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Insulin receptor substrate 2 (IRS-2)

 IRS2_HUMAN              Reviewed;        1338 AA.
Q9Y4H2; Q96RR2; Q9BZG0; Q9Y6I5;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 2.
12-SEP-2018, entry version 168.
RecName: Full=Insulin receptor substrate 2;
Short=IRS-2;
Name=IRS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9312143; DOI=10.1074/jbc.272.40.25267;
Ogihara T., Isobe T., Ichimura T., Taoka M., Funaki M., Sakoda H.,
Onishi Y., Inukai K., Anai M., Fukushima Y., Kikuchi M., Yazaki Y.,
Oka Y., Asano T.;
"14-3-3 protein binds to insulin receptor substrate-1, one of the
binding sites of which is in the phosphotyrosine binding domain.";
J. Biol. Chem. 272:25267-25274(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10077005; DOI=10.1210/mend.13.3.0256;
Vassen L., Wegrzyn W., Klein-Hitpass L.;
"Human insulin receptor substrate-2 (IRS-2) is a primary progesterone
response gene.";
Mol. Endocrinol. 13:485-494(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Heyne B.;
"Insulin receptor substrate 2 gene sequence.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
NUCLEOTIDE SEQUENCE OF 1-1337, AND VARIANTS SER-879 AND ALA-882.
Heyne B., Gehrisch S., Jaross W.;
"Two missense mutations in insulin receptor substrate 2 (G879S and
G882A).";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-391 AND
SER-560, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-350 AND THR-527, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-391 AND
SER-915, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-346; THR-350;
SER-365; SER-384; SER-388; SER-391; SER-523; THR-527; SER-577;
THR-579; THR-580; SER-594; SER-608; SER-620; SER-679; SER-735;
SER-736; SER-770; THR-779; SER-828; SER-915; SER-973; SER-1100;
THR-1159; SER-1162; SER-1174; SER-1176 AND SER-1203, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-388; SER-391;
SER-560; SER-594; TYR-675; SER-736; SER-915 AND SER-1176, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-560; SER-915
AND SER-1176, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; THR-350; THR-520;
THR-527; SER-560; SER-577; THR-579; SER-594; TYR-675; SER-679;
SER-682; SER-736; SER-805; SER-915; SER-973; SER-1100; SER-1174;
SER-1176; SER-1186 AND SER-1203, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594; SER-915; SER-973;
THR-1082 AND SER-1100, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-412, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[19]
VARIANT ASP-1057.
PubMed=12687350; DOI=10.1007/s00439-003-0935-3;
Lautier C., El Mkadem S.A., Renard E., Brun J.F., Gris J.-C.,
Bringer J., Grigorescu F.;
"Complex haplotypes of IRS2 gene are associated with severe obesity
and reveal heterogeneity in the effect of Gly1057Asp mutation.";
Hum. Genet. 113:34-43(2003).
-!- FUNCTION: May mediate the control of various cellular processes by
insulin.
-!- SUBUNIT: Interacts with PHIP. {ECO:0000250}.
-!- INTERACTION:
P27986:PIK3R1; NbExp=3; IntAct=EBI-1049582, EBI-79464;
Q96EB6:SIRT1; NbExp=2; IntAct=EBI-1049582, EBI-1802965;
P63104:YWHAZ; NbExp=2; IntAct=EBI-1049582, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
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EMBL; AB000732; BAA24500.1; -; Genomic_DNA.
EMBL; AF073310; AAD21531.1; -; mRNA.
EMBL; AF322115; AAG50013.1; -; Genomic_DNA.
EMBL; AF322114; AAG50013.1; JOINED; Genomic_DNA.
EMBL; AL162497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF288517; AAK83053.1; -; Genomic_DNA.
CCDS; CCDS9510.1; -.
RefSeq; NP_003740.2; NM_003749.2.
UniGene; Hs.442344; -.
PDB; 3FQW; X-ray; 1.93 A; C=1097-1105.
PDB; 3FQX; X-ray; 1.70 A; C=1097-1105.
PDBsum; 3FQW; -.
PDBsum; 3FQX; -.
ProteinModelPortal; Q9Y4H2; -.
SMR; Q9Y4H2; -.
BioGrid; 114209; 45.
ELM; Q9Y4H2; -.
IntAct; Q9Y4H2; 15.
MINT; Q9Y4H2; -.
STRING; 9606.ENSP00000365016; -.
iPTMnet; Q9Y4H2; -.
PhosphoSitePlus; Q9Y4H2; -.
BioMuta; IRS2; -.
DMDM; 62298062; -.
EPD; Q9Y4H2; -.
MaxQB; Q9Y4H2; -.
PaxDb; Q9Y4H2; -.
PeptideAtlas; Q9Y4H2; -.
PRIDE; Q9Y4H2; -.
ProteomicsDB; 86205; -.
DNASU; 8660; -.
Ensembl; ENST00000375856; ENSP00000365016; ENSG00000185950.
GeneID; 8660; -.
KEGG; hsa:8660; -.
UCSC; uc001vqv.4; human.
CTD; 8660; -.
DisGeNET; 8660; -.
EuPathDB; HostDB:ENSG00000185950.8; -.
GeneCards; IRS2; -.
HGNC; HGNC:6126; IRS2.
HPA; CAB016944; -.
HPA; HPA054664; -.
MalaCards; IRS2; -.
MIM; 600797; gene.
neXtProt; NX_Q9Y4H2; -.
OpenTargets; ENSG00000185950; -.
PharmGKB; PA375; -.
eggNOG; ENOG410IXEK; Eukaryota.
eggNOG; ENOG410Z9EP; LUCA.
GeneTree; ENSGT00530000063420; -.
HOVERGEN; HBG000542; -.
InParanoid; Q9Y4H2; -.
KO; K07187; -.
OMA; MHEYPLP; -.
OrthoDB; EOG091G02EF; -.
PhylomeDB; Q9Y4H2; -.
TreeFam; TF325994; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-112399; IRS-mediated signalling.
Reactome; R-HSA-112412; SOS-mediated signalling.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1266695; Interleukin-7 signaling.
Reactome; R-HSA-198203; PI3K/AKT activation.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-2428928; IRS-related events triggered by IGF1R.
Reactome; R-HSA-2586552; Signaling by Leptin.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-74713; IRS activation.
Reactome; R-HSA-74749; Signal attenuation.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; Q9Y4H2; -.
SIGNOR; Q9Y4H2; -.
ChiTaRS; IRS2; human.
EvolutionaryTrace; Q9Y4H2; -.
GeneWiki; IRS2; -.
GenomeRNAi; 8660; -.
PMAP-CutDB; Q9Y4H2; -.
PRO; PR:Q9Y4H2; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000185950; Expressed in 236 organ(s), highest expression level in decidua.
CleanEx; HS_IRS2; -.
Genevisible; Q9Y4H2; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
GO; GO:0005158; F:insulin receptor binding; IBA:GO_Central.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IBA:GO_Central.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
GO; GO:0006006; P:glucose metabolic process; TAS:ProtInc.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0055088; P:lipid homeostasis; TAS:BHF-UCL.
GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0002903; P:negative regulation of B cell apoptotic process; ISS:BHF-UCL.
GO; GO:0033673; P:negative regulation of kinase activity; ISS:BHF-UCL.
GO; GO:0010748; P:negative regulation of plasma membrane long-chain fatty acid transport; IMP:BHF-UCL.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; NAS:BHF-UCL.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:BHF-UCL.
GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IMP:BHF-UCL.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:BHF-UCL.
GO; GO:0032024; P:positive regulation of insulin secretion; ISS:BHF-UCL.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:BHF-UCL.
GO; GO:0009749; P:response to glucose; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd01204; PTB_IRS; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR039011; IRS.
InterPro; IPR002404; IRS_PTB.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR10614; PTHR10614; 1.
Pfam; PF02174; IRS; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00628; INSULINRSI.
SMART; SM00233; PH; 1.
SMART; SM00310; PTBI; 1.
PROSITE; PS51064; IRS_PTB; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Methylation;
Phosphoprotein; Polymorphism; Reference proteome; Transducer.
CHAIN 1 1338 Insulin receptor substrate 2.
/FTId=PRO_0000084239.
DOMAIN 16 144 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 194 298 IRS-type PTB. {ECO:0000255|PROSITE-
ProRule:PRU00389}.
MOTIF 540 543 YXXM motif 1.
MOTIF 598 601 YXXM motif 2.
MOTIF 653 656 YXXM motif 3.
MOTIF 675 678 YXXM motif 4.
MOTIF 742 745 YXXM motif 5.
MOTIF 823 826 YXXM motif 6.
MOTIF 1072 1075 YXXM motif 7.
COMPBIAS 19 28 Poly-Asn.
COMPBIAS 371 380 Poly-Ala.
COMPBIAS 447 452 Poly-Ser.
COMPBIAS 460 467 Poly-Pro.
COMPBIAS 533 537 Poly-Gly.
COMPBIAS 642 645 Poly-Ser.
COMPBIAS 694 701 Poly-Ala.
COMPBIAS 944 947 Poly-Ser.
COMPBIAS 1031 1038 Poly-Pro.
COMPBIAS 1265 1278 Poly-Pro.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 350 350 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231}.
MOD_RES 412 412 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 520 520 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 527 527 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 540 540 Phosphotyrosine; by INSR. {ECO:0000250}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 577 577 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 579 579 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 580 580 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 653 653 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:P81122}.
MOD_RES 675 675 Phosphotyrosine; by INSR.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 679 679 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 682 682 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 735 735 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 779 779 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 805 805 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 828 828 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 915 915 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 919 919 Phosphotyrosine; by INSR. {ECO:0000250}.
MOD_RES 973 973 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 978 978 Phosphotyrosine; by INSR. {ECO:0000250}.
MOD_RES 1082 1082 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1100 1100 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1159 1159 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1162 1162 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1174 1174 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1176 1176 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1186 1186 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1203 1203 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1253 1253 Phosphotyrosine; by INSR. {ECO:0000250}.
VARIANT 789 789 H -> Y (in dbSNP:rs35223808).
/FTId=VAR_033992.
VARIANT 879 879 G -> S (in dbSNP:rs549588978).
{ECO:0000269|Ref.5}.
/FTId=VAR_021557.
VARIANT 882 882 G -> A (in dbSNP:rs201499247).
{ECO:0000269|Ref.5}.
/FTId=VAR_021558.
VARIANT 999 999 V -> M (in dbSNP:rs35927012).
/FTId=VAR_033993.
VARIANT 1057 1057 G -> D (in dbSNP:rs1805097).
{ECO:0000269|PubMed:12687350}.
/FTId=VAR_014857.
CONFLICT 28 28 N -> NN (in Ref. 2; AAD21531).
{ECO:0000305}.
CONFLICT 39 41 KQK -> NEE (in Ref. 2; AAD21531).
{ECO:0000305}.
CONFLICT 59 59 E -> K (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 81 81 K -> N (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 107 107 A -> P (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 171 171 L -> V (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 371 371 A -> R (in Ref. 2; AAD21531).
{ECO:0000305}.
CONFLICT 379 382 GARP -> AQRL (in Ref. 2; AAD21531).
{ECO:0000305}.
CONFLICT 406 406 S -> I (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 410 419 GGRGSKVALL -> RAAGTKWHCF (in Ref. 1;
BAA24500). {ECO:0000305}.
CONFLICT 424 424 A -> G (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 436 438 AHS -> EHL (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 453 453 G -> D (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 456 456 S -> W (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 468 468 P -> L (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 662 662 L -> F (in Ref. 2; AAD21531).
{ECO:0000305}.
CONFLICT 704 704 S -> F (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 714 714 S -> F (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 848 848 S -> T (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 872 872 P -> R (in Ref. 2; AAD21531).
{ECO:0000305}.
CONFLICT 875 878 GRPE -> RRS (in Ref. 2; AAD21531).
{ECO:0000305}.
CONFLICT 956 956 S -> L (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 1252 1252 N -> K (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 1303 1303 G -> R (in Ref. 1; BAA24500).
{ECO:0000305}.
CONFLICT 1314 1338 LPPANTYASIDFLSHHLKEATIVKE -> PAPCPTTYAQH
(in Ref. 1; BAA24500). {ECO:0000305}.
SEQUENCE 1338 AA; 137334 MW; 58E569E8BDBAF3D7 CRC64;
MASPPRHGPP GPASGDGPNL NNNNNNNNHS VRKCGYLRKQ KHGHKRFFVL RGPGAGGDEA
TAGGGSAPQP PRLEYYESEK KWRSKAGAPK RVIALDCCLN INKRADAKHK YLIALYTKDE
YFAVAAENEQ EQEGWYRALT DLVSEGRAAA GDAPPAAAPA ASCSASLPGA LGGSAGAAGA
EDSYGLVAPA TAAYREVWQV NLKPKGLGQS KNLTGVYRLC LSARTIGFVK LNCEQPSVTL
QLMNIRRCGH SDSFFFIEVG RSAVTGPGEL WMQADDSVVA QNIHETILEA MKALKELFEF
RPRSKSQSSG SSATHPISVP GARRHHHLVN LPPSQTGLVR RSRTDSLAAT PPAAKCSSCR
VRTASEGDGG AAAGAAAAGA RPVSVAGSPL SPGPVRAPLS RSHTLSGGCG GRGSKVALLP
AGGALQHSRS MSMPVAHSPP AATSPGSLSS SSGHGSGSYP PPPGPHPPLP HPLHHGPGQR
PSSGSASASG SPSDPGFMSL DEYGSSPGDL RAFCSHRSNT PESIAETPPA RDGGGGGEFY
GYMTMDRPLS HCGRSYRRVS GDAAQDLDRG LRKRTYSLTT PARQRPVPQP SSASLDEYTL
MRATFSGSAG RLCPSCPASS PKVAYHPYPE DYGDIEIGSH RSSSSNLGAD DGYMPMTPGA
ALAGSGSGSC RSDDYMPMSP ASVSAPKQIL QPRAAAAAAA AVPSAGPAGP APTSAAGRTF
PASGGGYKAS SPAESSPEDS GYMRMWCGSK LSMEHADGKL LPNGDYLNVS PSDAVTTGTP
PDFFSAALHP GGEPLRGVPG CCYSSLPRSY KAPYTCGGDS DQYVLMSSPV GRILEEERLE
PQATPGPSQA ASAFGAGPTQ PPHPVVPSPV RPSGGRPEGF LGQRGRAVRP TRLSLEGLPS
LPSMHEYPLP PEPKSPGEYI NIDFGEPGAR LSPPAPPLLA SAASSSSLLS ASSPASSLGS
GTPGTSSDSR QRSPLSDYMN LDFSSPKSPK PGAPSGHPVG SLDGLLSPEA SSPYPPLPPR
PSASPSSSLQ PPPPPPAPGE LYRLPPASAV ATAQGPGAAS SLSSDTGDNG DYTEMAFGVA
ATPPQPIAAP PKPEAARVAS PTSGVKRLSL MEQVSGVEAF LQASQPPDPH RGAKVIRADP
QGGRRRHSSE TFSSTTTVTP VSPSFAHNPK RHNSASVENV SLRKSSEGGV GVGPGGGDEP
PTSPRQLQPA PPLAPQGRPW TPGQPGGLVG CPGSGGSPMR RETSAGFQNG LNYIAIDVRE
EPGLPPQPQP PPPPLPQPGD KSSWGRTRSL GGLISAVGVG STGGGCGGPG PGALPPANTY
ASIDFLSHHL KEATIVKE


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