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Signal transducer and activator of transcription 1

 STAT1_MOUSE             Reviewed;         749 AA.
P42225;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
12-SEP-2018, entry version 165.
RecName: Full=Signal transducer and activator of transcription 1;
Name=Stat1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
PubMed=7545930; DOI=10.1073/pnas.91.11.4806;
Zhong Z., Wen Z., Darnell J.E. Jr.;
"Stat3 and Stat4: members of the family of signal transducers and
activators of transcription.";
Proc. Natl. Acad. Sci. U.S.A. 91:4806-4810(1994).
[2]
PHOSPHORYLATION, FUNCTION, AND INTERACTION WITH SRC.
PubMed=9344858; DOI=10.1006/bbrc.1997.7493;
Cirri P., Chiarugi P., Marra F., Raugei G., Camici G., Manao G.,
Ramponi G.;
"c-Src activates both STAT1 and STAT3 in PDGF-stimulated NIH3T3
cells.";
Biochem. Biophys. Res. Commun. 239:493-497(1997).
[3]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=11294897; DOI=10.1091/mbc.12.4.931;
Hart K.C., Robertson S.C., Donoghue D.J.;
"Identification of tyrosine residues in constitutively activated
fibroblast growth factor receptor 3 involved in mitogenesis, Stat
activation, and phosphatidylinositol 3-kinase activation.";
Mol. Biol. Cell 12:931-942(2001).
[4]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
PubMed=12138178; DOI=10.1128/MCB.22.16.5662-5668.2002;
ten Hoeve J., de Jesus Ibarra-Sanchez M., Fu Y., Zhu W., Tremblay M.,
David M., Shuai K.;
"Identification of a nuclear Stat1 protein tyrosine phosphatase.";
Mol. Cell. Biol. 22:5662-5668(2002).
[5]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
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.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[6]
IDENTIFICATION IN THE ISGF3 COMPLEX, PHOSPHORYLATION AT SER-708 AND
SER-744, AND MUTAGENESIS OF SER-708 AND 744-SER--SER-747.
PubMed=17332413; DOI=10.1126/science.1136567;
Tenoever B.R., Ng S.L., Chua M.A., McWhirter S.M., Garcia-Sastre A.,
Maniatis T.;
"Multiple functions of the IKK-related kinase IKKepsilon in
interferon-mediated antiviral immunity.";
Science 315:1274-1278(2007).
[7]
FUNCTION, AND PHOSPHORYLATION AT TYR-701 IN RESPONSE TO CONSTITUTIVELY
ACTIVATED FGFR3.
PubMed=19088846; DOI=10.1371/journal.pone.0003961;
Krejci P., Salazar L., Kashiwada T.A., Chlebova K., Salasova A.,
Thompson L.M., Bryja V., Kozubik A., Wilcox W.R.;
"Analysis of STAT1 activation by six FGFR3 mutants associated with
skeletal dysplasia undermines dominant role of STAT1 in FGFR3
signaling in cartilage.";
PLoS ONE 3:E3961-E3961(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
PHOSPHORYLATION IN RESPONSE TO KIT SIGNALING.
PubMed=21135090; DOI=10.1074/jbc.M110.182642;
Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.;
"Mechanisms of STAT protein activation by oncogenic KIT mutants in
neoplastic mast cells.";
J. Biol. Chem. 286:5956-5966(2011).
[10]
FUNCTION, AND PHOSPHORYLATION AT TYR-701; SER-708 AND SER-727.
PubMed=22065572; DOI=10.1074/jbc.M111.285205;
Perwitasari O., Cho H., Diamond M.S., Gale M. Jr.;
"Inhibitor of kappaB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2
proteins define novel innate immune effector pathway against West Nile
virus infection.";
J. Biol. Chem. 286:44412-44423(2011).
[11]
INTERACTION WITH OTOP1.
PubMed=24379350; DOI=10.2337/db13-1139;
Wang G.X., Cho K.W., Uhm M., Hu C.R., Li S., Cozacov Z., Xu A.E.,
Cheng J.X., Saltiel A.R., Lumeng C.N., Lin J.D.;
"Otopetrin 1 protects mice from obesity-associated metabolic
dysfunction through attenuating adipose tissue inflammation.";
Diabetes 63:1340-1352(2014).
-!- FUNCTION: Signal transducer and transcription activator that
mediates cellular responses to interferons (IFNs), cytokine
KITLG/SCF and other cytokines and other growth factors. Following
type I IFN (IFN-alpha and IFN-beta) binding to cell surface
receptors, signaling via protein kinases leads to activation of
Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of
STAT1 and STAT2. The phosphorylated STATs dimerize and associate
with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription
factor, that enters the nucleus. ISGF3 binds to the IFN stimulated
response element (ISRE) to activate the transcription of IFN-
stimulated genes (ISG), which drive the cell in an antiviral
state. In response to type II IFN (IFN-gamma), STAT1 is
tyrosine- and serine-phosphorylated. It then forms a homodimer
termed IFN-gamma-activated factor (GAF), migrates into the nucleus
and binds to the IFN gamma activated sequence (GAS) to drive the
expression of the target genes, inducing a cellular antiviral
state. Becomes activated in response to KITLG/SCF and KIT
signaling. May mediate cellular responses to activated FGFR1,
FGFR2, FGFR3 and FGFR4. {ECO:0000269|PubMed:11294897,
ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:22065572,
ECO:0000269|PubMed:9344858}.
-!- SUBUNIT: Homodimerizes upon IFN-gamma induced phosphorylation (By
similarity). Heterodimer with STAT2 upon IFN-alpha/beta induced
phosphorylation (By similarity). The heterodimer STAT1:STAT2 forms
the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9
(PubMed:17332413). Interacts (phosphorylated at Ser-727) with
PIAS1 (dimethylated on arginine); the interaction results in
release of STAT1 from its target gene (By similarity). Interacts
with IFNAR1 (By similarity). Interacts with IFNAR2 (By
similarity). Found in a complex with NMI and CREBBP/CBP (By
similarity). Interacts with NMI which is required for CREBBP/CBP
recruitment to the complex (By similarity). Interacts with
PTK2/FAK1 (By similarity). Interacts with SRC (PubMed:9344858).
Interacts with ERBB4 (phosphorylated) (By similarity). Interacts
with PARP9 and DTX3L independently of IFN-beta or IFN-gamma-
mediated STAT1 'Tyr-701' phosphorylation (By similarity).
Interacts with histone acetyltransferase EP300/p300 in response to
INF-gamma stimulation (By similarity). Interacts with OTOP1
(PubMed:24379350). {ECO:0000250|UniProtKB:P42224,
ECO:0000269|PubMed:17332413, ECO:0000269|PubMed:24379350,
ECO:0000269|PubMed:9344858}.
-!- INTERACTION:
P29351:Ptpn6; NbExp=2; IntAct=EBI-647118, EBI-2620699;
P42228:Stat4; NbExp=2; IntAct=EBI-647118, EBI-6253572;
Q61069:Usf1; NbExp=2; IntAct=EBI-647118, EBI-2325635;
Q64705:Usf2; NbExp=3; IntAct=EBI-647118, EBI-647583;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11294897}.
Nucleus {ECO:0000269|PubMed:11294897}. Note=Translocated into the
nucleus upon tyrosine phosphorylation and dimerization, in
response to IFN-gamma and signaling by activated FGFR1, FGFR2,
FGFR3 or FGFR4. Monomethylation at Lys-525 is required for
phosphorylation at Tyr-701 and translocation into the nucleus.
Translocates into the nucleus in response to interferon-beta
stimulation. {ECO:0000250|UniProtKB:P42224}.
-!- INDUCTION: By IFN and EGF.
-!- PTM: 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. {ECO:0000269|PubMed:11294897,
ECO:0000269|PubMed:12138178, ECO:0000269|PubMed:17332413,
ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:21135090,
ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:9344858}.
-!- PTM: 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. {ECO:0000250|UniProtKB:P42224}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-
riboslyation prevents phosphorylation at Tyr-701.
{ECO:0000250|UniProtKB:P42224}.
-!- PTM: Monomethylated at Lys-525 by SETD2; monomethylation is
necessary for phosphorylation at Tyr-701, translocation into the
nucleus and activation of the antiviral defense.
{ECO:0000250|UniProtKB:P42224}.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
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EMBL; U06924; AAA19454.1; -; mRNA.
CCDS; CCDS56628.1; -.
UniGene; Mm.277406; -.
UniGene; Mm.487336; -.
ProteinModelPortal; P42225; -.
SMR; P42225; -.
DIP; DIP-38739N; -.
IntAct; P42225; 21.
STRING; 10090.ENSMUSP00000066743; -.
BindingDB; P42225; -.
ChEMBL; CHEMBL1667670; -.
iPTMnet; P42225; -.
PhosphoSitePlus; P42225; -.
SwissPalm; P42225; -.
EPD; P42225; -.
MaxQB; P42225; -.
PaxDb; P42225; -.
PeptideAtlas; P42225; -.
PRIDE; P42225; -.
MGI; MGI:103063; Stat1.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
HOVERGEN; HBG055669; -.
InParanoid; P42225; -.
PhylomeDB; P42225; -.
SABIO-RK; P42225; -.
ChiTaRS; Stat1; mouse.
PRO; PR:P42225; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0031730; F:CCR5 chemokine receptor binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:MGI.
GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
GO; GO:0042393; F:histone binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0008015; P:blood circulation; ISS:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0007259; P:JAK-STAT cascade; ISO:MGI.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
GO; GO:0072162; P:metanephric mesenchymal cell differentiation; ISS:UniProtKB.
GO; GO:0072136; P:metanephric mesenchymal cell proliferation involved in metanephros development; ISS:UniProtKB.
GO; GO:0046725; P:negative regulation by virus of viral protein levels in host cell; ISO:MGI.
GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0034240; P:negative regulation of macrophage fusion; IMP:MGI.
GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; ISS:UniProtKB.
GO; GO:0072308; P:negative regulation of metanephric nephron tubule epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0061326; P:renal tubule development; ISS:UniProtKB.
GO; GO:0009617; P:response to bacterium; IDA:MGI.
GO; GO:0051591; P:response to cAMP; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; ISO:MGI.
GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
GO; GO:0035456; P:response to interferon-beta; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
GO; GO:0009612; P:response to mechanical stimulus; ISO:MGI.
GO; GO:0007584; P:response to nutrient; ISO:MGI.
GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB.
GO; GO:0034340; P:response to type I interferon; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IMP:MGI.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
GO; GO:0060337; P:type I interferon signaling pathway; IMP:UniProtKB.
CDD; cd10372; SH2_STAT1; 1.
Gene3D; 1.10.532.10; -; 1.
Gene3D; 1.10.8.1200; -; 1.
Gene3D; 2.60.40.630; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR001217; STAT.
InterPro; IPR038295; STAT1_C_sf.
InterPro; IPR035859; STAT1_SH2.
InterPro; IPR022752; STAT1_TAZ2-bd_C.
InterPro; IPR036535; STAT_N_sf.
InterPro; IPR013800; STAT_TF_alpha.
InterPro; IPR015988; STAT_TF_coiled-coil.
InterPro; IPR013801; STAT_TF_DNA-bd.
InterPro; IPR012345; STAT_TF_DNA-bd_N.
InterPro; IPR013799; STAT_TF_prot_interaction.
PANTHER; PTHR11801; PTHR11801; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF12162; STAT1_TAZ2bind; 1.
Pfam; PF01017; STAT_alpha; 1.
Pfam; PF02864; STAT_bind; 1.
Pfam; PF02865; STAT_int; 1.
SMART; SM00964; STAT_int; 1.
SUPFAM; SSF47655; SSF47655; 1.
SUPFAM; SSF48092; SSF48092; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Acetylation; Activator; ADP-ribosylation; Coiled coil;
Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond;
Methylation; Nucleus; Phosphoprotein; Reference proteome; SH2 domain;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P42224}.
CHAIN 2 749 Signal transducer and activator of
transcription 1.
/FTId=PRO_0000182411.
DOMAIN 573 670 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
COILED 136 317 {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 114 114 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 175 175 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 296 296 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 366 366 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 525 525 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 637 637 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 657 657 ADP-ribosyl glutamic acid.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 665 665 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 701 701 Phosphotyrosine; by JAK1, JAK2 or TYK2.
{ECO:0000269|PubMed:19088846,
ECO:0000269|PubMed:22065572}.
MOD_RES 705 705 ADP-ribosyl glutamic acid.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 708 708 Phosphoserine; by IKKE.
{ECO:0000269|PubMed:17332413,
ECO:0000269|PubMed:22065572}.
MOD_RES 727 727 Phosphoserine; by MAPK14.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 744 744 Phosphoserine; by IKKE.
{ECO:0000305|PubMed:17332413}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P42224}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P42224}.
MUTAGEN 708 708 Missing: Strongly decreases ISGF3 binding
to the ISRE of IKBKE-dependent genes but
noo effect on ISGF3 binding to the ISRE
of IKBKE-independent genes.
{ECO:0000269|PubMed:17332413}.
MUTAGEN 744 747 SMMS->MM: No effect on ISGF3 binding to
ISREs. {ECO:0000269|PubMed:17332413}.
SEQUENCE 749 AA; 87197 MW; 249D919952BE65F1 CRC64;
MSQWFELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAAYDV SFATIRFHDL
LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPVQ MSMIIYNCLK EERKILENAQ
RFNQAQEGNI QNTVMLDKQK ELDSKVRNVK DQVMCIEQEI KTLEELQDEY DFKCKTSQNR
EGEANGVAKS DQKQEQLLLH KMFLMLDNKR KEIIHKIREL LNSIELTQNT LINDELVEWK
RRQQSACIGG PPNACLDQLQ TWFTIVAETL QQIRQQLKKL EELEQKFTYE PDPITKNKQV
LSDRTFLLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKSRLLVK LQESNLLTKV
KCHFDKDVNE KNTVKGFRKF NILGTHTKVM NMEESTNGSL AAELRHLQLK EQKNAGNRTN
EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVTE
PRNLSFFLNP PCAWWSQLSE VLSWQFSSVT KRGLNADQLS MLGEKLLGPN AGPDGLIPWT
RFCKENINDK NFSFWPWIDT ILELIKNDLL CLWNDGCIMG FISKERERAL LKDQQPGTFL
LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP
ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDDPKRTG YIKTELISVS EVHPSRLQTT
DNLLPMSPEE FDEMSRIVGP EFDSMMSTV


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15-288-22780 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.1 mg
15-288-22780 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg
18-003-43498 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg Aff Pur
18-003-43847 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg Aff Pur
FP-0102 Signal transducer and activator of transcription 4. 10 ug
FP-0101 Signal transducer and activator of transcription 3 10 ug
FP-0104 Signal transducer and activator of transcription 5B. 10ug
FP-0102 Signal transducer and activator of transcription 4. 10ug
FP-0101 Signal transducer and activator of transcription 3 10ug
FP-0103 Signal transducer and activator of transcription 5A. 10 ug
FP-0105 Signal transducer and activator of transcription 6 10ug
FP-0104 Signal transducer and activator of transcription 5B. 10 ug
FP-0105 Signal transducer and activator of transcription 6 10 ug
FP-0103 Signal transducer and activator of transcription 5A. 10ug
E02S0211 Rat Signal Transducer And Activator Of Transcription 5B ELISA 96T/kit
E02S0210 Rat Signal Transducer And Activator Of Transcription 5A ELISA 96T/kit
FP-0100 Signal transducer and activator of transcription 2 (p113). 10ug
E02S0206 Rat Signal Transducer And Activator Of Transcription 4 ELISA 96T/kit
pka-315 Recombinant Human Signal Transducer and Activator of Transcription 1 10
EM1378 Signal Transducer And Activator Of Transcription 2 Elisa Kit 96T
E02S0204 Rat Signal Transducer And Activator Of Transcription 3 ELISA 96T/kit


 

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