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Q01974 (ROR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase transmembrane receptor ROR2

EC=2.7.10.1
Alternative name(s):
Neurotrophic tyrosine kinase, receptor-related 2
Gene names
Name:ROR2
Synonyms:NTRKR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length943 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Homodimer; promotes osteogenesis. Binds YWHAB. Interacts with WTIP By similarity. Ref.7

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Developmental stage

Expressed at high levels during early embryonic development. The expression levels drop strongly around day 16 and there are only very low levels in adult tissues.

Involvement in disease

Brachydactyly B1 (BDB1) [MIM:113000]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. In brachydactyly type B1 the middle phalanges are short but in addition the terminal phalanges are rudimentary or absent. Both fingers and toes are affected. The thumbs and big toes are usually deformed. Symphalangism is also a feature.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Robinow syndrome autosomal recessive (RRS) [MIM:268310]: A recessive form of Robinow syndrome, a disease characterized by short-limb dwarfism, costovertebral segmentation defects and abnormalities of the head, face and external genitalia. The clinical signs are generally far more severe in recessive cases, particularly skeletal abnormalities. All patients with the recessive form suffer from vertebral segmentation abnormalities, resulting in scoliosis and chest deformities. Rib fusions are considered to be characteristic of the autosomal recessive form. Patients can also present brachydactyly, with extensive aplasia/hypoplasia of the phalanges and metacarpals/metatarsals, and brachy-syn-polydactyly of the hands and oligodactyly of the feet.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. ROR subfamily.

Contains 1 FZ (frizzled) domain.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 kringle domain.

Contains 1 protein kinase domain.

Sequence caution

The sequence BAD92391.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Dwarfism
   DomainImmunoglobulin domain
Kringle
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Sulfation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from electronic annotation. Source: Ensembl

Wnt signaling pathway, calcium modulating pathway

Inferred from electronic annotation. Source: Ensembl

Wnt signaling pathway, planar cell polarity pathway

Inferred from electronic annotation. Source: Ensembl

cartilage condensation

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from electronic annotation. Source: Ensembl

embryonic genitalia morphogenesis

Inferred from electronic annotation. Source: Ensembl

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

negative regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 19486338. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Traceable author statement Ref.1. Source: GOC

positive regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from direct assay PubMed 19486338. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

somitogenesis

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentclathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Wnt-protein binding

Inferred from physical interaction PubMed 19486338. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22939624. Source: IntAct

transmembrane receptor protein tyrosine kinase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSP90AB1P082382EBI-6422642,EBI-352572

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 943910Tyrosine-protein kinase transmembrane receptor ROR2
PRO_0000024460

Regions

Topological domain34 – 403370Extracellular Potential
Transmembrane404 – 42421Helical; Potential
Topological domain425 – 943519Cytoplasmic Potential
Domain55 – 14591Ig-like C2-type
Domain169 – 303135FZ
Domain316 – 39479Kringle
Domain473 – 746274Protein kinase
Nucleotide binding479 – 4879ATP By similarity
Compositional bias753 – 78230Ser/Thr-rich
Compositional bias784 – 85774Pro-rich
Compositional bias859 – 88224Ser/Thr-rich

Sites

Active site6151Proton acceptor By similarity
Binding site5071ATP By similarity

Amino acid modifications

Modified residue4691Sulfoserine; partial Ref.6
Modified residue4711Sulfoserine; partial Ref.6
Modified residue6461Phosphotyrosine; by autocatalysis By similarity
Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Disulfide bond83 ↔ 135 By similarity
Disulfide bond174 ↔ 239 By similarity
Disulfide bond182 ↔ 232 By similarity
Disulfide bond223 ↔ 264 By similarity
Disulfide bond252 ↔ 300 By similarity
Disulfide bond256 ↔ 286 By similarity
Disulfide bond316 ↔ 394 By similarity
Disulfide bond337 ↔ 377 By similarity
Disulfide bond365 ↔ 389 By similarity

Natural variations

Natural variant1821C → Y in RRS. Ref.10
VAR_010911
Natural variant1841R → C in RRS. Ref.9
VAR_010768
Natural variant1891R → W in RRS. Ref.9
VAR_010769
Natural variant2441R → Q. Ref.12
Corresponds to variant rs55737262 [ dbSNP | Ensembl ].
VAR_041787
Natural variant2451T → A. Ref.1 Ref.3 Ref.4 Ref.5 Ref.12
Corresponds to variant rs10820900 [ dbSNP | Ensembl ].
VAR_010912
Natural variant3491H → D. Ref.12
Corresponds to variant rs55983376 [ dbSNP | Ensembl ].
VAR_041788
Natural variant3661R → W in RRS. Ref.9
VAR_010770
Natural variant4901G → A. Ref.12
Corresponds to variant rs56197744 [ dbSNP | Ensembl ].
VAR_041789
Natural variant5301R → Q. Ref.12
Corresponds to variant rs35852786 [ dbSNP | Ensembl ].
VAR_041790
Natural variant5421V → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.12
VAR_041791
Natural variant5481P → S. Ref.12
Corresponds to variant rs35764413 [ dbSNP | Ensembl ].
VAR_041792
Natural variant5571S → L. Ref.12
Corresponds to variant rs56099091 [ dbSNP | Ensembl ].
VAR_041793
Natural variant6201N → K in RRS. Ref.9
VAR_010771
Natural variant6441D → N. Ref.12
Corresponds to variant rs55798732 [ dbSNP | Ensembl ].
VAR_041794
Natural variant6721D → N. Ref.12
Corresponds to variant rs55651110 [ dbSNP | Ensembl ].
VAR_041795
Natural variant6951G → R. Ref.12
Corresponds to variant rs34431454 [ dbSNP | Ensembl ].
VAR_041796
Natural variant7381R → C. Ref.12
Corresponds to variant rs56231927 [ dbSNP | Ensembl ].
VAR_041797
Natural variant7621S → L. Ref.12
Corresponds to variant rs34491822 [ dbSNP | Ensembl ].
VAR_041798
Natural variant8191V → I. Ref.3 Ref.4 Ref.12
Corresponds to variant rs10761129 [ dbSNP | Ensembl ].
VAR_010913
Natural variant9351D → E. Ref.12
Corresponds to variant rs41277835 [ dbSNP | Ensembl ].
VAR_041799

Secondary structure

................................................ 943
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01974 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: F926FB681A8312FE

FASTA943104,757
        10         20         30         40         50         60 
MARGSALPRR PLLCIPAVWA AAALLLSVSR TSGEVEVLDP NDPLGPLDGQ DGPIPTLKGY 

        70         80         90        100        110        120 
FLNFLEPVNN ITIVQGQTAI LHCKVAGNPP PNVRWLKNDA PVVQEPRRII IRKTEYGSRL 

       130        140        150        160        170        180 
RIQDLDTTDT GYYQCVATNG MKTITATGVL FVRLGPTHSP NHNFQDDYHE DGFCQPYRGI 

       190        200        210        220        230        240 
ACARFIGNRT IYVDSLQMQG EIENRITAAF TMIGTSTHLS DQCSQFAIPS FCHFVFPLCD 

       250        260        270        280        290        300 
ARSRTPKPRE LCRDECEVLE SDLCRQEYTI ARSNPLILMR LQLPKCEALP MPESPDAANC 

       310        320        330        340        350        360 
MRIGIPAERL GRYHQCYNGS GMDYRGTAST TKSGHQCQPW ALQHPHSHHL SSTDFPELGG 

       370        380        390        400        410        420 
GHAYCRNPGG QMEGPWCFTQ NKNVRMELCD VPSCSPRDSS KMGILYILVP SIAIPLVIAC 

       430        440        450        460        470        480 
LFFLVCMCRN KQKASASTPQ RRQLMASPSQ DMEMPLINQH KQAKLKEISL SAVRFMEELG 

       490        500        510        520        530        540 
EDRFGKVYKG HLFGPAPGEQ TQAVAIKTLK DKAEGPLREE FRHEAMLRAR LQHPNVVCLL 

       550        560        570        580        590        600 
GVVTKDQPLS MIFSYCSHGD LHEFLVMRSP HSDVGSTDDD RTVKSALEPP DFVHLVAQIA 

       610        620        630        640        650        660 
AGMEYLSSHH VVHKDLATRN VLVYDKLNVK ISDLGLFREV YAADYYKLLG NSLLPIRWMA 

       670        680        690        700        710        720 
PEAIMYGKFS IDSDIWSYGV VLWEVFSYGL QPYCGYSNQD VVEMIRNRQV LPCPDDCPAW 

       730        740        750        760        770        780 
VYALMIECWN EFPSRRPRFK DIHSRLRAWG NLSNYNSSAQ TSGASNTTQT SSLSTSPVSN 

       790        800        810        820        830        840 
VSNARYVGPK QKAPPFPQPQ FIPMKGQIRP MVPPPQLYVP VNGYQPVPAY GAYLPNFYPV 

       850        860        870        880        890        900 
QIPMQMAPQQ VPPQMVPKPS SHHSGSGSTS TGYVTTAPSN TSMADRAALL SEGADDTQNA 

       910        920        930        940 
PEDGAQSTVQ EAEEEEEGSV PETELLGDCD TLQVDEAQVQ LEA 

« Hide

References

« Hide 'large scale' references
[1]"A novel family of cell surface receptors with tyrosine kinase-like domain."
Masiakowski P., Carroll R.D.
J. Biol. Chem. 267:26181-26190(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-245.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-943, VARIANTS ALA-245 AND ILE-819.
Tissue: Brain.
[4]"Dominant mutations in ROR2, encoding an orphan receptor tyrosine kinase, cause brachydactyly type B."
Oldridge M., Fortuna A.M., Maringa M., Propping P., Mansour S., Pollitt C., DeChiara T.M., Kimble R.B., Valenzuela D.M., Yancopoulos G.D., Wilkie A.O.M.
Nat. Genet. 24:275-278(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-943, VARIANTS ALA-245 AND ILE-819.
[5]"Distinct mutations in the receptor tyrosine kinase gene ROR2 cause brachydactyly type B."
Schwabe G.C., Tinschert S., Buschow C., Meinecke P., Wolff G., Gillessen-Kaesbach G., Oldridge M., Wilkie A.O.M., Koemec R., Mundlos S.
Am. J. Hum. Genet. 67:822-831(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-574, VARIANT ALA-245.
[6]"O-sulfonation of serine and threonine: mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes."
Medzihradszky K.F., Darula Z., Perlson E., Fainzilber M., Chalkley R.J., Ball H., Greenbaum D., Bogyo M., Tyson D.R., Bradshaw R.A., Burlingame A.L.
Mol. Cell. Proteomics 3:429-440(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 465-474, SULFATION AT SER-469 AND SER-471, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta) phosphorylation and promotes osteoblast differentiation and bone formation."
Liu Y., Ross J.F., Bodine P.V.N., Billiard J.
Mol. Endocrinol. 21:3050-3061(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YWHAB, FUNCTION IN YWHAB PHOSPHORYLATION, DIMERIZATION, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Recessive Robinow syndrome, allelic to dominant brachydactyly type B, is caused by mutation of ROR2."
Afzal A.R., Rajab A., Fenske C.D., Oldridge M., Elanko N., Ternes-Pereira E., Tueysuez B., Murday V.A., Patton M.A., Wilkie A.O.M., Jeffery S.
Nat. Genet. 25:419-422(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RRS CYS-184; TRP-189; TRP-366 AND LYS-620.
[10]"Mutation of the gene encoding the ROR2 tyrosine kinase causes autosomal recessive Robinow syndrome."
van Bokhoven H., Celli J., Kayserili H., van Beusekom E., Balci S., Brussel W., Skovby F., Kerr B., Percin E.F., Akarsu N., Brunner H.G.
Nat. Genet. 25:423-426(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RRS TYR-182.
[11]Erratum
van Bokhoven H., Celli J., Kayserili H., van Beusekom E., Balci S., Brussel W., Skovby F., Kerr B., Percin E.F., Akarsu N., Brunner H.G.
Nat. Genet. 26:383-383(2000) [PubMed] [Europe PMC] [Abstract]
[12]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , 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 D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-244; ALA-245; ASP-349; ALA-490; GLN-530; MET-542; SER-548; LEU-557; ASN-644; ASN-672; ARG-695; CYS-738; LEU-762; ILE-819 AND GLU-935.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97639 mRNA. Translation: AAA60276.1.
AL391219, AL928802, AL583841 Genomic DNA. Translation: CAH70208.1.
AL928802, AL391219, AL583841 Genomic DNA. Translation: CAI17303.1.
AL583841, AL391219, AL928802 Genomic DNA. Translation: CAI15694.1.
AB209154 mRNA. Translation: BAD92391.1. Different initiation.
AH009681 Genomic DNA. Translation: AAG01184.2.
AH010002 Genomic DNA. Translation: AAG33132.1.
CCDSCCDS6691.1.
PIRB45082.
RefSeqNP_004551.2. NM_004560.3.
UniGeneHs.644776.
Hs.98255.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZZWX-ray2.90A/B464-751[»]
4GT4X-ray2.41A/B452-753[»]
ProteinModelPortalQ01974.
SMRQ01974. Positions 17-156, 282-420, 450-751.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110974. 7 interactions.
IntActQ01974. 1 interaction.
STRING9606.ENSP00000364860.

Chemistry

ChEMBLCHEMBL2375201.

PTM databases

PhosphoSiteQ01974.

Polymorphism databases

DMDM90110767.

Proteomic databases

MaxQBQ01974.
PaxDbQ01974.
PRIDEQ01974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375708; ENSP00000364860; ENSG00000169071.
GeneID4920.
KEGGhsa:4920.
UCSCuc004arj.2. human.

Organism-specific databases

CTD4920.
GeneCardsGC09M094325.
GeneReviewsROR2.
H-InvDBHIX0034840.
HGNCHGNC:10257. ROR2.
HPAHPA021868.
MIM113000. phenotype.
268310. phenotype.
602337. gene.
neXtProtNX_Q01974.
Orphanet1507. Autosomal recessive Robinow syndrome.
93383. Brachydactyly type B.
PharmGKBPA34629.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000049104.
HOVERGENHBG017736.
InParanoidQ01974.
KOK05123.
OMALQLPKCE.
PhylomeDBQ01974.
TreeFamTF106465.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkQ01974.

Gene expression databases

ArrayExpressQ01974.
BgeeQ01974.
CleanExHS_ROR2.
GenevestigatorQ01974.

Family and domain databases

Gene3D2.40.20.10. 1 hit.
2.60.40.10. 1 hit.
InterProIPR020067. Frizzled_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016247. Tyr_kinase_rcpt_ROR.
[Graphical view]
PfamPF01392. Fz. 1 hit.
PF07679. I-set. 1 hit.
PF00051. Kringle. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000624. TyrPK_TMrec_ROR. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00408. IGc2. 1 hit.
SM00130. KR. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEPS50038. FZ. 1 hit.
PS50835. IG_LIKE. 1 hit.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiROR2.
GenomeRNAi4920.
NextBio18945.
PROQ01974.
SOURCESearch...

Entry information

Entry nameROR2_HUMAN
AccessionPrimary (citable) accession number: Q01974
Secondary accession number(s): Q59GF5 expand/collapse secondary AC list , Q5SPI5, Q9HAY7, Q9HB61
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM