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Details on Person UniProt:Q16832 DDR2
| Class:Id | ReferenceGeneProduct:53502 |
|---|---|
| _chainChangeLog | signal peptide:1-21 added on Sat February 7 2015;chain:22-855 added on Sat February 7 2015 |
| _displayName | UniProt:Q16832 DDR2 |
| _timestamp | 2025-02-21 19:26:57 |
| chain | signal peptide:1-21 chain:22-855 |
| checksum | 78662021BC53E1A0 |
| comment | FUNCTION Tyrosine kinase involved in the regulation of tissues remodeling (PubMed:30449416). It functions as a 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.CATALYTIC ACTIVITY L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)ACTIVITY REGULATION 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.SUBUNIT 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.INTERACTION 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.INDUCTION Up-regulated during osteoblast differentiation (in vitro). Up-regulated in cartilage from osteoarthritis patients.PTM N-glycosylated.PTM Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. |
| description | recommendedName: Discoidin domain-containing receptor 2 shortName: Discoidin domain receptor 2 ecNumber: 2.7.10.1 alternativeName: CD167 antigen-like family member B alternativeName: Discoidin domain-containing receptor tyrosine kinase 2 alternativeName: Neurotrophic tyrosine kinase, receptor-related 3 alternativeName: Receptor protein-tyrosine kinase TKT alternativeName: Tyrosine-protein kinase TYRO10 cdAntigenNameCD167b/cdAntigenName |
| geneName | DDR2 NTRKR3 TKT TYRO10 |
| identifier | Q16832 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure ATP-binding Cell membrane Disease variant Disulfide bond Dwarfism Glycoprotein Kinase Membrane Nucleotide-binding Osteogenesis Phosphoprotein Proteomics identification Receptor Reference proteome Signal Transferase Transmembrane Transmembrane helix Tyrosine-protein kinase |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | DDR2 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8960118] ENSEMBL:ENSG00000162733 DDR2 [Homo sapiens] |
| secondaryIdentifier | DDR2_HUMAN Q7Z730 |
| sequenceLength | 855 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:211419] DDR2 [plasma membrane] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:Q16832 DDR2 (53502)
