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P42224 (STAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 177. 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 1-alpha/beta
Alternative name(s):
Transcription factor ISGF-3 components p91/p84
Gene names
Name:STAT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length750 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and 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 IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Ref.16 Ref.21 Ref.22 Ref.24 Ref.32

Subunit structure

Isoform alphahomodimerizes upon IFN-gamma induced phosphorylation. Heterodimer with STAT2 upon IFN-alpha/beta induced phosphorylation. The heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9. Interacts (phosphorylated at Ser 727) with PIAS1 (dimethylated on arginine); the interaction results in release of STAT1 from its target gene. Interacts with IFNAR1; the interaction requires the phosphorylation of IFNAR1 at 'Tyr-466'. Interacts with IFNAR2, NMI, PTK2/FAK1 and SRC. Interacts with ERBB4 (phosphorylated). Interacts with Sendai virus C', C, Y1 and Y2 proteins, Nipah virus P, V and W proteins, and rabies virus phosphoprotein preventing activation of ISRE and GAS promoter. Interacts with HCV core protein; the interaction results in STAT1 degradation. Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.26 Ref.29 Ref.30 Ref.34 Ref.44

Subcellular location

Cytoplasm. Nucleus. Note: Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to IFN-gamma and signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Ref.24

Post-translational modification

Phosphorylated on tyrosine and serine residues in response to a variety of cytokines/growth hormones including IFN-alpha, IFN-gamma, PDGF and EGF. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Upon EGF stimulation, phosphorylation on Tyr-701 (lacking in beta form) by JAK1, JAK2 or TYK2 promotes dimerization and subsequent translocation to the nucleus. Growth hormone (GH) activates STAT1 signaling only via JAK2. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylation on Ser-727 by several kinases including MAPK14, ERK1/2 and CAMKII on IFN-gamma stimulation, regulates STAT1 transcriptional activity. Phosphorylation on Ser-727 promotes sumoylation though increasing interaction with PIAS. Phosphorylation on Ser-727 by PRKCD induces apoptosis in response to DNA-damaging agents. Phosphorylated on tyrosine residues when PTK2/FAK1 is activated; most likely this is catalyzed by a SRC family kinase. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates interferon-mediated signaling. Upon viral infection or IFN induction, phosphorylation on Ser-708 occurs much later than phosphorylation on Tyr-701 and is required for the binding of ISGF3 on the ISREs of a subset of IFN-stimulated genes IKBKE-dependent. Phosphorylation at Tyr-701 and Ser-708 are mutually exclusive, phosphorylation at Ser-708 requires previous dephosphorylation of Tyr-701. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.19 Ref.20 Ref.24 Ref.27 Ref.28 Ref.29 Ref.32 Ref.38 Ref.39

Sumoylated with SUMO1, SUMO2 and SUMO3. Sumoylation is enhanced by IFN-gamma-induced phosphorylation on Ser-727, and by interaction with PIAS proteins. Enhances the transactivation activity. Ref.21 Ref.22 Ref.29

ISGylated. Ref.25

Involvement in disease

STAT1 deficiency complete (STAT1D) [MIM:613796]: A disorder characterized by susceptibility to severe mycobacterial and viral infections. Affected individuals can develop disseminated infections and die of viral illness.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.43 Ref.47

Mendelian susceptibility to mycobacterial disease (MSMD) [MIM:209950]: This rare condition confers predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. The pathogenic mechanism underlying MSMD is the impairment of interferon-gamma mediated immunity, whose severity determines the clinical outcome. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. MSMD is a genetically heterogeneous disease with autosomal recessive, autosomal dominant or X-linked inheritance.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.42 Ref.45 Ref.50

Candidiasis, familial, 7 (CANDF7) [MIM:614162]: A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
Note: The disease is caused by mutations affecting the gene represented in this entry. STAT1 mutations in patients with autosomal dominant candidiasis lead to defective responses of type 1 and type 17 helper T-cells, characterized by reduced production of interferon-alpha, interleukin-17, and interleukin-22. These cytokines are crucial for the antifungal defense of skin and mucosa (Ref.49). Ref.48 Ref.49

Sequence similarities

Belongs to the transcription factor STAT family.

Contains 1 SH2 domain.

Ontologies

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

Inferred from direct assay PubMed 22002246. Source: UniProtKB

JAK-STAT cascade involved in growth hormone signaling pathway

Traceable author statement. Source: Reactome

apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

blood circulation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to interferon-beta

Inferred from mutant phenotype PubMed 18035482. Source: BHF-UCL

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

interferon-gamma-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

metanephric mesenchymal cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric mesenchymal cell proliferation involved in metanephros development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 10848577. Source: UniProtKB

negative regulation of angiogenesis

Inferred from mutant phenotype PubMed 16585190. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 16585190. Source: UniProtKB

negative regulation of macrophage fusion

Inferred from electronic annotation. Source: Ensembl

negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of metanephric nephron tubule epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 10820245. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10973496. Source: UniProtKB

regulation of apoptotic process

Traceable author statement PubMed 12108949. Source: UniProtKB

regulation of interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

regulation of type I interferon-mediated signaling pathway

Traceable author statement. Source: Reactome

renal tubule development

Inferred from mutant phenotype PubMed 20861313. Source: UniProtKB

response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

response to cytokine

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to exogenous dsRNA

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from sequence or structural similarity. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21268089. Source: GOC

tumor necrosis factor-mediated signaling pathway

Inferred from direct assay PubMed 10848577. Source: UniProtKB

type I interferon signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 10692450PubMed 10973496. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear chromatin

Inferred from direct assay PubMed 18035482. Source: BHF-UCL

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10692450PubMed 10973496PubMed 16306601. Source: UniProtKB

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 18035482. Source: BHF-UCL

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 21268089. Source: BHF-UCL

RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 21268089. Source: BHF-UCL

calcium ion binding

Inferred from electronic annotation. Source: InterPro

double-stranded DNA binding

Inferred from direct assay Ref.41. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 22002246. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.14Ref.41. Source: IntAct

protein binding

Inferred from physical interaction PubMed 10848577PubMed 12867595PubMed 16306601PubMed 16531398. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.41. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 10973496PubMed 10820245. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

tumor necrosis factor receptor binding

Inferred from physical interaction PubMed 10848577. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: P42224-1)

Also known as: p91;

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 Beta (identifier: P42224-2)

Also known as: p84;

The sequence of this isoform differs from the canonical sequence as follows:
     713-750: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.40
Chain2 – 750749Signal transducer and activator of transcription 1-alpha/beta
PRO_0000182410

Regions

Domain573 – 67098SH2

Amino acid modifications

Modified residue21N-acetylserine Ref.40
Modified residue7011Phosphotyrosine; by JAK1, JAK2 or TYK2 Ref.13 Ref.27 Ref.32 Ref.38 Ref.39
Modified residue7081Phosphoserine; by IKKE Ref.39
Modified residue7271Phosphoserine; by MAPK14 Ref.12 Ref.24 Ref.29 Ref.31 Ref.33 Ref.35 Ref.36 Ref.38 Ref.39
Modified residue7451Phosphoserine; by IKKE By similarity
Cross-link703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.21 Ref.22

Natural variations

Alternative sequence713 – 75038Missing in isoform Beta.
VSP_006282
Natural variant301I → T.
Corresponds to variant rs34255470 [ dbSNP | Ensembl ].
VAR_034521
Natural variant1651D → G in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. Ref.48
VAR_065934
Natural variant1651D → H in CANDF7. Ref.48
VAR_065935
Natural variant1701Y → N in CANDF7. Ref.48
VAR_065936
Natural variant1741C → R in CANDF7. Ref.48
VAR_065937
Natural variant2011K → N in STAT1D; not deleterious in terms of most STAT1 functions; causes abnormal splicing out of exon 8 from most mRNAs thereby decreasing protein levels by approximately 70%. Ref.47
VAR_065815
Natural variant2021M → I in CANDF7. Ref.48
VAR_065938
Natural variant2021M → V in CANDF7. Ref.48
VAR_065939
Natural variant2671A → V in CANDF7. Ref.48 Ref.49
VAR_065940
Natural variant2711Q → P in CANDF7. Ref.48
VAR_065941
Natural variant2741R → Q in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. Ref.48
VAR_065942
Natural variant2741R → W in CANDF7. Ref.48 Ref.49
VAR_065943
Natural variant2861K → I in CANDF7. Ref.48
VAR_065944
Natural variant2881T → A in CANDF7. Ref.48
VAR_065945
Natural variant3201E → Q in MSMD; affects the DNA-binding activity of the protein. Ref.45
VAR_065816
Natural variant4631Q → H in MSMD; affects the DNA-binding activity of the protein. Ref.45
VAR_065817
Natural variant4911P → A in a breast cancer sample; somatic mutation. Ref.46
VAR_036001
Natural variant6001L → P in STAT1D; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency. Ref.43
VAR_018265
Natural variant6371K → E in MSMD; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. Ref.50
VAR_068713
Natural variant6731K → R in MSMD; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. Ref.50
VAR_068714
Natural variant7061L → S in MSMD; loss of GAF and ISGF3 activation; impairs the nuclear accumulation of GAF but not of ISGF3 in heterozygous cells stimulated by IFNs; affects phosphorylation of the protein. Ref.42 Ref.45
VAR_018266

Experimental info

Mutagenesis1101K → R: Sumoylated. Ref.22
Mutagenesis7011Y → E: Not phosphorylated at S-708 upon IFNB induction. Ref.29 Ref.39
Mutagenesis7011Y → F: No effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation. Phosphorylated at S-708 upon IFNB induction. Ref.29 Ref.39
Mutagenesis7031K → R: Abolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation. Ref.21 Ref.22
Mutagenesis7081S → A: Phosphorylated at Y-701 upon IFNB induction. Ref.39
Mutagenesis7081S → D: Not phosphorylated at Y-701 upon IFNB induction. Ref.39
Mutagenesis7271S → A: Decreased transcriptional activation. No effect on basal sumoylation. No enhancement of sumoylation on MAPK stimulation. No PRKCD-induced apoptosis. Upon IFNB induction, phosphorylated at Y-701 but not at S-708. Ref.24 Ref.29 Ref.39
Mutagenesis7271S → D: No change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation. Ref.24 Ref.29 Ref.39
Mutagenesis7271S → E: No change in enhancement of MAPK-induced sumoylation. Ref.24 Ref.29 Ref.39
Sequence conflict461A → T in ADA59516. Ref.2
Sequence conflict3071S → G in BAF85293. Ref.4
Sequence conflict7181Q → R in CAH18430. Ref.5

Secondary structure

..................................................................................................... 750
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha (p91) [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 054A813522364BA6

FASTA75087,335
        10         20         30         40         50         60 
MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV SFATIRFHDL 

        70         80         90        100        110        120 
LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ MSMIIYSCLK EERKILENAQ 

       130        140        150        160        170        180 
RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR 

       190        200        210        220        230        240 
EHETNGVAKS DQKQEQLLLK KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK 

       250        260        270        280        290        300 
RRQQSACIGG PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV 

       310        320        330        340        350        360 
LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK LQELNYNLKV 

       370        380        390        400        410        420 
KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL AAEFRHLQLK EQKNAGTRTN 

       430        440        450        460        470        480 
EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVAE 

       490        500        510        520        530        540 
PRNLSFFLTP PCARWAQLSE VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT 

       550        560        570        580        590        600 
RFCKENINDK NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL 

       610        620        630        640        650        660 
LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP 

       670        680        690        700        710        720 
ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG YIKTELISVS EVHPSRLQTT 

       730        740        750 
DNLLPMSPEE FDEVSRIVGS VEFDSMMNTV 

« Hide

Isoform Beta (p84) [UniParc].

Checksum: 31408601223700BB
Show »

FASTA71283,043

References

« Hide 'large scale' references
[1]"Proteins of transcription factor ISGF-3: one gene encodes the 91- and 84-kDa ISGF-3 proteins that are activated by interferon alpha."
Schindler C., Fu X.-Y., Improta T., Aebersold R., Darnell J.E. Jr.
Proc. Natl. Acad. Sci. U.S.A. 89:7836-7839(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), PROTEIN SEQUENCE OF 514-524; 654-660 AND 667-672.
[2]"Novel STAT1 alleles in a patient with impaired resistance to mycobacteria."
Kristensen I., Veirum J.E., Moeller B.K., Christiansen M.
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
[3]NIEHS SNPs program
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 ALPHA).
Tissue: Placenta and Testis.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 BETA).
Tissue: Brain.
[10]"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: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]"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.
[12]"Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation."
Wen Z., Zhong Z., Darnell J.E. Jr.
Cell 82:241-250(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-727, MUTAGENESIS.
[13]"Phosphorylation and activation of the DNA binding activity of purified Stat1 by the Janus protein-tyrosine kinases and the epidermal growth factor receptor."
Quelle F.W., Thierfelder W., Witthuhn B.A., Tang B., Cohen S., Ihle J.N.
J. Biol. Chem. 270:20775-20780(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-701.
[14]"The SH2 domains of Stat1 and Stat2 mediate multiple interactions in the transduction of IFN-alpha signals."
Gupta S., Yan H., Wong L.H., Ralph S., Krolewski J., Schindler C.
EMBO J. 15:1075-1084(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TYROSINE PHOSPHORYLATION, HETERODIMERIZATION, DNA-BINDING, MUTAGENESIS.
[15]"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.
[16]"Inhibition of Stat1-mediated gene activation by PIAS1."
Liu B., Liao J., Rao X., Kushner S.A., Chung C.D., Chang D.D., Shuai K.
Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIAS1, FUNCTION.
Tissue: B-cell.
[17]"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.
[18]"Sendai virus C protein physically associates with Stat1."
Takeuchi K., Komatsu T., Yokoo J., Kato A., Shioda T., Nagai Y., Gotoh B.
Genes Cells 6:545-557(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SENDAI VIRUS C PROTEIN.
[19]"Focal adhesion kinase activates Stat1 in integrin-mediated cell migration and adhesion."
Xie B., Zhao J., Kitagawa M., Durbin J., Madri J.A., Guan J.L., Fu X.Y.
J. Biol. Chem. 276:19512-19523(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION.
[20]"Identification of a nuclear Stat1 protein tyrosine phosphatase."
ten Hoeve J., de Jesus Ibarra-Sanchez M., Fu Y., Zhu W., Tremblay M., David M., Shuai K.
Mol. Cell. Biol. 22:5662-5668(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
[21]"PIAS proteins promote SUMO-1 conjugation to STAT1."
Ungureanu D., Vanhatupa S., Kotaja N., Yang J., Aittomaeki S., Jaenne O.A., Palvimo J.J., Silvennoinen O.
Blood 102:3311-3313(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-703, FUNCTION, MUTAGENESIS OF LYS-703.
[22]"SUMO modification of STAT1 and its role in PIAS-mediated inhibition of gene activation."
Rogers R.S., Horvath C.M., Matunis M.J.
J. Biol. Chem. 278:30091-30097(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-703, FUNCTION, MUTAGENESIS OF LYS-110 AND LYS-703.
[23]"Signal transduction via the stem cell factor receptor/c-Kit."
Ronnstrand L.
Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[24]"Protein kinase Cdelta regulates apoptosis via activation of STAT1."
DeVries T.A., Kalkofen R.L., Matassa A.A., Reyland M.E.
J. Biol. Chem. 279:45603-45612(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-727, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-727.
[25]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[26]"Hepatitis C virus expression suppresses interferon signaling by degrading STAT1."
Lin W., Choe W.H., Hiasa Y., Kamegaya Y., Blackard J.T., Schmidt E.V., Chung R.T.
Gastroenterology 128:1034-1041(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HEPATITIS C VIRUS CORE PROTEIN.
[27]"Sustained phosphorylation of mutated FGFR3 is a crucial feature of genetic dwarfism and induces apoptosis in the ATDC5 chondrogenic cell line via PLCgamma-activated STAT1."
Harada D., Yamanaka Y., Ueda K., Nishimura R., Morishima T., Seino Y., Tanaka H.
Bone 41:273-281(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION IN RESPONSE TO ACTIVATED FGFR3, PHOSPHORYLATION AT TYR-701.
[28]"Fibroblast growth factor receptor-induced phosphorylation of STAT1 at the Golgi apparatus without translocation to the nucleus."
Citores L., Bai L., Sorensen V., Olsnes S.
J. Cell. Physiol. 212:148-156(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION IN RESPONSE TO ACTIVATED FGFR1; FGFR2; FGFR3 AND FGFR4.
[29]"MAPK-induced Ser727 phosphorylation promotes SUMOylation of STAT1."
Vanhatupa S., Ungureanu D., Paakkunainen M., Silvennoinen O.
Biochem. J. 409:179-185(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-727, INTERACTION WITH PIAS1, SUMOYLATION, MUTAGENESIS OF TYR-701 AND SER-727.
[30]"System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties."
Kaushansky A., Gordus A., Budnik B.A., Lane W.S., Rush J., MacBeath G.
Chem. Biol. 15:808-817(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4.
[31]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"Analysis of STAT1 activation by six FGFR3 mutants associated with skeletal dysplasia undermines dominant role of STAT1 in FGFR3 signaling in cartilage."
Krejci P., Salazar L., Kashiwada T.A., Chlebova K., Salasova A., Thompson L.M., Bryja V., Kozubik A., Wilcox W.R.
PLoS ONE 3:E3961-E3961(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-701 IN RESPONSE TO CONSTITUTIVELY ACTIVATED FGFR3.
[33]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling."
Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.
Genes Dev. 23:118-132(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIAS1.
[35]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[36]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"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].
[38]"Mechanisms of STAT protein activation by oncogenic KIT mutants in neoplastic mast cells."
Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.
J. Biol. Chem. 286:5956-5966(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-701 IN RESPONSE TO KIT SIGNALING, PHOSPHORYLATION AT SER-727.
[39]"Inhibitor of kappaB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2 proteins define novel innate immune effector pathway against West Nile virus infection."
Perwitasari O., Cho H., Diamond M.S., Gale M. Jr.
J. Biol. Chem. 286:44412-44423(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-701; SER-708 AND SER-727, MUTAGENESIS OF TYR-701; SER-708 AND SER-727.
[40]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[41]"Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA."
Chen X., Vinkemeier U., Zhao Y., Jeruzalmi D., Darnell J.E. Jr., Kuriyan J.
Cell 93:827-839(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 136-710.
[42]"Impairment of mycobacterial but not viral immunity by a germline human STAT1 mutation."
Dupuis S., Dargemont C., Fieschi C., Thomassin N., Rosenzweig S., Harris J., Holland S.M., Schreiber R.D., Casanova J.-L.
Science 293:300-303(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MSMD SER-706.
[43]"Impaired response to interferon-alpha/beta and lethal viral disease in human STAT1 deficiency."
Dupuis S., Jouanguy E., Al-Hajjar S., Fieschi C., Al-Mohsen I.Z., Al-Jumaah S., Yang K., Chapgier A., Eidenschenk C., Eid P., Al-Ghonaium A., Tufenkeji H., Frayha H., Al-Gazlan S., Al-Rayes H., Schreiber R.D., Gresser I., Casanova J.L.
Nat. Genet. 33:388-391(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STAT1D PRO-600.
[44]"Nipah virus V and W proteins have a common STAT1-binding domain yet inhibit STAT1 activation from the cytoplasmic and nuclear compartments, respectively."
Shaw M.L., Garcia-Sastre A., Palese P., Basler C.F.
J. Virol. 78:5633-5641(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NIPAH V AND W PROTEINS.
[45]"Novel STAT1 alleles in otherwise healthy patients with mycobacterial disease."
Chapgier A., Boisson-Dupuis S., Jouanguy E., Vogt G., Feinberg J., Prochnicka-Chalufour A., Casrouge A., Yang K., Soudais C., Fieschi C., Santos O.F., Bustamante J., Picard C., de Beaucoudrey L., Emile J.F., Arkwright P.D., Schreiber R.D., Rolinck-Werninghaus C. expand/collapse author list , Rosen-Wolff A., Magdorf K., Roesler J., Casanova J.L.
PLoS Genet. 2:E131-E131(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MSMD GLN-320 AND HIS-463, CHARACTERIZATION OF VARIANTS GLN-320; HIS-463 AND SER-706.
[46]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-491.
[47]"A novel form of human STAT1 deficiency impairing early but not late responses to interferons."
Kong X.F., Ciancanelli M., Al-Hajjar S., Alsina L., Zumwalt T., Bustamante J., Feinberg J., Audry M., Prando C., Bryant V., Kreins A., Bogunovic D., Halwani R., Zhang X.X., Abel L., Chaussabel D., Al-Muhsen S., Casanova J.L., Boisson-Dupuis S.
Blood 116:5895-5906(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STAT1D ASN-201, CHARACTERIZATION OF VARIANT STAT1D ASN-201.
[48]"Gain-of-function human STAT1 mutations impair IL-17 immunity and underlie chronic mucocutaneous candidiasis."
Liu L., Okada S., Kong X.F., Kreins A.Y., Cypowyj S., Abhyankar A., Toubiana J., Itan Y., Audry M., Nitschke P., Masson C., Toth B., Flatot J., Migaud M., Chrabieh M., Kochetkov T., Bolze A., Borghesi A. expand/collapse author list , Toulon A., Hiller J., Eyerich S., Eyerich K., Gulacsy V., Chernyshova L., Chernyshov V., Bondarenko A., Maria Cortes Grimaldo R., Blancas-Galicia L., Madrigal Beas I.M., Roesler J., Magdorf K., Engelhard D., Thumerelle C., Burgel P.R., Hoernes M., Drexel B., Seger R., Kusuma T., Jansson A.F., Sawalle-Belohradsky J., Belohradsky B., Jouanguy E., Bustamante J., Bue M., Karin N., Wildbaum G., Bodemer C., Lortholary O., Fischer A., Blanche S., Al-Muhsen S., Reichenbach J., Kobayashi M., Rosales F.E., Lozano C.T., Kilic S.S., Oleastro M., Etzioni A., Traidl-Hoffmann C., Renner E.D., Abel L., Picard C., Marodi L., Boisson-Dupuis S., Puel A., Casanova J.L.
J. Exp. Med. 208:1635-1648(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CANDF7 GLY-165; HIS-165; ASN-170; ARG-174; ILE-202; VAL-202; VAL-267; PRO-271; GLN-274; TRP-274; ILE-286 AND ALA-288, CHARACTERIZATION OF VARIANTS CANDF7 GLY-165 AND GLN-274.
[49]"STAT1 mutations in autosomal dominant chronic mucocutaneous candidiasis."
van de Veerdonk F.L., Plantinga T.S., Hoischen A., Smeekens S.P., Joosten L.A., Gilissen C., Arts P., Rosentul D.C., Carmichael A.J., Smits-van der Graaf C.A., Kullberg B.J., van der Meer J.W., Lilic D., Veltman J.A., Netea M.G.
N. Engl. J. Med. 365:54-61(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CANDF7 VAL-267 AND TRP-274.
[50]"Dominant-negative STAT1 SH2 domain mutations in unrelated patients with Mendelian susceptibility to mycobacterial disease."
Tsumura M., Okada S., Sakai H., Yasunaga S., Ohtsubo M., Murata T., Obata H., Yasumi T., Kong X.F., Abhyankar A., Heike T., Nakahata T., Nishikomori R., Al-Muhsen S., Boisson-Dupuis S., Casanova J.L., Alzahrani M., Shehri M.A. expand/collapse author list , Elghazali G., Takihara Y., Kobayashi M.
Hum. Mutat. 33:1377-1387(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MSMD GLU-637 AND ARG-673, CHARACTERIZATION OF VARIANTS MSMD GLU-637 AND ARG-673.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
STAT1base

STAT1 mutation db

Wikipedia

STAT1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97935 mRNA. Translation: AAB64012.1.
M97936 mRNA. No translation available.
GU211347 mRNA. Translation: ADA59516.1.
AY865620 Genomic DNA. Translation: AAW56072.1.
AK292604 mRNA. Translation: BAF85293.1.
AK315002 mRNA. Translation: BAG37497.1.
CR749636 mRNA. Translation: CAH18430.1.
BT007241 mRNA. Translation: AAP35905.1.
AC067945 Genomic DNA. Translation: AAY24183.1.
CH471058 Genomic DNA. Translation: EAX10850.1.
CH471058 Genomic DNA. Translation: EAX10851.1.
CH471058 Genomic DNA. Translation: EAX10852.1.
CH471058 Genomic DNA. Translation: EAX10855.1.
BC002704 mRNA. Translation: AAH02704.1.
U18662 Genomic DNA. No translation available.
U18663 Genomic DNA. No translation available.
U18664 Genomic DNA. No translation available.
U18665 Genomic DNA. No translation available.
U18666 Genomic DNA. No translation available.
U18667 Genomic DNA. No translation available.
U18668 Genomic DNA. No translation available.
U18669 Genomic DNA. No translation available.
U18670 Genomic DNA. No translation available.
CCDSCCDS2309.1. [P42224-1]
CCDS42793.1. [P42224-2]
PIRA46159.
RefSeqNP_009330.1. NM_007315.3. [P42224-1]
NP_644671.1. NM_139266.2. [P42224-2]
XP_006712781.1. XM_006712718.1. [P42224-1]
UniGeneHs.642990.
Hs.743244.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BF5X-ray2.90A136-710[»]
1YVLX-ray3.00A/B1-683[»]
2KA6NMR-B710-750[»]
ProteinModelPortalP42224.
SMRP42224. Positions 2-750.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112649. 130 interactions.
DIPDIP-218N.
IntActP42224. 50 interactions.
MINTMINT-120840.
STRING9606.ENSP00000354394.

Chemistry

BindingDBP42224.
ChEMBLCHEMBL6101.
DrugBankDB01073. Fludarabine.

PTM databases

PhosphoSiteP42224.

Polymorphism databases

DMDM2507413.

Proteomic databases

MaxQBP42224.
PaxDbP42224.
PeptideAtlasP42224.
PRIDEP42224.

Protocols and materials databases

DNASU6772.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361099; ENSP00000354394; ENSG00000115415. [P42224-1]
ENST00000392322; ENSP00000376136; ENSG00000115415. [P42224-2]
ENST00000409465; ENSP00000386244; ENSG00000115415. [P42224-1]
GeneID6772.
KEGGhsa:6772.
UCSCuc002usj.2. human. [P42224-1]

Organism-specific databases

CTD6772.
GeneCardsGC02M191829.
HGNCHGNC:11362. STAT1.
HPACAB004049.
HPA000931.
HPA000982.
MIM209950. phenotype.
600555. gene.
613796. phenotype.
614162. phenotype.
neXtProtNX_P42224.
Orphanet391487. Autoimmune enteropathy and endocrinopathy-susceptibility to chronic infections syndrome.
1334. Chronic mucocutaneous candidiasis.
319595. Mendelian susceptibility to mycobacterial diseases due to partial STAT1 deficiency.
391311. Susceptibility to viral and mycobacterial infections.
PharmGKBPA36183.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310130.
HOVERGENHBG055669.
InParanoidP42224.
KOK11220.
OMAKNKQVLW.
OrthoDBEOG73JKTT.
PhylomeDBP42224.
TreeFamTF318648.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP42224.

Gene expression databases

ArrayExpressP42224.
BgeeP42224.
CleanExHS_STAT1.
GenevestigatorP42224.

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.
IPR022752. STAT1_TAZ2-bd_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.
PF12162. STAT1_TAZ2bind. 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

ChiTaRSSTAT1. human.
EvolutionaryTraceP42224.
GeneWikiSTAT1.
GenomeRNAi6772.
NextBio26428.
PMAP-CutDBP42224.
PROP42224.
SOURCESearch...

Entry information

Entry nameSTAT1_HUMAN
AccessionPrimary (citable) accession number: P42224
Secondary accession number(s): A8K989 expand/collapse secondary AC list , B2RCA0, D2KFR8, D3DPI7, Q53S88, Q53XW4, Q68D00, Q9UDL5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 177 of the entry and version 2 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 2

Human chromosome 2: entries, gene names and cross-references to MIM