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Biol.24325-336SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-703IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]On the role of STAT1 and STAT6 ADP-ribosylation in the regulation of macrophage activation.Begitt A.Cavey J.Droescher M.Vinkemeier U.doi:10.1038/s41467-018-04522-z2018Nat. Commun.92144COMMENT ON ADP-RIBOSYLATIONHerpes Simplex Virus Type 2 Inhibits Type I IFN Signaling Mediated by the Novel E3 Ubiquitin Protein Ligase Activity of Viral Protein ICP22.Zhang M.Fu M.Li M.Hu H.Gong S.Hu Q.doi:10.4049/jimmunol.20004182020J. Immunol.2051281-1292UBIQUITINATION BY HERPES SIMPLEX VIRUS 2 PROTEIN ICP22 (MICROBIAL INFECTION)Interleukin-35 inhibits lipopolysaccharide-induced endothelial cell activation by downregulating inflammation and apoptosis.Li M.Liu Y.Fu Y.Gong R.Xia H.Huang X.Wu Y.doi:10.1016/j.yexcr.2021.1127842021Exp. Cell Res.407112784FUNCTIONINTERACTION WITH STAT4Suppression of JAK-STAT Signaling by Epstein-Barr Virus Tegument Protein BGLF2 through Recruitment of SHP1 Phosphatase and Promotion of STAT2 Degradation.Jangra S.Bharti A.Lui W.Y.Chaudhary V.Botelho M.G.Yuen K.S.Jin D.Y.doi:10.1128/jvi.01027-212021J. Virol.95e0102721INTERACTION WITH EPSTEIN-BARR VIRUS TEGUMENT PROTEIN BGLF2 (MICROBIAL INFECTION)A family of conserved bacterial virulence factors dampens interferon responses by blocking calcium signaling.Alphonse N.Wanford J.J.Voak A.A.Gay J.Venkhaya S.Burroughs O.Mathew S.Lee T.Evans S.L.Zhao W.Frowde K.Alrehaili A.Dickenson R.E.Munk M.Panina S.Mahmood I.F.Llorian M.Stanifer M.L.Boulant S.Berchtold M.W.Bergeron J.R.C.Wack A.Lesser C.F.Odendall C.doi:10.1016/j.cell.2022.04.0282022Cell1852354-2369FUNCTIONPHOSPHORYLATIONCrystal 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.doi:10.1016/s0092-8674(00)81443-91998Cell93827-839X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 136-710COILED-COILImpairment 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.doi:10.1126/science.10611542001Science293300-303VARIANT IMD31A SER-706Impaired 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.doi:10.1038/ng10972003Nat. Genet.33388-391VARIANT IMD31B PRO-600Novel 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.doi:10.1371/journal.pgen.00201312006PLoS Genet.2E131VARIANTS IMD31A GLN-320 AND HIS-463CHARACTERIZATION OF VARIANTS GLN-320; HIS-463 AND SER-706The 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.doi:10.1126/science.11334272006Science314268-274VARIANT [LARGE SCALE ANALYSIS] ALA-491A 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.doi:10.1182/blood-2010-04-2805862010Blood1165895-5906VARIANT IMD31B ASN-201CHARACTERIZATION OF VARIANT IMD31B ASN-201Gain-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.doi:10.1084/jem.201109582011J. Exp. Med.2081635-1648VARIANTS IMD31C GLY-165; HIS-165; ASN-170; ARG-174; ILE-202; VAL-202; VAL-267; PRO-271; GLN-274; TRP-274; ILE-286 AND ALA-288CHARACTERIZATION OF VARIANTS IMD31C GLY-165 AND GLN-274STAT1 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.doi:10.1056/nejmoa11001022011N. Engl. J. Med.36554-61VARIANTS IMD31C VAL-267 AND TRP-274Dominant-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.doi:10.1002/humu.221132012Hum. Mutat.331377-1387VARIANTS IMD31A GLU-637 AND ARG-673CHARACTERIZATION OF VARIANTS IMD31A GLU-637 AND ARG-673New and recurrent gain-of-function STAT1 mutations in patients with chronic mucocutaneous candidiasis from Eastern and Central Europe.Soltesz B.Toth B.Shabashova N.Bondarenko A.Okada S.Cypowyj S.Abhyankar A.Csorba G.Tasko S.Sarkadi A.K.Mehes L.Rozsival P.Neumann D.Chernyshova L.Tulassay Z.Puel A.Casanova J.L.Sediva A.Litzman J.Marodi L.doi:10.1136/jmedgenet-2013-1015702013J. Med. Genet.50567-578VARIANTS IMD31C GLY-165; LYS-179; GLN-274; TRP-274; ARG-285 AND MET-385CHARACTERIZATION OF VARIANTS IMD31C LYS-179; GLN-274; TRP-274; ARG-285 AND MET-385CHARACTERIZATION OF VARIANT IMD31B CYS-701Two novel gain-of-function mutations of STAT1 responsible for chronic mucocutaneous candidiasis disease: impaired production of IL-17A and IL-22, and the presence of anti-IL-17F autoantibody.Yamazaki Y.Yamada M.Kawai T.Morio T.Onodera M.Ueki M.Watanabe N.Takada H.Takezaki S.Chida N.Kobayashi I.Ariga T.doi:10.4049/jimmunol.14014672014J. Immunol.1934880-4887VARIANTS IMD31C GLU-278 AND ASP-384CHARACTERIZATION OF VARIANTS IMD31C GLU-278; ASP-384 AND MET-385A novel gain-of-function STAT1 mutation resulting in basal phosphorylation of STAT1 and increased distal IFN-gamma-mediated responses in chronic mucocutaneous candidiasis.Martinez-Martinez L.Martinez-Saavedra M.T.Fuentes-Prior P.Barnadas M.Rubiales M.V.Noda J.Badell I.Rodriguez-Gallego C.Calle-Martin O.L.doi:10.1016/j.molimm.2015.09.0142015Mol. Immunol.68597-605VARIANT IMD31C ASN-298CHARACTERIZATION OF VARIANT IMD31C ASN-298NIEHS-SNPsSTAT1base; STAT1 mutation dbWikipedia; STAT1 entry2.90A=136-7103.00A/B=1-683B=710-7502.00A=1-1262.00A=132-6842.97A=132-713324ISGF3 complexSTAT1/STAT3 complexSTAT1/STAT4 complexSTAT1 homodimer1932 sites, 1 glycan2 sites, 1 O-linked glycan (2 sites)2673 antibodies from 55 providers3 antibodieshumanSTAT1Low tissue specificitygenephenotypephenotypephenotypeAutoimmune enteropathy and endocrinopathy-susceptibility to chronic infections syndromeMendelian susceptibility to mycobacterial diseases due to partial STAT1 deficiencySusceptibility to viral and mycobacterial infections due to STAT1 deficiencyEukaryotaInterleukin-6 signalingISG15 antiviral mechanismSignaling by SCF-KITSignaling by cytosolic FGFR1 fusion mutantsDownstream signal transductionDownregulation of SMAD2/3:SMAD4 transcriptional activityInterleukin-4 and Interleukin-13 signalingInterferon gamma signalingRegulation of IFNG signalingInterleukin-20 family signalingRegulation of RUNX2 expression and activityInterleukin-35 SignallingInterleukin-9 signalingNOTCH3 Intracellular Domain Regulates TranscriptionInterleukin-27 signalingInterleukin-21 signalingInterferon alpha/beta signalingRegulation of IFNA/IFNB signalingSignaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutantsSignaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutantsSignaling by PDGFRA extracellular domain mutantsSignaling by CSF3 (G-CSF)Signaling by CSF1 (M-CSF) in myeloid cellsInactivation of CSF3 (G-CSF) signalingSARS-CoV-2 activates/modulates innate and adaptive immune responsesGrowth hormone receptor signalingPKR-mediated signaling34 hits in 1188 CRISPR screenshumanTchemProteinExpressed in epithelium of nasopharynx and 208 other cell types or tissuesbaseline and differentialSH2_STAT1STAT1_CCDSTAT1_DBDEF-handSH2 domainsignal transducer and activator of transcription 1STAT transcription factor, all-alpha domainSTAT transcription factor, DNA-binding domainSTAT transcription factor, N-terminal domainp53-like_TF_DNA-bd_sfSH2SH2_dom_sfSTATSTAT1_C_sfSTAT1_SH2STAT1_TAZ2-bd_CSTAT_linkerSTAT_N_sfSTAT_TF_alphaSTAT_TF_coiled-coilSTAT_TF_DNA-bdSTAT_TF_DNA-bd_NSTAT_TF_prot_interactionSIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTIONSIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 1-ALPHA_BETASH2STAT1_TAZ2bindSTAT_alphaSTAT_bindSTAT_intSTAT_linkerSTAT_intp53-like transcription factorsSH2 domainSTATTranscription factor STAT-4 N-domainSH2HSSignal transducer and activator of transcription 1-alpha/betaTranscription factor ISGF-3 components p91/p84STAT1Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors (PubMed:9724754, PubMed:12855578, PubMed:12764129, PubMed:15322115, PubMed:34508746, PubMed:35568036, PubMed:23940278). 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 (PubMed:28753426, PubMed:35568036). 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 (PubMed:28753426, PubMed:35568036). In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated (PubMed:26479788). 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 (PubMed:8156998). Becomes activated in response to KITLG/SCF and KIT signaling (PubMed:15526160). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:19088846). Involved in food tolerance in small intestine: associates with the Gasdermin-D, p13 cleavage product (13 kDa GSDMD) and promotes transcription of CIITA, inducing type 1 regulatory T (Tr1) cells in upper small intestine (By similarity).Isoform alpha homodimerizes upon IFN-gamma induced phosphorylation (PubMed:8605877, PubMed:28753426). Heterodimer with STAT2 upon IFN-alpha/beta induced phosphorylation (PubMed:8605877). The heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9 (By similarity). Interacts (phosphorylated at Ser-727) with PIAS1; the interaction results in release of STAT1 from its target gene (PubMed:9724754, PubMed:17897103). Interacts with IFNAR1; the interaction requires the phosphorylation of IFNAR1 at 'Tyr-466' (PubMed:9121453). Interacts with IFNAR2 (PubMed:9121453). Found in a complex with NMI and CREBBP/CBP (PubMed:9989503). Interacts with NMI which is required for CREBBP/CBP recruitment to the complex (PubMed:9989503). Interacts with PTK2/FAK1 (PubMed:11278462). Interacts with SRC (By similarity). Interacts with ERBB4 (phosphorylated) (PubMed:18721752). Interacts with PARP9 and DTX3L independently of IFN-beta or IFN-gamma-mediated STAT1 'Tyr-701' phosphorylation (PubMed:26479788). Interacts with histone acetyltransferase EP300/p300 in response to INF-gamma stimulation (PubMed:16257975, PubMed:26479788). Interacts with OTOP1 (By similarity). Interacts with IFNGR1 (PubMed:8156998). Interacts with STAT4 (PubMed:34508746).(Microbial infection) Interacts with Sendai virus C', C, Y1 and Y2 proteins, preventing activation of ISRE and GAS promoter.(Microbial infection) Interacts with Nipah virus P, V and W proteins preventing activation of ISRE and GAS promoter.(Microbial infection) Interacts with Rabies virus phosphoprotein preventing activation of ISRE and GAS promoter.(Microbial infection) Interacts with HCV core protein; the interaction results in STAT1 degradation.(Microbial infection) Interacts with ebolavirus protein VP24.(Microbial infection) Interacts with Epstein-Barr virus (EBV) tegument protein BGLF2; this interaction leads to STAT1 dephosphorylation and inhibition.Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to IFN-gamma and signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4 (PubMed:15322115). Monomethylation at Lys-525 is required for phosphorylation at Tyr-701 and translocation into the nucleus (PubMed:28753426). Translocates into the nucleus in response to interferon-beta stimulation (PubMed:26479788).Deubiquitinated by USP13; leading to STAT1 stabilization and positive regulation of type I and type II IFN signalings.Phosphorylated on tyrosine and serine residues in response to a variety of cytokines/growth hormones including IFN-alpha, IFN-gamma, PDGF and EGF (PubMed:28753426, PubMed:26479788). Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus (PubMed:21135090). Upon EGF stimulation, phosphorylation on Tyr-701 (lacking in beta form) by JAK1, JAK2 or TYK2 promotes dimerization and subsequent translocation to the nucleus (PubMed:7657660, PubMed:28753426). Growth hormone (GH) activates STAT1 signaling only via JAK2 (PubMed:7657660). Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:17561467, PubMed:19088846). Phosphorylation on Ser-727 by several kinases including MAPK14, ERK1/2, CAMK2/CAMKII and CK2 in response to IFN-gamma stimulation, is required for maximal transcriptional activity (PubMed:7543024, PubMed:15322115, PubMed:16799645, PubMed:17897103). Phosphorylated on Ser-727 by CAMK2/CAMKII in response to IFN-gamma stimulation and calcium mobilization, promoting activity (PubMed:11972023, PubMed:16257975). Phosphorylated by CAMK2/CAMKII in response to IFN-beta stimulation and calcium mobilization in epithelial cells, promoting activity (PubMed:35568036). Phosphorylation on Ser-727 promotes sumoylation though increasing interaction with PIAS (PubMed:17897103). Phosphorylation on Ser-727 by PRKCD induces apoptosis in response to DNA-damaging agents (PubMed:15322115). Phosphorylated on tyrosine residues when PTK2/FAK1 is activated; most likely this is catalyzed by a SRC family kinase (PubMed:11278462). Dephosphorylation on tyrosine residues by PTPN2 negatively regulates interferon-mediated signaling (PubMed:12138178). 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 (PubMed:22065572). Phosphorylation at Tyr-701 and Ser-708 are mutually exclusive, phosphorylation at Ser-708 requires previous dephosphorylation of Tyr-701 (PubMed:22065572).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.ISGylated.Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-ribosylation prevents phosphorylation at Tyr-701 (PubMed:27796300). However, the role of ADP-ribosylation in the prevention of phosphorylation has been called into question and the lack of phosphorylation may be due to sumoylation of Lys-703 (PubMed:29858569).Monomethylated at Lys-525 by SETD2; monomethylation is necessary for phosphorylation at Tyr-701, translocation into the nucleus and activation of the antiviral defense.(Microbial infection) Ubiquitinated by Herpes simplex virus 2 E3 ubiquitin ligase ICP22.The disease is caused by variants affecting the gene represented in this entry.The disease is caused by variants affecting the gene represented in this entry.The disease is caused by variants 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 (PubMed:21714643).Belongs to the transcription factor STAT family.Has been shown to be mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14 which prevents phosphorylation at Tyr-701 (PubMed:27796300). However, the role of ADP-ribosylation in the prevention of phosphorylation has been called into question (PubMed:29858569). It has been suggested that the lack of phosphorylation may be due to sumoylation of Lys-703 (PubMed:29858569).Removed1Signal transducer and activator of transcription 1-alpha/beta872042750SH2573670136317Required for recruitment of EP300/p300724N-acetylserineN6-methyllysine114N6-methyllysine175N6-methyllysine296N6-methyllysine366N6-methyllysine525N6-methyllysine637ADP-ribosyl glutamic acid; by PARP14657N6-methyllysine665Phosphotyrosine; by JAK1, JAK2 or TYK2701ADP-ribosyl glutamic acid; by PARP14705Phosphoserine; by IKKE708Phosphoserine; by CAMK2 and MAPK14727Phosphoserine; by IKKE745Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateIn isoform Beta.713T30In IMD31C; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation.G165In IMD31C.HIn IMD31C.N170In IMD31C.R174In IMD31C; gain of function; increases transactivation activity in response to IFNG.K179In IMD31B; 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%.N201In IMD31C.I202In IMD31C.VIn IMD31C.V267In IMD31C.P271In IMD31C; gain of function; increases STAT1 phosphorylation due to impaired nuclear dephosphorylation; increases transactivation activity in response to IFNG.Q274In IMD31C; gain of function; increases phosphorylation in response to IFNG, IFNA and IL27 due to a loss of dephosphorylation.WIn IMD31C; gain of function; increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation.E278In IMD31C; gain of function; increases transactivation activity in response to IFNG.R285In IMD31C.I286In IMD31C.A288In IMD31C; gain of function; increases basal STAT1 phosphorylation levels which are 10-20 fold higher than controls after IFNG stimulation.N298In IMD31A; affects the DNA-binding activity of the protein.Q320In IMD31C; gain of function; increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation.D384In IMD31C; gain of function; increases phosphorylation in response to IFNG, IFNA and IL27 due to a loss of dephosphorylation.M385In IMD31A; affects the DNA-binding activity of the protein.H463In a breast cancer sample; somatic mutation.A491In IMD31B; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency.P600In IMD31A; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27.EIn IMD31A; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27.R673In IMD31B; disrupts transactivation activity in response to IFNG.CIn IMD31A; 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.S706Sumoylated.R110No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation.ANo effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation.ANo effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation.ANo effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation.AStrongly reduced IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. Does not affect ability to homodimerize.ANo effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation.AA636Enhances STAT1 nuclear translocation and interferon (IFN)-stimulated gene (ISG) expression in response to IFN-beta stimulation. Reduces viral load in infected cultured cells.CEC656658Loss of ADP-ribosylation and increased Tyr-701 phosphorylation; when associated with Q-705.QNo effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation.ANot phosphorylated at S-708 upon IFNB induction.ENo effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation. Phosphorylated at S-708 upon IFNB induction.FAbolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation.RLoss of ADP-ribosylation and increased Tyr-701 phosphorylation; when associated with Q-657.QPhosphorylated at Y-701 upon IFNB induction.ANot phosphorylated at Y-701 upon IFNB induction.DImpaired phosphorylation at S-727.ADecreased 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.ANo change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation.DNo change in enhancement of MAPK-induced sumoylation.ET46G307R718381221232628333540435073779499122134176192233235247257293315324334336341349352354355357359365370373374376380387389391395396398401411421425426428433441444451455460461464477484488495509516527539542550552554568570574584591592594598603612618621624627631641644650652654659668677678680709711728738739742743746748false2false2false7false4false3false6false2false2false4false6false4false3false3false3false4false2false4false16false8true6true2true2true2true2true2true5true2true4false8false3true2false4STAT1DDB1E2F1EGFREIF1ADERBB2FOSIFNAR1IFNAR2IFNGR1JAK1KPNA1MAVSOTUD4PTK2RIGIRXRASTAT2STAT3NOPG106SUL47STAT1KDM3ASTAT11997-11-01287335928d3192950db622b5cc70171385c78dAlphap91MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTVBetap84MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue