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Showing Protein Tyrosine-protein kinase transmembrane receptor ROR2 (HMDBP01178)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP01178
Secondary Accession Numbers
  • 6474
Name Tyrosine-protein kinase transmembrane receptor ROR2
Synonyms
  1. Neurotrophic tyrosine kinase, receptor-related 2
Gene Name ROR2
Protein Type Enzyme
Biological Properties
General Function Involved in protein kinase activity
Specific Function Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. It seems to be required for cartilage and growth plate development. Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation
Pathways Not Available
Reactions Not Available
GO Classification
Component
integral to plasma membrane
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
protein tyrosine kinase activity
transmembrane receptor protein tyrosine kinase activity
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
protein binding
protein kinase activity
Process
phosphorus metabolic process
phosphate metabolic process
enzyme linked receptor protein signaling pathway
transmembrane receptor protein tyrosine kinase signaling pathway
metabolic process
cellular metabolic process
protein amino acid phosphorylation
signaling
signaling pathway
cell surface receptor linked signaling pathway
phosphorylation
Cellular Location
  1. Membrane
  2. Single-pass type I membrane protein
Gene Properties
Chromosome Location Chromosome:9
Locus 9q22
SNPs ROR2
Gene Sequence 
>2832 bp
ATGGCCCGGGGCTCGGCGCTCCCGCGGCGGCCGCTGCTGTGCATCCCGGCCGTCTGGGCG
GCCGCCGCGCTTCTGCTCTCAGTGTCCCGGACTTCAGGTGAAGTGGAGGTTCTGGATCCG
AACGACCCTTTAGGACCCCTTGATGGGCAGGACGGCCCGATTCCAACTCTGAAAGGTTAC
TTTCTGAATTTTCTGGAGCCAGTAAACAATATCACCATTGTCCAAGGCCAGACGGCAATT
CTGCACTGCAAGGTGGCAGGAAACCCACCCCCTAACGTGCGGTGGCTAAAGAATGATGCC
CCGGTGGTGCAGGAGCCGCGGCGGATCATCATCCGGAAGACAGAATATGGTTCACGACTG
CGAATCCAGGACCTGGACACGACAGACACTGGCTACTACCAGTGCGTGGCCACCAACGGG
ATGAAGACCATTACCGCCACTGGCGTCCTGTTTGTGCGGCTGGGTCCAACGCACAGCCCA
AATCATAACTTTCAGGATGATTACCACGAGGATGGGTTCTGCCAGCCTTACCGGGGAATT
GCCTGTGCACGCTTCATTGGCAACCGGACCATTTATGTGGACTCGCTTCAGATGCAGGGG
GAGATTGAAAACCGAATCACAGCGGCCTTCACCATGATCGGCACGTCTACGCACCTGTCG
GACCAGTGCTCACAGTTCGCCATCCCATCCTTCTGCCACTTCGTGTTTCCTCTGTGCGAC
GCGCGCTCCCGGACACCCAAGCCGCGTGAGCTGTGCCGCGACGAGTGCGAGGTGCTGGAG
AGCGACCTGTGCCGCCAGGAGTACACCATCGCCCGCTCCAACCCGCTCATCCTCATGCGG
CTTCAGCTGCCCAAGTGTGAGGCGCTGCCCATGCCTGAGAGCCCCGACGCTGCCAACTGC
ATGCGCATTGGCATCCCAGCCGAGAGGCTGGGCCGCTACCATCAGTGCTATAACGGCTCA
GGCATGGATTACAGAGGAACGGCAAGCACCACCAAGTCAGGCCACCAGTGCCAGCCGTGG
GCCCTGCAGCACCCCCACAGCCACCACCTGTCCAGCACAGACTTCCCTGAGCTTGGAGGG
GGGCACGCCTACTGCCGGAACCCCGGAGGCCAGATGGAGGGCCCCTGGTGCTTTACGCAG
AATAAAAACGTACGCATGGAACTGTGTGACGTACCCTCGTGTAGTCCCCGAGACAGCAGC
AAGATGGGGATTCTGTACATCTTGGTCCCCAGCATCGCAATTCCACTGGTCATCGCTTGC
CTTTTCTTCTTGGTTTGCATGTGCCGGAATAAGCAGAAGGCATCTGCGTCCACACCGCAG
CGGCGACAGCTGATGGCCTCGCCCAGCCAAGACATGGAAATGCCCCTCATTAACCAGCAC
AAACAGGCCAAACTCAAAGAGATCAGCCTGTCTGCGGTGAGGTTCATGGAGGAGCTGGGA
GAGGACCGGTTTGGGAAAGTCTACAAAGGTCACCTGTTCGGCCCTGCCCCGGGGGAGCAG
ACCCAGGCTGTGGCCATCAAAACGCTGAAGGACAAAGCGGAGGGGCCCCTGCGGGAGGAG
TTCCGGCATGAGGCTATGCTGCGAGCACGGCTGCAACACCCCAACGTCGTCTGCCTGCTG
GGCGTGGTGACCAAGGACCAGCCCCTGAGCATGATCTTCAGCTACTGTTCGCACGGCGAC
CTCCACGAATTCCTGGTCATGCGCTCGCCGCACTCGGACGTGGGCAGCACCGATGATGAC
CGCACGGTGAAGTCCGCCCTGGAGCCCCCCGACTTCGTGCACCTTGTGGCACAGATCGCG
GCGGGGATGGAGTACCTATCCAGCCACCACGTGGTTCACAAGGACCTGGCCACCCGCAAT
GTGCTAGTGTACGACAAGCTGAACGTGAAGATCTCAGACTTGGGCCTCTTCCGAGAGGTG
TATGCCGCCGATTACTACAAGCTGCTGGGGAACTCGCTGCTGCCTATCCGCTGGATGGCC
CCAGAGGCCATCATGTACGGCAAGTTCTCCATCGACTCAGACATCTGGTCCTACGGTGTG
GTCCTGTGGGAGGTCTTCAGCTACGGCCTGCAGCCCTACTGCGGGTACTCCAACCAGGAT
GTGGTGGAGATGATCCGGAACCGGCAGGTGCTGCCTTGCCCCGATGACTGTCCCGCCTGG
GTGTATGCCCTCATGATCGAGTGCTGGAACGAGTTCCCCAGCCGGCGGCCCCGCTTCAAG
GACATCCACAGCCGGCTCCGAGCCTGGGGCAACCTTTCCAACTACAACAGCTCGGCGCAG
ACCTCGGGGGCCAGCAACACCACGCAGACCAGCTCCCTGAGCACCAGCCCAGTGAGCAAT
GTGAGCAACGCCCGCTACGTGGGGCCCAAGCAGAAGGCCCCGCCCTTCCCACAGCCCCAG
TTCATCCCCATGAAGGGCCAGATCAGACCCATGGTGCCCCCGCCGCAGCTCTACGTCCCC
GTCAACGGCTACCAGCCGGTGCCGGCCTATGGGGCCTACCTGCCCAACTTCTACCCGGTG
CAGATCCCAATGCAGATGGCCCCGCAGCAGGTGCCTCCTCAGATGGTCCCCAAGCCCAGC
TCACACCACAGTGGCAGTGGCTCCACCAGCACAGGCTACGTCACCACGGCCCCCTCCAAC
ACATCCATGGCAGACAGGGCAGCCCTGCTCTCAGAGGGCGCTGATGACACACAGAACGCC
CCAGAAGATGGGGCCCAGAGCACCGTGCAGGAAGCAGAGGAGGAGGAGGAAGGCTCTGTC
CCAGAGACTGAGCTGCTGGGGGACTGTGACACTCTGCAGGTGGACGAGGCCCAAGTCCAG
CTGGAAGCTTGA
Protein Properties
Number of Residues 943
Molecular Weight 104756.4
Theoretical pI 6.53
Pfam Domain Function
Signals
  • 1-33
Transmembrane Regions
  • 404-424
Protein Sequence 
>Tyrosine-protein kinase transmembrane receptor ROR2
MARGSALPRRPLLCIPAVWAAAALLLSVSRTSGEVEVLDPNDPLGPLDGQDGPIPTLKGY
FLNFLEPVNNITIVQGQTAILHCKVAGNPPPNVRWLKNDAPVVQEPRRIIIRKTEYGSRL
RIQDLDTTDTGYYQCVATNGMKTITATGVLFVRLGPTHSPNHNFQDDYHEDGFCQPYRGI
ACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTHLSDQCSQFAIPSFCHFVFPLCD
ARSRTPKPRELCRDECEVLESDLCRQEYTIARSNPLILMRLQLPKCEALPMPESPDAANC
MRIGIPAERLGRYHQCYNGSGMDYRGTASTTKSGHQCQPWALQHPHSHHLSSTDFPELGG
GHAYCRNPGGQMEGPWCFTQNKNVRMELCDVPSCSPRDSSKMGILYILVPSIAIPLVIAC
LFFLVCMCRNKQKASASTPQRRQLMASPSQDMEMPLINQHKQAKLKEISLSAVRFMEELG
EDRFGKVYKGHLFGPAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRARLQHPNVVCLL
GVVTKDQPLSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDRTVKSALEPPDFVHLVAQIA
AGMEYLSSHHVVHKDLATRNVLVYDKLNVKISDLGLFREVYAADYYKLLGNSLLPIRWMA
PEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVVEMIRNRQVLPCPDDCPAW
VYALMIECWNEFPSRRPRFKDIHSRLRAWGNLSNYNSSAQTSGASNTTQTSSLSTSPVSN
VSNARYVGPKQKAPPFPQPQFIPMKGQIRPMVPPPQLYVPVNGYQPVPAYGAYLPNFYPV
QIPMQMAPQQVPPQMVPKPSSHHSGSGSTSTGYVTTAPSNTSMADRAALLSEGADDTQNA
PEDGAQSTVQEAEEEEEGSVPETELLGDCDTLQVDEAQVQLEA
GenBank ID Protein 19743898
UniProtKB/Swiss-Prot ID Q01974
UniProtKB/Swiss-Prot Entry Name ROR2_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_004560.2
GeneCard ID ROR2
GenAtlas ID ROR2
HGNC ID HGNC:10257
References
General References
  1. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed:17525332 ]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  3. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed:17344846 ]
  4. Masiakowski P, Carroll RD: A novel family of cell surface receptors with tyrosine kinase-like domain. J Biol Chem. 1992 Dec 25;267(36):26181-90. [PubMed:1334494 ]
  5. Oldridge M, Fortuna AM, Maringa M, Propping P, Mansour S, Pollitt C, DeChiara TM, Kimble RB, Valenzuela DM, Yancopoulos GD, Wilkie AO: Dominant mutations in ROR2, encoding an orphan receptor tyrosine kinase, cause brachydactyly type B. Nat Genet. 2000 Mar;24(3):275-8. [PubMed:10700182 ]
  6. Schwabe GC, Tinschert S, Buschow C, Meinecke P, Wolff G, Gillessen-Kaesbach G, Oldridge M, Wilkie AO, Komec R, Mundlos S: Distinct mutations in the receptor tyrosine kinase gene ROR2 cause brachydactyly type B. Am J Hum Genet. 2000 Oct;67(4):822-31. Epub 2000 Sep 12. [PubMed:10986040 ]
  7. Medzihradszky KF, Darula Z, Perlson E, Fainzilber M, Chalkley RJ, Ball H, Greenbaum D, Bogyo M, Tyson DR, Bradshaw RA, Burlingame AL: O-sulfonation of serine and threonine: mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes. Mol Cell Proteomics. 2004 May;3(5):429-40. Epub 2004 Jan 29. [PubMed:14752058 ]
  8. Liu Y, Ross JF, Bodine PV, Billiard J: Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta) phosphorylation and promotes osteoblast differentiation and bone formation. Mol Endocrinol. 2007 Dec;21(12):3050-61. Epub 2007 Aug 23. [PubMed:17717073 ]
  9. Afzal AR, Rajab A, Fenske CD, Oldridge M, Elanko N, Ternes-Pereira E, Tuysuz B, Murday VA, Patton MA, Wilkie AO, Jeffery S: Recessive Robinow syndrome, allelic to dominant brachydactyly type B, is caused by mutation of ROR2. Nat Genet. 2000 Aug;25(4):419-22. [PubMed:10932186 ]
  10. van Bokhoven H, Celli J, Kayserili H, van Beusekom E, Balci S, Brussel W, Skovby F, Kerr B, Percin EF, Akarsu N, Brunner HG: Mutation of the gene encoding the ROR2 tyrosine kinase causes autosomal recessive Robinow syndrome. Nat Genet. 2000 Aug;25(4):423-6. [PubMed:10932187 ]
  11. Authors unspecified: Corrections/Erratum Nat Genet. 2000 Nov;26(3):383. [PubMed:11062486 ]