DDR2
entrez
4921
canonical
uniprot
Q16832
canonical
ensembl
ENSG00000162733
resolver
ensp
ENSP00000356898
resolver
ensp
ENSP00000356899
resolver
ensp
ENSP00000400309
resolver
ensp
ENSP00000547219
resolver
ensp
ENSP00000547220
resolver
ensp
ENSP00000547221
resolver
ensp
ENSP00000547222
resolver
ensp
ENSP00000547223
resolver
ensp
ENSP00000547225
resolver
ensp
ENSP00000547226
resolver
ensp
ENSP00000547228
resolver
ensp
ENSP00000547229
resolver
ensp
ENSP00000547230
resolver
ensp
ENSP00000636553
resolver
ensp
ENSP00000636554
resolver
ensp
ENSP00000795827
resolver
enst
ENST00000367921
resolver
enst
ENST00000367922
resolver
enst
ENST00000446985
resolver
enst
ENST00000877160
resolver
enst
ENST00000877161
resolver
enst
ENST00000877162
resolver
enst
ENST00000877163
resolver
enst
ENST00000877164
resolver
enst
ENST00000877166
resolver
enst
ENST00000877167
resolver
enst
ENST00000877169
resolver
enst
ENST00000877170
resolver
enst
ENST00000877171
resolver
enst
ENST00000966494
resolver
enst
ENST00000966495
resolver
genesymbol
DDR2
resolver
genesymbol_syn
NTRKR3
resolver
genesymbol_syn
TKT
resolver
genesymbol_syn
TYRO10
resolver
hgnc
HGNC:2731
resolver
uniprot
Q7Z730
resolver
uniprot_entry
DDR2_HUMAN
resolver
uniprot_sec
Q7Z730
resolver
activity_regulation
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. {ECO:0000269|PubMed:16186108}.
uniprot
proteins
amino_acid_sequence
MILIPRMLLVLFLLLPILSSAKAQVNPAICRYPLGMSGGQIPDEDITASSQWSESTAAKYGRLDSEEGDGAWCPEIPVEPDDLKEFLQIDLHTLHFITLVGTQGRHAGGHGIEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSMNVCMRVELYGCVWLDGLVSYNAPAGQQFVLPGGSIIYLNDSVYDGAVGYSMTEGLGQLTDGVSGLDDFTQTHEYHVWPGYDYVGWRNESATNGYIEIMFEFDRIRNFTTMKVHCNNMFAKGVKIFKEVQCYFRSEASEWEPNAISFPLVLDDVNPSARFVTVPLHHRMASAIKCQYHFADTWMMFSEITFQSDAAMYNNSEALPTSPMAPTTYDPMLKVDDSNTRILIGCLVAIIFILLAIIVIILWRQFWQKMLEKASRRMLDDEMTVSLSLPSDSSMFNNNRSSSPSEQGSNSTYDRIFPLRPDYQEPSRLIRKLPEFAPGEEESGCSGVVKPVQPSGPEGVPHYAEADIVNLQGVTGGNTYSVPAVTMDLLSGKDVAVEEFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQGDE
uniprot
proteins
disease_involvement
DISEASE: Spondyloepimetaphyseal dysplasia, short limb-hand type (SEMD-SL) [MIM:271665]: A bone disease characterized by short-limbed dwarfism, a narrow chest with pectus excavatum, brachydactyly in the hands and feet, a characteristic craniofacial appearance and premature calcifications. The radiological findings are distinctive and comprise short long bones throughout the skeleton with striking epiphyses that are stippled, flattened and fragmented and flared, irregular metaphyses. Platyspondyly in the spine with wide intervertebral spaces is observed and some vertebral bodies are pear-shaped with central humps, anterior protrusions and posterior scalloping. {ECO:0000269|PubMed:19110212, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:26463668}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Warburg-Cinotti syndrome (WRCN) [MIM:618175]: An autosomal dominant disease characterized by progressive corneal neovascularization, keloid formation, chronic skin ulcers, wasting of subcutaneous tissue, flexion contractures of the fingers, and acro-osteolysis. {ECO:0000269|PubMed:30449416}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
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. {ECO:0000269|PubMed:16186104, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:17665456, ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20004161, ECO:0000269|PubMed:20564243, ECO:0000269|PubMed:20734453, ECO:0000269|PubMed:30449416, ECO:0000269|PubMed:9659899}.
uniprot
proteins
mass_dalton
96736
uniprot
proteins
mutagenesis
MUTAGEN 52; /note="W->A: Abolishes collagen binding."; /evidence="ECO:0000269|PubMed:20004161, ECO:0000269|PubMed:20223752"; MUTAGEN 608; /note="K->A: Abolishes kinase activity."; /evidence="ECO:0000269|PubMed:16186108"; MUTAGEN 736; /note="Y->F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-740 and F-741."; /evidence="ECO:0000269|PubMed:16186108"; MUTAGEN 740; /note="Y->F: Promotes autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-741."; /evidence="ECO:0000269|PubMed:16186108"; MUTAGEN 741; /note="Y->F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-740."; /evidence="ECO:0000269|PubMed:16186108
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:20223752}.; PTM: Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues. {ECO:0000269|PubMed:16186104, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20004161, ECO:0000269|PubMed:9659899}.
uniprot
proteins
protein_family
Insulin receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16140923
uniprot
proteins
pubmed
16186104
uniprot
proteins
pubmed
16186108
uniprot
proteins
pubmed
16626936
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17665456
uniprot
proteins
pubmed
17703188
uniprot
proteins
pubmed
18201965
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19110212
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
20004161
uniprot
proteins
pubmed
20223752
uniprot
proteins
pubmed
20564243
uniprot
proteins
pubmed
20734453
uniprot
proteins
pubmed
21568710
uniprot
proteins
pubmed
26463668
uniprot
proteins
pubmed
30449416
uniprot
proteins
pubmed
8247548
uniprot
proteins
pubmed
9659899
uniprot
proteins
sequence_length
855
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}; Single-pass type I membrane protein {ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}.
uniprot
proteins
transmembrane_region
TRANSMEM 400..421; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins