P42224 (STAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal transducer and activator of transcription 1-alpha/beta

Alternative name(s):
Transcription factor ISGF-3 components p91/p84

Gene names

Name:

STAT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	750 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. 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.20 Ref.21 Ref.23 Ref.31
Subunit structure	Isoform alpha homodimerizes upon IFN-gamma induced phosphorylation. Heterodimer with STAT2 upon IFN-alpha/beta induced phosphorylation. Interacts with NMI. 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 By similarity. Interacts with HCV core protein; the interaction results in STAT1 degradation. Interacts with PIAS1; the interaction requires phosphorylation on Ser-727 and inhibits STAT1 activation. Interacts with IFNAR1; the interaction requires the phosphorylation of IFNAR1 at 'Tyr-466'. Interacts with IFNAR2. Interacts with PIAS1 (dimethylated on arginine); the interaction results in release of STAT1 from its target gene. Interacts with SRC By similarity. Interacts with ERBB4 (phosphorylated). Interacts with PTK2/FAK1. Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.25 Ref.28 Ref.29 Ref.33 Ref.41
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.23
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. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. 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. 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 PKCdelta 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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.19 Ref.23 Ref.26 Ref.27 Ref.28 Ref.31 Ref.37 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.20 Ref.21 Ref.28 ISGylated. Ref.24
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.40 Ref.44 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.39 Ref.42 Ref.47 Familial candidiasis 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.46). Ref.45 Ref.46
Sequence similarities	Belongs to the transcription factor STAT family. Contains 1 SH2 domain.

Ontologies

Keywords
Biological process	Antiviral defense Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	SH2 domain
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade involved in growth hormone signaling pathway Traceable author statement. Source: Reactome blood circulation Inferred from sequence or structural similarity. Source: UniProtKB cellular response to interferon-beta Inferred from mutant phenotype PubMed 18035482. Source: BHF-UCL defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB interferon-gamma-mediated signaling pathway Inferred from direct assay PubMed 21268089. Source: BHF-UCL lipopolysaccharide-mediated signaling pathway Inferred from electronic annotation. Source: Compara 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 cascade 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 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 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 exogenous dsRNA Inferred from electronic annotation. Source: Compara tumor necrosis factor-mediated signaling pathway Inferred from direct assay PubMed 10848577. Source: UniProtKB type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	axon Inferred from sequence or structural similarity. 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
Molecular_function	RNA 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.38. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.38. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 10820245. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDB1	Q16531	2	EBI-1057697,EBI-350322
E2F1	Q01094	2	EBI-1057697,EBI-448924
MAVS	Q7Z434	3	EBI-1057697,EBI-995373
RXRA	P19793	2	EBI-1057697,EBI-78598
STAT2	P52630	4	EBI-1057697,EBI-1546963

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 750

750

Signal transducer and activator of transcription 1-alpha/beta

PRO_0000182410

Regions

Domain

573 – 670

98

SH2

Amino acid modifications

Modified residue

701

1

Phosphotyrosine; by JAK1, JAK2 or TYK2 Ref.13 Ref.26 Ref.31 Ref.37

Modified residue

727

1

Phosphoserine; by MAPK14 Ref.12 Ref.23 Ref.28 Ref.30 Ref.32 Ref.34 Ref.35 Ref.37

Cross-link

703

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.20 Ref.21

Natural variations

Alternative sequence

713 – 750

38

Missing in isoform Beta.

VSP_006282

Natural variant

30

1

I → T.
Corresponds to variant rs34255470 [ dbSNP | Ensembl ].

VAR_034521

Natural variant

165

1

D → G in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. Ref.45

VAR_065934

Natural variant

165

1

D → H in CANDF7. Ref.45

VAR_065935

Natural variant

170

1

Y → N in CANDF7. Ref.45

VAR_065936

Natural variant

174

1

C → R in CANDF7. Ref.45

VAR_065937

Natural variant

201

1

K → 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.44

VAR_065815

Natural variant

202

1

M → I in CANDF7. Ref.45

VAR_065938

Natural variant

202

1

M → V in CANDF7. Ref.45

VAR_065939

Natural variant

267

1

A → V in CANDF7. Ref.45 Ref.46

VAR_065940

Natural variant

271

1

Q → P in CANDF7. Ref.45

VAR_065941

Natural variant

274

1

R → Q in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. Ref.45

VAR_065942

Natural variant

274

1

R → W in CANDF7. Ref.45 Ref.46

VAR_065943

Natural variant

286

1

K → I in CANDF7. Ref.45

VAR_065944

Natural variant

288

1

T → A in CANDF7. Ref.45

VAR_065945

Natural variant

320

1

E → Q in MSMD; affects the DNA-binding activity of the protein. Ref.42

VAR_065816

Natural variant

463

1

Q → H in MSMD; affects the DNA-binding activity of the protein. Ref.42

VAR_065817

Natural variant

491

1

P → A in a breast cancer sample; somatic mutation. Ref.43

VAR_036001

Natural variant

600

1

L → P in STAT1D; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency. Ref.40

VAR_018265

Natural variant

637

1

K → E in MSMD; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. Ref.47

VAR_068713

Natural variant

673

1

K → R in MSMD; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. Ref.47

VAR_068714

Natural variant

706

1

L → 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.39 Ref.42

VAR_018266

Experimental info

Mutagenesis

110

1

K → R: Sumoylated. Ref.21

Mutagenesis

701

1

Y → F: No effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation. Ref.28

Mutagenesis

703

1

K → R: Abolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation. Ref.20 Ref.21

Mutagenesis

727

1

S → A: Decreased transcriptional activation. No effect on basal sumoylation. No enhancement of sumoylation on MAPK stimulation. No PKCdelta-induced apoptosis. Ref.23 Ref.28

Mutagenesis

727

1

S → D: No change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation. Ref.23 Ref.28

Mutagenesis

727

1

S → E: No change in enhancement of MAPK-induced sumoylation. Ref.23 Ref.28

Sequence conflict

46

1

A → T in ADA59516. Ref.2

Sequence conflict

307

1

S → G in BAF85293. Ref.4

Sequence conflict

718

1

Q → R in CAH18430. Ref.5

Secondary structure

1

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750

Helix Strand Turn

Details...

Helix

3 – 7

5

Turn

12 – 14

3

Helix

15 – 19

5

Helix

28 – 33

6

Helix

35 – 40

6

Helix

43 – 46

4

Helix

50 – 74

25

Helix

77 – 94

18

Helix

98 – 117

20

Helix

121 – 125

5

Helix

137 – 179

43

Helix

189 – 192

4

Helix

193 – 195

3

Helix

198 – 247

50

Helix

257 – 286

30

Helix

293 – 316

24

Beta strand

317 – 321

5

Beta strand

334 – 336

3

Beta strand

339 – 347

9

Helix

352 – 354

3

Turn

355 – 357

3

Beta strand

359 – 365

7

Helix

370 – 373

4

Beta strand

374 – 376

3

Beta strand

380 – 382

3

Beta strand

386 – 389

4

Beta strand

391 – 395

5

Turn

396 – 398

3

Beta strand

399 – 408

10

Beta strand

421 – 425

5

Beta strand

433 – 441

9

Beta strand

444 – 451

8

Beta strand

455 – 460

6

Helix

461 – 463

3

Helix

464 – 477

14

Helix

486 – 488

3

Helix

495 – 509

15

Helix

516 – 526

11

Helix

539 – 543

5

Beta strand

550 – 552

3

Helix

554 – 568

15

Helix

570 – 574

5

Helix

584 – 590

7

Turn

591 – 593

3

Beta strand

601 – 603

3

Beta strand

612 – 616

5

Beta strand

621 – 624

4

Beta strand

627 – 631

5

Helix

636 – 640

5

Helix

644 – 649

6

Beta strand

657 – 659

3

Helix

673 – 677

5

Turn

678 – 680

3

Helix

728 – 738

11

Turn

739 – 742

4

Helix

743 – 745

3

Turn

746 – 748

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha (p91) [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 054A813522364BA6	FASTA	750	87,335
	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
	Isoform Beta (p84) [UniParc]. Checksum: 31408601223700BB	FASTA	712	83,043
	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 ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG YIKTELISVS EV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[31]	"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.
[32]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"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.
[34]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[35]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"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].
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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. , 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.
[43]	"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. , 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.
[44]	"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.
[45]	"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. , 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.
[46]	"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.
[47]	"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. , 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.

IPI

IPI00030781.
IPI00218188.

PIR

A46159.

RefSeq

NP_009330.1. NM_007315.3.
NP_644671.1. NM_139266.2.

UniGene

Hs.642990.
Hs.743244.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BF5	X-ray	2.90	A	136-710	[»]
1YVL	X-ray	3.00	A/B	1-683	[»]
2KA6	NMR	-	B	710-750	[»]

ProteinModelPortal

P42224.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-218N.

IntAct

P42224. 35 interactions.

MINT

MINT-120840.

STRING

9606.ENSP00000354394.

PTM databases

PhosphoSite

P42224.

Polymorphism databases

DMDM

2507413.

Proteomic databases

PaxDb

P42224.

PeptideAtlas

P42224.

PRIDE

P42224.

Protocols and materials databases

DNASU

6772.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361099; ENSP00000354394; ENSG00000115415.
ENST00000392322; ENSP00000376136; ENSG00000115415.
ENST00000409465; ENSP00000386244; ENSG00000115415.

GeneID

6772.

KEGG

hsa:6772.

UCSC

uc002usj.2. human.

Organism-specific databases

CTD

6772.

GeneCards

GC02M191829.

HGNC

HGNC:11362. STAT1.

HPA

CAB004049.
HPA000931.
HPA000982.

MIM

209950. phenotype.
600555. gene.
613796. phenotype.
614162. phenotype.

neXtProt

NX_P42224.

Orphanet

1334. Chronic mucocutaneous candidiasis.
319595. Mendelian susceptibility to mycobacterial diseases due to partial STAT1 deficiency.

PharmGKB

PA36183.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG310130.

HOVERGEN

HBG055669.

InParanoid

P42224.

KO

K11220.

OMA

NMLTTEP.

OrthoDB

EOG4N5VWB.

PhylomeDB

P42224.

Enzyme and pathway databases

Pathway_Interaction_DB

epopathway. EPO signaling pathway.
fgf_pathway. FGF signaling pathway.
ifngpathway. IFN-gamma pathway.
il12_2pathway. IL12-mediated signaling events.
il2_1pathway. IL2-mediated signaling events.
il23pathway. IL23-mediated signaling events.
il27pathway. IL27-mediated signaling events.
il6_7pathway. IL6-mediated signaling events.
pdgfrbpathway. PDGFR-beta signaling pathway.
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
tnfpathway. TNF receptor signaling pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

SignaLink

P42224.

Gene expression databases

ArrayExpress

P42224.

Bgee

P42224.

CleanEx

HS_STAT1.

Genevestigator

P42224.

GermOnline

ENSG00000115415. Homo sapiens.

Family and domain databases

Gene3D

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.

InterPro

IPR011992. EF-hand-like_dom.
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR022752. STAT1_TAZ2-bd_C.
IPR013800. STAT_TF_alpha.
IPR015988. STAT_TF_coiled-coil.
IPR001217. STAT_TF_core.
IPR013801. STAT_TF_DNA-bd.
IPR012345. STAT_TF_DNA-bd_sub.
IPR013799. STAT_TF_prot_interaction.
[Graphical view]

PANTHER

PTHR11801. PTHR11801. 1 hit.

Pfam

PF00017. 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]

SMART

SM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]

SUPFAM

SSF49417. P53_like_DNA_bnd. 1 hit.
SSF47655. STAT. 1 hit.
SSF48092. STAT. 1 hit.

PROSITE

PS50001. SH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P42224.

ChEMBL

CHEMBL6101.

ChiTaRS

STAT1. human.

DrugBank

DB01073. Fludarabine.

EvolutionaryTrace

P42224.

GenomeRNAi

6772.

NextBio

26428.

PMAP-CutDB

P42224.

SOURCE

Search...

Entry information

Entry name

STAT1_HUMAN

Accession

Primary (citable) accession number: P42224
Secondary accession number(s): A8K989 , 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:	May 29, 2013
This is version 165 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.