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DDR1 (discoidin domain receptor tyrosine kinase 1)

Identity

Other namesCAK
CD167
DDR
EDDR1
HGK2
MCK10
NEP
NTRK4
PTK3
PTK3A
RTK6
TRKE
HGNC (Hugo) DDR1
LocusID (NCBI) 780
Location 6p21.33
Location_base_pair Starts at 30856465 and ends at 30867933 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

 
  Genomic organisation of the DDR1 gene on chromosome 6. Exons that are implicated in the alternative splicing process of the DDR1 gene are represented by open boxes. The alternative splicing process of exon 10 to exon 14 generates 5 DDR1 isoforms, which are affixed a-e.
Description The DDR1 gene comprises 17 exons and spans 12 kb of the genomic sequence on chromosome 6 (from position 30851861 bp to 30867933 bp in the positive strand orientation).
Transcription The 3840-bp mRNA is transcribed in a centromeric to telomeric orientation. Alternative splicing can occur, and 5 named isoforms (DDR1a-e) are recognised.
Pseudogene No pseudogene has been described.

Protein

 
  Schematic diagram of the DDR1 protein and localization of the DDR1 Tyrosine phosphorylated sites at intracellular domain.
Description DDR1 belongs to the DDRs subfamily of tyrosine kinase receptors. This subfamily is composed of only two members, DDR1 and DDR2, and it is distinguished by an extracellular domain that is homologous to the carbohydrate-binding lectin discoidin-I in Dictyostelium discoideum. The Discoidin domain is essential for the ability of DDRs to bind ligands. To-date, collagen is the only unique DDR1 ligand that has been identified. Five isoforms of DDR1 that are generated by alternative splicing have been described. The longest DDR1 transcript codes for the full-length receptor (DDR1c isoform) and is composed of 919 amino acids. DDR1a and DDR1b isoforms lack 37 amino acids in the juxtamembrane domain or 6 amino acids in the kinase domain. DDR1d and DDR1e isoforms are C-terminally truncated receptors. DDR1d lacks exons 11 and 12 causing a frame-shift mutation that generates a stop codon and premature termination of transcription. Finally, DDR1e lacks exons 11 and 12 as well as the first half of exon 10 (Alves et al., 1995).
Expression DDR1 is ubiquitously expressed in a variety of epithelial tissues (Alves et al., 1995; Curat and Vogel, 2002; Ferri et al., 2004; Hou et al., 2001; Mohan et al., 2001; Sakamoto et al., 2001; Tanaka et al., 1998). DDR1 is also expressed in endothelial blood capillary cells and oligodendrocytes in the human brain (Franco-Pons et al., 2009; Roig et al., 2010). DDR1 is significantly overexpressed in several human cancers (Barker et al., 1995; Colas et al., 2011; Ford et al., 2007; Hajdu et al., 2010; Heinzelmann-Schwarz et al., 2004; Laval et al., 1994; Nemoto et al., 1997; Park et al., 2007; Tun et al., 2011; Weiner et al., 1996; Weiner et al., 2000; Yamanaka et al., 2006; Yoshida et al., 2007) and carcinoma cell lines (Alves et al., 1995; Gu et al., 2011; Park et al., 2007; Sakuma et al., 1996).
Localisation Transmembrane.
Function Receptor tyrosine kinases are key components of several signal transduction pathways. These kinases control multiple cellular processes, including motility, proliferation, differentiation, metabolism and survival.
DDR1 is actively involved in tumorigenesis and promotes the proliferation of neoplasic cells. The interaction of DDR1 and Notch1 displays a prosurvival effect (Kim et al., 2011). DDR1 participates in the collective migration of cancer cells by coordinating the cell polarity regulators Par3 and Par6 (Hidalgo-Carcedo et al., 2011).
Homology - P. troglodytes, discoidin domain receptor tyrosine kinase 1, DDR1
- C. lupus, discoidin domain receptor tyrosine kinase 1, DDR1
- M. musculus, discoidin domain receptor family member 1, Ddr1
- R. norvegicus, discoidin domain receptor tyrosine kinase 1

Mutations

Note Few somatic mutations have been described. Four mutations (G1486T, A496S, CC2469/2470TT, R824W) have been identified in a cohort of 26 primary lung neoplasms (Davies et al., 2005). One somatic mutation (A803V) was found in 4 acute myeloid leukaemia patients (Tomasson et al., 2008).
 

Implicated in

Entity Breast cancer
Note DDR1 overexpression was observed in human primary breast tumours samples compared to that in normal breast tissues (Barker et al., 1995). In addition, invasive ductal and lobular carcinomas showed differential expression of DDR1. DDR1 was downregulated in lobular carcinomas (Turashvili et al., 2007a; Turashvili et al., 2007b).
  
Entity Osteosarcoma
Note The DDR1 promoter presents a potential p53 binding-site. A previous study has shown that p53 expression upregulated the mRNA expression levels of DDR1 in human osteosarcoma cells (Sakuma et al., 1996).
  
Entity Oesophageal cancer
Note The overexpression of DDR1 was reported in 12 carcinomatous oesophageal tissues compared to that in normal tissues. Furthermore, a positive correlation was identified between DDR1 mRNA expression and the proliferative activity of the tumoural cells (Nemoto et al., 1997).
  
Entity Ovarian cancer
Note DDR1 was highly expressed in 158 histological subtypes of primary epithelial ovarian cancers (EOC) compared to that in normal ovarian surface epithelium samples (Heinzelmann-Schwarz et al., 2004).
  
Entity Endometrial cancer
Note DDR1 has been implicated as a potential molecular marker of endometrial cancer (Colas et al., 2011; Domenyuk et al., 2007). A gene expression screening of 52 carcinomas samples showed differential expression of several genes, including the DDR1 gene. These data were also demonstrated in 50 tumoural and non-tumoural uterine aspirates (Colas et al., 2011).
  
Entity Brain tumours
Note DDR1 was originally isolated in malignant childhood brain tumours, which overexpressed DDR1 (Weiner et al., 1996). Replicable findings were found in metastatic brain neoplasms and glioma cells (Yamanaka et al., 2006; Weiner et al., 2000). In glioma cells, DDR1 was involved in cell proliferation and invasion via cell interactions with the extracellular matrix (Ram et al., 2005; Yamanaka et al., 2006). Moreover, a study on DDR1a and DDR1b isoforms overexpression in glioma cells has identified distinct roles for each DDR1 isoforms in the cell attachment process, which is mediated by collagen I (Ram et al., 2005). The analysis of the expression profile in mice that had PDGF-induced glioma showed overexpression of DDR1 (Johansson et al., 2005).
  
Entity Primary central nervous system lymphoma (PCNSL)
Note A PCNSL pathway analysis revealed upregulation of DDR1 expression in the extracellular matrix and the adhesion-related pathways (Tun et al., 2011).
  
Entity Pituitary adenoma
Note In different subtypes of pituitary adenoma, DDR1 expression was related to the hormonal background. DDR1 was more highly expressed in macroadenomas, compared to microadenomas, and in PRL- and GH-producing adenomas (Yoshida et al., 2007).
  
Entity Lung cancer
Note DDR1 was upregulated in tumour lung tissue compared to that in normal tissue and was an independent favourable predictor for prognosis (Ford et al., 2007). Similarly, DDR1 was highly phosphorylated in non-small cell lung cancer (NSCLC) (Rikova et al., 2007).
One study described the presence of DDR1 somatic mutations in lung cancer (Davies et al., 2005). However, no mutations were detected in another lung cancer study (Ford et al., 2007).
  
Entity Liver cancer
Note DDR1a and DDR1b isoforms were overexpressed in hepatocellular carcinoma cell lines HLE and Huh-7. DDR1 isoform overexpression enhanced the migration and invasion of the hepatocellular carcinoma cell lines in association with the matrix metalloproteinases MMP2 and MMP9 (Park et al., 2007).
The downregulation of miR-199a-5p, which is a direct target of DDR1, deregulated DDR1 functionality and increased cell invasion in human hepatocellular carcinoma (HCC) (Shen et al., 2010).
Finally, a profiling study on receptor tyrosine kinase phosphorylation in cholangiocarcinoma patients showed high levels of phosphorylation of DDR1 and other tyrosine kinases in tumour tissues in comparison to para-tumour tissues (Gu et al., 2011).
  
Entity Mesenchymal neoplasm
Note Solitary fibrous tumour (SFT) expression profiling of 23 samples showed an over-expression of several receptor tyrosine kinase genes, including DDR1. However, no mutations were identified using cDNA sequencing (Hajdu et al., 2010).
  

External links

Nomenclature
HGNC (Hugo)DDR1   2730
Cards
AtlasDDR1ID40280ch6p21
Entrez_Gene (NCBI)DDR1  780  discoidin domain receptor tyrosine kinase 1
GeneCards (Weizmann)DDR1
Ensembl (Hinxton)ENSG00000204580 [Gene_View]  chr6:30856465-30867933 [Contig_View]  DDR1 [Vega]
AceView (NCBI)DDR1
Genatlas (Paris)DDR1
WikiGenes780
SOURCE (Princeton)NM_001202521 NM_001202522 NM_001202523 NM_001954 NM_013993 NM_013994
Genomic and cartography
GoldenPath (UCSC)DDR1  -  6p21.33   chr6:30856465-30867933 +  6p21.33   [Description]    (hg19-Feb_2009)
EnsemblDDR1 - 6p21.33 [CytoView]
Mapping of homologs : NCBIDDR1 [Mapview]
OMIM600408   
Gene and transcription
Genbank (Entrez)AB210021 AF353182 AF353183 AK130776 AK291621
RefSeq transcript (Entrez)NM_001202521 NM_001202522 NM_001202523 NM_001954 NM_013993 NM_013994
RefSeq genomic (Entrez)AC_000138 NC_000006 NC_018917 NG_029066 NT_007592 NT_113891 NT_167244 NT_167245 NT_167246 NT_167247 NT_167248 NW_001838980 NW_004929326
Consensus coding sequences : CCDS (NCBI)DDR1
Cluster EST : UnigeneHs.631988 [ NCBI ]
CGAP (NCI)Hs.631988
Alternative Splicing : Fast-db (Paris)GSHG0025588
Alternative Splicing GalleryENSG00000204580
Gene ExpressionDDR1 [ NCBI-GEO ]     DDR1 [ SEEK ]   DDR1 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ08345 (Uniprot)
NextProtQ08345  [Medical]
With graphics : InterProQ08345
Splice isoforms : SwissVarQ08345 (Swissvar)
Catalytic activity : Enzyme2.7.10.1 [ Enzyme-Expasy ]   2.7.10.12.7.10.1 [ IntEnz-EBI ]   2.7.10.1 [ BRENDA ]   2.7.10.1 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)FA58C_1 (PS01285)    FA58C_2 (PS01286)    FA58C_3 (PS50022)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_TYR (PS00109)    RECEPTOR_TYR_KIN_II (PS00239)   
Domains : Interpro (EBI)Coagulation_fac_5/8-C_type_dom    Galactose-bd-like    Kinase-like_dom    Prot_kinase_dom    Ser-Thr/Tyr_kinase_cat_dom    Tyr_kinase_AS    Tyr_kinase_cat_dom    Tyr_kinase_rcpt_2_CS   
Related proteins : CluSTrQ08345
Domain families : Pfam (Sanger)F5_F8_type_C (PF00754)    Pkinase_Tyr (PF07714)   
Domain families : Pfam (NCBI)pfam00754    pfam07714   
Domain families : Smart (EMBL)FA58C (SM00231)  TyrKc (SM00219)  
DMDM Disease mutations780
Blocks (Seattle)Q08345
PDB (SRS)3ZOS    4AG4    4BKJ   
PDB (PDBSum)3ZOS    4AG4    4BKJ   
PDB (IMB)3ZOS    4AG4    4BKJ   
PDB (RSDB)3ZOS    4AG4    4BKJ   
Human Protein AtlasENSG00000204580
Peptide AtlasQ08345
HPRD02678
IPIIPI00001477   IPI00219996   IPI00910318   IPI00657861   IPI00922197   IPI01020875   IPI00747286   IPI00964061   IPI00985399   IPI01009821   IPI00968184   IPI00964288   IPI01013376   IPI00796394   IPI00789128   IPI00789817   IPI00790169   IPI00790861   IPI01011183   IPI00966862   IPI00965006   IPI00964969   IPI00967680   IPI00966760   IPI00967143   IPI00966308   IPI00967668   IPI00965307   IPI01010088   IPI00965787   IPI00967954   IPI00966591   IPI00965287   IPI00965766   IPI01013844   IPI00967386   IPI00964238   IPI00954432   IPI00965545   IPI00968231   IPI00965809   IPI00966153   IPI00966799   
Protein Interaction databases
DIP (DOE-UCLA)Q08345
IntAct (EBI)Q08345
FunCoupENSG00000204580
BioGRIDDDR1
InParanoidQ08345
Interologous Interaction database Q08345
IntegromeDBDDR1
STRING (EMBL)DDR1
Ontologies - Pathways
Ontology : AmiGOregulation of cell growth  regulation of cell-matrix adhesion  transmembrane receptor protein tyrosine kinase activity  protein binding  collagen binding  collagen binding  ATP binding  extracellular region  plasma membrane  integral to plasma membrane  cell adhesion  embryo implantation  lactation  negative regulation of cell proliferation  regulation of extracellular matrix disassembly  smooth muscle cell migration  extracellular matrix organization  protein tyrosine kinase collagen receptor activity  collagen-activated tyrosine kinase receptor signaling pathway  collagen-activated tyrosine kinase receptor signaling pathway  peptidyl-tyrosine autophosphorylation  ear development  wound healing, spreading of cells  protein autophosphorylation  metal ion binding  branching involved in mammary gland duct morphogenesis  mammary gland alveolus development  smooth muscle cell-matrix adhesion  
Ontology : EGO-EBIregulation of cell growth  regulation of cell-matrix adhesion  transmembrane receptor protein tyrosine kinase activity  protein binding  collagen binding  collagen binding  ATP binding  extracellular region  plasma membrane  integral to plasma membrane  cell adhesion  embryo implantation  lactation  negative regulation of cell proliferation  regulation of extracellular matrix disassembly  smooth muscle cell migration  extracellular matrix organization  protein tyrosine kinase collagen receptor activity  collagen-activated tyrosine kinase receptor signaling pathway  collagen-activated tyrosine kinase receptor signaling pathway  peptidyl-tyrosine autophosphorylation  ear development  wound healing, spreading of cells  protein autophosphorylation  metal ion binding  branching involved in mammary gland duct morphogenesis  mammary gland alveolus development  smooth muscle cell-matrix adhesion  
REACTOMEDDR1
Protein Interaction DatabaseDDR1
Wikipedia pathwaysDDR1
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)DDR1
SNP (GeneSNP Utah)DDR1
SNP : HGBaseDDR1
Genetic variants : HAPMAPDDR1
1000_GenomesDDR1 
ICGC programENSG00000204580 
Somatic Mutations in Cancer : COSMICDDR1 
CONAN: Copy Number AnalysisDDR1 
Mutations and Diseases : HGMDDDR1
OMIM600408   
GENETestsDDR1
Disease Genetic AssociationDDR1
Huge Navigator DDR1 [HugePedia]  DDR1 [HugeCancerGEM]
Genomic VariantsDDR1  DDR1 [DGVbeta]
Exome VariantDDR1
dbVarDDR1
ClinVarDDR1
snp3D : Map Gene to Disease780
General knowledge
Homologs : HomoloGeneDDR1
Homology/Alignments : Family Browser (UCSC)DDR1
Phylogenetic Trees/Animal Genes : TreeFamDDR1
Chemical/Protein Interactions : CTD780
Chemical/Pharm GKB GenePA24348
Clinical trialDDR1
Cancer Resource (Charite)ENSG00000204580
Other databases
Probes
Litterature
PubMed104 Pubmed reference(s) in Entrez
CoreMineDDR1
iHOPDDR1

Bibliography

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PMID 8622863
 
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Overexpression of protein tyrosine kinases in human esophageal cancer.
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PMID 11126911
 
Identification of two novel, kinase-deficient variants of discoidin domain receptor 1: differential expression in human colon cancer cell lines.
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Am J Pathol. 2004 May;164(5):1575-85.
PMID 15111304
 
Overexpression of the cell adhesion molecules DDR1, Claudin 3, and Ep-CAM in metaplastic ovarian epithelium and ovarian cancer.
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Somatic mutations of the protein kinase gene family in human lung cancer.
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Expression analysis of genes involved in brain tumor progression driven by retroviral insertional mutagenesis in mice.
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PMID 15750623
 
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Identification of expressed genes characterizing long-term survival in malignant glioma patients.
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PMID 17001518
 
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Discoidin domain receptor 1, a tyrosine kinase receptor, is upregulated in an experimental model of remyelination and during oligodendrocyte differentiation in vitro.
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IGF2 over-expression in solitary fibrous tumours is independent of anatomical location and is related to loss of imprinting.
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PMID 20527023
 
Role of microRNA-199a-5p and discoidin domain receptor 1 in human hepatocellular carcinoma invasion.
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Mol Cancer. 2010 Aug 27;9:227.
PMID 20799954
 
Molecular markers of endometrial carcinoma detected in uterine aspirates.
Colas E, Perez C, Cabrera S, Pedrola N, Monge M, Castellvi J, Eyzaguirre F, Gregorio J, Ruiz A, Llaurado M, Rigau M, Garcia M, Ertekin T, Montes M, Lopez-Lopez R, Carreras R, Xercavins J, Ortega A, Maes T, Rosell E, Doll A, Abal M, Reventos J, Gil-Moreno A.
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PMID 21207424
 
Survey of tyrosine kinase signaling reveals ROS kinase fusions in human cholangiocarcinoma.
Gu TL, Deng X, Huang F, Tucker M, Crosby K, Rimkunas V, Wang Y, Deng G, Zhu L, Tan Z, Hu Y, Wu C, Nardone J, MacNeill J, Ren J, Reeves C, Innocenti G, Norris B, Yuan J, Yu J, Haack H, Shen B, Peng C, Li H, Zhou X, Liu X, Rush J, Comb MJ.
PLoS One. 2011 Jan 6;6(1):e15640.
PMID 21253578
 
Collective cell migration requires suppression of actomyosin at cell-cell contacts mediated by DDR1 and the cell polarity regulators Par3 and Par6.
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Nat Cell Biol. 2011 Jan;13(1):49-58. Epub 2010 Dec 19.
PMID 21170030
 
DDR1 receptor tyrosine kinase promotes prosurvival pathway through Notch1 activation.
Kim HG, Hwang SY, Aaronson SA, Mandinova A, Lee SW.
J Biol Chem. 2011 May 20;286(20):17672-81. Epub 2011 Mar 13.
PMID 21398698
 
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Contributor(s)

Written05-2011Barbara Roig, Elisabet Vilella
Hospital Psiquiatic Universitari Institut Pere Mata, IISPV, Universitat Rovira i Virgili, C/Sant Llorenc 21, 43201 REUS, Spain

Citation

This paper should be referenced as such :
Roig B, Vilella E . DDR1 (discoidin domain receptor tyrosine kinase 1). Atlas Genet Cytogenet Oncol Haematol. May 2011 .
URL : http://AtlasGeneticsOncology.org/Genes/DDR1ID40280ch6p21.html

The various updated versions of this paper are referenced and archived by INIST as such :
http://documents.irevues.inist.fr/bitstream/handle/2042/46052/05-2011-DDR1ID40280ch6p21.pdf   [ Bibliographic record ]

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