ID   C9J5X1_HUMAN            Unreviewed;      1366 AA.
AC   C9J5X1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   13-FEB-2019, entry version 96.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN   Name=IGF1R {ECO:0000313|Ensembl:ENSP00000453007};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000453007, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000453007, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA   Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA   Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA   Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA   Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA   Sneddon K.M., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA   Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA   Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human
RT   chromosome 15.";
RL   Nature 440:671-675(2006).
RN   [2] {ECO:0000213|PubMed:18691976}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [3] {ECO:0000213|PubMed:19369195}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [4] {ECO:0000213|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:ra3-RA3(2010).
RN   [5] {ECO:0000313|Ensembl:ENSP00000453007}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2012) to UniProtKB.
RN   [6] {ECO:0000313|Ensembl:ENSP00000496919}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (OCT-2018) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         EC=2.7.10.1; Evidence={ECO:0000256|RuleBase:RU000312,
CC         ECO:0000256|SAAS:SAAS01124082};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000312}.
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DR   EMBL; AC055807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC069029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC118658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC118660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001278787.1; NM_001291858.1.
DR   UniGene; Hs.643120; -.
DR   UniGene; Hs.714012; -.
DR   ProteinModelPortal; C9J5X1; -.
DR   IntAct; C9J5X1; 1.
DR   PRIDE; C9J5X1; -.
DR   Ensembl; ENST00000558762; ENSP00000453007; ENSG00000140443.
DR   Ensembl; ENST00000649865; ENSP00000496919; ENSG00000140443.
DR   GeneID; 3480; -.
DR   UCSC; uc010bon.4; human.
DR   CTD; 3480; -.
DR   EuPathDB; HostDB:ENSG00000140443.13; -.
DR   HGNC; HGNC:5465; IGF1R.
DR   OpenTargets; ENSG00000140443; -.
DR   eggNOG; KOG4258; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   GeneTree; ENSGT00940000156682; -.
DR   HOGENOM; HOG000038045; -.
DR   OrthoDB; 223327at2759; -.
DR   ChiTaRS; IGF1R; human.
DR   GenomeRNAi; 3480; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   Bgee; ENSG00000140443; Expressed in 233 organ(s), highest expression level in caput epididymis.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043560; F:insulin receptor substrate binding; IEA:InterPro.
DR   GO; GO:0005520; F:insulin-like growth factor binding; ISS:AgBase.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:InterPro.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd00064; FU; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 3.80.20.20; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000620; Insulin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00261; FU; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; SSF49265; 3.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000620-2,
KW   ECO:0000256|SAAS:SAAS00708816}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Kinase {ECO:0000256|SAAS:SAAS00582553};
KW   Membrane {ECO:0000256|SAAS:SAAS00602683, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000620-2,
KW   ECO:0000256|SAAS:SAAS00708816};
KW   Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW   Proteomics identification {ECO:0000213|EPD:C9J5X1,
KW   ECO:0000213|MaxQB:C9J5X1, ECO:0000213|PeptideAtlas:C9J5X1};
KW   Receptor {ECO:0000256|RuleBase:RU000312,
KW   ECO:0000256|SAAS:SAAS00600436};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Repeat {ECO:0000256|SAAS:SAAS00786331};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|SAAS:SAAS00582553};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00602683,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00602683,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|SAAS:SAAS00582553}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31   1366       Tyrosine-protein kinase receptor.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5017521292.
FT   TRANSMEM    932    957       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      491    609       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      610    708       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      735    828       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      834    927       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      998   1273       Protein kinase.
FT                                {ECO:0000259|PROSITE:PS50011}.
FT   NP_BIND    1079   1085       ATP. {ECO:0000256|PIRSR:PIRSR000620-2}.
FT   NP_BIND    1138   1139       ATP. {ECO:0000256|PIRSR:PIRSR000620-2}.
FT   COILED      704    724       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE   1134   1134       Proton acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000620-1}.
FT   BINDING    1008   1008       ATP. {ECO:0000256|PIRSR:PIRSR000620-2}.
FT   BINDING    1032   1032       ATP. {ECO:0000256|PIRSR:PIRSR000620-2}.
FT   BINDING    1152   1152       ATP. {ECO:0000256|PIRSR:PIRSR000620-2}.
SQ   SEQUENCE   1366 AA;  154791 MW;  EFC88F7D7718D938 CRC64;
     MKSGSGGGSP TSLWGLLFLS AALSLWPTSG EICGPGIDIR NDYQQLKRLE NCTVIEGYLH
     ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF PNLTVIRGWK LFYNYALVIF
     EMTNLKDIGL YNLRNITRGA IRIEKNADLC YLSTVDWSLI LDAVSNNYIV GNKPPKECGD
     LCPGTMEEKP MCEKTTINNE YNYRCWTTNR CQKMCPSTCG KRACTENNEC CHPECLGSCS
     APDNDTACVA CRHYYYAGVC VPACPPNTYR FEGWRCVDRD FCANILSAES SDSEGFVIHD
     GECMQECPSG FIRNGSQSMY CIPCEGPCPK VCEEEKKTKT IDSVTSAQML QGCTIFKGNL
     LINIRRGNNI ASELENFMGL IEVVTGYVKI RHSHALVSLS FLKNLRLILG EEQLEGNYSF
     YVLDNQNLQQ LWDWDHRNLT IKAGKMYFAF NPKLCVSEIY RMEEVTGTKG RQSKGDINTR
     NNGERASCES DVLHFTSTTT SKNRIIITWH RYRPPDYRDL ISFTVYYKEA PFKNVTEYDG
     QDACGSNSWN MVDVDLPPNK DVEPGILLHG LKPWTQYAVY VKAVTLTMVE NDHIRGAKSE
     ILYIRTNASV PSIPLDVLSA SNSSSQLIVK WNPPSLPNGN LSYYIVRWQR QPQDGYLYRH
     NYCSKDKIPI RKYADGTIDI EEVTENPKTE VCGGEKGPCC ACPKTEAEKQ AEKEEAEYRK
     VFENFLHNSI FVPRPERKRR DVMQVANTTM SSRSRNTTAA DTYNITDPEE LETEYPFFES
     RVDNKERTVI SNLRPFTLYR IDIHSCNHEA EKLGCSASNF VFARTMPAEG ADDIPGPVTW
     EPRPENSIFL KWPEPENPNG LILMYEIKYG SQVEDQRECV SRQEYRKYGG AKLNRLNPGN
     YTARIQATSL SGNGSWTDPV FFYVQAKRYE NFIHLIIALP VAVLLIVGGL VIMLYVFHRK
     RNNSRLGNGV LYASVNPEYF SAADVYVPDE WEVAREKITM SRELGQGSFG MVYEGVAKGV
     VKDEPETRVA IKTVNEAASM RERIEFLNEA SVMKEFNCHH VVRLLGVVSQ GQPTLVIMEL
     MTRGDLKSYL RSLRPEMENN PVLAPPSLSK MIQMAGEIAD GMAYLNANKF VHRDLAARNC
     MVAEDFTVKI GDFGMTRDIY ETDYYRKGGK GLLPVRWMSP ESLKDGVFTT YSDVWSFGVV
     LWEIATLAEQ PYQGLSNEQV LRFVMEGGLL DKPDNCPDML FELMRMCWQY NPKMRPSFLE
     IISSIKEEME PGFREVSFYY SEENKLPEPE ELDLEPENME SVPLDPSASS SSLPLPDRHS
     GHKAENGPGP GVLVLRASFD ERQPYAHMNG GRKNERALPL PQSSTC
//