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Database: UniProt
Entry: IRS1B_XENLA
LinkDB: IRS1B_XENLA
Original site: IRS1B_XENLA 
ID   IRS1B_XENLA             Reviewed;        1088 AA.
AC   P84770;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   22-FEB-2023, entry version 60.
DE   RecName: Full=Insulin receptor substrate 1-B;
DE            Short=IRS1-B;
DE            Short=xIRS-1-B;
DE   AltName: Full=XIRS-L';
GN   Name=irs1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary {ECO:0000269|PubMed:7791763};
RX   PubMed=7791763; DOI=10.1128/mcb.15.7.3563;
RA   Liu X.J., Sorisky A., Zhu L., Pawson T.;
RT   "Molecular cloning of an amphibian insulin receptor substrate 1-like cDNA
RT   and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus
RT   oocyte maturation.";
RL   Mol. Cell. Biol. 15:3563-3570(1995).
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 with the NPXY motif of tyrosine-phosphorylated igf1r
CC       and insr via the PTB domain. Binds to phosphatidylinositol 3-kinase p85
CC       subunit at a low level in vitro prior to phosphorylation. Binding is
CC       greatly enhanced following tyrosine phosphorylation by insr and
CC       probably occurs via the phosphorylated YXXM motifs (By similarity).
CC       {ECO:0000250|UniProtKB:P35568, ECO:0000250|UniProtKB:Q91615}.
CC   -!- PTM: Phosphorylation of Tyr-785 is required for grb2-binding.
CC       {ECO:0000250}.
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DR   AlphaFoldDB; P84770; -.
DR   SMR; P84770; -.
DR   IntAct; P84770; 1.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR   CDD; cd01257; PH_IRS; 1.
DR   CDD; cd01204; PTB_IRS; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; INSULIN RECEPTOR SUBSTRATE; 1.
DR   PANTHER; PTHR10614:SF11; INSULIN RECEPTOR SUBSTRATE 1; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00628; INSULINRSI.
DR   SMART; SM01244; IRS; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS51064; IRS_PTB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome; Repeat; Transducer.
FT   CHAIN           1..1088
FT                   /note="Insulin receptor substrate 1-B"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000223525"
FT   DOMAIN          15..117
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          259..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..787
FT                   /note="GRB2-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   REGION          840..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           460..463
FT                   /note="YXXM motif 1"
FT                   /evidence="ECO:0000255"
FT   MOTIF           521..524
FT                   /note="YXXM motif 2"
FT                   /evidence="ECO:0000255"
FT   MOTIF           567..570
FT                   /note="YXXM motif 3"
FT                   /evidence="ECO:0000255"
FT   MOTIF           584..587
FT                   /note="YXXM motif 4"
FT                   /evidence="ECO:0000255"
FT   MOTIF           612..615
FT                   /note="YXXM motif 5"
FT                   /evidence="ECO:0000255"
FT   MOTIF           654..657
FT                   /note="YXXM motif 6"
FT                   /evidence="ECO:0000255"
FT   MOTIF           823..826
FT                   /note="YXXM motif 7"
FT                   /evidence="ECO:0000255"
FT   MOTIF           875..878
FT                   /note="YXXM motif 8"
FT                   /evidence="ECO:0000255"
FT   MOTIF           909..912
FT                   /note="YXXM motif 9"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        261..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..865
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..994
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         48
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         460
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         567
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         584
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         612
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         785
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         823
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         875
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1037
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1069
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1088 AA;  119106 MW;  1D656F5849D39B34 CRC64;
     MASPTDPQAQ ENFSDVRKVG YLRKPKSMHK RFFVLRAASE SSLARLEYYE NEKKWRHKSG
     APKRSIPLES CFNINKRADS KNKHLVALYT KDECFAIAAE CEQEQEGWYQ ALVDLHNRGK
     THHQHHNHDG AVNGVHDGLN GDEVYGEVTP PGLAFKEVWQ VIMKPKGLGQ LKNLVGIYRL
     CLTNRTISLV KLNSDAAAVV LQLMNIRRCG HSENFFFIEV GRSAVTGAGE FWMQVDDSVV
     AQNMHETILE AMKALSDEFR PRSKSQSSSN CSNPISVPLR RHHLNHPPPS QVGLNRRART
     ESATATSPAG GAAKHGSSSF RVRASSDGEG TMSRPASMEG SPVSPSASRT QSHRHRGSSR
     LHPPLNHSRS IPMPATRCSP SATSPVSLSS SSTSGHGSTS DCMCPRRSSA SISGSPSDGG
     FISSDEYGSS PCDFRSSFRS VTPDSMGHTP PAREEELNNY ICMGKSSSHL QRGPQQRYQP
     SRGEELTDFD KVFRKRTHSS GTSPPTVSHQ KTPSQSSIEE YTEMMPTHPV RLTSFRHSAF
     VPTYSYPEEC LDLHLEGSRA NHKDDGYMPM SPGVAPVSTK TNDYMPMSPK SVSAPQQIIN
     PRWHSAVDSN GYMMMSPSGS CSPDNTNYSK IWTNGTNPKL SIDSIEGKLP CSDYINMSPA
     SGSTTSTPPD SYLNSVEEST KPVYSYFSLP RSFKHVHRKS EDGNLRISAN SGHNLYTEDS
     SSSSTSSDSL GGQDPQQPRK GEGCIQGKRL TRPTRLSLEN SSKASTLPRV REPALPPEPK
     SPGEYVNIEF NDKVFSGGLV PSMCSLPFVQ SRVVPQRENL SEYMNMDLGV WRAKTSYAST
     SSYEPPNKPV NSVCPTETCS SSRPPIRGKP ISRDYMSMQL GSLCPDYSQV PPTRLSAKSI
     TLSSSKSNYA EMSSGRVSDN IPAIAPASNS SLSEASRSSL LGQGSGPSAF TRVSLSPNRN
     PSAKVIRAGD PQGRRRHSSE TFSSTPTTAR VTTGPVSGED VKRHSSASFE NVWLRPGEIA
     RRDSLQPSDH THNGLNYIDL DLAKDLSSLD HCNSHQSGVS HPSDDLSPYA SITFHKLEEH
     RSQAETEE
//
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