Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Epithelial discoidin domain-containing receptor 1  

UniProtKB / Swiss-Prot ID :  DDR1_HUMAN

Gene Name (Synonyms) : 
DDR1, CAK, EDDR1, NEP, NTRK4, PTK3A, RTK6, TRKE  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Single-pass type I membrane protein. Isoform 3: Secreted (Potential). Isoform 4: Cell membrane; Single-pass type I membrane protein. 

Protein Function :  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. 

Transmembrane Topology (topPTM) : DDR1_HUMAN 

Protein Sequence MGPEALSSLLLLLLVASGDADMKGHFDPAKCRYALGMQDRTIPDSDISASSSWSDSTAARHSRLESSDGD...
Predicted Secondary Structure CCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEEEECCCCCCCCEEECCCCCC...
Protein Variant
LocationDescription
17S -> G (in dbSNP:rs55901302). VAR_041492
100V -> A (in dbSNP:rs34544756). VAR_041493
169R -> Q (in dbSNP:rs55980643). VAR_041494
170A -> D (in dbSNP:rs56231803). VAR_041495
306R -> W (in dbSNP:rs56024191). VAR_041496
496S -> A (in a lung squamous cell carcinomasample; somatic mutation).
833L -> V (in dbSNP:rs2524235). VAR_049716
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GGLGKEFSR
CCCHHHHHE
61.71Phosphositeplus
Link-
153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GVVLKDLGP
CCEECCCCC
39.02Phosphositeplus
Link-
484PhosphotyrosineEPPPYQEPR
CCCCCCCCC
31.14Phosphositeplus
Link-
513PhosphotyrosineSNPAYRLLL
CCCCCCCCC
11.75PhosphoELM
Link-
513PhosphotyrosineSNPAYRLLL
CCCCCCCCC
11.75Phosphositeplus
Link-
513Phosphotyrosine (DDR1)SNPAYRLLL
CCCCCCCCC
11.75HPRD
Link-
513Phosphotyrosine; by autocatalysis.SNPAYRLLL
CCCCCCCCC
11.75UniProtKB
Link-
520PhosphotyrosineLLATYARPP
CCCCCCCCC
8.59Phosphositeplus
Link-
631PhosphoserineCEVDSPQDL
EEECCCCCC
29.63Phosphositeplus
Link
631Phosphoserine.CEVDSPQDL
EEECCCCCC
29.63UniProtKB
Link
703PhosphotyrosineMITDYMENG
EEEEECCCC
9.55Phosphositeplus
Link
740PhosphotyrosinePTISYPMLL
CCCCHHHHH
6.71Phosphositeplus
Link
788PhosphoserineDFGMSRNLY
CCCEEEEEC
20.56PhosphoELM
Link
788PhosphoserineDFGMSRNLY
CCCEEEEEC
20.56Phosphositeplus
Link
792PhosphotyrosineSRNLYAGDY
EEEECCCCC
16.46HPRD
Link
792PhosphotyrosineSRNLYAGDY
EEEECCCCC
16.46PhosphoELM
Link
792PhosphotyrosineSRNLYAGDY
EEEECCCCC
16.46Phosphositeplus
Link
796PhosphotyrosineYAGDYYRVQ
CCCCCEEEE
7.70HPRD
Link
796PhosphotyrosineYAGDYYRVQ
CCCCCEEEE
7.70PhosphoELM
Link
796PhosphotyrosineYAGDYYRVQ
CCCCCEEEE
7.70Phosphositeplus
Link
797PhosphotyrosineAGDYYRVQG
CCCCEEEEC
14.73HPRD
Link
797PhosphotyrosineAGDYYRVQG
CCCCEEEEC
14.73PhosphoELM
Link
797PhosphotyrosineAGDYYRVQG
CCCCEEEEC
14.73Phosphositeplus
Link
869PhosphotyrosineGRQVYLSRP
CCCCCCCCC
7.22Phosphositeplus
Link
881PhosphotyrosinePQGLYELML
CHHHHHHHH
17.53Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RGS2_HUMANphysical interactionMINT-63731MINT16169070
S25BP_HUMANphysical interactionEBI-728871
intact16169070
TTHY_HUMANphysical interactionEBI-728874
intact16169070
CA165_HUMANphysical interactionEBI-736544
intact16169070
WDR57_HUMANphysical interactionEBI-734239
intact16169070
CO2A1_HUMANin vivoHPRD:02678HPRD9659900
CO3A1_HUMANin vivoHPRD:02678HPRD9659900
CO5A2_HUMANin vivoHPRD:02678HPRD9659900
COBA1_HUMANin vivoHPRD:02678HPRD9659900
PLCG1_HUMANin vitro
in vivo
HPRD:02678HPRD10783152
DDR1_HUMANin vitroHPRD:02678HPRD9659899
RGS2_HUMANyeast 2-hybridHPRD:02678HPRD16169070
S25BP_HUMANyeast 2-hybridHPRD:02678HPRD16169070
NCK2_HUMANyeast 2-hybridHPRD:02678HPRD16337946
PTN11_HUMANin vivo
yeast 2-hybrid
HPRD:02678HPRD16337946
WDR57_HUMANyeast 2-hybridHPRD:02678HPRD16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The discoidin domain receptor tyrosine kinases are activated bycollagen.";
Vogel W., Gish G.D., Alves F., Pawson T.;
Mol. Cell 1:13-23(1997).
Cited for: FUNCTION AS COLLAGEN RECEPTOR, PHOSPHORYLATION AT TYR-513, INTERACTIONWITH SHC1, AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures