ROR2_HUMAN
ID ROR2_HUMAN Reviewed; 943 AA.
AC Q01974; Q59GF5; Q5SPI5; Q9HAY7; Q9HB61;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Tyrosine-protein kinase transmembrane receptor ROR2;
DE EC=2.7.10.1 {ECO:0000269|PubMed:17717073};
DE AltName: Full=Neurotrophic tyrosine kinase, receptor-related 2;
DE Flags: Precursor;
GN Name=ROR2; Synonyms=NTRKR2;
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], AND VARIANT ALA-245.
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-943, AND VARIANTS ALA-245 AND
RP ILE-819.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-943, AND VARIANTS ALA-245 AND
RP ILE-819.
RX PubMed=10700182; DOI=10.1038/73495;
RA Oldridge M., Fortuna A.M., Maringa M., Propping P., Mansour S., Pollitt C.,
RA DeChiara T.M., Kimble R.B., Valenzuela D.M., Yancopoulos G.D.,
RA Wilkie A.O.M.;
RT "Dominant mutations in ROR2, encoding an orphan receptor tyrosine kinase,
RT cause brachydactyly type B.";
RL Nat. Genet. 24:275-278(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-574, AND VARIANT ALA-245.
RX PubMed=10986040; DOI=10.1086/303084;
RA Schwabe G.C., Tinschert S., Buschow C., Meinecke P., Wolff G.,
RA Gillessen-Kaesbach G., Oldridge M., Wilkie A.O.M., Koemec R., Mundlos S.;
RT "Distinct mutations in the receptor tyrosine kinase gene ROR2 cause
RT brachydactyly type B.";
RL Am. J. Hum. Genet. 67:822-831(2000).
RN [6]
RP PROTEIN SEQUENCE OF 465-474, SULFATION AT SER-469 AND SER-471, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14752058; DOI=10.1074/mcp.m300140-mcp200;
RA Medzihradszky K.F., Darula Z., Perlson E., Fainzilber M., Chalkley R.J.,
RA Ball H., Greenbaum D., Bogyo M., Tyson D.R., Bradshaw R.A.,
RA Burlingame A.L.;
RT "O-sulfonation of serine and threonine: mass spectrometric detection and
RT characterization of a new posttranslational modification in diverse
RT proteins throughout the eukaryotes.";
RL Mol. Cell. Proteomics 3:429-440(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH YWHAB, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17717073; DOI=10.1210/me.2007-0323;
RA Liu Y., Ross J.F., Bodine P.V.N., Billiard J.;
RT "Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta)
RT phosphorylation and promotes osteoblast differentiation and bone
RT formation.";
RL Mol. Endocrinol. 21:3050-3061(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP FUNCTION, LACK OF CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-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 [10]
RP VARIANTS RRS1 CYS-184; TRP-189; TRP-366 AND LYS-620.
RX PubMed=10932186; DOI=10.1038/78107;
RA Afzal A.R., Rajab A., Fenske C.D., Oldridge M., Elanko N.,
RA Ternes-Pereira E., Tueysuez B., Murday V.A., Patton M.A., Wilkie A.O.M.,
RA Jeffery S.;
RT "Recessive Robinow syndrome, allelic to dominant brachydactyly type B, is
RT caused by mutation of ROR2.";
RL Nat. Genet. 25:419-422(2000).
RN [11]
RP VARIANT RRS1 TYR-182.
RX PubMed=10932187; DOI=10.1038/78113;
RA van Bokhoven H., Celli J., Kayserili H., van Beusekom E., Balci S.,
RA Brussel W., Skovby F., Kerr B., Percin E.F., Akarsu N., Brunner H.G.;
RT "Mutation of the gene encoding the ROR2 tyrosine kinase causes autosomal
RT recessive Robinow syndrome.";
RL Nat. Genet. 25:423-426(2000).
RN [12]
RP ERRATUM OF PUBMED:10932187.
RX PubMed=11062486; DOI=10.1038/81722;
RA van Bokhoven H., Celli J., Kayserili H., van Beusekom E., Balci S.,
RA Brussel W., Skovby F., Kerr B., Percin E.F., Akarsu N., Brunner H.G.;
RL Nat. Genet. 26:383-383(2000).
RN [13]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-244; ALA-245; ASP-349; ALA-490;
RP GLN-530; MET-542; SER-548; LEU-557; ASN-644; ASN-672; ARG-695; CYS-738;
RP LEU-762; ILE-819 AND GLU-935.
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).
CC -!- FUNCTION: Tyrosine-protein kinase receptor which may be involved in the
CC early formation of the chondrocytes. It seems to be required for
CC cartilage and growth plate development (By similarity). Phosphorylates
CC YWHAB, leading to induction of osteogenesis and bone formation
CC (PubMed:17717073). In contrast, has also been shown to have very little
CC tyrosine kinase activity in vitro. May act as a receptor for wnt ligand
CC WNT5A which may result in the inhibition of WNT3A-mediated signaling
CC (PubMed:25029443). {ECO:0000250|UniProtKB:Q9Z138,
CC ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:25029443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:17717073};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17717073};
CC -!- SUBUNIT: Homodimer; promotes osteogenesis. Binds YWHAB
CC (PubMed:17717073). Interacts with WTIP (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z138, ECO:0000269|PubMed:17717073}.
CC -!- INTERACTION:
CC Q01974; Q9NP73-4: ALG13; NbExp=3; IntAct=EBI-6422642, EBI-10186621;
CC Q01974; Q03989: ARID5A; NbExp=3; IntAct=EBI-6422642, EBI-948603;
CC Q01974; O14503: BHLHE40; NbExp=3; IntAct=EBI-6422642, EBI-711810;
CC Q01974; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-6422642, EBI-12809220;
CC Q01974; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-6422642, EBI-11976299;
CC Q01974; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-6422642, EBI-946029;
CC Q01974; Q8N813: C3orf56; NbExp=3; IntAct=EBI-6422642, EBI-18115268;
CC Q01974; Q03060-25: CREM; NbExp=3; IntAct=EBI-6422642, EBI-12884642;
CC Q01974; O43186: CRX; NbExp=4; IntAct=EBI-6422642, EBI-748171;
CC Q01974; Q15038: DAZAP2; NbExp=8; IntAct=EBI-6422642, EBI-724310;
CC Q01974; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-6422642, EBI-12193763;
CC Q01974; P53539: FOSB; NbExp=3; IntAct=EBI-6422642, EBI-2806743;
CC Q01974; P08238: HSP90AB1; NbExp=2; IntAct=EBI-6422642, EBI-352572;
CC Q01974; Q2M1V0: ISX; NbExp=3; IntAct=EBI-6422642, EBI-6426064;
CC Q01974; A4D0Q3: KIAA1218; NbExp=3; IntAct=EBI-6422642, EBI-14308786;
CC Q01974; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-6422642, EBI-10241353;
CC Q01974; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-6422642, EBI-11962084;
CC Q01974; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-6422642, EBI-18394498;
CC Q01974; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-6422642, EBI-10258746;
CC Q01974; P35548: MSX2; NbExp=3; IntAct=EBI-6422642, EBI-6447480;
CC Q01974; P78337: PITX1; NbExp=3; IntAct=EBI-6422642, EBI-748265;
CC Q01974; O15496: PLA2G10; NbExp=3; IntAct=EBI-6422642, EBI-726466;
CC Q01974; Q16633: POU2AF1; NbExp=3; IntAct=EBI-6422642, EBI-943588;
CC Q01974; O43741: PRKAB2; NbExp=3; IntAct=EBI-6422642, EBI-1053424;
CC Q01974; P86480: PRR20D; NbExp=3; IntAct=EBI-6422642, EBI-12754095;
CC Q01974; O95416: SOX14; NbExp=5; IntAct=EBI-6422642, EBI-9087806;
CC Q01974; Q6ZVD7: STOX1; NbExp=3; IntAct=EBI-6422642, EBI-3923644;
CC Q01974; O43711: TLX3; NbExp=3; IntAct=EBI-6422642, EBI-3939165;
CC Q01974; O95231: VENTX; NbExp=3; IntAct=EBI-6422642, EBI-10191303;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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: Brachydactyly B1 (BDB1) [MIM:113000]: A form of brachydactyly.
CC Brachydactyly defines a group of inherited malformations characterized
CC by shortening of the digits due to abnormal development of the
CC phalanges and/or the metacarpals. In brachydactyly type B1 the middle
CC phalanges are short but in addition the terminal phalanges are
CC rudimentary or absent. Both fingers and toes are affected. The thumbs
CC and big toes are usually deformed. Symphalangism is also a feature.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Robinow syndrome, autosomal recessive 1 (RRS1) [MIM:268310]: A
CC recessive form of Robinow syndrome, a disease characterized by short-
CC limb dwarfism, costovertebral segmentation defects and abnormalities of
CC the head, face and external genitalia. The clinical signs are generally
CC far more severe in recessive cases, particularly skeletal
CC abnormalities. All patients with the recessive form suffer from
CC vertebral segmentation abnormalities, resulting in scoliosis and chest
CC deformities. Rib fusions are considered to be characteristic of the
CC autosomal recessive form. Patients can also present brachydactyly, with
CC extensive aplasia/hypoplasia of the phalanges and
CC metacarpals/metatarsals, and brachy-syn-polydactyly of the hands and
CC oligodactyly of the feet. {ECO:0000269|PubMed:10932186,
CC ECO:0000269|PubMed:10932187}. Note=The disease is caused by variants
CC 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 catalytic activity of the kinase domain is controversial.
CC {ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:25029443}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92391.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ROR2ID43476ch9q22.html";
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DR EMBL; M97639; AAA60276.1; -; mRNA.
DR EMBL; AL391219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB209154; BAD92391.1; ALT_INIT; mRNA.
DR EMBL; AH009681; AAG01184.2; -; Genomic_DNA.
DR EMBL; AH010002; AAG33132.1; -; Genomic_DNA.
DR CCDS; CCDS6691.1; -.
DR PIR; B45082; B45082.
DR RefSeq; NP_001305133.1; NM_001318204.1.
DR RefSeq; NP_004551.2; NM_004560.3.
DR PDB; 3ZZW; X-ray; 2.90 A; A/B=464-751.
DR PDB; 4GT4; X-ray; 2.41 A; A/B=452-753.
DR PDB; 6OSH; X-ray; 1.12 A; K=314-394.
DR PDB; 6OSN; X-ray; 1.08 A; A=314-394.
DR PDB; 6OSV; X-ray; 1.34 A; K=314-394.
DR PDBsum; 3ZZW; -.
DR PDBsum; 4GT4; -.
DR PDBsum; 6OSH; -.
DR PDBsum; 6OSN; -.
DR PDBsum; 6OSV; -.
DR AlphaFoldDB; Q01974; -.
DR SMR; Q01974; -.
DR BioGRID; 110974; 232.
DR IntAct; Q01974; 63.
DR MINT; Q01974; -.
DR STRING; 9606.ENSP00000364860; -.
DR ChEMBL; CHEMBL2375201; -.
DR GlyGen; Q01974; 5 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q01974; -.
DR PhosphoSitePlus; Q01974; -.
DR BioMuta; ROR2; -.
DR DMDM; 90110767; -.
DR CPTAC; CPTAC-2781; -.
DR EPD; Q01974; -.
DR jPOST; Q01974; -.
DR MassIVE; Q01974; -.
DR MaxQB; Q01974; -.
DR PaxDb; Q01974; -.
DR PeptideAtlas; Q01974; -.
DR PRIDE; Q01974; -.
DR ProteomicsDB; 58028; -.
DR ABCD; Q01974; 6 sequenced antibodies.
DR Antibodypedia; 13579; 691 antibodies from 39 providers.
DR DNASU; 4920; -.
DR Ensembl; ENST00000375708.4; ENSP00000364860.3; ENSG00000169071.15.
DR GeneID; 4920; -.
DR KEGG; hsa:4920; -.
DR MANE-Select; ENST00000375708.4; ENSP00000364860.3; NM_004560.4; NP_004551.2.
DR UCSC; uc004arj.3; human.
DR CTD; 4920; -.
DR DisGeNET; 4920; -.
DR GeneCards; ROR2; -.
DR GeneReviews; ROR2; -.
DR HGNC; HGNC:10257; ROR2.
DR HPA; ENSG00000169071; Low tissue specificity.
DR MalaCards; ROR2; -.
DR MIM; 113000; phenotype.
DR MIM; 268310; phenotype.
DR MIM; 602337; gene.
DR neXtProt; NX_Q01974; -.
DR OpenTargets; ENSG00000169071; -.
DR Orphanet; 1507; Autosomal recessive Robinow syndrome.
DR Orphanet; 572385; Brachydactyly type B1.
DR PharmGKB; PA34629; -.
DR VEuPathDB; HostDB:ENSG00000169071; -.
DR eggNOG; KOG1026; Eukaryota.
DR GeneTree; ENSGT00940000153947; -.
DR HOGENOM; CLU_000288_30_4_1; -.
DR InParanoid; Q01974; -.
DR OMA; YYKMVHR; -.
DR OrthoDB; 471114at2759; -.
DR PhylomeDB; Q01974; -.
DR TreeFam; TF106465; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; Q01974; -.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR SignaLink; Q01974; -.
DR SIGNOR; Q01974; -.
DR BioGRID-ORCS; 4920; 9 hits in 1111 CRISPR screens.
DR ChiTaRS; ROR2; human.
DR GeneWiki; ROR2; -.
DR GenomeRNAi; 4920; -.
DR Pharos; Q01974; Tbio.
DR PRO; PR:Q01974; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q01974; protein.
DR Bgee; ENSG00000169071; Expressed in muscle layer of sigmoid colon and 123 other tissues.
DR ExpressionAtlas; Q01974; baseline and differential.
DR Genevisible; Q01974; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:WormBase.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:1905517; P:macrophage migration; IEA:Ensembl.
DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IEA:Ensembl.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; IEA:Ensembl.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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 IDEAL; IID00560; -.
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; ATP-binding; Cell membrane; Developmental protein;
KW Direct protein sequencing; Disease variant; Disulfide bond; Dwarfism;
KW Glycoprotein; Immunoglobulin domain; Kinase; Kringle; Magnesium; Membrane;
KW Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Sulfation; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Wnt signaling pathway.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..943
FT /note="Tyrosine-protein kinase transmembrane receptor ROR2"
FT /id="PRO_0000024460"
FT TOPO_DOM 34..403
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..943
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..145
FT /note="Ig-like C2-type"
FT DOMAIN 169..303
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 316..394
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 757..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..923
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 615
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 479..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 469
FT /note="Sulfoserine; partial"
FT /evidence="ECO:0000269|PubMed:14752058"
FT MOD_RES 471
FT /note="Sulfoserine; partial"
FT /evidence="ECO:0000269|PubMed:14752058"
FT MOD_RES 646
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 785
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z138"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..135
FT /evidence="ECO:0000250"
FT DISULFID 174..239
FT /evidence="ECO:0000250"
FT DISULFID 182..232
FT /evidence="ECO:0000250"
FT DISULFID 223..264
FT /evidence="ECO:0000250"
FT DISULFID 252..300
FT /evidence="ECO:0000250"
FT DISULFID 256..286
FT /evidence="ECO:0000250"
FT DISULFID 316..394
FT /evidence="ECO:0000250"
FT DISULFID 337..377
FT /evidence="ECO:0000250"
FT DISULFID 365..389
FT /evidence="ECO:0000250"
FT VARIANT 182
FT /note="C -> Y (in RRS1)"
FT /evidence="ECO:0000269|PubMed:10932187"
FT /id="VAR_010911"
FT VARIANT 184
FT /note="R -> C (in RRS1; dbSNP:rs121909084)"
FT /evidence="ECO:0000269|PubMed:10932186"
FT /id="VAR_010768"
FT VARIANT 189
FT /note="R -> W (in RRS1; dbSNP:rs199975149)"
FT /evidence="ECO:0000269|PubMed:10932186"
FT /id="VAR_010769"
FT VARIANT 244
FT /note="R -> Q (in dbSNP:rs55737262)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041787"
FT VARIANT 245
FT /note="T -> A (in dbSNP:rs10820900)"
FT /evidence="ECO:0000269|PubMed:10700182,
FT ECO:0000269|PubMed:10986040, ECO:0000269|PubMed:1334494,
FT ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_010912"
FT VARIANT 349
FT /note="H -> D (in dbSNP:rs55983376)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041788"
FT VARIANT 366
FT /note="R -> W (in RRS1)"
FT /evidence="ECO:0000269|PubMed:10932186"
FT /id="VAR_010770"
FT VARIANT 490
FT /note="G -> A (in dbSNP:rs56197744)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041789"
FT VARIANT 530
FT /note="R -> Q (in dbSNP:rs35852786)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041790"
FT VARIANT 542
FT /note="V -> M (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs140213020)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041791"
FT VARIANT 548
FT /note="P -> S (in dbSNP:rs35764413)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041792"
FT VARIANT 557
FT /note="S -> L (in dbSNP:rs56099091)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041793"
FT VARIANT 620
FT /note="N -> K (in RRS1)"
FT /evidence="ECO:0000269|PubMed:10932186"
FT /id="VAR_010771"
FT VARIANT 644
FT /note="D -> N (in dbSNP:rs55798732)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041794"
FT VARIANT 672
FT /note="D -> N (in dbSNP:rs55651110)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041795"
FT VARIANT 695
FT /note="G -> R (in dbSNP:rs34431454)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041796"
FT VARIANT 738
FT /note="R -> C (in dbSNP:rs56231927)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041797"
FT VARIANT 762
FT /note="S -> L (in dbSNP:rs34491822)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041798"
FT VARIANT 819
FT /note="V -> I (in dbSNP:rs10761129)"
FT /evidence="ECO:0000269|PubMed:10700182,
FT ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_010913"
FT VARIANT 935
FT /note="D -> E (in dbSNP:rs41277835)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041799"
FT MUTAGEN 482
FT /note="D->G: Slight increase in kinase activity."
FT /evidence="ECO:0000269|PubMed:25029443"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6OSN"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:6OSN"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6OSN"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6OSN"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:6OSN"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:6OSN"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:4GT4"
FT STRAND 473..481
FT /evidence="ECO:0007829|PDB:4GT4"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:4GT4"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 518..530
FT /evidence="ECO:0007829|PDB:4GT4"
FT STRAND 539..543
FT /evidence="ECO:0007829|PDB:4GT4"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:4GT4"
FT STRAND 550..554
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 561..566
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 589..608
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:4GT4"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:4GT4"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 639..644
FT /evidence="ECO:0007829|PDB:4GT4"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 661..666
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 671..686
FT /evidence="ECO:0007829|PDB:4GT4"
FT TURN 687..689
FT /evidence="ECO:0007829|PDB:4GT4"
FT TURN 692..695
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 698..706
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 719..728
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 733..735
FT /evidence="ECO:0007829|PDB:4GT4"
FT HELIX 739..747
FT /evidence="ECO:0007829|PDB:4GT4"
SQ SEQUENCE 943 AA; 104757 MW; F926FB681A8312FE CRC64;
MARGSALPRR PLLCIPAVWA AAALLLSVSR TSGEVEVLDP NDPLGPLDGQ DGPIPTLKGY
FLNFLEPVNN ITIVQGQTAI LHCKVAGNPP PNVRWLKNDA PVVQEPRRII IRKTEYGSRL
RIQDLDTTDT GYYQCVATNG MKTITATGVL FVRLGPTHSP NHNFQDDYHE DGFCQPYRGI
ACARFIGNRT IYVDSLQMQG EIENRITAAF TMIGTSTHLS DQCSQFAIPS FCHFVFPLCD
ARSRTPKPRE LCRDECEVLE SDLCRQEYTI ARSNPLILMR LQLPKCEALP MPESPDAANC
MRIGIPAERL GRYHQCYNGS GMDYRGTAST TKSGHQCQPW ALQHPHSHHL SSTDFPELGG
GHAYCRNPGG QMEGPWCFTQ NKNVRMELCD VPSCSPRDSS KMGILYILVP SIAIPLVIAC
LFFLVCMCRN KQKASASTPQ RRQLMASPSQ DMEMPLINQH KQAKLKEISL SAVRFMEELG
EDRFGKVYKG HLFGPAPGEQ TQAVAIKTLK DKAEGPLREE FRHEAMLRAR LQHPNVVCLL
GVVTKDQPLS MIFSYCSHGD LHEFLVMRSP HSDVGSTDDD RTVKSALEPP DFVHLVAQIA
AGMEYLSSHH VVHKDLATRN VLVYDKLNVK ISDLGLFREV YAADYYKLLG NSLLPIRWMA
PEAIMYGKFS IDSDIWSYGV VLWEVFSYGL QPYCGYSNQD VVEMIRNRQV LPCPDDCPAW
VYALMIECWN EFPSRRPRFK DIHSRLRAWG NLSNYNSSAQ TSGASNTTQT SSLSTSPVSN
VSNARYVGPK QKAPPFPQPQ FIPMKGQIRP MVPPPQLYVP VNGYQPVPAY GAYLPNFYPV
QIPMQMAPQQ VPPQMVPKPS SHHSGSGSTS TGYVTTAPSN TSMADRAALL SEGADDTQNA
PEDGAQSTVQ EAEEEEEGSV PETELLGDCD TLQVDEAQVQ LEA
