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Q01974

- ROR2_HUMAN

UniProt

Q01974 - ROR2_HUMAN

Protein

Tyrosine-protein kinase transmembrane receptor ROR2

Gene

ROR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    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.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei507 – 5071ATPPROSITE-ProRule annotation
    Active sitei615 – 6151Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi479 – 4879ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

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

    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

    GO - Cellular componenti

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

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 943910Tyrosine-protein kinase transmembrane receptor ROR2PRO_0000024460Add
    BLAST

    Amino acid modifications

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

    Binary interactionsi

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

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    943
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini34 – 403370ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini425 – 943519CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei404 – 42421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 14591Ig-like C2-typeAdd
    BLAST
    Domaini169 – 303135FZPROSITE-ProRule annotationAdd
    BLAST
    Domaini316 – 39479KringlePROSITE-ProRule annotationAdd
    BLAST
    Domaini473 – 746274Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. ROR subfamily.PROSITE-ProRule annotation
    Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation
    Contains 1 kringle domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 161 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