IRS1_MOUSE
ID IRS1_MOUSE Reviewed; 1233 AA.
AC P35569;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Insulin receptor substrate 1;
DE Short=IRS-1;
GN Name=Irs1; Synonyms=Irs-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8167159; DOI=10.1016/0167-4889(94)90261-5;
RA Araki E., Haag B.L. III, Kahn C.R.;
RT "Cloning of the mouse insulin receptor substrate-1 (IRS-1) gene and
RT complete sequence of mouse IRS-1.";
RL Biochim. Biophys. Acta 1221:353-356(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8448209; DOI=10.1016/0167-4781(93)90222-y;
RA Keller S.R., Aebersold R., Garner C.W., Lienhard G.E.;
RT "The insulin-elicited 160 kDa phosphotyrosine protein in mouse adipocytes
RT is an insulin receptor substrate 1: identification by cloning.";
RL Biochim. Biophys. Acta 1172:323-326(1993).
RN [3]
RP INTERACTION WITH FER.
RX PubMed=11006284; DOI=10.1074/jbc.m006665200;
RA Iwanishi M., Czech M.P., Cherniack A.D.;
RT "The protein-tyrosine kinase fer associates with signaling complexes
RT containing insulin receptor substrate-1 and phosphatidylinositol 3-
RT kinase.";
RL J. Biol. Chem. 275:38995-39000(2000).
RN [4]
RP INTERACTION WITH PHIP.
RX PubMed=11018022; DOI=10.1074/jbc.c000611200;
RA Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
RT "Cloning and characterization of PHIP, a novel insulin receptor substrate-1
RT pleckstrin homology domain interacting protein.";
RL J. Biol. Chem. 275:40492-40497(2000).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=10749573; DOI=10.1172/jci9017;
RA Ogata N., Chikazu D., Kubota N., Terauchi Y., Tobe K., Azuma Y., Ohta T.,
RA Kadowaki T., Nakamura K., Kawaguchi H.;
RT "Insulin receptor substrate-1 in osteoblast is indispensable for
RT maintaining bone turnover.";
RL J. Clin. Invest. 105:935-943(2000).
RN [6]
RP PHOSPHORYLATION AT SER-789.
RX PubMed=11598104; DOI=10.1074/jbc.c100483200;
RA Jakobsen S.N., Hardie D.G., Morrice N., Tornqvist H.E.;
RT "5'-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in mouse
RT C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside.";
RL J. Biol. Chem. 276:46912-46916(2001).
RN [7]
RP INTERACTION WITH UBTF AND PIK3CA, AND EFFECT ON CELL AND BODY SIZE.
RX PubMed=15197263; DOI=10.1073/pnas.0403328101;
RA Drakas R., Tu X., Baserga R.;
RT "Control of cell size through phosphorylation of upstream binding factor 1
RT by nuclear phosphatidylinositol 3-kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9272-9276(2004).
RN [8]
RP PHOSPHORYLATION AT SER-632.
RX PubMed=16098829; DOI=10.1016/j.cmet.2005.06.011;
RA Furukawa N., Ongusaha P., Jahng W.J., Araki K., Choi C.S., Kim H.J.,
RA Lee Y.H., Kaibuchi K., Kahn B.B., Masuzaki H., Kim J.K., Lee S.W.,
RA Kim Y.B.;
RT "Role of Rho-kinase in regulation of insulin action and glucose
RT homeostasis.";
RL Cell Metab. 2:119-129(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 AND SER-1097, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-414; SER-887;
RP SER-1096 AND SER-1097, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP INTERACTION WITH EIF2AK2.
RX PubMed=22948222; DOI=10.1210/en.2012-1400;
RA Carvalho-Filho M.A., Carvalho B.M., Oliveira A.G., Guadagnini D., Ueno M.,
RA Dias M.M., Tsukumo D.M., Hirabara S.M., Reis L.F., Curi R.,
RA Carvalheira J.B., Saad M.J.;
RT "Double-stranded RNA-activated protein kinase is a key modulator of insulin
RT sensitivity in physiological conditions and in obesity in mice.";
RL Endocrinology 153:5261-5274(2012).
RN [12]
RP INTERACTION WITH GKAP1, AND PHOSPHORYLATION.
RX PubMed=25586176; DOI=10.1074/jbc.m114.624759;
RA Ando Y., Shinozawa Y., Iijima Y., Yu B.C., Sone M., Ooi Y., Watanaka Y.,
RA Chida K., Hakuno F., Takahashi S.;
RT "Tumor necrosis factor (TNF)-alpha-induced repression of GKAP42 protein
RT levels through cGMP-dependent kinase (cGK)-Ialpha causes insulin resistance
RT in 3T3-L1 adipocytes.";
RL J. Biol. Chem. 290:5881-5892(2015).
RN [13]
RP INTERACTION WITH DGKZ, AND IDENTIFICATION IN A COMPLEX WITH DGKZ AND
RP PIP5K1A.
RX PubMed=27739494; DOI=10.1038/srep35438;
RA Liu T., Yu B., Kakino M., Fujimoto H., Ando Y., Hakuno F., Takahashi S.I.;
RT "A novel IRS-1-associated protein, DGKzeta regulates GLUT4 translocation in
RT 3T3-L1 adipocytes.";
RL Sci. Rep. 6:35438-35438(2016).
CC -!- FUNCTION: May mediate the control of various cellular processes by
CC insulin. When phosphorylated by the insulin receptor binds specifically
CC to various cellular proteins containing SH2 domains such as
CC phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates
CC phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via phosphorylated YXXM motifs) with PIK3R1 (By
CC similarity). Interacts with ROCK1 (By similarity). Interacts with GRB2
CC (By similarity). Interacts with SOCS7 (By similarity). Interacts (via
CC IRS-type PTB domain) with IGF1R and INSR (via the tyrosine-
CC phosphorylated NPXY motif) (By similarity). Interacts with UBTF and
CC PIK3CA (PubMed:15197263). Interacts (via PH domain) with PHIP
CC (PubMed:11018022). Interacts with FER (PubMed:11006284). Interacts with
CC ALK (By similarity). Interacts with EIF2AK2/PKR (PubMed:22948222).
CC Interacts with GKAP1 (PubMed:25586176). Interacts with DGKZ in the
CC absence of insulin; insulin stimulation decreases this interaction
CC (PubMed:27739494). Found in a ternary complex with DGKZ and PIP5K1A in
CC the absence of insulin stimulation (PubMed:27739494).
CC {ECO:0000250|UniProtKB:P35568, ECO:0000250|UniProtKB:P35570,
CC ECO:0000269|PubMed:11006284, ECO:0000269|PubMed:11018022,
CC ECO:0000269|PubMed:15197263, ECO:0000269|PubMed:22948222,
CC ECO:0000269|PubMed:25586176, ECO:0000269|PubMed:27739494}.
CC -!- INTERACTION:
CC P35569; Q03963: Eif2ak2; NbExp=2; IntAct=EBI-400825, EBI-2603444;
CC P35569; P26450: Pik3r1; NbExp=3; IntAct=EBI-400825, EBI-641764;
CC P35569; Q1XH17: Trim72; NbExp=4; IntAct=EBI-400825, EBI-16034016;
CC P35569; Q13625-2: TP53BP2; Xeno; NbExp=2; IntAct=EBI-400825, EBI-287091;
CC -!- TISSUE SPECIFICITY: Expressed in osteoblasts, but not in osteoclasts.
CC {ECO:0000269|PubMed:10749573}.
CC -!- PTM: Serine phosphorylation of IRS1 is a mechanism for insulin
CC resistance. Ser-307 phosphorylation inhibits insulin action through
CC disruption of IRS1 interaction with the insulin receptor (By
CC similarity). Phosphorylation of Tyr-891 is required for GRB2-binding
CC (By similarity). Phosphorylated by ALK. Phosphorylated at Ser-265, Ser-
CC 302, Ser-632 and Ser-1097 by RPS6KB1; phosphorylation induces
CC accelerated degradation of IRS1 (By similarity). Phosphorylated on
CC tyrosine residues in response to insulin (PubMed:25586176). In skeletal
CC muscles, dephosphorylated on Tyr-608 by TNS2 under anabolic conditions;
CC dephosphorylation results in the proteasomal degradation of IRS1 (By
CC similarity). {ECO:0000250|UniProtKB:P35568,
CC ECO:0000250|UniProtKB:P35570, ECO:0000269|PubMed:25586176}.
CC -!- PTM: Ubiquitinated by the Cul7-RING(FBXW8) complex in a mTOR-dependent
CC manner, leading to its degradation: the Cul7-RING(FBXW8) complex
CC recognizes and binds IRS1 previously phosphorylated by S6 kinase
CC (RPS6KB1 or RPS6KB2). {ECO:0000250}.
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DR EMBL; L24563; AAA39335.1; -; mRNA.
DR EMBL; X69722; CAA49378.1; -; mRNA.
DR PIR; S30185; S30185.
DR RefSeq; NP_034700.2; NM_010570.4.
DR PDB; 1AYB; X-ray; 3.00 A; P=887-898.
DR PDB; 5AXI; X-ray; 2.50 A; E=606-610.
DR PDBsum; 1AYB; -.
DR PDBsum; 5AXI; -.
DR AlphaFoldDB; P35569; -.
DR BMRB; P35569; -.
DR SMR; P35569; -.
DR BioGRID; 200788; 20.
DR CORUM; P35569; -.
DR DIP; DIP-32456N; -.
DR IntAct; P35569; 51.
DR MINT; P35569; -.
DR STRING; 10090.ENSMUSP00000063795; -.
DR iPTMnet; P35569; -.
DR PhosphoSitePlus; P35569; -.
DR SwissPalm; P35569; -.
DR jPOST; P35569; -.
DR MaxQB; P35569; -.
DR PaxDb; P35569; -.
DR PeptideAtlas; P35569; -.
DR PRIDE; P35569; -.
DR ProteomicsDB; 269333; -.
DR DNASU; 16367; -.
DR GeneID; 16367; -.
DR KEGG; mmu:16367; -.
DR CTD; 3667; -.
DR MGI; MGI:99454; Irs1.
DR eggNOG; ENOG502QUNU; Eukaryota.
DR InParanoid; P35569; -.
DR OrthoDB; 298675at2759; -.
DR PhylomeDB; P35569; -.
DR Reactome; R-MMU-109704; PI3K Cascade.
DR Reactome; R-MMU-112399; IRS-mediated signalling.
DR Reactome; R-MMU-112412; SOS-mediated signalling.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-198203; PI3K/AKT activation.
DR Reactome; R-MMU-201556; Signaling by ALK.
DR Reactome; R-MMU-2428928; IRS-related events triggered by IGF1R.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-74713; IRS activation.
DR Reactome; R-MMU-74749; Signal attenuation.
DR BioGRID-ORCS; 16367; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Irs1; mouse.
DR EvolutionaryTrace; P35569; -.
DR PRO; PR:P35569; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P35569; protein.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005899; C:insulin receptor complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005158; F:insulin receptor binding; ISS:UniProtKB.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:MGI.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISO:MGI.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0071398; P:cellular response to fatty acid; IMP:ARUK-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
DR GO; GO:0010631; P:epithelial cell migration; IGI:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IMP:MGI.
DR GO; GO:0030879; P:mammary gland development; IGI:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR GO; GO:0090275; P:negative regulation of somatostatin secretion; ISO:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IGI:MGI.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0070094; P:positive regulation of glucagon secretion; ISO:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:MGI.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:MGI.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:MGI.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IGI:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0031000; P:response to caffeine; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR CDD; cd01204; PTB_IRS; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR039011; IRS.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10614; PTHR10614; 1.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00628; INSULINRSI.
DR SMART; SM00233; PH; 1.
DR SMART; SM00310; PTBI; 1.
DR PROSITE; PS51064; IRS_PTB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome; Repeat; Transducer;
KW Ubl conjugation.
FT CHAIN 1..1233
FT /note="Insulin receptor substrate 1"
FT /id="PRO_0000084237"
FT DOMAIN 12..115
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 155..259
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 3..133
FT /note="Mediates interaction with PHIP"
FT /evidence="ECO:0000250"
FT REGION 257..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..893
FT /note="GRB2-binding"
FT /evidence="ECO:0000250"
FT REGION 1015..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 460..463
FT /note="YXXM motif 1"
FT MOTIF 546..549
FT /note="YXXM motif 2"
FT MOTIF 608..611
FT /note="YXXM motif 3"
FT MOTIF 628..631
FT /note="YXXM motif 4"
FT MOTIF 658..661
FT /note="YXXM motif 5"
FT MOTIF 727..730
FT /note="YXXM motif 6"
FT MOTIF 935..938
FT /note="YXXM motif 7"
FT MOTIF 983..986
FT /note="YXXM motif 8"
FT MOTIF 1006..1009
FT /note="YXXM motif 9"
FT COMPBIAS 261..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 99
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 265
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 302
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 307
FT /note="Phosphoserine; by IKKB, MAPK8 and RPS6KB1"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 460
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 522
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 608
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 628
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 632
FT /note="Phosphoserine; by RPS6KB1 and ROCK2"
FT /evidence="ECO:0000305|PubMed:16098829"
FT MOD_RES 658
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 789
FT /note="Phosphoserine; by AMPK and SIK2"
FT /evidence="ECO:0000269|PubMed:11598104"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 891
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 935
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 983
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1173
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 1220
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT CONFLICT 1038..1039
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1182
FT /note="H -> R (in Ref. 2; CAA49378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1233 AA; 130723 MW; C0E9B2D890DADD87 CRC64;
MASPPDTDGF SDVRKVGYLR KPKSMHKRFF VLRAASEAGG PARLEYYENE KKWRHKSSAP
KRSIPLESCF NINKRADSKN KHLVALYTRD EHFAIAADSE AEQDSWYQAL LQLHNRAKAH
HDGAGGGCGG SCSGSSGVGE AGEDLSYDTG PGPAFKEVWQ VILKPKGLGQ TKNLIGIYRL
CLTSKTISFV KLNSEAAAVV LQLMNIRRCG HSENFFFIEV GRSAVTGPGE FWMQVDDSVV
AQNMHETILE AMRAMSDEFR PRSKSQSSSS CSNPISVPLR RHHLNNPPPS QVGLTRRSRT
ESITATSPAS MVGGKPGSFR VRASSDGEGT MSRPASVDGS PVSPSTNRTH AHRHRGSSRL
HPPLNHSRSI PMPSSRCSPS ATSPVSLSSS STSGHGSTSD CLFPRRSSAS VSGSPSDGGF
ISSDEYGSSP CDFRSSFRSV TPDSLGHTPP ARGEEELSNY ICMGGKGAST LAAPNGHYIL
SRGGNGHRYI PGANLGTSPA LPGDEAAGAA DLDNRFRKRT HSAGTSPTIS HQKTPSQSSV
ASIEEYTEMM PAAYPPGGGS GGRLPGYRHS AFVPTHSYPE EGLEMHHLER RGGHHRPDTS
NLHTDDGYMP MSPGVAPVPS NRKGNGDYMP MSPKSVSAPQ QIINPIRRHP QRVDPNGYMM
MSPSGSCSPD IGGGSSSSSS ISAAPSGSSY GKPWTNGVGG HHTHALPHAK PPVESGGGKL
LPCTGDYMNM SPVGDSNTSS PSECYYGPED PQHKPVLSYY SLPRSFKHTQ RPGEPEEGAR
HQHLRLSSSS GRLRYTATAE DSSSSTSSDS LGGGYCGARP ESSLTHPHHH VLQPHLPRKV
DTAAQTNSRL ARPTRLSLGD PKASTLPRVR EQQQQQQSSL HPPEPKSPGE YVNIEFGSGQ
PGYLAGPATS RSSPSVRCPP QLHPAPREET GSEEYMNMDL GPGRRATWQE SGGVELGRIG
PAPPGSATVC RPTRSVPNSR GDYMTMQIGC PRQSYVDTSP VAPVSYADMR TGIAAEKASL
PRPTGAAPPP SSTASSSASV TPQGATAEQA THSSLLGGPQ GPGGMSAFTR VNLSPNHNQS
AKVIRADTQG CRRRHSSETF SAPTRAGNTV PFGAGAAVGG SGGGGGGGSE DVKRHSSASF
ENVWLRPGDL GGVSKESAPV CGAAGGLEKS LNYIDLDLAK EHSQDCPSQQ QSLPPPPPHQ
PLGSNEGNSP RRSSEDLSNY ASISFQKQPE DRQ
