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Q01974

- ROR2_HUMAN

UniProt

Q01974 - ROR2_HUMAN

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Protein
Tyrosine-protein kinase transmembrane receptor ROR2
Gene
ROR2, NTRKR2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei507 – 5071ATP By similarity
Active sitei615 – 6151Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi479 – 4879ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. Wnt-protein binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. transmembrane receptor protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

  1. JNK cascade Source: Ensembl
  2. Wnt signaling pathway, calcium modulating pathway Source: Ensembl
  3. Wnt signaling pathway, planar cell polarity pathway Source: Ensembl
  4. cartilage condensation Source: Ensembl
  5. cell differentiation Source: Ensembl
  6. embryonic genitalia morphogenesis Source: Ensembl
  7. inner ear morphogenesis Source: Ensembl
  8. multicellular organismal development Source: ProtInc
  9. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  10. negative regulation of cell proliferation Source: UniProtKB
  11. peptidyl-tyrosine phosphorylation Source: GOC
  12. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  13. positive regulation of cell migration Source: UniProtKB
  14. positive regulation of transcription, DNA-templated Source: Ensembl
  15. signal transduction Source: ProtInc
  16. somitogenesis Source: Ensembl
  17. transmembrane receptor protein tyrosine kinase signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_172581. PCP/CE pathway.
REACT_172631. WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
SignaLinkiQ01974.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase transmembrane receptor ROR2 (EC:2.7.10.1)
Alternative name(s):
Neurotrophic tyrosine kinase, receptor-related 2
Gene namesi
Name:ROR2
Synonyms:NTRKR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:10257. ROR2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 403370Extracellular Reviewed prediction
Add
BLAST
Transmembranei404 – 42421Helical; Reviewed prediction
Add
BLAST
Topological domaini425 – 943519Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. clathrin-coated endocytic vesicle membrane Source: Reactome
  2. integral component of plasma membrane Source: ProtInc
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti182 – 1821C → Y in RRS. 1 Publication
VAR_010911
Natural varianti184 – 1841R → C in RRS. 1 Publication
VAR_010768
Natural varianti189 – 1891R → W in RRS. 1 Publication
VAR_010769
Natural varianti366 – 3661R → W in RRS. 1 Publication
VAR_010770
Natural varianti620 – 6201N → K in RRS. 1 Publication
VAR_010771

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi113000. phenotype.
268310. phenotype.
Orphaneti1507. Autosomal recessive Robinow syndrome.
93383. Brachydactyly type B.
PharmGKBiPA34629.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333 Reviewed prediction
Add
BLAST
Chaini34 – 943910Tyrosine-protein kinase transmembrane receptor ROR2
PRO_0000024460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi83 ↔ 135 By similarity
Disulfide bondi174 ↔ 239 By similarity
Disulfide bondi182 ↔ 232 By similarity
Glycosylationi188 – 1881N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi223 ↔ 264 By similarity
Disulfide bondi252 ↔ 300 By similarity
Disulfide bondi256 ↔ 286 By similarity
Disulfide bondi316 ↔ 394 By similarity
Glycosylationi318 – 3181N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi337 ↔ 377 By similarity
Disulfide bondi365 ↔ 389 By similarity
Modified residuei469 – 4691Sulfoserine; partial1 Publication
Modified residuei471 – 4711Sulfoserine; partial1 Publication
Modified residuei646 – 6461Phosphotyrosine; by autocatalysis By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiQ01974.
PaxDbiQ01974.
PRIDEiQ01974.

PTM databases

PhosphoSiteiQ01974.

Expressioni

Developmental stagei

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.

Gene expression databases

ArrayExpressiQ01974.
BgeeiQ01974.
CleanExiHS_ROR2.
GenevestigatoriQ01974.

Organism-specific databases

HPAiHPA021868.

Interactioni

Subunit structurei

Homodimer; promotes osteogenesis. Binds YWHAB. Interacts with WTIP By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-6422642,EBI-352572

Protein-protein interaction databases

BioGridi110974. 7 interactions.
IntActiQ01974. 1 interaction.
STRINGi9606.ENSP00000364860.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi470 – 4723
Beta strandi473 – 4819
Beta strandi486 – 4927
Beta strandi502 – 5087
Helixi518 – 53013
Beta strandi539 – 5435
Beta strandi545 – 5484
Beta strandi550 – 5545
Helixi561 – 5666
Helixi589 – 60820
Helixi618 – 6203
Beta strandi621 – 6233
Helixi625 – 6273
Beta strandi629 – 6313
Helixi639 – 6446
Beta strandi648 – 6525
Helixi656 – 6583
Helixi661 – 6666
Helixi671 – 68616
Turni687 – 6893
Turni692 – 6954
Helixi698 – 7069
Helixi719 – 72810
Helixi733 – 7353
Helixi739 – 7479

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZZWX-ray2.90A/B464-751[»]
4GT4X-ray2.41A/B452-753[»]
ProteinModelPortaliQ01974.
SMRiQ01974. Positions 17-156, 282-420, 450-751.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 14591Ig-like C2-type
Add
BLAST
Domaini169 – 303135FZ
Add
BLAST
Domaini316 – 39479Kringle
Add
BLAST
Domaini473 – 746274Protein kinase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi753 – 78230Ser/Thr-rich
Add
BLAST
Compositional biasi784 – 85774Pro-rich
Add
BLAST
Compositional biasi859 – 88224Ser/Thr-rich
Add
BLAST

Sequence similaritiesi

Contains 1 kringle domain.

Keywords - Domaini

Immunoglobulin domain, Kringle, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000049104.
HOVERGENiHBG017736.
InParanoidiQ01974.
KOiK05123.
OMAiLQLPKCE.
PhylomeDBiQ01974.
TreeFamiTF106465.

Family and domain databases

Gene3Di2.40.20.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR020067. 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]
PfamiPF01392. Fz. 1 hit.
PF07679. I-set. 1 hit.
PF00051. Kringle. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000624. TyrPK_TMrec_ROR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00408. IGc2. 1 hit.
SM00130. KR. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiPS50038. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01974-1 [UniParc]FASTAAdd to Basket

« Hide

MARGSALPRR PLLCIPAVWA AAALLLSVSR TSGEVEVLDP NDPLGPLDGQ    50
DGPIPTLKGY FLNFLEPVNN ITIVQGQTAI LHCKVAGNPP PNVRWLKNDA 100
PVVQEPRRII IRKTEYGSRL RIQDLDTTDT GYYQCVATNG MKTITATGVL 150
FVRLGPTHSP NHNFQDDYHE DGFCQPYRGI ACARFIGNRT IYVDSLQMQG 200
EIENRITAAF TMIGTSTHLS DQCSQFAIPS FCHFVFPLCD ARSRTPKPRE 250
LCRDECEVLE SDLCRQEYTI ARSNPLILMR LQLPKCEALP MPESPDAANC 300
MRIGIPAERL GRYHQCYNGS GMDYRGTAST TKSGHQCQPW ALQHPHSHHL 350
SSTDFPELGG GHAYCRNPGG QMEGPWCFTQ NKNVRMELCD VPSCSPRDSS 400
KMGILYILVP SIAIPLVIAC LFFLVCMCRN KQKASASTPQ RRQLMASPSQ 450
DMEMPLINQH KQAKLKEISL SAVRFMEELG EDRFGKVYKG HLFGPAPGEQ 500
TQAVAIKTLK DKAEGPLREE FRHEAMLRAR LQHPNVVCLL GVVTKDQPLS 550
MIFSYCSHGD LHEFLVMRSP HSDVGSTDDD RTVKSALEPP DFVHLVAQIA 600
AGMEYLSSHH VVHKDLATRN VLVYDKLNVK ISDLGLFREV YAADYYKLLG 650
NSLLPIRWMA PEAIMYGKFS IDSDIWSYGV VLWEVFSYGL QPYCGYSNQD 700
VVEMIRNRQV LPCPDDCPAW VYALMIECWN EFPSRRPRFK DIHSRLRAWG 750
NLSNYNSSAQ TSGASNTTQT SSLSTSPVSN VSNARYVGPK QKAPPFPQPQ 800
FIPMKGQIRP MVPPPQLYVP VNGYQPVPAY GAYLPNFYPV QIPMQMAPQQ 850
VPPQMVPKPS SHHSGSGSTS TGYVTTAPSN TSMADRAALL SEGADDTQNA 900
PEDGAQSTVQ EAEEEEEGSV PETELLGDCD TLQVDEAQVQ LEA 943
Length:943
Mass (Da):104,757
Last modified:March 7, 2006 - v2
Checksum:iF926FB681A8312FE
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti182 – 1821C → Y in RRS. 1 Publication
VAR_010911
Natural varianti184 – 1841R → C in RRS. 1 Publication
VAR_010768
Natural varianti189 – 1891R → W in RRS. 1 Publication
VAR_010769
Natural varianti244 – 2441R → Q.1 Publication
Corresponds to variant rs55737262 [ dbSNP | Ensembl ].
VAR_041787
Natural varianti245 – 2451T → A.5 Publications
Corresponds to variant rs10820900 [ dbSNP | Ensembl ].
VAR_010912
Natural varianti349 – 3491H → D.1 Publication
Corresponds to variant rs55983376 [ dbSNP | Ensembl ].
VAR_041788
Natural varianti366 – 3661R → W in RRS. 1 Publication
VAR_010770
Natural varianti490 – 4901G → A.1 Publication
Corresponds to variant rs56197744 [ dbSNP | Ensembl ].
VAR_041789
Natural varianti530 – 5301R → Q.1 Publication
Corresponds to variant rs35852786 [ dbSNP | Ensembl ].
VAR_041790
Natural varianti542 – 5421V → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041791
Natural varianti548 – 5481P → S.1 Publication
Corresponds to variant rs35764413 [ dbSNP | Ensembl ].
VAR_041792
Natural varianti557 – 5571S → L.1 Publication
Corresponds to variant rs56099091 [ dbSNP | Ensembl ].
VAR_041793
Natural varianti620 – 6201N → K in RRS. 1 Publication
VAR_010771
Natural varianti644 – 6441D → N.1 Publication
Corresponds to variant rs55798732 [ dbSNP | Ensembl ].
VAR_041794
Natural varianti672 – 6721D → N.1 Publication
Corresponds to variant rs55651110 [ dbSNP | Ensembl ].
VAR_041795
Natural varianti695 – 6951G → R.1 Publication
Corresponds to variant rs34431454 [ dbSNP | Ensembl ].
VAR_041796
Natural varianti738 – 7381R → C.1 Publication
Corresponds to variant rs56231927 [ dbSNP | Ensembl ].
VAR_041797
Natural varianti762 – 7621S → L.1 Publication
Corresponds to variant rs34491822 [ dbSNP | Ensembl ].
VAR_041798
Natural varianti819 – 8191V → I.3 Publications
Corresponds to variant rs10761129 [ dbSNP | Ensembl ].
VAR_010913
Natural varianti935 – 9351D → E.1 Publication
Corresponds to variant rs41277835 [ dbSNP | Ensembl ].
VAR_041799

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6691.1.
PIRiB45082.
RefSeqiNP_004551.2. NM_004560.3.
UniGeneiHs.644776.
Hs.98255.

Genome annotation databases

EnsembliENST00000375708; ENSP00000364860; ENSG00000169071.
GeneIDi4920.
KEGGihsa:4920.
UCSCiuc004arj.2. human.

Polymorphism databases

DMDMi90110767.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6691.1.
PIRi B45082.
RefSeqi NP_004551.2. NM_004560.3.
UniGenei Hs.644776.
Hs.98255.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZZW X-ray 2.90 A/B 464-751 [» ]
4GT4 X-ray 2.41 A/B 452-753 [» ]
ProteinModelPortali Q01974.
SMRi Q01974. Positions 17-156, 282-420, 450-751.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110974. 7 interactions.
IntActi Q01974. 1 interaction.
STRINGi 9606.ENSP00000364860.

Chemistry

ChEMBLi CHEMBL2375201.

PTM databases

PhosphoSitei Q01974.

Polymorphism databases

DMDMi 90110767.

Proteomic databases

MaxQBi Q01974.
PaxDbi Q01974.
PRIDEi Q01974.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375708 ; ENSP00000364860 ; ENSG00000169071 .
GeneIDi 4920.
KEGGi hsa:4920.
UCSCi uc004arj.2. human.

Organism-specific databases

CTDi 4920.
GeneCardsi GC09M094325.
GeneReviewsi ROR2.
H-InvDB HIX0034840.
HGNCi HGNC:10257. ROR2.
HPAi HPA021868.
MIMi 113000. phenotype.
268310. phenotype.
602337. gene.
neXtProti NX_Q01974.
Orphaneti 1507. Autosomal recessive Robinow syndrome.
93383. Brachydactyly type B.
PharmGKBi PA34629.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000049104.
HOVERGENi HBG017736.
InParanoidi Q01974.
KOi K05123.
OMAi LQLPKCE.
PhylomeDBi Q01974.
TreeFami TF106465.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_172581. PCP/CE pathway.
REACT_172631. WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
SignaLinki Q01974.

Miscellaneous databases

GeneWikii ROR2.
GenomeRNAii 4920.
NextBioi 18945.
PROi Q01974.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q01974.
Bgeei Q01974.
CleanExi HS_ROR2.
Genevestigatori Q01974.

Family and domain databases

Gene3Di 2.40.20.10. 1 hit.
2.60.40.10. 1 hit.
InterProi IPR020067. 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 ]
Pfami PF01392. Fz. 1 hit.
PF07679. I-set. 1 hit.
PF00051. Kringle. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000624. TyrPK_TMrec_ROR. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00408. IGc2. 1 hit.
SM00130. KR. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEi PS50038. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. "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.
    , 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.

Entry informationi

Entry nameiROR2_HUMAN
AccessioniPrimary (citable) accession number: Q01974
Secondary accession number(s): Q59GF5
, Q5SPI5, Q9HAY7, Q9HB61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 7, 2006
Last modified: September 3, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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