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P42224

- STAT1_HUMAN

UniProt

P42224 - STAT1_HUMAN

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Protein

Signal transducer and activator of transcription 1-alpha/beta

Gene
STAT1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 FGFR4.5 Publications

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. double-stranded DNA binding Source: UniProtKB
  3. enzyme binding Source: UniProtKB
  4. identical protein binding Source: IntAct
  5. protein binding Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  8. RNA polymerase II core promoter sequence-specific DNA binding Source: BHF-UCL
  9. RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  10. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  11. signal transducer activity Source: InterPro
  12. tumor necrosis factor receptor binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. blood circulation Source: UniProtKB
  3. cellular response to insulin stimulus Source: Ensembl
  4. cellular response to interferon-beta Source: BHF-UCL
  5. cytokine-mediated signaling pathway Source: Reactome
  6. defense response to virus Source: UniProtKB-KW
  7. interferon-gamma-mediated signaling pathway Source: UniProtKB
  8. JAK-STAT cascade Source: UniProtKB
  9. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  10. lipopolysaccharide-mediated signaling pathway Source: Ensembl
  11. metanephric mesenchymal cell differentiation Source: UniProtKB
  12. metanephric mesenchymal cell proliferation involved in metanephros development Source: UniProtKB
  13. negative regulation of angiogenesis Source: UniProtKB
  14. negative regulation of endothelial cell proliferation Source: UniProtKB
  15. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  16. negative regulation of macrophage fusion Source: Ensembl
  17. negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis Source: UniProtKB
  18. negative regulation of metanephric nephron tubule epithelial cell differentiation Source: UniProtKB
  19. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  20. positive regulation of mesenchymal cell proliferation Source: UniProtKB
  21. positive regulation of smooth muscle cell proliferation Source: UniProtKB
  22. positive regulation of transcription, DNA-templated Source: UniProtKB
  23. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  24. regulation of apoptotic process Source: UniProtKB
  25. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
  26. regulation of type I interferon-mediated signaling pathway Source: Reactome
  27. renal tubule development Source: UniProtKB
  28. response to cAMP Source: UniProtKB
  29. response to cytokine Source: UniProtKB
  30. response to drug Source: Ensembl
  31. response to exogenous dsRNA Source: Ensembl
  32. response to hydrogen peroxide Source: Ensembl
  33. response to mechanical stimulus Source: Ensembl
  34. response to nutrient Source: Ensembl
  35. response to peptide hormone Source: UniProtKB
  36. transcription from RNA polymerase II promoter Source: GOC
  37. tumor necrosis factor-mediated signaling pathway Source: UniProtKB
  38. type I interferon signaling pathway Source: UniProtKB
  39. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

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

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_111133. Growth hormone receptor signaling.
REACT_115831. ISG15 antiviral mechanism.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_17025. Downstream signal transduction.
REACT_24980. Regulation of IFNG signaling.
REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.
REACT_27307. Interleukin-6 signaling.
SignaLinkiP42224.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription 1-alpha/beta
Alternative name(s):
Transcription factor ISGF-3 components p91/p84
Gene namesi
Name:STAT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11362. STAT1.

Subcellular locationi

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 FGFR4.1 Publication

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. dendrite Source: UniProtKB
  5. nuclear chromatin Source: BHF-UCL
  6. nucleolus Source: HPA
  7. nucleoplasm Source: Reactome
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti201 – 2011K → 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%. 1 Publication
VAR_065815
Natural varianti600 – 6001L → P in STAT1D; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency. 1 Publication
VAR_018265
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.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti320 – 3201E → Q in MSMD; affects the DNA-binding activity of the protein. 1 Publication
VAR_065816
Natural varianti463 – 4631Q → H in MSMD; affects the DNA-binding activity of the protein. 1 Publication
VAR_065817
Natural varianti637 – 6371K → E in MSMD; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 Publication
VAR_068713
Natural varianti673 – 6731K → R in MSMD; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 Publication
VAR_068714
Natural varianti706 – 7061L → 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. 2 Publications
VAR_018266
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 (1 Publication).2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651D → G in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 1 Publication
VAR_065934
Natural varianti165 – 1651D → H in CANDF7. 1 Publication
VAR_065935
Natural varianti170 – 1701Y → N in CANDF7. 1 Publication
VAR_065936
Natural varianti174 – 1741C → R in CANDF7. 1 Publication
VAR_065937
Natural varianti202 – 2021M → I in CANDF7. 1 Publication
VAR_065938
Natural varianti202 – 2021M → V in CANDF7. 1 Publication
VAR_065939
Natural varianti267 – 2671A → V in CANDF7. 2 Publications
VAR_065940
Natural varianti271 – 2711Q → P in CANDF7. 1 Publication
VAR_065941
Natural varianti274 – 2741R → Q in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 1 Publication
VAR_065942
Natural varianti274 – 2741R → W in CANDF7. 2 Publications
VAR_065943
Natural varianti286 – 2861K → I in CANDF7. 1 Publication
VAR_065944
Natural varianti288 – 2881T → A in CANDF7. 1 Publication
VAR_065945

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi110 – 1101K → R: Sumoylated. 1 Publication
Mutagenesisi701 – 7011Y → E: Not phosphorylated at S-708 upon IFNB induction. 2 Publications
Mutagenesisi701 – 7011Y → F: No effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation. Phosphorylated at S-708 upon IFNB induction. 2 Publications
Mutagenesisi703 – 7031K → R: Abolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation. 2 Publications
Mutagenesisi708 – 7081S → A: Phosphorylated at Y-701 upon IFNB induction. 1 Publication
Mutagenesisi708 – 7081S → D: Not phosphorylated at Y-701 upon IFNB induction. 1 Publication
Mutagenesisi727 – 7271S → 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. 3 Publications
Mutagenesisi727 – 7271S → D: No change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation. 3 Publications
Mutagenesisi727 – 7271S → E: No change in enhancement of MAPK-induced sumoylation. 3 Publications

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi209950. phenotype.
613796. phenotype.
614162. phenotype.
Orphaneti391487. 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.
PharmGKBiPA36183.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 750749Signal transducer and activator of transcription 1-alpha/betaPRO_0000182410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei701 – 7011Phosphotyrosine; by JAK1, JAK2 or TYK25 Publications
Cross-linki703 – 703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications
Modified residuei708 – 7081Phosphoserine; by IKKE1 Publication
Modified residuei727 – 7271Phosphoserine; by MAPK149 Publications
Modified residuei745 – 7451Phosphoserine; by IKKE By similarity

Post-translational modificationi

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-701.14 Publications
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.3 Publications
ISGylated.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP42224.
PaxDbiP42224.
PeptideAtlasiP42224.
PRIDEiP42224.

PTM databases

PhosphoSiteiP42224.

Miscellaneous databases

PMAP-CutDBP42224.

Expressioni

Gene expression databases

ArrayExpressiP42224.
BgeeiP42224.
CleanExiHS_STAT1.
GenevestigatoriP42224.

Organism-specific databases

HPAiCAB004049.
HPA000931.
HPA000982.

Interactioni

Subunit structurei

Isoform alpha homodimerizes 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.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-1057697,EBI-1057697
P03255-12EBI-1057697,EBI-6692439From a different organism.
P03255-22EBI-1057697,EBI-6859460From a different organism.
P266645EBI-1057697,EBI-6941357From a different organism.
P279582EBI-1057697,EBI-6377335From a different organism.
DDB1Q165312EBI-1057697,EBI-350322
DDX58O957864EBI-1057697,EBI-995350
E2F1Q010942EBI-1057697,EBI-448924
ERBB2P046262EBI-1057697,EBI-641062
H1LP072393EBI-1057697,EBI-7789600From a different organism.
IFNGR1P152605EBI-1057697,EBI-1030755
MAVSQ7Z4343EBI-1057697,EBI-995373
RXRAP197932EBI-1057697,EBI-78598
STAT2P5263014EBI-1057697,EBI-1546963

Protein-protein interaction databases

BioGridi112649. 130 interactions.
DIPiDIP-218N.
IntActiP42224. 50 interactions.
MINTiMINT-120840.
STRINGi9606.ENSP00000354394.

Structurei

Secondary structure

1
750
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 75
Turni12 – 143
Helixi15 – 195
Helixi28 – 336
Helixi35 – 406
Helixi43 – 464
Helixi50 – 7425
Helixi77 – 9418
Helixi98 – 11720
Helixi121 – 1255
Helixi137 – 17943
Helixi189 – 1924
Helixi193 – 1953
Helixi198 – 24750
Helixi257 – 28630
Helixi293 – 31624
Beta strandi317 – 3215
Beta strandi334 – 3363
Beta strandi339 – 3479
Helixi352 – 3543
Turni355 – 3573
Beta strandi359 – 3657
Helixi370 – 3734
Beta strandi374 – 3763
Beta strandi380 – 3823
Beta strandi386 – 3894
Beta strandi391 – 3955
Turni396 – 3983
Beta strandi399 – 40810
Beta strandi421 – 4255
Beta strandi433 – 4419
Beta strandi444 – 4518
Beta strandi455 – 4606
Helixi461 – 4633
Helixi464 – 47714
Helixi486 – 4883
Helixi495 – 50915
Helixi516 – 52611
Helixi539 – 5435
Beta strandi550 – 5523
Helixi554 – 56815
Helixi570 – 5745
Helixi584 – 5907
Turni591 – 5933
Beta strandi601 – 6033
Beta strandi612 – 6165
Beta strandi621 – 6244
Beta strandi627 – 6315
Helixi636 – 6405
Helixi644 – 6496
Beta strandi657 – 6593
Helixi673 – 6775
Turni678 – 6803
Helixi728 – 73811
Turni739 – 7424
Helixi743 – 7453
Turni746 – 7483

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BF5X-ray2.90A136-710[»]
1YVLX-ray3.00A/B1-683[»]
2KA6NMR-B710-750[»]
ProteinModelPortaliP42224.
SMRiP42224. Positions 2-750.

Miscellaneous databases

EvolutionaryTraceiP42224.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini573 – 67098SH2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili136 – 317182Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGiNOG310130.
HOVERGENiHBG055669.
InParanoidiP42224.
KOiK11220.
OMAiKNKQVLW.
OrthoDBiEOG73JKTT.
PhylomeDBiP42224.
TreeFamiTF318648.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.532.10. 1 hit.
1.20.1050.20. 1 hit.
2.60.40.630. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR001217. STAT.
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]
PANTHERiPTHR11801. PTHR11801. 1 hit.
PfamiPF00017. 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]
SMARTiSM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]
SUPFAMiSSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Alpha (identifier: P42224-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV    50
SFATIRFHDL LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ 100
MSMIIYSCLK EERKILENAQ RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK 150
DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR EHETNGVAKS DQKQEQLLLK 200
KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK RRQQSACIGG 250
PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV 300
LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK 350
LQELNYNLKV KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL 400
AAEFRHLQLK EQKNAGTRTN EGPLIVTEEL HSLSFETQLC QPGLVIDLET 450
TSLPVVVISN VSQLPSGWAS ILWYNMLVAE PRNLSFFLTP PCARWAQLSE 500
VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT RFCKENINDK 550
NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL 600
LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN 650
YKVMAAENIP ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG 700
YIKTELISVS EVHPSRLQTT DNLLPMSPEE FDEVSRIVGS VEFDSMMNTV 750
Length:750
Mass (Da):87,335
Last modified:November 1, 1997 - v2
Checksum:i054A813522364BA6
GO
Isoform Beta (identifier: P42224-2) [UniParc]FASTAAdd to Basket

Also known as: p84

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

Show »
Length:712
Mass (Da):83,043
Checksum:i31408601223700BB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti30 – 301I → T.
Corresponds to variant rs34255470 [ dbSNP | Ensembl ].
VAR_034521
Natural varianti165 – 1651D → G in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 1 Publication
VAR_065934
Natural varianti165 – 1651D → H in CANDF7. 1 Publication
VAR_065935
Natural varianti170 – 1701Y → N in CANDF7. 1 Publication
VAR_065936
Natural varianti174 – 1741C → R in CANDF7. 1 Publication
VAR_065937
Natural varianti201 – 2011K → 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%. 1 Publication
VAR_065815
Natural varianti202 – 2021M → I in CANDF7. 1 Publication
VAR_065938
Natural varianti202 – 2021M → V in CANDF7. 1 Publication
VAR_065939
Natural varianti267 – 2671A → V in CANDF7. 2 Publications
VAR_065940
Natural varianti271 – 2711Q → P in CANDF7. 1 Publication
VAR_065941
Natural varianti274 – 2741R → Q in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 1 Publication
VAR_065942
Natural varianti274 – 2741R → W in CANDF7. 2 Publications
VAR_065943
Natural varianti286 – 2861K → I in CANDF7. 1 Publication
VAR_065944
Natural varianti288 – 2881T → A in CANDF7. 1 Publication
VAR_065945
Natural varianti320 – 3201E → Q in MSMD; affects the DNA-binding activity of the protein. 1 Publication
VAR_065816
Natural varianti463 – 4631Q → H in MSMD; affects the DNA-binding activity of the protein. 1 Publication
VAR_065817
Natural varianti491 – 4911P → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_036001
Natural varianti600 – 6001L → P in STAT1D; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency. 1 Publication
VAR_018265
Natural varianti637 – 6371K → E in MSMD; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 Publication
VAR_068713
Natural varianti673 – 6731K → R in MSMD; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 Publication
VAR_068714
Natural varianti706 – 7061L → 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. 2 Publications
VAR_018266

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei713 – 75038Missing in isoform Beta. VSP_006282Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461A → T in ADA59516. 1 Publication
Sequence conflicti307 – 3071S → G in BAF85293. 1 Publication
Sequence conflicti718 – 7181Q → R in CAH18430. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2309.1. [P42224-1]
CCDS42793.1. [P42224-2]
PIRiA46159.
RefSeqiNP_009330.1. NM_007315.3. [P42224-1]
NP_644671.1. NM_139266.2. [P42224-2]
XP_006712781.1. XM_006712718.1. [P42224-1]
UniGeneiHs.642990.
Hs.743244.

Genome annotation databases

EnsembliENST00000361099; ENSP00000354394; ENSG00000115415. [P42224-1]
ENST00000392322; ENSP00000376136; ENSG00000115415. [P42224-2]
ENST00000409465; ENSP00000386244; ENSG00000115415. [P42224-1]
GeneIDi6772.
KEGGihsa:6772.
UCSCiuc002usj.2. human. [P42224-1]

Polymorphism databases

DMDMi2507413.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
STAT1base

STAT1 mutation db

Wikipedia

STAT1 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS2309.1. [P42224-1 ]
CCDS42793.1. [P42224-2 ]
PIRi A46159.
RefSeqi NP_009330.1. NM_007315.3. [P42224-1 ]
NP_644671.1. NM_139266.2. [P42224-2 ]
XP_006712781.1. XM_006712718.1. [P42224-1 ]
UniGenei Hs.642990.
Hs.743244.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P42224.
SMRi P42224. Positions 2-750.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112649. 130 interactions.
DIPi DIP-218N.
IntActi P42224. 50 interactions.
MINTi MINT-120840.
STRINGi 9606.ENSP00000354394.

Chemistry

BindingDBi P42224.
ChEMBLi CHEMBL6101.
DrugBanki DB01073. Fludarabine.

PTM databases

PhosphoSitei P42224.

Polymorphism databases

DMDMi 2507413.

Proteomic databases

MaxQBi P42224.
PaxDbi P42224.
PeptideAtlasi P42224.
PRIDEi P42224.

Protocols and materials databases

DNASUi 6772.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361099 ; ENSP00000354394 ; ENSG00000115415 . [P42224-1 ]
ENST00000392322 ; ENSP00000376136 ; ENSG00000115415 . [P42224-2 ]
ENST00000409465 ; ENSP00000386244 ; ENSG00000115415 . [P42224-1 ]
GeneIDi 6772.
KEGGi hsa:6772.
UCSCi uc002usj.2. human. [P42224-1 ]

Organism-specific databases

CTDi 6772.
GeneCardsi GC02M191829.
HGNCi HGNC:11362. STAT1.
HPAi CAB004049.
HPA000931.
HPA000982.
MIMi 209950. phenotype.
600555. gene.
613796. phenotype.
614162. phenotype.
neXtProti NX_P42224.
Orphaneti 391487. 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.
PharmGKBi PA36183.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG310130.
HOVERGENi HBG055669.
InParanoidi P42224.
KOi K11220.
OMAi KNKQVLW.
OrthoDBi EOG73JKTT.
PhylomeDBi P42224.
TreeFami TF318648.

Enzyme and pathway databases

Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_111133. Growth hormone receptor signaling.
REACT_115831. ISG15 antiviral mechanism.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_17025. Downstream signal transduction.
REACT_24980. Regulation of IFNG signaling.
REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.
REACT_27307. Interleukin-6 signaling.
SignaLinki P42224.

Miscellaneous databases

ChiTaRSi STAT1. human.
EvolutionaryTracei P42224.
GeneWikii STAT1.
GenomeRNAii 6772.
NextBioi 26428.
PMAP-CutDB P42224.
PROi P42224.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42224.
Bgeei P42224.
CleanExi HS_STAT1.
Genevestigatori P42224.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.532.10. 1 hit.
1.20.1050.20. 1 hit.
2.60.40.630. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR001217. STAT.
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 ]
PANTHERi PTHR11801. PTHR11801. 1 hit.
Pfami 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 ]
SMARTi SM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view ]
SUPFAMi SSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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. 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. 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. 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. Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
  21. 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. 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. 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. 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, COILED-COIL.
  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. 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. Cited for: VARIANTS MSMD GLN-320 AND HIS-463, CHARACTERIZATION OF VARIANTS GLN-320; HIS-463 AND SER-706.
  46. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-491.
  47. 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.
    , 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. Cited for: VARIANTS CANDF7 VAL-267 AND TRP-274.
  50. Cited for: VARIANTS MSMD GLU-637 AND ARG-673, CHARACTERIZATION OF VARIANTS MSMD GLU-637 AND ARG-673.

Entry informationi

Entry nameiSTAT1_HUMAN
AccessioniPrimary (citable) accession number: P42224
Secondary accession number(s): A8K989
, B2RCA0, D2KFR8, D3DPI7, Q53S88, Q53XW4, Q68D00, Q9UDL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 178 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

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