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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.
10-FEB-2021, entry version 183.
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:
Q9Y4H2; P27986: PIK3R1; NbExp=3; IntAct=EBI-1049582, EBI-79464;
Q9Y4H2; Q96EB6: SIRT1; NbExp=2; IntAct=EBI-1049582, EBI-1802965;
Q9Y4H2; P63104: YWHAZ; NbExp=3; 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.
PDB; 3FQW; X-ray; 1.93 A; C=1097-1105.
PDB; 3FQX; X-ray; 1.70 A; C=1097-1105.
PDBsum; 3FQW; -.
PDBsum; 3FQX; -.
SMR; Q9Y4H2; -.
BioGRID; 114209; 55.
ELM; Q9Y4H2; -.
IntAct; Q9Y4H2; 19.
MINT; Q9Y4H2; -.
STRING; 9606.ENSP00000365016; -.
iPTMnet; Q9Y4H2; -.
PhosphoSitePlus; Q9Y4H2; -.
BioMuta; IRS2; -.
DMDM; 62298062; -.
EPD; Q9Y4H2; -.
jPOST; Q9Y4H2; -.
MassIVE; Q9Y4H2; -.
MaxQB; Q9Y4H2; -.
PaxDb; Q9Y4H2; -.
PeptideAtlas; Q9Y4H2; -.
PRIDE; Q9Y4H2; -.
ProteomicsDB; 86205; -.
Antibodypedia; 25473; 339 antibodies.
DNASU; 8660; -.
Ensembl; ENST00000375856; ENSP00000365016; ENSG00000185950.
GeneID; 8660; -.
KEGG; hsa:8660; -.
UCSC; uc001vqv.4; human.
CTD; 8660; -.
DisGeNET; 8660; -.
GeneCards; IRS2; -.
HGNC; HGNC:6126; IRS2.
HPA; ENSG00000185950; Tissue enhanced (bone).
MalaCards; IRS2; -.
MIM; 600797; gene.
neXtProt; NX_Q9Y4H2; -.
OpenTargets; ENSG00000185950; -.
PharmGKB; PA375; -.
VEuPathDB; HostDB:ENSG00000185950.8; -.
eggNOG; ENOG502QUNU; Eukaryota.
GeneTree; ENSGT00940000161407; -.
HOGENOM; CLU_004902_1_0_1; -.
InParanoid; Q9Y4H2; -.
OMA; YKAPYTC; -.
OrthoDB; 298675at2759; -.
PhylomeDB; Q9Y4H2; -.
TreeFam; TF325994; -.
PathwayCommons; Q9Y4H2; -.
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-9006335; Signaling by Erythropoietin.
Reactome; R-HSA-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
Reactome; R-HSA-9027277; Erythropoietin activates Phospholipase C gamma (PLCG).
Reactome; R-HSA-9027283; Erythropoietin activates STAT5.
Reactome; R-HSA-9027284; Erythropoietin activates RAS.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; Q9Y4H2; -.
SIGNOR; Q9Y4H2; -.
BioGRID-ORCS; 8660; 146 hits in 879 CRISPR screens.
ChiTaRS; IRS2; human.
EvolutionaryTrace; Q9Y4H2; -.
GeneWiki; IRS2; -.
GenomeRNAi; 8660; -.
Pharos; Q9Y4H2; Tbio.
PRO; PR:Q9Y4H2; -.
Proteomes; UP000005640; Chromosome 13.
RNAct; Q9Y4H2; protein.
Bgee; ENSG00000185950; Expressed in decidua and 249 other tissues.
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: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: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:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007420; P:brain development; 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 long-chain fatty acid import across plasma membrane; 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 population 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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; 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; Cytoplasm; Methylation; Phosphoprotein; Reference proteome;
Transducer.
CHAIN 1..1338
/note="Insulin receptor substrate 2"
/id="PRO_0000084239"
DOMAIN 16..144
/note="PH"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
DOMAIN 194..298
/note="IRS-type PTB"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
MOTIF 540..543
/note="YXXM motif 1"
MOTIF 598..601
/note="YXXM motif 2"
MOTIF 653..656
/note="YXXM motif 3"
MOTIF 675..678
/note="YXXM motif 4"
MOTIF 742..745
/note="YXXM motif 5"
MOTIF 823..826
/note="YXXM motif 6"
MOTIF 1072..1075
/note="YXXM motif 7"
COMPBIAS 19..28
/note="Poly-Asn"
COMPBIAS 371..380
/note="Poly-Ala"
COMPBIAS 447..452
/note="Poly-Ser"
COMPBIAS 460..467
/note="Poly-Pro"
COMPBIAS 533..537
/note="Poly-Gly"
COMPBIAS 642..645
/note="Poly-Ser"
COMPBIAS 694..701
/note="Poly-Ala"
COMPBIAS 944..947
/note="Poly-Ser"
COMPBIAS 1031..1038
/note="Poly-Pro"
COMPBIAS 1265..1278
/note="Poly-Pro"
MOD_RES 306
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
MOD_RES 346
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 350
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163"
MOD_RES 365
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 384
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 388
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087, ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231"
MOD_RES 391
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087, ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:20068231"
MOD_RES 412
/note="Omega-N-methylarginine"
/evidence="ECO:0000244|PubMed:24129315"
MOD_RES 520
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 523
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 527
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163"
MOD_RES 540
/note="Phosphotyrosine; by INSR"
/evidence="ECO:0000250"
MOD_RES 560
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
MOD_RES 577
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163"
MOD_RES 579
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163"
MOD_RES 580
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 594
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 608
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 620
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 653
/note="Phosphotyrosine; by INSR"
/evidence="ECO:0000250|UniProtKB:P81122"
MOD_RES 675
/note="Phosphotyrosine; by INSR"
/evidence="ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163"
MOD_RES 679
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163"
MOD_RES 682
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 735
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 736
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
MOD_RES 770
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 779
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 805
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 828
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 915
/note="Phosphoserine"
/evidence="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
/note="Phosphotyrosine; by INSR"
/evidence="ECO:0000250"
MOD_RES 973
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
MOD_RES 978
/note="Phosphotyrosine; by INSR"
/evidence="ECO:0000250"
MOD_RES 1082
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 1100
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
MOD_RES 1159
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 1162
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 1174
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163"
MOD_RES 1176
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
MOD_RES 1186
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 1203
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163"
MOD_RES 1253
/note="Phosphotyrosine; by INSR"
/evidence="ECO:0000250"
VARIANT 789
/note="H -> Y (in dbSNP:rs35223808)"
/id="VAR_033992"
VARIANT 879
/note="G -> S (in dbSNP:rs549588978)"
/evidence="ECO:0000269|Ref.5"
/id="VAR_021557"
VARIANT 882
/note="G -> A (in dbSNP:rs201499247)"
/evidence="ECO:0000269|Ref.5"
/id="VAR_021558"
VARIANT 999
/note="V -> M (in dbSNP:rs35927012)"
/id="VAR_033993"
VARIANT 1057
/note="G -> D (in dbSNP:rs1805097)"
/evidence="ECO:0000269|PubMed:12687350"
/id="VAR_014857"
CONFLICT 28
/note="N -> NN (in Ref. 2; AAD21531)"
/evidence="ECO:0000305"
CONFLICT 39..41
/note="KQK -> NEE (in Ref. 2; AAD21531)"
/evidence="ECO:0000305"
CONFLICT 59
/note="E -> K (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 81
/note="K -> N (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 107
/note="A -> P (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 171
/note="L -> V (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 371
/note="A -> R (in Ref. 2; AAD21531)"
/evidence="ECO:0000305"
CONFLICT 379..382
/note="GARP -> AQRL (in Ref. 2; AAD21531)"
/evidence="ECO:0000305"
CONFLICT 406
/note="S -> I (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 410..419
/note="GGRGSKVALL -> RAAGTKWHCF (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 424
/note="A -> G (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 436..438
/note="AHS -> EHL (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 453
/note="G -> D (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 456
/note="S -> W (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 468
/note="P -> L (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 662
/note="L -> F (in Ref. 2; AAD21531)"
/evidence="ECO:0000305"
CONFLICT 704
/note="S -> F (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 714
/note="S -> F (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 848
/note="S -> T (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 872
/note="P -> R (in Ref. 2; AAD21531)"
/evidence="ECO:0000305"
CONFLICT 875..878
/note="GRPE -> RRS (in Ref. 2; AAD21531)"
/evidence="ECO:0000305"
CONFLICT 956
/note="S -> L (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 1252
/note="N -> K (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 1303
/note="G -> R (in Ref. 1; BAA24500)"
/evidence="ECO:0000305"
CONFLICT 1314..1338
/note="LPPANTYASIDFLSHHLKEATIVKE -> PAPCPTTYAQH (in Ref. 1;
BAA24500)"
/evidence="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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WP1183: Toll-like receptor signaling pathway
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WP1367: TGF-beta Receptor Signaling Pathway
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Related Genes :
[Irs1 Irs-1] Insulin receptor substrate 1 (IRS-1) (pp185)
[Irs1 Irs-1] Insulin receptor substrate 1 (IRS-1)
[BAIAP2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Protein BAP2) (Fas ligand-associated factor 3) (FLAF3) (Insulin receptor substrate p53/p58) (IRS-58) (IRSp53/58) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53)
[IRS1] Insulin receptor substrate 1 (IRS-1)
[IRS4] Insulin receptor substrate 4 (IRS-4) (160 kDa phosphotyrosine protein) (py160) (Phosphoprotein of 160 kDa) (pp160)
[Baiap2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase substrate protein p53)
[Irs4] Insulin receptor substrate 4 (IRS-4) (Phosphoprotein of 160 kDa) (pp160)
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[INSR] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[daf-2 Y55D5A.5] Insulin-like receptor (IR) (EC 2.7.10.1) (Abnormal dauer formation protein 2) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta]
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain] (Fragment)
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Baiap2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase 53 kDa substrate)
[InR dinr Dir-a Inr-a CG18402] Insulin-like receptor (dIR) (dInr) (EC 2.7.10.1) (dIRH) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta 1; Insulin-like receptor subunit beta 2]
[DOK4] Docking protein 4 (Downstream of tyrosine kinase 4) (Insulin receptor substrate 5) (IRS-5) (IRS5)
[DOK5 C20orf180] Docking protein 5 (Downstream of tyrosine kinase 5) (Insulin receptor substrate 6) (IRS-6) (IRS6)
[Krt71 K6irs1 Kb34 Krt2-6g Krt6g] Keratin, type II cytoskeletal 71 (Cytokeratin-6G) (CK-6G) (Cytokeratin-71) (CK-71) (Keratin-6G) (K6G) (Keratin-71) (K71) (Type II inner root sheath-specific keratin-K6irs1) (mK6irs) (mK6irs1/Krt2-6g) (Type-II keratin Kb34)
[IGF2R MPRI] Cation-independent mannose-6-phosphate receptor (CI Man-6-P receptor) (CI-MPR) (M6PR) (300 kDa mannose 6-phosphate receptor) (MPR 300) (Insulin-like growth factor 2 receptor) (Insulin-like growth factor II receptor) (IGF-II receptor) (M6P/IGF2 receptor) (M6P/IGF2R) (CD antigen CD222)
[Igf2r] Cation-independent mannose-6-phosphate receptor (CI Man-6-P receptor) (CI-MPR) (M6PR) (300 kDa mannose 6-phosphate receptor) (MPR 300) (Insulin-like growth factor 2 receptor) (Insulin-like growth factor II receptor) (IGF-II receptor) (M6P/IGF2 receptor) (M6P/IGF2R) (CD antigen CD222)
[IGF2R M6P] Cation-independent mannose-6-phosphate receptor (CI Man-6-P receptor) (CI-MPR) (M6PR) (300 kDa mannose 6-phosphate receptor) (MPR 300) (Insulin-like growth factor 2 receptor) (Insulin-like growth factor II receptor) (IGF-II receptor) (CD antigen CD222)
[irs1-a] Insulin receptor substrate 1-A (IRS1-A) (xIRS-1-A) (XIRS-L)
[IGF2 PP1446] Insulin-like growth factor II (IGF-II) (Somatomedin-A) (T3M-11-derived growth factor) [Cleaved into: Insulin-like growth factor II; Insulin-like growth factor II Ala-25 Del; Preptin]
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[Znf106 H3a Sh3bp3 Sirm Zfp106 Znf474] Zinc finger protein 106 (Zfp-106) (H3a minor histocompatibility antigen) (Son of insulin receptor mutant) (Zinc finger protein 474)
[Ptpre Ptpe] Receptor-type tyrosine-protein phosphatase epsilon (Protein-tyrosine phosphatase epsilon) (R-PTP-epsilon) (EC 3.1.3.48)
[Slc2a4 Glut4] Solute carrier family 2, facilitated glucose transporter member 4 (GT2) (Glucose transporter type 4, insulin-responsive) (GLUT-4)
[Frs2 Frs2a] Fibroblast growth factor receptor substrate 2 (FGFR substrate 2) (FGFR-signaling adaptor SNT) (FRS2-alpha) (Suc1-associated neurotrophic factor target 1) (SNT-1)

Bibliography :
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