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Q08345

- DDR1_HUMAN

UniProt

Q08345 - DDR1_HUMAN

Protein

Epithelial discoidin domain-containing receptor 1

Gene

DDR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing By similarity. Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11.By similarity9 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by the multi-targeted cancer drugs imatinib and ponatinib.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi211 – 2111Calcium 1; via carbonyl oxygen
    Metal bindingi230 – 2301Calcium 1
    Metal bindingi230 – 2301Calcium 2; via carbonyl oxygen
    Metal bindingi233 – 2331Calcium 2
    Metal bindingi235 – 2351Calcium 2; via carbonyl oxygen
    Metal bindingi253 – 2531Calcium 1; via carbonyl oxygen
    Metal bindingi255 – 2551Calcium 1; via carbonyl oxygen
    Metal bindingi360 – 3601Calcium 2; via carbonyl oxygen
    Metal bindingi361 – 3611Calcium 2
    Binding sitei655 – 6551ATP
    Active sitei766 – 7661Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi616 – 6249ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. branching involved in mammary gland duct morphogenesis Source: Ensembl
    2. cell adhesion Source: ProtInc
    3. collagen-activated tyrosine kinase receptor signaling pathway Source: UniProtKB
    4. ear development Source: Ensembl
    5. embryo implantation Source: Ensembl
    6. extracellular matrix organization Source: Reactome
    7. lactation Source: UniProtKB-KW
    8. mammary gland alveolus development Source: Ensembl
    9. negative regulation of cell proliferation Source: Ensembl
    10. peptidyl-tyrosine autophosphorylation Source: UniProtKB
    11. protein autophosphorylation Source: UniProtKB
    12. regulation of cell growth Source: Ensembl
    13. regulation of cell-matrix adhesion Source: Ensembl
    14. regulation of extracellular matrix disassembly Source: UniProtKB
    15. smooth muscle cell-matrix adhesion Source: UniProtKB
    16. smooth muscle cell migration Source: UniProtKB
    17. wound healing, spreading of cells Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Lactation, Pregnancy

    Keywords - Ligandi

    ATP-binding, Calcium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
    SignaLinkiQ08345.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epithelial discoidin domain-containing receptor 1 (EC:2.7.10.1)
    Short name:
    Epithelial discoidin domain receptor 1
    Alternative name(s):
    CD167 antigen-like family member A
    Cell adhesion kinase
    Discoidin receptor tyrosine kinase
    HGK2
    Mammary carcinoma kinase 10
    Short name:
    MCK-10
    Protein-tyrosine kinase 3A
    Protein-tyrosine kinase RTK-6
    TRK E
    Tyrosine kinase DDR
    Tyrosine-protein kinase CAK
    CD_antigen: CD167a
    Gene namesi
    Name:DDR1
    Synonyms:CAK, EDDR1, NEP, NTRK4, PTK3A, RTK6, TRKE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2730. DDR1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: ProtInc
    4. plasma membrane Source: Reactome
    5. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi105 – 1051R → A: Inhibits collagen-induced phosphorylation. 1 Publication
    Mutagenesisi211 – 2111N → A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. 1 Publication
    Mutagenesisi211 – 2111N → Q: Sustained phosphorylation regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. Located intracellularly and at the cell surface. Displays a reduced rate of receptor internalization, which is not altered in the presence of collagen. Able to bind collagen as wild-type. Exhibits enhanced collagen-independent receptor dimerization. Complete loss of the collagen-independent constitutive activation; when associated with A-655. 1 Publication
    Mutagenesisi213 – 2131S → A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. 1 Publication
    Mutagenesisi260 – 2601N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen. 1 Publication
    Mutagenesisi371 – 3711N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen. 1 Publication
    Mutagenesisi379 – 3791T → A: Phosphorylates in response to collagen, but at lower levels compared to wild-type. Phosphorylates in response to collagen, but at lower levels compared to wild-type; when associated with A-393. 1 Publication
    Mutagenesisi393 – 3931T → A: Phosphorylates in response to collagen, but at lower levels compared to wild-type. Phosphorylates in response to collagen, but at lower levels compared to wild-type; when associated with A-379. 1 Publication
    Mutagenesisi394 – 3941N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen. 1 Publication
    Mutagenesisi655 – 6551K → A: Loss of kinase activity. Complete loss of the collagen-independent constitutive activation; when associated with Q-211. 1 Publication
    Mutagenesisi707 – 7071G → A: Confers over 20-fold resistance to the ability of an inhibitor to inhibit autophosphorylation. 1 Publication
    Mutagenesisi740 – 7401Y → F: Abolishes interaction with PTPN11. 1 Publication

    Organism-specific databases

    PharmGKBiPA24348.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 913895Epithelial discoidin domain-containing receptor 1PRO_0000016742Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 1851 PublicationPROSITE-ProRule annotation
    Disulfide bondi74 ↔ 1771 PublicationPROSITE-ProRule annotation
    Glycosylationi211 – 2111N-linked (GlcNAc...)2 Publications
    Glycosylationi260 – 2601N-linked (GlcNAc...)2 Publications
    Disulfide bondi303 ↔ 3481 PublicationPROSITE-ProRule annotation
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi394 – 3941N-linked (GlcNAc...)Sequence Analysis
    Modified residuei484 – 4841Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei513 – 5131Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei520 – 5201Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei631 – 6311Phosphoserine1 Publication
    Modified residuei740 – 7401Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei792 – 7921Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei796 – 7961Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei797 – 7971Phosphotyrosine; by autocatalysis1 Publication

    Post-translational modificationi

    Autophosphorylated in response to fibrillar collagen binding.
    Glycosylation of Asn-211, but apparently not of Asn-260, Asn-371, or Asn-394, prevents autophosphorylation from occurring in the absence of collagen.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ08345.
    PaxDbiQ08345.
    PRIDEiQ08345.

    PTM databases

    PhosphoSiteiQ08345.

    Miscellaneous databases

    PMAP-CutDBQ2L6H3.

    Expressioni

    Tissue specificityi

    Detected in T-47D, MDA-MB-175 and HBL-100 breast carcinoma cells, A-431 epidermoid carcinoma cells, SW48 and SNU-C2B colon carcinoma cells and Hs 294T melanoma cells (at protein level). Expressed at low levels in most adult tissues and is highest in the brain, lung, placenta and kidney. Lower levels of expression are detected in melanocytes, heart, liver, skeletal muscle and pancreas. Abundant in breast carcinoma cell lines. In the colonic mucosa, expressed in epithelia but not in the connective tissue of the lamina propria. In the thyroid gland, expressed in the epithelium of the thyroid follicles. In pancreas, expressed in the islets of Langerhans cells, but not in the surrounding epithelial cells of the exocrine pancreas. In kidney, expressed in the epithelia of the distal tubules. Not expressed in connective tissue, endothelial cells, adipose tissue, muscle cells or cells of hematopoietic origin.3 Publications

    Gene expression databases

    ArrayExpressiQ08345.
    BgeeiQ08345.
    CleanExiHS_DDR1.
    GenevestigatoriQ08345.

    Organism-specific databases

    HPAiCAB010162.
    CAB025656.
    HPA057194.

    Interactioni

    Subunit structurei

    Homodimer. Interacts (via PPxY motif) with WWC1 (via WW domains) in a collagen-regulated manner. Forms a tripartite complex with WWC1 and PRKCZ, but predominantly in the absence of collagen. Interacts (tyrosine phosphorylated) with SHC1. Interacts with SRC. Interacts with MYH9. Interacts with CDH1. Interacts with PTPN11. Interacts with NCK2.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK2O436393EBI-711879,EBI-713635
    PTPN11Q061244EBI-711879,EBI-297779

    Protein-protein interaction databases

    BioGridi107234. 10 interactions.
    DIPiDIP-39698N.
    IntActiQ08345. 12 interactions.
    MINTiMINT-1383336.

    Structurei

    Secondary structure

    1
    913
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni37 – 393
    Helixi44 – 463
    Beta strandi47 – 504
    Helixi55 – 573
    Helixi59 – 613
    Turni68 – 703
    Beta strandi71 – 733
    Beta strandi87 – 10317
    Helixi107 – 1093
    Beta strandi116 – 12712
    Beta strandi129 – 1313
    Beta strandi145 – 1484
    Beta strandi151 – 16919
    Beta strandi171 – 1733
    Beta strandi178 – 1869
    Beta strandi191 – 1977
    Beta strandi204 – 2063
    Beta strandi217 – 2204
    Beta strandi223 – 2264
    Helixi230 – 2323
    Beta strandi245 – 2484
    Turni251 – 2544
    Beta strandi256 – 2594
    Helixi260 – 2623
    Beta strandi266 – 28722
    Helixi291 – 2933
    Beta strandi299 – 3068
    Beta strandi308 – 3125
    Beta strandi314 – 3163
    Beta strandi318 – 3214
    Beta strandi332 – 35120
    Beta strandi353 – 36715
    Helixi607 – 6093
    Beta strandi610 – 61910
    Beta strandi622 – 63110
    Helixi632 – 6343
    Beta strandi637 – 6393
    Beta strandi651 – 6577
    Helixi663 – 67816
    Beta strandi687 – 6915
    Beta strandi693 – 6964
    Beta strandi698 – 7025
    Helixi709 – 7146
    Helixi740 – 75920
    Helixi769 – 7713
    Beta strandi772 – 7743
    Helixi776 – 7783
    Beta strandi780 – 7823
    Helixi790 – 7956
    Beta strandi797 – 8004
    Beta strandi803 – 8053
    Helixi807 – 8093
    Helixi812 – 8176
    Helixi822 – 83716
    Turni838 – 8403
    Turni844 – 8474
    Helixi850 – 86213
    Helixi878 – 88710
    Helixi892 – 8943
    Helixi898 – 9069
    Turni907 – 9093
    Helixi910 – 9123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZOSX-ray1.92A/B601-913[»]
    4AG4X-ray2.80A29-367[»]
    4BKJX-ray1.70A/B601-913[»]
    4CKRX-ray2.20A601-913[»]
    ProteinModelPortaliQ08345.
    SMRiQ08345. Positions 30-367, 602-913.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 417397ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini439 – 913475CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei418 – 43821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 185155F5/8 type CPROSITE-ProRule annotationAdd
    BLAST
    Domaini610 – 905296Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni192 – 367176DS-like domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi481 – 4844PPxY motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi377 – 41539Gly/Pro-richAdd
    BLAST
    Compositional biasi476 – 601126Gly/Pro-richAdd
    BLAST

    Domaini

    The Gly/Pro-rich domains may be required for an unusual geometry of interaction with ligand or substrates.

    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.
    InParanoidiQ08345.
    KOiK05124.
    OMAiCRFLFAG.
    PhylomeDBiQ08345.
    TreeFamiTF317840.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR029566. DDR1.
    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:SF65. PTHR24416:SF65. 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]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q08345-1) [UniParc]FASTAAdd to Basket

    Also known as: CAK I, DDR1b

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS    50
    SSWSDSTAAR HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV 100
    GTQGRHAGGL GKEFSRSYRL RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV 150
    VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV ELYGCLWRDG LLSYTAPVGQ 200
    TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD FRKSQELRVW 250
    PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG 300
    VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF 350
    LFAGPWLLFS EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL 400
    EPRGQQPVAK AEGSPTAILI GCLVAIILLL LLIIALMLWR LHWRRLLSKA 450
    ERRVLEEELT VHLSVPGDTI LINNRPGPRE PPPYQEPRPR GNPPHSAPCV 500
    PNGSALLLSN PAYRLLLATY ARPPRGPGPP TPAWAKPTNT QAYSGDYMEP 550
    EKPGAPLLPP PPQNSVPHYA EADIVTLQGV TGGNTYAVPA LPPGAVGDGP 600
    PRVDFPRSRL RFKEKLGEGQ FGEVHLCEVD SPQDLVSLDF PLNVRKGHPL 650
    LVAVKILRPD ATKNARNDFL KEVKIMSRLK DPNIIRLLGV CVQDDPLCMI 700
    TDYMENGDLN QFLSAHQLED KAAEGAPGDG QAAQGPTISY PMLLHVAAQI 750
    ASGMRYLATL NFVHRDLATR NCLVGENFTI KIADFGMSRN LYAGDYYRVQ 800
    GRAVLPIRWM AWECILMGKF TTASDVWAFG VTLWEVLMLC RAQPFGQLTD 850
    EQVIENAGEF FRDQGRQVYL SRPPACPQGL YELMLRCWSR ESEQRPPFSQ 900
    LHRFLAEDAL NTV 913
    Length:913
    Mass (Da):101,128
    Last modified:February 1, 1995 - v1
    Checksum:iC96913EA906C481E
    GO
    Isoform 2 (identifier: Q08345-2) [UniParc]FASTAAdd to Basket

    Also known as: CAK II, DDR1a, Short

    The sequence of this isoform differs from the canonical sequence as follows:
         506-542: Missing.

    Show »
    Length:876
    Mass (Da):97,174
    Checksum:iE02881598CC7CD0B
    GO
    Isoform 3 (identifier: Q08345-4) [UniParc]FASTAAdd to Basket

    Also known as: DDR1d

    The sequence of this isoform differs from the canonical sequence as follows:
         190-243: GLLSYTAPVG...GVVGLDDFRK → CSMGVWASWQ...MWRWSLSLTG
         244-913: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:243
    Mass (Da):27,130
    Checksum:i36872B8FB29835D0
    GO
    Isoform 4 (identifier: Q08345-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         665-665: A → ASFSLFS

    Show »
    Length:919
    Mass (Da):101,796
    Checksum:i2094224F6AE943F5
    GO
    Isoform 5 (identifier: Q08345-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSLPRCCPHPLRPEGSGAM
         506-542: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:894
    Mass (Da):99,064
    Checksum:iD46EECFC939B7585
    GO

    Sequence cautioni

    The sequence BAE06103.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence ACF47649.1 differs from that shown. Reason: Erroneous termination at position 287. Translated as Cys.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941L → V in AAA02866. (PubMed:8390675)Curated
    Sequence conflicti94 – 941L → V in AAC50917. (PubMed:8977099)Curated
    Sequence conflicti165 – 1651R → H in AAH70070. (PubMed:15489334)Curated
    Sequence conflicti285 – 2862VH → MW in ACF47649. (PubMed:18593464)Curated
    Sequence conflicti741 – 7411P → Q in AAH70070. (PubMed:15489334)Curated
    Sequence conflicti847 – 86721QLTDE…DQGRQ → SAHRRAGHRERGGVLPGPGP A in CAA66871. (PubMed:8796349)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171S → G.1 Publication
    Corresponds to variant rs55901302 [ dbSNP | Ensembl ].
    VAR_041492
    Natural varianti100 – 1001V → A.1 Publication
    Corresponds to variant rs34544756 [ dbSNP | Ensembl ].
    VAR_041493
    Natural varianti169 – 1691R → Q.1 Publication
    Corresponds to variant rs55980643 [ dbSNP | Ensembl ].
    VAR_041494
    Natural varianti170 – 1701A → D.1 Publication
    Corresponds to variant rs56231803 [ dbSNP | Ensembl ].
    VAR_041495
    Natural varianti306 – 3061R → W.1 Publication
    Corresponds to variant rs56024191 [ dbSNP | Ensembl ].
    VAR_041496
    Natural varianti496 – 4961S → A in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041497
    Natural varianti833 – 8331L → V.2 Publications
    Corresponds to variant rs2524235 [ dbSNP | Ensembl ].
    VAR_049716

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MSLPRCCPHPLRPEGSGAM in isoform 5. 1 PublicationVSP_043582
    Alternative sequencei190 – 24354GLLSY…DDFRK → CSMGVWASWQMVWWGWMTLG RVRSCGSGQAMTMWDGATTA SPVAMWRWSLSLTG in isoform 3. 1 PublicationVSP_036916Add
    BLAST
    Alternative sequencei244 – 913670Missing in isoform 3. 1 PublicationVSP_036917Add
    BLAST
    Alternative sequencei506 – 54237Missing in isoform 2 and isoform 5. 7 PublicationsVSP_002953Add
    BLAST
    Alternative sequencei665 – 6651A → ASFSLFS in isoform 4. 1 PublicationVSP_038057

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74979 mRNA. Translation: CAA52915.1.
    L11315 mRNA. Translation: AAA02866.1.
    Z29093 mRNA. Translation: CAA82335.1.
    L20817 mRNA. Translation: AAA18019.1.
    U48705 Genomic DNA. Translation: AAC50917.1.
    X98208
    , X99023, X99024, X99025, X99026, X99027, X99028, X99029, X99030, X99031, X99032, X99033, X99034 Genomic DNA. Translation: CAA66871.1.
    L57508 mRNA. Translation: AAB05208.1.
    EU826613 mRNA. Translation: ACF47649.1. Sequence problems.
    EU826614 mRNA. Translation: ACF47650.1.
    AK291621 mRNA. Translation: BAF84310.1.
    AK294793 mRNA. Translation: BAH11886.1.
    AB210021 mRNA. Translation: BAE06103.1. Different initiation.
    BA000025 Genomic DNA. Translation: BAB63318.1.
    CR759747 Genomic DNA. Translation: CAQ06757.1.
    CR759747 Genomic DNA. Translation: CAQ06756.1.
    AB088102 Genomic DNA. Translation: BAC54935.1.
    AB103608 Genomic DNA. Translation: BAF31270.1.
    AL662854 Genomic DNA. Translation: CAI17434.1.
    AL662870 Genomic DNA. Translation: CAI18441.1.
    AL773541, AL773589 Genomic DNA. Translation: CAI18450.1.
    AL773589, AL773541 Genomic DNA. Translation: CAI18534.1.
    AL662854 Genomic DNA. Translation: CAI17433.1.
    AL662870 Genomic DNA. Translation: CAI18442.1.
    AL773541, AL773589 Genomic DNA. Translation: CAI18451.1.
    AL773589, AL773541 Genomic DNA. Translation: CAI18533.1.
    AB202100 Genomic DNA. Translation: BAE78621.1.
    BX927194 Genomic DNA. Translation: CAQ09768.1.
    BX927194 Genomic DNA. Translation: CAQ09767.1.
    CH471081 Genomic DNA. Translation: EAX03335.1.
    CH471081 Genomic DNA. Translation: EAX03338.1.
    BC008716 mRNA. Translation: AAH08716.1.
    BC013400 mRNA. Translation: AAH13400.1.
    BC070070 mRNA. Translation: AAH70070.1.
    CCDSiCCDS34385.1. [Q08345-1]
    CCDS4690.1. [Q08345-2]
    CCDS47396.1. [Q08345-5]
    CCDS56411.1. [Q08345-6]
    PIRiA48280.
    A49508.
    RefSeqiNP_001189450.1. NM_001202521.1.
    NP_001189451.1. NM_001202522.1.
    NP_001189452.1. NM_001202523.1. [Q08345-6]
    NP_001945.3. NM_001954.4. [Q08345-2]
    NP_054699.2. NM_013993.2. [Q08345-1]
    NP_054700.2. NM_013994.2. [Q08345-5]
    XP_005249443.1. XM_005249386.2. [Q08345-1]
    XP_005249444.1. XM_005249387.2. [Q08345-2]
    XP_005249446.1. XM_005249389.1. [Q08345-2]
    XP_005272931.1. XM_005272874.2. [Q08345-1]
    XP_005272932.1. XM_005272875.2. [Q08345-2]
    XP_005272934.1. XM_005272877.1. [Q08345-2]
    XP_005275085.1. XM_005275028.2. [Q08345-1]
    XP_005275087.1. XM_005275030.2. [Q08345-2]
    XP_005275088.1. XM_005275031.2. [Q08345-2]
    XP_005275220.1. XM_005275163.2. [Q08345-1]
    XP_005275221.1. XM_005275164.2. [Q08345-2]
    XP_005275223.1. XM_005275166.1. [Q08345-2]
    XP_005275515.1. XM_005275458.2. [Q08345-1]
    XP_005275516.1. XM_005275459.2. [Q08345-2]
    XP_005275518.1. XM_005275461.1. [Q08345-2]
    XP_006715249.1. XM_006715186.1. [Q08345-1]
    XP_006715250.1. XM_006715187.1. [Q08345-1]
    XP_006715251.1. XM_006715188.1. [Q08345-1]
    XP_006715252.1. XM_006715189.1. [Q08345-1]
    XP_006725565.1. XM_006725502.1. [Q08345-1]
    XP_006725566.1. XM_006725503.1. [Q08345-1]
    XP_006725567.1. XM_006725504.1. [Q08345-1]
    XP_006725568.1. XM_006725505.1. [Q08345-1]
    XP_006725783.1. XM_006725720.1. [Q08345-1]
    XP_006725891.1. XM_006725828.1. [Q08345-1]
    XP_006725892.1. XM_006725829.1. [Q08345-1]
    XP_006725893.1. XM_006725830.1. [Q08345-1]
    XP_006725894.1. XM_006725831.1. [Q08345-1]
    XP_006726081.1. XM_006726018.1. [Q08345-1]
    XP_006726082.1. XM_006726019.1. [Q08345-1]
    XP_006726083.1. XM_006726020.1. [Q08345-1]
    XP_006726084.1. XM_006726021.1. [Q08345-1]
    UniGeneiHs.631988.

    Genome annotation databases

    EnsembliENST00000259875; ENSP00000259875; ENSG00000137332. [Q08345-2]
    ENST00000324771; ENSP00000318217; ENSG00000204580. [Q08345-1]
    ENST00000376567; ENSP00000365751; ENSG00000204580. [Q08345-2]
    ENST00000376568; ENSP00000365752; ENSG00000204580. [Q08345-1]
    ENST00000376569; ENSP00000365753; ENSG00000204580. [Q08345-2]
    ENST00000376570; ENSP00000365754; ENSG00000204580. [Q08345-2]
    ENST00000376575; ENSP00000365759; ENSG00000204580. [Q08345-5]
    ENST00000383377; ENSP00000372868; ENSG00000137332. [Q08345-1]
    ENST00000400410; ENSP00000383261; ENSG00000137332. [Q08345-2]
    ENST00000400411; ENSP00000383262; ENSG00000137332. [Q08345-2]
    ENST00000400414; ENSP00000383265; ENSG00000137332. [Q08345-1]
    ENST00000400486; ENSP00000383334; ENSG00000215522. [Q08345-2]
    ENST00000400488; ENSP00000383336; ENSG00000215522. [Q08345-2]
    ENST00000400489; ENSP00000383337; ENSG00000215522. [Q08345-2]
    ENST00000400491; ENSP00000383338; ENSG00000215522. [Q08345-1]
    ENST00000400492; ENSP00000383339; ENSG00000215522. [Q08345-1]
    ENST00000412329; ENSP00000391805; ENSG00000230456. [Q08345-1]
    ENST00000415092; ENSP00000405540; ENSG00000230456. [Q08345-2]
    ENST00000418800; ENSP00000407699; ENSG00000204580. [Q08345-2]
    ENST00000419412; ENSP00000416183; ENSG00000234078. [Q08345-2]
    ENST00000421229; ENSP00000415730; ENSG00000234078. [Q08345-2]
    ENST00000427053; ENSP00000416145; ENSG00000230456. [Q08345-2]
    ENST00000429699; ENSP00000401397; ENSG00000234078. [Q08345-1]
    ENST00000430933; ENSP00000397769; ENSG00000234078. [Q08345-1]
    ENST00000446312; ENSP00000405998; ENSG00000204580. [Q08345-4]
    ENST00000449518; ENSP00000414285; ENSG00000230456. [Q08345-1]
    ENST00000452441; ENSP00000405039; ENSG00000204580. [Q08345-1]
    ENST00000453510; ENSP00000401208; ENSG00000230456. [Q08345-2]
    ENST00000454612; ENSP00000406091; ENSG00000204580. [Q08345-2]
    ENST00000454774; ENSP00000400393; ENSG00000234078. [Q08345-2]
    ENST00000482873; ENSP00000421978; ENSG00000204580. [Q08345-4]
    ENST00000508312; ENSP00000422442; ENSG00000204580. [Q08345-6]
    ENST00000513240; ENSP00000427552; ENSG00000204580. [Q08345-5]
    ENST00000548133; ENSP00000449611; ENSG00000230456. [Q08345-5]
    ENST00000548962; ENSP00000448115; ENSG00000230456. [Q08345-4]
    ENST00000549026; ENSP00000449238; ENSG00000215522. [Q08345-4]
    ENST00000550384; ENSP00000447474; ENSG00000234078. [Q08345-4]
    ENST00000550395; ENSP00000449255; ENSG00000215522. [Q08345-5]
    ENST00000552068; ENSP00000449190; ENSG00000234078. [Q08345-5]
    ENST00000552721; ENSP00000449307; ENSG00000137332. [Q08345-4]
    ENST00000553015; ENSP00000448377; ENSG00000137332. [Q08345-5]
    GeneIDi780.
    KEGGihsa:780.
    UCSCiuc003nrq.3. human. [Q08345-2]
    uc003nrr.3. human. [Q08345-1]
    uc003nrv.3. human. [Q08345-5]
    uc011dms.2. human. [Q08345-6]
    uc011dmu.1. human. [Q08345-4]

    Polymorphism databases

    DMDMi729008.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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
    X74979 mRNA. Translation: CAA52915.1 .
    L11315 mRNA. Translation: AAA02866.1 .
    Z29093 mRNA. Translation: CAA82335.1 .
    L20817 mRNA. Translation: AAA18019.1 .
    U48705 Genomic DNA. Translation: AAC50917.1 .
    X98208
    , X99023 , X99024 , X99025 , X99026 , X99027 , X99028 , X99029 , X99030 , X99031 , X99032 , X99033 , X99034 Genomic DNA. Translation: CAA66871.1 .
    L57508 mRNA. Translation: AAB05208.1 .
    EU826613 mRNA. Translation: ACF47649.1 . Sequence problems.
    EU826614 mRNA. Translation: ACF47650.1 .
    AK291621 mRNA. Translation: BAF84310.1 .
    AK294793 mRNA. Translation: BAH11886.1 .
    AB210021 mRNA. Translation: BAE06103.1 . Different initiation.
    BA000025 Genomic DNA. Translation: BAB63318.1 .
    CR759747 Genomic DNA. Translation: CAQ06757.1 .
    CR759747 Genomic DNA. Translation: CAQ06756.1 .
    AB088102 Genomic DNA. Translation: BAC54935.1 .
    AB103608 Genomic DNA. Translation: BAF31270.1 .
    AL662854 Genomic DNA. Translation: CAI17434.1 .
    AL662870 Genomic DNA. Translation: CAI18441.1 .
    AL773541 , AL773589 Genomic DNA. Translation: CAI18450.1 .
    AL773589 , AL773541 Genomic DNA. Translation: CAI18534.1 .
    AL662854 Genomic DNA. Translation: CAI17433.1 .
    AL662870 Genomic DNA. Translation: CAI18442.1 .
    AL773541 , AL773589 Genomic DNA. Translation: CAI18451.1 .
    AL773589 , AL773541 Genomic DNA. Translation: CAI18533.1 .
    AB202100 Genomic DNA. Translation: BAE78621.1 .
    BX927194 Genomic DNA. Translation: CAQ09768.1 .
    BX927194 Genomic DNA. Translation: CAQ09767.1 .
    CH471081 Genomic DNA. Translation: EAX03335.1 .
    CH471081 Genomic DNA. Translation: EAX03338.1 .
    BC008716 mRNA. Translation: AAH08716.1 .
    BC013400 mRNA. Translation: AAH13400.1 .
    BC070070 mRNA. Translation: AAH70070.1 .
    CCDSi CCDS34385.1. [Q08345-1 ]
    CCDS4690.1. [Q08345-2 ]
    CCDS47396.1. [Q08345-5 ]
    CCDS56411.1. [Q08345-6 ]
    PIRi A48280.
    A49508.
    RefSeqi NP_001189450.1. NM_001202521.1.
    NP_001189451.1. NM_001202522.1.
    NP_001189452.1. NM_001202523.1. [Q08345-6 ]
    NP_001945.3. NM_001954.4. [Q08345-2 ]
    NP_054699.2. NM_013993.2. [Q08345-1 ]
    NP_054700.2. NM_013994.2. [Q08345-5 ]
    XP_005249443.1. XM_005249386.2. [Q08345-1 ]
    XP_005249444.1. XM_005249387.2. [Q08345-2 ]
    XP_005249446.1. XM_005249389.1. [Q08345-2 ]
    XP_005272931.1. XM_005272874.2. [Q08345-1 ]
    XP_005272932.1. XM_005272875.2. [Q08345-2 ]
    XP_005272934.1. XM_005272877.1. [Q08345-2 ]
    XP_005275085.1. XM_005275028.2. [Q08345-1 ]
    XP_005275087.1. XM_005275030.2. [Q08345-2 ]
    XP_005275088.1. XM_005275031.2. [Q08345-2 ]
    XP_005275220.1. XM_005275163.2. [Q08345-1 ]
    XP_005275221.1. XM_005275164.2. [Q08345-2 ]
    XP_005275223.1. XM_005275166.1. [Q08345-2 ]
    XP_005275515.1. XM_005275458.2. [Q08345-1 ]
    XP_005275516.1. XM_005275459.2. [Q08345-2 ]
    XP_005275518.1. XM_005275461.1. [Q08345-2 ]
    XP_006715249.1. XM_006715186.1. [Q08345-1 ]
    XP_006715250.1. XM_006715187.1. [Q08345-1 ]
    XP_006715251.1. XM_006715188.1. [Q08345-1 ]
    XP_006715252.1. XM_006715189.1. [Q08345-1 ]
    XP_006725565.1. XM_006725502.1. [Q08345-1 ]
    XP_006725566.1. XM_006725503.1. [Q08345-1 ]
    XP_006725567.1. XM_006725504.1. [Q08345-1 ]
    XP_006725568.1. XM_006725505.1. [Q08345-1 ]
    XP_006725783.1. XM_006725720.1. [Q08345-1 ]
    XP_006725891.1. XM_006725828.1. [Q08345-1 ]
    XP_006725892.1. XM_006725829.1. [Q08345-1 ]
    XP_006725893.1. XM_006725830.1. [Q08345-1 ]
    XP_006725894.1. XM_006725831.1. [Q08345-1 ]
    XP_006726081.1. XM_006726018.1. [Q08345-1 ]
    XP_006726082.1. XM_006726019.1. [Q08345-1 ]
    XP_006726083.1. XM_006726020.1. [Q08345-1 ]
    XP_006726084.1. XM_006726021.1. [Q08345-1 ]
    UniGenei Hs.631988.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZOS X-ray 1.92 A/B 601-913 [» ]
    4AG4 X-ray 2.80 A 29-367 [» ]
    4BKJ X-ray 1.70 A/B 601-913 [» ]
    4CKR X-ray 2.20 A 601-913 [» ]
    ProteinModelPortali Q08345.
    SMRi Q08345. Positions 30-367, 602-913.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107234. 10 interactions.
    DIPi DIP-39698N.
    IntActi Q08345. 12 interactions.
    MINTi MINT-1383336.

    Chemistry

    BindingDBi Q08345.
    ChEMBLi CHEMBL5319.
    DrugBanki DB00619. Imatinib.
    GuidetoPHARMACOLOGYi 1843.

    PTM databases

    PhosphoSitei Q08345.

    Polymorphism databases

    DMDMi 729008.

    Proteomic databases

    MaxQBi Q08345.
    PaxDbi Q08345.
    PRIDEi Q08345.

    Protocols and materials databases

    DNASUi 780.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259875 ; ENSP00000259875 ; ENSG00000137332 . [Q08345-2 ]
    ENST00000324771 ; ENSP00000318217 ; ENSG00000204580 . [Q08345-1 ]
    ENST00000376567 ; ENSP00000365751 ; ENSG00000204580 . [Q08345-2 ]
    ENST00000376568 ; ENSP00000365752 ; ENSG00000204580 . [Q08345-1 ]
    ENST00000376569 ; ENSP00000365753 ; ENSG00000204580 . [Q08345-2 ]
    ENST00000376570 ; ENSP00000365754 ; ENSG00000204580 . [Q08345-2 ]
    ENST00000376575 ; ENSP00000365759 ; ENSG00000204580 . [Q08345-5 ]
    ENST00000383377 ; ENSP00000372868 ; ENSG00000137332 . [Q08345-1 ]
    ENST00000400410 ; ENSP00000383261 ; ENSG00000137332 . [Q08345-2 ]
    ENST00000400411 ; ENSP00000383262 ; ENSG00000137332 . [Q08345-2 ]
    ENST00000400414 ; ENSP00000383265 ; ENSG00000137332 . [Q08345-1 ]
    ENST00000400486 ; ENSP00000383334 ; ENSG00000215522 . [Q08345-2 ]
    ENST00000400488 ; ENSP00000383336 ; ENSG00000215522 . [Q08345-2 ]
    ENST00000400489 ; ENSP00000383337 ; ENSG00000215522 . [Q08345-2 ]
    ENST00000400491 ; ENSP00000383338 ; ENSG00000215522 . [Q08345-1 ]
    ENST00000400492 ; ENSP00000383339 ; ENSG00000215522 . [Q08345-1 ]
    ENST00000412329 ; ENSP00000391805 ; ENSG00000230456 . [Q08345-1 ]
    ENST00000415092 ; ENSP00000405540 ; ENSG00000230456 . [Q08345-2 ]
    ENST00000418800 ; ENSP00000407699 ; ENSG00000204580 . [Q08345-2 ]
    ENST00000419412 ; ENSP00000416183 ; ENSG00000234078 . [Q08345-2 ]
    ENST00000421229 ; ENSP00000415730 ; ENSG00000234078 . [Q08345-2 ]
    ENST00000427053 ; ENSP00000416145 ; ENSG00000230456 . [Q08345-2 ]
    ENST00000429699 ; ENSP00000401397 ; ENSG00000234078 . [Q08345-1 ]
    ENST00000430933 ; ENSP00000397769 ; ENSG00000234078 . [Q08345-1 ]
    ENST00000446312 ; ENSP00000405998 ; ENSG00000204580 . [Q08345-4 ]
    ENST00000449518 ; ENSP00000414285 ; ENSG00000230456 . [Q08345-1 ]
    ENST00000452441 ; ENSP00000405039 ; ENSG00000204580 . [Q08345-1 ]
    ENST00000453510 ; ENSP00000401208 ; ENSG00000230456 . [Q08345-2 ]
    ENST00000454612 ; ENSP00000406091 ; ENSG00000204580 . [Q08345-2 ]
    ENST00000454774 ; ENSP00000400393 ; ENSG00000234078 . [Q08345-2 ]
    ENST00000482873 ; ENSP00000421978 ; ENSG00000204580 . [Q08345-4 ]
    ENST00000508312 ; ENSP00000422442 ; ENSG00000204580 . [Q08345-6 ]
    ENST00000513240 ; ENSP00000427552 ; ENSG00000204580 . [Q08345-5 ]
    ENST00000548133 ; ENSP00000449611 ; ENSG00000230456 . [Q08345-5 ]
    ENST00000548962 ; ENSP00000448115 ; ENSG00000230456 . [Q08345-4 ]
    ENST00000549026 ; ENSP00000449238 ; ENSG00000215522 . [Q08345-4 ]
    ENST00000550384 ; ENSP00000447474 ; ENSG00000234078 . [Q08345-4 ]
    ENST00000550395 ; ENSP00000449255 ; ENSG00000215522 . [Q08345-5 ]
    ENST00000552068 ; ENSP00000449190 ; ENSG00000234078 . [Q08345-5 ]
    ENST00000552721 ; ENSP00000449307 ; ENSG00000137332 . [Q08345-4 ]
    ENST00000553015 ; ENSP00000448377 ; ENSG00000137332 . [Q08345-5 ]
    GeneIDi 780.
    KEGGi hsa:780.
    UCSCi uc003nrq.3. human. [Q08345-2 ]
    uc003nrr.3. human. [Q08345-1 ]
    uc003nrv.3. human. [Q08345-5 ]
    uc011dms.2. human. [Q08345-6 ]
    uc011dmu.1. human. [Q08345-4 ]

    Organism-specific databases

    CTDi 780.
    GeneCardsi GC06P030848.
    GC06Pj30838.
    GC06Pk30839.
    GC06Pl30893.
    GC06Pn30838.
    HGNCi HGNC:2730. DDR1.
    HPAi CAB010162.
    CAB025656.
    HPA057194.
    MIMi 600408. gene.
    neXtProti NX_Q08345.
    PharmGKBi PA24348.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000043102.
    HOVERGENi HBG005461.
    InParanoidi Q08345.
    KOi K05124.
    OMAi CRFLFAG.
    PhylomeDBi Q08345.
    TreeFami TF317840.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
    SignaLinki Q08345.

    Miscellaneous databases

    ChiTaRSi DDR1. human.
    GeneWikii DDR1.
    GenomeRNAii 780.
    NextBioi 3152.
    PMAP-CutDB Q2L6H3.
    PROi Q08345.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08345.
    Bgeei Q08345.
    CleanExi HS_DDR1.
    Genevestigatori Q08345.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR029566. DDR1.
    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:SF65. PTHR24416:SF65. 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. "Molecular cloning of trkE, a novel trk-related putative tyrosine kinase receptor isolated from normal human keratinocytes and widely expressed by normal human tissues."
      di Marco E., Cutuli N., Guerra L., Cancedda R., de Luca M.
      J. Biol. Chem. 268:24290-24295(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain and Keratinocyte.
    2. "A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain."
      Johnson J.D., Edman J.C., Rutter W.J.
      Proc. Natl. Acad. Sci. U.S.A. 90:5677-5681(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-833.
      Tissue: Placenta.
    3. "Isolation and characterization of an epithelial-specific receptor tyrosine kinase from an ovarian cancer cell line."
      Laval S., Butler R., Shelling A.N., Hanby A.M., Poulsom R., Ganesan T.S.
      Cell Growth Differ. 5:1173-1183(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Ovary.
    4. "Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain."
      Perez J.L., Shen X., Finkernagel S., Sciorra L., Jenkins N.A., Gilbert D.J., Copeland N.G., Wong T.W.
      Oncogene 9:211-219(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal liver.
    5. "Receptor protein tyrosine kinase DDR is up-regulated by p53 protein."
      Sakuma S., Tada M., Saya H., Sawamura Y., Shinohe Y., Abe H.
      FEBS Lett. 398:165-169(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-833.
    6. "The genomic structure of discoidin receptor tyrosine kinase."
      Playford M.P., Butler R.J., Wang X.C., Katso R.M., Cooke I.E., Ganesan T.S.
      Genome Res. 6:620-627(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Identification of two isoforms of the Cak receptor kinase that are coexpressed in breast tumor cell lines."
      Perez J.L., Jing S.Q., Wong T.W.
      Oncogene 12:1469-1477(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Lung.
    8. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
      Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
      Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-286 (ISOFORMS 1/2/4).
    9. "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] (ISOFORMS 2 AND 5).
      Tissue: Brain and Placenta.
    10. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
      Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    11. "Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity."
      Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.
      , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S.
      Genetics 173:1555-1570(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Tissue: Peripheral blood leukocyte.
    12. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    14. "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] (ISOFORM 2).
      Tissue: Brain and Muscle.
    15. "Glycosylation at Asn211 regulates the activation state of the discoidin domain receptor 1 (DDR1)."
      Fu H.L., Valiathan R.R., Payne L., Kumarasiri M., Mahasenan K.V., Mobashery S., Huang P., Fridman R.
      J. Biol. Chem. 289:9275-9287(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 480-490; 515-525 AND 790-798, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-484; TYR-513; TYR-520; TYR-792; TYR-796 AND TYR-797, GLYCOSYLATION AT ASN-211 AND ASN-260, MUTAGENESIS OF ARG-105; ASN-211; SER-213; ASN-260; ASN-371; THR-379; THR-393; ASN-394 AND LYS-655.
    16. "Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer."
      Alves F., Vogel W., Mossie K., Millauer B., Hoefler H., Ullrich A.
      Oncogene 10:609-618(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-550 (ISOFORMS 1/4), NUCLEOTIDE SEQUENCE [MRNA] OF 501-550 AND 651-694 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 651-694 (ISOFORM 4), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
      Tissue: Mammary carcinoma.
    17. "Expression of growth factor receptors, the focal adhesion kinase, and other tyrosine kinases in human soft tissue tumors."
      Weiner T.M., Liu E.T., Craven R.J., Cance W.G.
      Ann. Surg. Oncol. 1:18-27(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 771-824 (ISOFORMS 1/2/4).
    18. "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
      Lee S.-T., Strunk K.M., Spritz R.A.
      Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 772-823 (ISOFORMS 1/2/4), TISSUE SPECIFICITY.
      Tissue: Melanocyte.
    19. "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, PHOSPHORYLATION AT TYR-513, INTERACTION WITH SHC1, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION.
    20. "Tyrosine kinase activity of discoidin domain receptor 1 is necessary for smooth muscle cell migration and matrix metalloproteinase expression."
      Hou G., Vogel W.F., Bendeck M.P.
      Circ. Res. 90:1147-1149(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Pinpointing phosphotyrosine-dependent interactions downstream of the collagen receptor DDR1."
      Koo D.H., McFadden C., Huang Y., Abdulhussein R., Friese-Hamim M., Vogel W.F.
      FEBS Lett. 580:15-22(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTPN11 AND NCK2, PHOSPHORYLATION AT TYR-740, MUTAGENESIS OF TYR-740.
    22. "Discoidin domain receptor-1a (DDR1a) promotes glioma cell invasion and adhesion in association with matrix metalloproteinase-2."
      Ram R., Lorente G., Nikolich K., Urfer R., Foehr E., Nagavarapu U.
      J. Neurooncol. 76:239-248(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling."
      Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W., Daly R.J., Ormandy C.J.
      Biochim. Biophys. Acta 1783:383-393(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WWC1 AND PRKCZ.
    24. "The collagen receptor DDR1 regulates cell spreading and motility by associating with myosin IIA."
      Huang Y., Arora P., McCulloch C.A., Vogel W.F.
      J. Cell Sci. 122:1637-1646(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH MYH9.
    25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "DDR1 regulates the stabilization of cell surface E-cadherin and E-cadherin-mediated cell aggregation."
      Eswaramoorthy R., Wang C.K., Chen W.C., Tang M.J., Ho M.L., Hwang C.C., Wang H.M., Wang C.Z.
      J. Cell. Physiol. 224:387-397(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDH1.
    27. "Collagen stimulates discoidin domain receptor 1-mediated migration of smooth muscle cells through Src."
      Lu K.K., Trcka D., Bendeck M.P.
      Cardiovasc. Pathol. 20:71-76(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SRC.
    28. "Discoidin domain receptor 1 regulates bronchial epithelial repair and matrix metalloproteinase production."
      Roberts M.E., Magowan L., Hall I.P., Johnson S.R.
      Eur. Respir. J. 37:1482-1493(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "Collagen binding specificity of the discoidin domain receptors: binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1."
      Xu H., Raynal N., Stathopoulos S., Myllyharju J., Farndale R.W., Leitinger B.
      Matrix Biol. 30:16-26(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS COLLAGEN RECEPTOR, AUTOPHOSPHORYLATION.
    30. "Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory Fab fragment reveals features important for signaling."
      Carafoli F., Mayer M.C., Shiraishi K., Pecheva M.A., Chan L.Y., Nan R., Leitinger B., Hohenester E.
      Structure 20:688-697(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 29-367 IN COMPLEX WITH INHIBITORY ANTIBODY, SUBUNIT, CALCIUM-BINDING SITES, GLYCOSYLATION AT ASN-211 AND ASN-260, DISULFIDE BONDS.
    31. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 601-913 IN COMPLEX WITH INHIBITOR, AUTOPHOSPHORYLATION, MUTAGENESIS OF GLY-707.
    32. "Structural mechanisms determining inhibition of the collagen receptor DDR1 by selective and multi-targeted type II kinase inhibitors."
      Canning P., Tan L., Chu K., Lee S.W., Gray N.S., Bullock A.N.
      J. Mol. Biol. 426:2457-2470(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 601-913 IN COMPLEXES WITH INHIBITORS IMATINIB AND PONATINIB, ENZYME REGULATION, AUTOPHOSPHORYLATION.
    33. "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] GLY-17; ALA-100; GLN-169; ASP-170; TRP-306 AND ALA-496.

    Entry informationi

    Entry nameiDDR1_HUMAN
    AccessioniPrimary (citable) accession number: Q08345
    Secondary accession number(s): B5A975
    , B5A976, B7Z2K0, Q14196, Q16562, Q2L6H3, Q4LE50, Q5ST11, Q5ST12, Q6NSK4, Q9UD35, Q9UD36, Q9UD37, Q9UD86, Q9UDL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 167 of the entry and version 1 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 cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 6
      Human chromosome 6: 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