Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q16832

- DDR2_HUMAN

UniProt

Q16832 - DDR2_HUMAN

Protein

Discoidin domain-containing receptor 2

Gene

DDR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing.8 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.2 PublicationsPROSITE-ProRule annotation

    Enzyme regulationi

    Present in an inactive state in the absence of collagen binding and phosphorylation by SRC. Tyrosine phosphorylation enhances the affinity for ATP and the catalytic activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei608 – 6081ATPCurated
    Active sitei710 – 7101Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi569 – 5779ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. biomineral tissue development Source: UniProtKB
    2. cell adhesion Source: ProtInc
    3. chondrocyte proliferation Source: UniProtKB
    4. collagen-activated tyrosine kinase receptor signaling pathway Source: UniProtKB
    5. collagen fibril organization Source: UniProtKB
    6. endochondral bone growth Source: UniProtKB
    7. extracellular matrix organization Source: Reactome
    8. ossification Source: UniProtKB-KW
    9. peptidyl-tyrosine phosphorylation Source: UniProtKB
    10. positive regulation of extracellular matrix disassembly Source: UniProtKB
    11. positive regulation of fibroblast migration Source: UniProtKB
    12. positive regulation of fibroblast proliferation Source: UniProtKB
    13. positive regulation of osteoblast differentiation Source: UniProtKB
    14. positive regulation of protein kinase activity Source: UniProtKB
    15. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    16. protein autophosphorylation Source: UniProtKB
    17. regulation of bone mineralization Source: UniProtKB
    18. regulation of extracellular matrix disassembly Source: UniProtKB
    19. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Osteogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
    SignaLinkiQ16832.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Discoidin domain-containing receptor 2 (EC:2.7.10.1)
    Short name:
    Discoidin domain receptor 2
    Alternative name(s):
    CD167 antigen-like family member B
    Discoidin domain-containing receptor tyrosine kinase 2
    Neurotrophic tyrosine kinase, receptor-related 3
    Receptor protein-tyrosine kinase TKT
    Tyrosine-protein kinase TYRO10
    CD_antigen: CD167b
    Gene namesi
    Name:DDR2
    Synonyms:NTRKR3, TKT, TYRO10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2731. DDR2.

    Subcellular locationi

    Cell membrane 3 Publications; Single-pass type I membrane protein 3 Publications

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: ProtInc
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Spondyloepimetaphyseal dysplasia short limb-hand type (SEMD-SL) [MIM:271665]: A bone disease characterized by short-limbed dwarfism, a narrow chest with pectus excavatum, brachydactyly in the hands and feet, a characteristic craniofacial appearance and premature calcifications. The radiological findings are distinctive and comprise short long bones throughout the skeleton with striking epiphyses that are stippled, flattened and fragmented and flared, irregular metaphyses. Platyspondyly in the spine with wide intervertebral spaces is observed and some vertebral bodies are pear-shaped with central humps, anterior protrusions and posterior scalloping.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti113 – 1131E → K in SEMD-SL; abolishes collagen binding. 1 Publication
    VAR_065719
    Natural varianti713 – 7131T → I in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
    VAR_063050
    Natural varianti726 – 7261I → R in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
    VAR_063051
    Natural varianti752 – 7521R → C in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
    VAR_063052

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521W → A: Abolishes collagen binding. 2 Publications
    Mutagenesisi608 – 6081K → A: Abolishes kinase activity. 1 Publication
    Mutagenesisi736 – 7361Y → F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-740 and F-741. 1 Publication
    Mutagenesisi740 – 7401Y → F: Promotes autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-741. 1 Publication
    Mutagenesisi741 – 7411Y → F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-740. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi271665. phenotype.
    Orphaneti93358. Spondyloepimetaphyseal dysplasia - short limb - abnormal calcification.
    PharmGKBiPA27196.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 855834Discoidin domain-containing receptor 2PRO_0000016746Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 185
    Disulfide bondi73 ↔ 177
    Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis
    Modified residuei461 – 4611Phosphoserine
    Modified residuei471 – 4711Phosphotyrosine; by SRC and autocatalysisBy similarity
    Modified residuei674 – 6741Phosphoserine
    Modified residuei736 – 7361Phosphotyrosine; by SRC and autocatalysis1 Publication
    Modified residuei740 – 7401Phosphotyrosine; by SRC and autocatalysis1 Publication
    Modified residuei741 – 7411Phosphotyrosine; by SRC and autocatalysis1 Publication

    Post-translational modificationi

    N-glycosylated.1 Publication
    Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues.5 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ16832.
    PaxDbiQ16832.
    PRIDEiQ16832.

    PTM databases

    PhosphoSiteiQ16832.

    Expressioni

    Tissue specificityi

    Detected in osteocytes, osteoblastic cells in subchondral bone, bone lining cells, tibia and cartilage (at protein level). Detected at high levels in heart and lung, and at low levels in brain, placenta, liver, skeletal muscle, pancreas, and kidney.3 Publications

    Inductioni

    Up-regulated during osteoblast differentiation (in vitro). Up-regulated in cartilage from osteoarthritis patients.2 Publications

    Gene expression databases

    ArrayExpressiQ16832.
    BgeeiQ16832.
    CleanExiHS_DDR2.
    HS_TKT.
    GenevestigatoriQ16832.

    Interactioni

    Subunit structurei

    Binds hydroxyproline-rich sequence motifs in fibrillar, glycosylated collagen, such as the GQOGVMGFO motif, where O stands for hydroxyproline. Interacts with SRC. Interacts (tyrosine phosphorylated) with SHC1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COL11A2P139422EBI-1381484,EBI-2515504
    HSP90AB1P082382EBI-1381484,EBI-352572

    Protein-protein interaction databases

    BioGridi110975. 6 interactions.
    DIPiDIP-39699N.
    IntActiQ16832. 4 interactions.
    MINTiMINT-233614.
    STRINGi9606.ENSP00000356898.

    Structurei

    Secondary structure

    1
    855
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni27 – 293
    Beta strandi33 – 353
    Turni36 – 383
    Beta strandi39 – 413
    Helixi43 – 453
    Beta strandi46 – 494
    Helixi54 – 563
    Helixi58 – 603
    Beta strandi70 – 723
    Beta strandi87 – 10317
    Helixi107 – 1093
    Beta strandi116 – 12813
    Beta strandi139 – 1424
    Beta strandi145 – 1495
    Beta strandi151 – 16919
    Beta strandi171 – 1744
    Beta strandi178 – 1869

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WUHX-ray1.60A26-190[»]
    2Z4FNMR-A26-186[»]
    ProteinModelPortaliQ16832.
    SMRiQ16832. Positions 26-369, 459-851.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16832.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 399378ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini422 – 855434CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei400 – 42122HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 185156F5/8 type CPROSITE-ProRule annotationAdd
    BLAST
    Domaini563 – 849287Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
    Contains 1 F5/8 type C domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000043102.
    HOVERGENiHBG005461.
    InParanoidiQ16832.
    KOiK05125.
    OMAiASAIKCQ.
    OrthoDBiEOG77Q4W2.
    PhylomeDBiQ16832.
    TreeFamiTF317840.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR029553. DDR2.
    IPR008979. Galactose-bd-like.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR002011. Tyr_kinase_rcpt_2_CS.
    [Graphical view]
    PANTHERiPTHR24416:SF297. PTHR24416:SF297. 1 hit.
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00231. FA58C. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS01285. FA58C_1. 1 hit.
    PS01286. FA58C_2. 1 hit.
    PS50022. FA58C_3. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q16832-1 [UniParc]FASTAAdd to Basket

    « Hide

    MILIPRMLLV LFLLLPILSS AKAQVNPAIC RYPLGMSGGQ IPDEDITASS    50
    QWSESTAAKY GRLDSEEGDG AWCPEIPVEP DDLKEFLQID LHTLHFITLV 100
    GTQGRHAGGH GIEFAPMYKI NYSRDGTRWI SWRNRHGKQV LDGNSNPYDI 150
    FLKDLEPPIV ARFVRFIPVT DHSMNVCMRV ELYGCVWLDG LVSYNAPAGQ 200
    QFVLPGGSII YLNDSVYDGA VGYSMTEGLG QLTDGVSGLD DFTQTHEYHV 250
    WPGYDYVGWR NESATNGYIE IMFEFDRIRN FTTMKVHCNN MFAKGVKIFK 300
    EVQCYFRSEA SEWEPNAISF PLVLDDVNPS ARFVTVPLHH RMASAIKCQY 350
    HFADTWMMFS EITFQSDAAM YNNSEALPTS PMAPTTYDPM LKVDDSNTRI 400
    LIGCLVAIIF ILLAIIVIIL WRQFWQKMLE KASRRMLDDE MTVSLSLPSD 450
    SSMFNNNRSS SPSEQGSNST YDRIFPLRPD YQEPSRLIRK LPEFAPGEEE 500
    SGCSGVVKPV QPSGPEGVPH YAEADIVNLQ GVTGGNTYSV PAVTMDLLSG 550
    KDVAVEEFPR KLLTFKEKLG EGQFGEVHLC EVEGMEKFKD KDFALDVSAN 600
    QPVLVAVKML RADANKNARN DFLKEIKIMS RLKDPNIIHL LAVCITDDPL 650
    CMITEYMENG DLNQFLSRHE PPNSSSSDVR TVSYTNLKFM ATQIASGMKY 700
    LSSLNFVHRD LATRNCLVGK NYTIKIADFG MSRNLYSGDY YRIQGRAVLP 750
    IRWMSWESIL LGKFTTASDV WAFGVTLWET FTFCQEQPYS QLSDEQVIEN 800
    TGEFFRDQGR QTYLPQPAIC PDSVYKLMLS CWRRDTKNRP SFQEIHLLLL 850
    QQGDE 855
    Length:855
    Mass (Da):96,736
    Last modified:November 25, 2008 - v2
    Checksum:i78662021BC53E1A0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti642 – 6421A → S in CAA52777. (PubMed:8247548)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051R → S in a lung large cell carcinoma sample; somatic mutation. 2 Publications
    VAR_041498
    Natural varianti113 – 1131E → K in SEMD-SL; abolishes collagen binding. 1 Publication
    VAR_065719
    Natural varianti441 – 4411M → I.1 Publication
    Corresponds to variant rs34722354 [ dbSNP | Ensembl ].
    VAR_041499
    Natural varianti478 – 4781R → C.1 Publication
    Corresponds to variant rs34869543 [ dbSNP | Ensembl ].
    VAR_041500
    Natural varianti543 – 5431V → F.1 Publication
    Corresponds to variant rs55973200 [ dbSNP | Ensembl ].
    VAR_041501
    Natural varianti713 – 7131T → I in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
    VAR_063050
    Natural varianti726 – 7261I → R in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
    VAR_063051
    Natural varianti752 – 7521R → C in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
    VAR_063052

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74764 mRNA. Translation: CAA52777.1.
    AK314388 mRNA. Translation: BAG37013.1.
    AK095975 mRNA. Translation: BAG53183.1.
    AL445197 Genomic DNA. Translation: CAI15941.1.
    CH471067 Genomic DNA. Translation: EAW90713.1.
    BC052998 mRNA. Translation: AAH52998.1.
    CCDSiCCDS1241.1.
    PIRiS42621.
    RefSeqiNP_001014796.1. NM_001014796.1.
    NP_006173.2. NM_006182.2.
    XP_006711407.1. XM_006711344.1.
    UniGeneiHs.275757.
    Hs.593833.

    Genome annotation databases

    EnsembliENST00000367921; ENSP00000356898; ENSG00000162733.
    ENST00000367922; ENSP00000356899; ENSG00000162733.
    GeneIDi4921.
    KEGGihsa:4921.
    UCSCiuc001gcf.3. human.

    Polymorphism databases

    DMDMi215273969.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74764 mRNA. Translation: CAA52777.1 .
    AK314388 mRNA. Translation: BAG37013.1 .
    AK095975 mRNA. Translation: BAG53183.1 .
    AL445197 Genomic DNA. Translation: CAI15941.1 .
    CH471067 Genomic DNA. Translation: EAW90713.1 .
    BC052998 mRNA. Translation: AAH52998.1 .
    CCDSi CCDS1241.1.
    PIRi S42621.
    RefSeqi NP_001014796.1. NM_001014796.1.
    NP_006173.2. NM_006182.2.
    XP_006711407.1. XM_006711344.1.
    UniGenei Hs.275757.
    Hs.593833.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WUH X-ray 1.60 A 26-190 [» ]
    2Z4F NMR - A 26-186 [» ]
    ProteinModelPortali Q16832.
    SMRi Q16832. Positions 26-369, 459-851.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110975. 6 interactions.
    DIPi DIP-39699N.
    IntActi Q16832. 4 interactions.
    MINTi MINT-233614.
    STRINGi 9606.ENSP00000356898.

    Chemistry

    BindingDBi Q16832.
    ChEMBLi CHEMBL5122.
    GuidetoPHARMACOLOGYi 1844.

    PTM databases

    PhosphoSitei Q16832.

    Polymorphism databases

    DMDMi 215273969.

    Proteomic databases

    MaxQBi Q16832.
    PaxDbi Q16832.
    PRIDEi Q16832.

    Protocols and materials databases

    DNASUi 4921.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367921 ; ENSP00000356898 ; ENSG00000162733 .
    ENST00000367922 ; ENSP00000356899 ; ENSG00000162733 .
    GeneIDi 4921.
    KEGGi hsa:4921.
    UCSCi uc001gcf.3. human.

    Organism-specific databases

    CTDi 4921.
    GeneCardsi GC01P162601.
    HGNCi HGNC:2731. DDR2.
    MIMi 191311. gene.
    271665. phenotype.
    neXtProti NX_Q16832.
    Orphaneti 93358. Spondyloepimetaphyseal dysplasia - short limb - abnormal calcification.
    PharmGKBi PA27196.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000043102.
    HOVERGENi HBG005461.
    InParanoidi Q16832.
    KOi K05125.
    OMAi ASAIKCQ.
    OrthoDBi EOG77Q4W2.
    PhylomeDBi Q16832.
    TreeFami TF317840.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
    SignaLinki Q16832.

    Miscellaneous databases

    EvolutionaryTracei Q16832.
    GeneWikii Discoidin_domain-containing_receptor_2.
    GenomeRNAii 4921.
    NextBioi 18949.
    PROi Q16832.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16832.
    Bgeei Q16832.
    CleanExi HS_DDR2.
    HS_TKT.
    Genevestigatori Q16832.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR029553. DDR2.
    IPR008979. Galactose-bd-like.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR002011. Tyr_kinase_rcpt_2_CS.
    [Graphical view ]
    PANTHERi PTHR24416:SF297. PTHR24416:SF297. 1 hit.
    Pfami PF00754. F5_F8_type_C. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00231. FA58C. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS01285. FA58C_1. 1 hit.
    PS01286. FA58C_2. 1 hit.
    PS50022. FA58C_3. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure, expression and chromosomal mapping of TKT from man and mouse: a new subclass of receptor tyrosine kinases with a factor VIII-like domain."
      Karn T., Holtrich U., Braeuninger A., Boehme B., Wolf G., Ruebsamen-Waigmann H., Strebhardt K.
      Oncogene 8:3433-3440(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Heart and Thymus.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Hair follicle dermal papilla and Uterus.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skin.
    6. "The discoidin domain receptor tyrosine kinases are activated by collagen."
      Vogel W., Gish G.D., Alves F., Pawson T.
      Mol. Cell 1:13-23(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS COLLAGEN RECEPTOR AND IN UP-REGULATION OF MMP1, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    7. "Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src stimulates intramolecular autophosphorylation and Shc signaling complex formation."
      Yang K., Kim J.H., Kim H.J., Park I.S., Kim I.Y., Yang B.S.
      J. Biol. Chem. 280:39058-39066(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF MMP1 AND MMP2, PHOSPHORYLATION AT TYR-736; TYR-740 AND TYR-741, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH SHC1, MUTAGENESIS OF LYS-608; TYR-736; TYR-740 AND TYR-741.
    8. "Discoidin domain receptor 2 mediates tumor cell cycle arrest induced by fibrillar collagen."
      Wall S.J., Werner E., Werb Z., DeClerck Y.A.
      J. Biol. Chem. 280:40187-40194(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS COLLAGEN RECEPTOR, PHOSPHORYLATION.
    9. "Increased expression of the collagen receptor discoidin domain receptor 2 in articular cartilage as a key event in the pathogenesis of osteoarthritis."
      Xu L., Peng H., Glasson S., Lee P.L., Hu K., Ijiri K., Olsen B.R., Goldring M.B., Li Y.
      Arthritis Rheum. 56:2663-2673(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UP-REGULATION OF MMP13, INDUCTION, TISSUE SPECIFICITY.
    10. "Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen."
      Konitsiotis A.D., Raynal N., Bihan D., Hohenester E., Farndale R.W., Leitinger B.
      J. Biol. Chem. 283:6861-6868(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS COLLAGEN RECEPTOR, SUBCELLULAR LOCATION, PHOSPHORYLATION, SUBUNIT.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Transcriptional upregulation of DDR2 by ATF4 facilitates osteoblastic differentiation through p38 MAPK-mediated Runx2 activation."
      Lin K.L., Chou C.H., Hsieh S.C., Hwa S.Y., Lee M.T., Wang F.F.
      J. Bone Miner. Res. 25:2489-2503(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION VIA ACTIVATION OF RUNX2, INDUCTION, TISSUE SPECIFICITY.
    14. "An essential role of discoidin domain receptor 2 (DDR2) in osteoblast differentiation and chondrocyte maturation via modulation of Runx2 activation."
      Zhang Y., Su J., Yu J., Bu X., Ren T., Liu X., Yao L.
      J. Bone Miner. Res. 26:604-617(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION AND CHONDROCYTE MATURATION VIA ACTIVATION OF RUNX2.
    15. "Sensing extracellular matrix: an update on discoidin domain receptor function."
      Vogel W.F., Abdulhussein R., Ford C.E.
      Cell. Signal. 18:1108-1116(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    16. Cited for: REVIEW.
    17. "Structural basis of the collagen-binding mode of discoidin domain receptor 2."
      Ichikawa O., Osawa M., Nishida N., Goshima N., Nomura N., Shimada I.
      EMBO J. 26:4168-4176(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 22-186, INTERACTION WITH COLLAGEN, DISULFIDE BONDS.
    18. "Crystallographic insight into collagen recognition by discoidin domain receptor 2."
      Carafoli F., Bihan D., Stathopoulos S., Konitsiotis A.D., Kvansakul M., Farndale R.W., Leitinger B., Hohenester E.
      Structure 17:1573-1581(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 26-190 IN COMPLEX WITH COLLAGEN PEPTIDE, DISULFIDE BONDS, MUTAGENESIS OF TRP-52, FUNCTION IN COLLAGEN BINDING, CATALYTIC ACTIVITY, PHOSPHORYLATION.
    19. "Somatic mutations of the protein kinase gene family in human lung cancer."
      Davies H., Hunter C., Smith R., Stephens P., Greenman C., Bignell G., Teague J., Butler A., Edkins S., Stevens C., Parker A., O'Meara S., Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J.
      , Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R., Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R., Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A., West S., Widaa S., Yates A., Brasseur F., Cooper C.S., Flanagan A.M., Green A., Knowles M., Leung S.Y., Looijenga L.H., Malkowicz B., Pierotti M.A., Teh B.T., Yuen S.T., Lakhani S.R., Easton D.F., Weber B.L., Goldstraw P., Nicholson A.G., Wooster R., Stratton M.R., Futreal P.A.
      Cancer Res. 65:7591-7595(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-105.
    20. "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] SER-105; ILE-441; CYS-478 AND PHE-543.
    21. Cited for: VARIANTS SEMD-SL ILE-713; ARG-726 AND CYS-752.
    22. "Trafficking defects and loss of ligand binding are the underlying causes of all reported DDR2 missense mutations found in SMED-SL patients."
      Ali B.R., Xu H., Akawi N.A., John A., Karuvantevida N.S., Langer R., Al-Gazali L., Leitinger B.
      Hum. Mol. Genet. 19:2239-2250(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SEMD-SL LYS-113, CHARACTERIZATION OF VARIANTS SEMD-SL LYS-113; ILE-713; ARG-726 AND CYS-752, MUTAGENESIS OF TRP-52, GLYCOSYLATION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiDDR2_HUMAN
    AccessioniPrimary (citable) accession number: Q16832
    Secondary accession number(s): Q7Z730
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 148 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, Reference proteome

    Documents

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

    External Data

    Dasty 3