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Protein Page:
DDR2 (human)

Overview
DDR2 This tyrosine kinase receptor for fibrillar collagen mediates fibroblast migration and proliferation. Contributes to cutaneous wound healing. Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, tyrosine (receptor); EC 2.7.10.1; Membrane protein, integral; Protein kinase, TK; Kinase, protein; EC 2.7.1.112; TK group; DDR family
Cellular Component: integral to plasma membrane; apical plasma membrane; plasma membrane
Molecular Function: collagen binding; protein binding; transmembrane receptor protein tyrosine kinase activity; ATP binding
Biological Process: ossification; extracellular matrix organization and biogenesis; collagen fibril organization; peptidyl-tyrosine phosphorylation; protein amino acid autophosphorylation; signal transduction; positive regulation of osteoblast differentiation; positive regulation of fibroblast proliferation; biomineral formation; positive regulation of protein kinase activity; positive regulation of transcription factor activity; cell adhesion; regulation of bone mineralization
Reference #:  Q16832 (UniProtKB)
Alt. Names/Synonyms: CD167 antigen-like family member B; cell migration-inducing protein 20; DDR2; Discoidin domain receptor 2; discoidin domain receptor family, member 2; discoidin domain receptor tyrosine kinase 2; Discoidin domain-containing receptor 2; MIG20a; migration-inducing gene 16 protein; neurotrophic tyrosine kinase receptor related 3; Neurotrophic tyrosine kinase, receptor-related 3; NTRKR3; Receptor protein-tyrosine kinase TKT; TKT; TYRO10; Tyrosine-protein kinase TYRO10
Gene Symbols: DDR2
Molecular weight: 96,736 Da
Basal Isoelectric point: 5.2  Predict pI for various phosphorylation states
CST Pathways:  Tyrosine Kinases & Substrates
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DDR2

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: Y471‑p
phosphorylation: Y736‑p, Y740‑p, Y741‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 2 S459-p SMFNNNRsSsPSEQG
0 3 S461-p FNNNRsSsPSEQGSN
1 8 Y471-p EQGSNSTyDRIFPLR
0 97 Y481-p IFPLRPDyQEPsRLI
0 2 S485-p RPDyQEPsRLIRKLP
0 1 S501 FAPGEEESGCSGVVK
0 5 Y521 GPEGVPHYAEADIVN
0 1 S675-p RHEPPNSsSSDVRTV
1 435 Y736-p FGMSRNLysGDyyRI
0 11 S737-p GMSRNLysGDyyRIQ
1 392 Y740-p RNLysGDyyRIQGRA
1 24 Y741-p NLysGDyyRIQGRAV
  DDR2 iso3  
S69 SMFNNNRSSSPSEQG
S71 FNNNRSSSPSEQGSN
Y81 EQGSNSTYDRIFPLR
Y91 IFPLRPDYQEPSRLI
S95 RPDYQEPSRLIRKLP
S111-p FAPGEEEsGEDDVVG
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

 
S459-p SMFNNNRsSsPSEQE
S461-p FNNNRsSsPSEQESN
Y471-p EQESNSTyDRIFPLR
Y481-p IFPLRPDyQEPSRLI
S485 RPDyQEPSRLIRKLP
S501 FAPGEEESGCSGVVK
Y521-p GPEGVPHyAEADIVN
S674 SRHEPLSSCSSDATV
Y735-p FGMSRNLysGDyyRI
S736-p GMSRNLysGDyyRIQ
Y739-p RNLysGDyyRIQGRA
Y740-p NLysGDyyRIQGRAV
  rat

 
S459 SMFNNNHSSSPSEQE
S461 FNNNHSSSPSEQESN
Y471 EQESNSTYDRIFPLR
Y481 IFPLRPDYQEPSRLI
S485 RPDYQEPSRLIRKLP
S501 FAPGEEESGCSGVVK
Y521 GPEGVPHYAEADIVN
S674 SRHEPLSSGSSNATV
Y735-p FGMSRNLySGDyYRI
S736 GMSRNLySGDyYRIQ
Y739-p RNLySGDyYRIQGRA
Y740 NLySGDyYRIQGRAV
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