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P52630

- STAT2_HUMAN

UniProt

P52630 - STAT2_HUMAN

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Protein

Signal transducer and activator of transcription 2

Gene

STAT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. DNA binding Source: UniProtKB-KW
  3. identical protein binding Source: IntAct
  4. sequence-specific DNA binding transcription factor activity Source: InterPro
  5. signal transducer activity Source: ProtInc

GO - Biological processi

  1. cytokine-mediated signaling pathway Source: Reactome
  2. defense response to virus Source: UniProtKB-KW
  3. JAK-STAT cascade Source: ProtInc
  4. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  5. regulation of type I interferon-mediated signaling pathway Source: Reactome
  6. transcription, DNA-templated Source: UniProtKB-KW
  7. type I interferon signaling pathway Source: Reactome
  8. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Antiviral defense, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.
SignaLinkiP52630.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription 2
Alternative name(s):
p113
Gene namesi
Name:STAT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:11363. STAT2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi374 – 3741R → A: Prevents the nuclear import; when associated with A-375. 1 Publication
Mutagenesisi375 – 3751K → A: Prevents the nuclear import; when associated with A-374. 1 Publication
Mutagenesisi409 – 4091R → A: Prevents the nuclear import; when associated with A-415. 1 Publication
Mutagenesisi415 – 4151K → A: Prevents the nuclear import; when associated with A-409. 1 Publication
Mutagenesisi690 – 6901Y → F: Reduces phosphorylation of STAT1 in response to IFN-ALPHA. 1 Publication

Organism-specific databases

PharmGKBiPA36184.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 851851Signal transducer and activator of transcription 2PRO_0000182413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei283 – 2831Phosphoserine1 Publication
Modified residuei287 – 2871Phosphoserine1 Publication
Modified residuei294 – 2941Phosphothreonine1 Publication
Modified residuei690 – 6901Phosphotyrosine; by JAK2 Publications

Post-translational modificationi

Tyrosine phosphorylated in response to IFN-alpha. Phosphorylation at Ser-287 negatively regulates the transcriptional response.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP52630.
PaxDbiP52630.
PeptideAtlasiP52630.
PRIDEiP52630.

PTM databases

PhosphoSiteiP52630.

Expressioni

Gene expression databases

BgeeiP52630.
CleanExiHS_STAT2.
ExpressionAtlasiP52630. baseline and differential.
GenevestigatoriP52630.

Organism-specific databases

HPAiCAB003858.
HPA018888.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1546963,EBI-1546963
IFNAR1P171814EBI-1546963,EBI-1547250
IFNAR2P485512EBI-1546963,EBI-958408
IRF9Q009786EBI-1546963,EBI-626526
P/VP0C7744EBI-1546963,EBI-3650423From a different organism.
P/VP112072EBI-1546963,EBI-6148694From a different organism.
STAT1P4222414EBI-1546963,EBI-1057697

Protein-protein interaction databases

BioGridi112650. 23 interactions.
DIPiDIP-38511N.
IntActiP52630. 22 interactions.
MINTiMINT-1526706.
STRINGi9606.ENSP00000315768.

Structurei

Secondary structure

1
851
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi793 – 7964Combined sources
Helixi802 – 8065Combined sources
Turni812 – 8143Combined sources
Helixi824 – 8274Combined sources
Helixi831 – 8344Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KA4NMR-B786-838[»]
ProteinModelPortaliP52630.
SMRiP52630. Positions 2-699, 783-838.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52630.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini572 – 66796SH2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG303257.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000220792.
HOVERGENiHBG055669.
InParanoidiP52630.
KOiK11221.
OMAiAFGRYYQ.
OrthoDBiEOG71K62B.
PhylomeDBiP52630.
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.
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]
PANTHERiPTHR11801. PTHR11801. 1 hit.
PfamiPF00017. 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]
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P52630-3) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAQWEMLQNL DSPFQDQLHQ LYSHSLLPVD IRQYLAVWIE DQNWQEAALG
60 70 80 90 100
SDDSKATMLF FHFLDQLNYE CGRCSQDPES LLLQHNLRKF CRDIQPFSQD
110 120 130 140 150
PTQLAEMIFN LLLEEKRILI QAQRAQLEQG EPVLETPVES QQHEIESRIL
160 170 180 190 200
DLRAMMEKLV KSISQLKDQQ DVFCFRYKIQ AKGKTPSLDP HQTKEQKILQ
210 220 230 240 250
ETLNELDKRR KEVLDASKAL LGRLTTLIEL LLPKLEEWKA QQQKACIRAP
260 270 280 290 300
IDHGLEQLET WFTAGAKLLF HLRQLLKELK GLSCLVSYQD DPLTKGVDLR
310 320 330 340 350
NAQVTELLQR LLHRAFVVET QPCMPQTPHR PLILKTGSKF TVRTRLLVRL
360 370 380 390 400
QEGNESLTVE VSIDRNPPQL QGFRKFNILT SNQKTLTPEK GQSQGLIWDF
410 420 430 440 450
GYLTLVEQRS GGSGKGSNKG PLGVTEELHI ISFTVKYTYQ GLKQELKTDT
460 470 480 490 500
LPVVIISNMN QLSIAWASVL WFNLLSPNLQ NQQFFSNPPK APWSLLGPAL
510 520 530 540 550
SWQFSSYVGR GLNSDQLSML RNKLFGQNCR TEDPLLSWAD FTKRESPPGK
560 570 580 590 600
LPFWTWLDKI LELVHDHLKD LWNDGRIMGF VSRSQERRLL KKTMSGTFLL
610 620 630 640 650
RFSESSEGGI TCSWVEHQDD DKVLIYSVQP YTKEVLQSLP LTEIIRHYQL
660 670 680 690 700
LTEENIPENP LRFLYPRIPR DEAFGCYYQE KVNLQERRKY LKHRLIVVSN
710 720 730 740 750
RQVDELQQPL ELKPEPELES LELELGLVPE PELSLDLEPL LKAGLDLGPE
760 770 780 790 800
LESVLESTLE PVIEPTLCMV SQTVPEPDQG PVSQPVPEPD LPCDLRHLNT
810 820 830 840 850
EPMEIFRNCV KIEEIMPNGD PLLAGQNTVD EVYVSRPSHF YTDGPLMPSD

F
Length:851
Mass (Da):97,916
Last modified:October 1, 1996 - v1
Checksum:iE4C74674CB7A3215
GO
Isoform 2 (identifier: P52630-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:847
Mass (Da):97,457
Checksum:i3587443D40AF5E5B
GO

Sequence cautioni

The sequence AAB36226.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAB36227.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti240 – 2401A → T in BAG59489. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661Q → H.
Corresponds to variant rs2066816 [ dbSNP | Ensembl ].
VAR_014896
Natural varianti220 – 2201L → P.
Corresponds to variant rs2066817 [ dbSNP | Ensembl ].
VAR_014897
Natural varianti246 – 2461C → S.
Corresponds to variant rs2228259 [ dbSNP | Ensembl ].
VAR_052072
Natural varianti448 – 4481T → M.1 Publication
Corresponds to variant rs2066815 [ dbSNP | Ensembl ].
VAR_014898
Natural varianti464 – 4641I → V.1 Publication
Corresponds to variant rs2066811 [ dbSNP | Ensembl ].
VAR_014899
Natural varianti501 – 5011S → I.
Corresponds to variant rs2066809 [ dbSNP | Ensembl ].
VAR_014900
Natural varianti594 – 5941M → I.1 Publication
Corresponds to variant rs2066807 [ dbSNP | Ensembl ].
VAR_014901
Natural varianti826 – 8261Q → H.1 Publication
Corresponds to variant rs2229363 [ dbSNP | Ensembl ].
VAR_019213

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei96 – 994Missing in isoform 2. 1 PublicationVSP_046705

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS55836.1. [P52630-4]
CCDS8917.1. [P52630-3]
PIRiA46160.
RefSeqiNP_005410.1. NM_005419.3. [P52630-3]
NP_938146.1. NM_198332.1. [P52630-4]
UniGeneiHs.530595.

Genome annotation databases

EnsembliENST00000314128; ENSP00000315768; ENSG00000170581. [P52630-3]
ENST00000557235; ENSP00000450751; ENSG00000170581. [P52630-4]
GeneIDi6773.
KEGGihsa:6773.
UCSCiuc001slc.3. human. [P52630-3]

Polymorphism databases

DMDMi1711552.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS55836.1. [P52630-4 ]
CCDS8917.1. [P52630-3 ]
PIRi A46160.
RefSeqi NP_005410.1. NM_005419.3. [P52630-3 ]
NP_938146.1. NM_198332.1. [P52630-4 ]
UniGenei Hs.530595.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KA4 NMR - B 786-838 [» ]
ProteinModelPortali P52630.
SMRi P52630. Positions 2-699, 783-838.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112650. 23 interactions.
DIPi DIP-38511N.
IntActi P52630. 22 interactions.
MINTi MINT-1526706.
STRINGi 9606.ENSP00000315768.

PTM databases

PhosphoSitei P52630.

Polymorphism databases

DMDMi 1711552.

Proteomic databases

MaxQBi P52630.
PaxDbi P52630.
PeptideAtlasi P52630.
PRIDEi P52630.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314128 ; ENSP00000315768 ; ENSG00000170581 . [P52630-3 ]
ENST00000557235 ; ENSP00000450751 ; ENSG00000170581 . [P52630-4 ]
GeneIDi 6773.
KEGGi hsa:6773.
UCSCi uc001slc.3. human. [P52630-3 ]

Organism-specific databases

CTDi 6773.
GeneCardsi GC12M056735.
HGNCi HGNC:11363. STAT2.
HPAi CAB003858.
HPA018888.
MIMi 600556. gene.
neXtProti NX_P52630.
PharmGKBi PA36184.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG303257.
GeneTreei ENSGT00760000119236.
HOGENOMi HOG000220792.
HOVERGENi HBG055669.
InParanoidi P52630.
KOi K11221.
OMAi AFGRYYQ.
OrthoDBi EOG71K62B.
PhylomeDBi P52630.
TreeFami TF318648.

Enzyme and pathway databases

Reactomei REACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.
SignaLinki P52630.

Miscellaneous databases

ChiTaRSi STAT2. human.
EvolutionaryTracei P52630.
GeneWikii STAT2.
GenomeRNAii 6773.
NextBioi 26434.
PROi P52630.
SOURCEi Search...

Gene expression databases

Bgeei P52630.
CleanExi HS_STAT2.
ExpressionAtlasi P52630. baseline and differential.
Genevestigatori P52630.

Family and domain databases

Gene3Di 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.
InterProi IPR011992. 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 ]
PANTHERi PTHR11801. PTHR11801. 1 hit.
Pfami PF00017. 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 ]
SMARTi SM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view ]
SUPFAMi SSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiSTAT2_HUMAN
AccessioniPrimary (citable) accession number: P52630
Secondary accession number(s): B4DLC7
, G3V2M6, Q16430, Q16431, Q9UDL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3