mazzon M., Jones M., Davidson A., Chain B., Jacobs M.
J. Infect. Dis. 200:1261-1270(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DENGUE VIRUS NS5.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Identification of STAT2 serine 287 as a novel regulatory phosphorylation site in type I interferon-induced cellular responses."
Steen H.C., Nogusa S., Thapa R.J., Basagoudanavar S.H., Gill A.L., Merali S., Barrero C.A., Balachandran S., Gamero A.M.
J. Biol. Chem. 288:747-758(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-283; SER-287 AND THR-294, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97934 mRNA. No translation available.
U18671 Genomic DNA. Translation: AAA98760.1.
S81491 Genomic DNA. Translation: AAB36226.1. Sequence problems.
S81491 Genomic DNA. Translation: AAB36227.1. Sequence problems.
AY525126 Genomic DNA. Translation: AAS00091.1.
AK296939 mRNA. Translation: BAG59489.1.
AC025574 Genomic DNA. No translation available.
BC051284 mRNA. Translation: AAH51284.1.
CCDSCCDS55836.1. [P52630-4]
CCDS8917.1. [P52630-3]
PIRA46160.
RefSeqNP_005410.1. NM_005419.3. [P52630-3]
NP_938146.1. NM_198332.1. [P52630-4]
UniGeneHs.530595.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KA4NMR-B786-838[»]
ProteinModelPortalP52630.
SMRP52630. Positions 2-699, 783-838.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112650. 21 interactions.
DIPDIP-38511N.
IntActP52630. 21 interactions.
MINTMINT-1526706.
STRING9606.ENSP00000315768.

PTM databases

PhosphoSiteP52630.

Polymorphism databases

DMDM1711552.

Proteomic databases

MaxQBP52630.
PaxDbP52630.
PeptideAtlasP52630.
PRIDEP52630.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314128; ENSP00000315768; ENSG00000170581. [P52630-3]
ENST00000557235; ENSP00000450751; ENSG00000170581. [P52630-4]
GeneID6773.
KEGGhsa:6773.
UCSCuc001slc.3. human. [P52630-3]

Organism-specific databases

CTD6773.
GeneCardsGC12M056735.
HGNCHGNC:11363. STAT2.
HPACAB003858.
HPA018888.
MIM600556. gene.
neXtProtNX_P52630.
PharmGKBPA36184.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303257.
HOGENOMHOG000220792.
HOVERGENHBG055669.
InParanoidP52630.
KOK11221.
OMAAFGRYYQ.
OrthoDBEOG71K62B.
PhylomeDBP52630.
TreeFamTF318648.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP52630.

Gene expression databases

ArrayExpressP52630.
BgeeP52630.
CleanExHS_STAT2.
GenevestigatorP52630.

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...

Other

ChiTaRSSTAT2. human.
EvolutionaryTraceP52630.
GeneWikiSTAT2.
GenomeRNAi6773.
NextBio26434.
PROP52630.
SOURCESearch...

Entry information

Entry nameSTAT2_HUMAN
AccessionPrimary (citable) accession number: P52630
Secondary accession number(s): B4DLC7 expand/collapse secondary AC list , G3V2M6, Q16430, Q16431, Q9UDL4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM