ROR1_HUMAN
ID ROR1_HUMAN Reviewed; 937 AA.
AC Q01973; Q5VVX6; Q66K77; Q92776;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Inactive tyrosine-protein kinase transmembrane receptor ROR1 {ECO:0000305};
DE AltName: Full=Neurotrophic tyrosine kinase, receptor-related 1;
DE Flags: Precursor;
GN Name=ROR1; Synonyms=NTRKR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT MET-518.
RX PubMed=1334494; DOI=10.1016/s0021-9258(18)35733-8;
RA Masiakowski P., Carroll R.D.;
RT "A novel family of cell surface receptors with tyrosine kinase-like
RT domain.";
RL J. Biol. Chem. 267:26181-26190(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=8875995;
RA Reddy U.R., Phatak S., Pleasure D.;
RT "Human neural tissues express a truncated Ror1 receptor tyrosine kinase,
RT lacking both extracellular and transmembrane domains.";
RL Oncogene 13:1555-1559(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP LACK OF CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-482.
RX PubMed=25029443; DOI=10.1371/journal.pone.0102695;
RA Bainbridge T.W., DeAlmeida V.I., Izrael-Tomasevic A., Chalouni C., Pan B.,
RA Goldsmith J., Schoen A.P., Quinones G.A., Kelly R., Lill J.R., Sandoval W.,
RA Costa M., Polakis P., Arnott D., Rubinfeld B., Ernst J.A.;
RT "Evolutionary divergence in the catalytic activity of the CAM-1, ROR1 and
RT ROR2 kinase domains.";
RL PLoS ONE 9:E102695-E102695(2014).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-562.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-144; LEU-150; VAL-301; MET-518;
RP ILE-567; ARG-624; CYS-646 AND ASN-776.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [9]
RP INVOLVEMENT IN DFNB108, VARIANT DFNB108 THR-736, CHARACTERIZATION OF
RP VARIANT DFNB108 THR-736, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27162350; DOI=10.1073/pnas.1522512113;
RA Diaz-Horta O., Abad C., Sennaroglu L., Foster J. II, DeSmidt A.,
RA Bademci G., Tokgoz-Yilmaz S., Duman D., Cengiz F.B., Grati M., Fitoz S.,
RA Liu X.Z., Farooq A., Imtiaz F., Currall B.B., Morton C.C., Nishita M.,
RA Minami Y., Lu Z., Walz K., Tekin M.;
RT "ROR1 is essential for proper innervation of auditory hair cells and
RT hearing in humans and mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:5993-5998(2016).
CC -!- FUNCTION: Has very low kinase activity in vitro and is unlikely to
CC function as a tyrosine kinase in vivo (PubMed:25029443). Receptor for
CC ligand WNT5A which activate downstream NFkB signaling pathway and may
CC result in the inhibition of WNT3A-mediated signaling (PubMed:25029443,
CC PubMed:27162350). In inner ear, crucial for spiral ganglion neurons to
CC innervate auditory hair cells (PubMed:27162350).
CC {ECO:0000269|PubMed:25029443, ECO:0000269|PubMed:27162350}.
CC -!- INTERACTION:
CC Q01973; P00533: EGFR; NbExp=8; IntAct=EBI-6082337, EBI-297353;
CC Q01973; P12931: SRC; NbExp=9; IntAct=EBI-6082337, EBI-621482;
CC Q01973; P05480: Src; Xeno; NbExp=2; IntAct=EBI-6082337, EBI-298680;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27162350}; Single-
CC pass type I membrane protein. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9Z139}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Long;
CC IsoId=Q01973-1; Sequence=Displayed;
CC Name=Short; Synonyms=T-ROR1;
CC IsoId=Q01973-2; Sequence=VSP_005008;
CC Name=3;
CC IsoId=Q01973-3; Sequence=VSP_043663, VSP_043664;
CC -!- TISSUE SPECIFICITY: Expressed strongly in human heart, lung and kidney,
CC but weakly in the CNS. Isoform Short is strongly expressed in fetal and
CC adult CNS and in a variety of human cancers, including those
CC originating from CNS or PNS neuroectoderm.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels during early embryonic
CC development. The expression levels drop strongly around day 16 and
CC there are only very low levels in adult tissues.
CC -!- DISEASE: Deafness, autosomal recessive, 108 (DFNB108) [MIM:617654]: A
CC form of non-syndromic sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner ear,
CC the nerve pathways to the brain, or the area of the brain that receives
CC sound information. {ECO:0000269|PubMed:27162350}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ROR subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: The kinase domain has very low catalytic activity in vitro.
CC {ECO:0000269|PubMed:25029443}.
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DR EMBL; M97675; AAA60275.1; -; mRNA.
DR EMBL; U38894; AAC50714.1; -; mRNA.
DR EMBL; AL137859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL808029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL808030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06556.1; -; Genomic_DNA.
DR EMBL; BC080541; AAH80541.1; -; mRNA.
DR CCDS; CCDS41344.1; -. [Q01973-3]
DR CCDS; CCDS626.1; -. [Q01973-1]
DR PIR; A45082; A45082.
DR RefSeq; NP_001077061.1; NM_001083592.1. [Q01973-3]
DR RefSeq; NP_005003.2; NM_005012.3. [Q01973-1]
DR PDB; 5Z55; NMR; -; A=312-394.
DR PDB; 6BA5; X-ray; 1.62 A; M/N/O/P=311-391.
DR PDB; 6BAN; X-ray; 1.95 A; M/N/O/P=311-391.
DR PDB; 6TU9; X-ray; 1.94 A; A/B=453-752.
DR PDBsum; 5Z55; -.
DR PDBsum; 6BA5; -.
DR PDBsum; 6BAN; -.
DR PDBsum; 6TU9; -.
DR AlphaFoldDB; Q01973; -.
DR SMR; Q01973; -.
DR BioGRID; 110973; 43.
DR DIP; DIP-29734N; -.
DR IntAct; Q01973; 29.
DR MINT; Q01973; -.
DR STRING; 9606.ENSP00000360120; -.
DR ChEMBL; CHEMBL4665585; -.
DR GlyGen; Q01973; 4 sites.
DR iPTMnet; Q01973; -.
DR PhosphoSitePlus; Q01973; -.
DR SwissPalm; Q01973; -.
DR BioMuta; ROR1; -.
DR DMDM; 118572711; -.
DR EPD; Q01973; -.
DR jPOST; Q01973; -.
DR MassIVE; Q01973; -.
DR MaxQB; Q01973; -.
DR PaxDb; Q01973; -.
DR PeptideAtlas; Q01973; -.
DR PRIDE; Q01973; -.
DR ProteomicsDB; 58025; -. [Q01973-1]
DR ProteomicsDB; 58026; -. [Q01973-2]
DR ProteomicsDB; 58027; -. [Q01973-3]
DR ABCD; Q01973; 29 sequenced antibodies.
DR Antibodypedia; 33360; 621 antibodies from 40 providers.
DR DNASU; 4919; -.
DR Ensembl; ENST00000371079.6; ENSP00000360120.1; ENSG00000185483.13. [Q01973-1]
DR Ensembl; ENST00000371080.5; ENSP00000360121.1; ENSG00000185483.13. [Q01973-3]
DR GeneID; 4919; -.
DR KEGG; hsa:4919; -.
DR MANE-Select; ENST00000371079.6; ENSP00000360120.1; NM_005012.4; NP_005003.2.
DR UCSC; uc001dbi.5; human. [Q01973-1]
DR CTD; 4919; -.
DR DisGeNET; 4919; -.
DR GeneCards; ROR1; -.
DR HGNC; HGNC:10256; ROR1.
DR HPA; ENSG00000185483; Tissue enhanced (parathyroid).
DR MalaCards; ROR1; -.
DR MIM; 602336; gene.
DR MIM; 617654; phenotype.
DR neXtProt; NX_Q01973; -.
DR OpenTargets; ENSG00000185483; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA34628; -.
DR VEuPathDB; HostDB:ENSG00000185483; -.
DR eggNOG; KOG1026; Eukaryota.
DR GeneTree; ENSGT00940000153947; -.
DR HOGENOM; CLU_701993_0_0_1; -.
DR InParanoid; Q01973; -.
DR OMA; HGHSESM; -.
DR OrthoDB; 471114at2759; -.
DR PhylomeDB; Q01973; -.
DR TreeFam; TF106465; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; Q01973; -.
DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR SignaLink; Q01973; -.
DR SIGNOR; Q01973; -.
DR BioGRID-ORCS; 4919; 16 hits in 1103 CRISPR screens.
DR ChiTaRS; ROR1; human.
DR GeneWiki; ROR1; -.
DR GenomeRNAi; 4919; -.
DR Pharos; Q01973; Tbio.
DR PRO; PR:Q01973; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q01973; protein.
DR Bgee; ENSG00000185483; Expressed in germinal epithelium of ovary and 152 other tissues.
DR ExpressionAtlas; Q01973; baseline and differential.
DR Genevisible; Q01973; HS.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1904929; F:coreceptor activity involved in Wnt signaling pathway, planar cell polarity pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc.
DR GO; GO:0042813; F:Wnt receptor activity; IMP:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR CDD; cd00108; KR; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR016247; Tyr_kinase_rcpt_ROR.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000624; TyrPK_TMrec_ROR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00130; KR; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell projection; Deafness;
KW Disease variant; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Kinase; Kringle; Membrane; Non-syndromic deafness; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..937
FT /note="Inactive tyrosine-protein kinase transmembrane
FT receptor ROR1"
FT /id="PRO_0000024458"
FT TOPO_DOM 30..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..937
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..147
FT /note="Ig-like C2-type"
FT DOMAIN 165..299
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 312..391
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 473..746
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 753..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 645
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 79..131
FT /evidence="ECO:0000250"
FT DISULFID 170..235
FT /evidence="ECO:0000250"
FT DISULFID 178..228
FT /evidence="ECO:0000250"
FT DISULFID 219..260
FT /evidence="ECO:0000250"
FT DISULFID 248..296
FT /evidence="ECO:0000250"
FT DISULFID 252..282
FT /evidence="ECO:0000250"
FT DISULFID 313..391
FT /evidence="ECO:0000250"
FT DISULFID 334..374
FT /evidence="ECO:0000250"
FT DISULFID 362..386
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..549
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8875995"
FT /id="VSP_005008"
FT VAR_SEQ 392..393
FT /note="DS -> GK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043663"
FT VAR_SEQ 394..937
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043664"
FT VARIANT 144
FT /note="G -> E (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041779"
FT VARIANT 150
FT /note="F -> L (in an ovarian mucinous carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041780"
FT VARIANT 301
FT /note="I -> V (in a renal clear cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041781"
FT VARIANT 518
FT /note="T -> M (in dbSNP:rs7527017)"
FT /evidence="ECO:0000269|PubMed:1334494,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_041782"
FT VARIANT 562
FT /note="E -> D (in a breast cancer sample; somatic mutation;
FT dbSNP:rs760789417)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035713"
FT VARIANT 567
FT /note="R -> I (in a colorectal adenocarcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041783"
FT VARIANT 624
FT /note="G -> R (in dbSNP:rs55832740)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041784"
FT VARIANT 646
FT /note="Y -> C (in dbSNP:rs34109134)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041785"
FT VARIANT 736
FT /note="R -> T (in DFNB108; impairs plasma membrane
FT location; abolishes downstream NFkB activation;
FT dbSNP:rs1553163562)"
FT /evidence="ECO:0000269|PubMed:27162350"
FT /id="VAR_079530"
FT VARIANT 776
FT /note="S -> N (in a colorectal adenocarcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041786"
FT MUTAGEN 482
FT /note="C->G: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:25029443"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6BA5"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:6BA5"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6BA5"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:6BA5"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6BA5"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:6BA5"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6BA5"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:6TU9"
FT STRAND 473..481
FT /evidence="ECO:0007829|PDB:6TU9"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:6TU9"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 514..527
FT /evidence="ECO:0007829|PDB:6TU9"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:6TU9"
FT STRAND 544..547
FT /evidence="ECO:0007829|PDB:6TU9"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 560..566
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 589..608
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:6TU9"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:6TU9"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 636..640
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 661..666
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 671..686
FT /evidence="ECO:0007829|PDB:6TU9"
FT TURN 692..695
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 698..706
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 719..728
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 733..735
FT /evidence="ECO:0007829|PDB:6TU9"
FT HELIX 739..748
FT /evidence="ECO:0007829|PDB:6TU9"
SQ SEQUENCE 937 AA; 104283 MW; 0EC0E4762A90C6C7 CRC64;
MHRPRRRGTR PPLLALLAAL LLAARGAAAQ ETELSVSAEL VPTSSWNISS ELNKDSYLTL
DEPMNNITTS LGQTAELHCK VSGNPPPTIR WFKNDAPVVQ EPRRLSFRST IYGSRLRIRN
LDTTDTGYFQ CVATNGKEVV SSTGVLFVKF GPPPTASPGY SDEYEEDGFC QPYRGIACAR
FIGNRTVYME SLHMQGEIEN QITAAFTMIG TSSHLSDKCS QFAIPSLCHY AFPYCDETSS
VPKPRDLCRD ECEILENVLC QTEYIFARSN PMILMRLKLP NCEDLPQPES PEAANCIRIG
IPMADPINKN HKCYNSTGVD YRGTVSVTKS GRQCQPWNSQ YPHTHTFTAL RFPELNGGHS
YCRNPGNQKE APWCFTLDEN FKSDLCDIPA CDSKDSKEKN KMEILYILVP SVAIPLAIAL
LFFFICVCRN NQKSSSAPVQ RQPKHVRGQN VEMSMLNAYK PKSKAKELPL SAVRFMEELG
ECAFGKIYKG HLYLPGMDHA QLVAIKTLKD YNNPQQWTEF QQEASLMAEL HHPNIVCLLG
AVTQEQPVCM LFEYINQGDL HEFLIMRSPH SDVGCSSDED GTVKSSLDHG DFLHIAIQIA
AGMEYLSSHF FVHKDLAARN ILIGEQLHVK ISDLGLSREI YSADYYRVQS KSLLPIRWMP
PEAIMYGKFS SDSDIWSFGV VLWEIFSFGL QPYYGFSNQE VIEMVRKRQL LPCSEDCPPR
MYSLMTECWN EIPSRRPRFK DIHVRLRSWE GLSSHTSSTT PSGGNATTQT TSLSASPVSN
LSNPRYPNYM FPSQGITPQG QIAGFIGPPI PQNQRFIPIN GYPIPPGYAA FPAAHYQPTG
PPRVIQHCPP PKSRSPSSAS GSTSTGHVTS LPSSGSNQEA NIPLLPHMSI PNHPGGMGIT
VFGNKSQKPY KIDSKQASLL GDANIHGHTE SMISAEL
