DDR1
entrez
780
canonical
uniprot
Q08345
canonical
ensembl
ENSG00000137332
resolver
ensembl
ENSG00000204580
resolver
ensembl
ENSG00000215522
resolver
ensembl
ENSG00000230456
resolver
ensembl
ENSG00000234078
resolver
ensp
ENSP00000365752
resolver
ensp
ENSP00000365753
resolver
ensp
ENSP00000365754
resolver
ensp
ENSP00000405039
resolver
ensp
ENSP00000405998
resolver
ensp
ENSP00000407699
resolver
ensp
ENSP00000422442
resolver
ensp
ENSP00000427552
resolver
ensp
ENSP00000447357
resolver
ensp
ENSP00000448460
resolver
ensp
ENSP00000448797
resolver
ensp
ENSP00000578986
resolver
ensp
ENSP00000578987
resolver
ensp
ENSP00000578990
resolver
ensp
ENSP00000578991
resolver
ensp
ENSP00000578992
resolver
ensp
ENSP00000579003
resolver
ensp
ENSP00000579007
resolver
ensp
ENSP00000579008
resolver
ensp
ENSP00000579010
resolver
ensp
ENSP00000579012
resolver
ensp
ENSP00000607480
resolver
ensp
ENSP00000607482
resolver
ensp
ENSP00000607483
resolver
ensp
ENSP00000607488
resolver
ensp
ENSP00000607489
resolver
ensp
ENSP00000607490
resolver
ensp
ENSP00000607497
resolver
ensp
ENSP00000607498
resolver
ensp
ENSP00000626481
resolver
ensp
ENSP00000626483
resolver
ensp
ENSP00000626485
resolver
ensp
ENSP00000678612
resolver
enst
ENST00000446312
resolver
enst
ENST00000548693
resolver
enst
ENST00000550666
resolver
enst
ENST00000552434
resolver
genesymbol
DDR1
resolver
genesymbol_syn
CAK
resolver
genesymbol_syn
EDDR1
resolver
genesymbol_syn
NEP
resolver
genesymbol_syn
NTRK4
resolver
genesymbol_syn
PTK3A
resolver
genesymbol_syn
RTK6
resolver
genesymbol_syn
TRKE
resolver
hgnc
HGNC:2730
resolver
uniprot
A0A0A0MSX3
resolver
uniprot
B5A975
resolver
uniprot
B5A976
resolver
uniprot
B7Z2K0
resolver
uniprot
Q14196
resolver
uniprot
Q16562
resolver
uniprot
Q2L6H3
resolver
uniprot
Q4LE50
resolver
uniprot
Q5ST11
resolver
uniprot
Q5ST12
resolver
uniprot
Q6NSK4
resolver
uniprot
Q96T61
resolver
uniprot
Q96T62
resolver
uniprot
Q9UD35
resolver
uniprot
Q9UD36
resolver
uniprot
Q9UD37
resolver
uniprot
Q9UD86
resolver
uniprot
Q9UDL2
resolver
uniprot_entry
A0A0A0MSX3_HUMAN
resolver
uniprot_entry
DDR1_HUMAN
resolver
uniprot_entry
Q96T61_HUMAN
resolver
uniprot_entry
Q96T62_HUMAN
resolver
uniprot_sec
B5A975
resolver
uniprot_sec
B5A976
resolver
uniprot_sec
B7Z2K0
resolver
uniprot_sec
Q14196
resolver
uniprot_sec
Q16562
resolver
uniprot_sec
Q2L6H3
resolver
uniprot_sec
Q4LE50
resolver
uniprot_sec
Q5ST11
resolver
uniprot_sec
Q5ST12
resolver
uniprot_sec
Q6NSK4
resolver
uniprot_sec
Q9UD35
resolver
uniprot_sec
Q9UD36
resolver
uniprot_sec
Q9UD37
resolver
uniprot_sec
Q9UD86
resolver
uniprot_sec
Q9UDL2
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the multi-targeted cancer drugs imatinib and ponatinib. {ECO:0000269|PubMed:24768818}.
uniprot
proteins
amino_acid_sequence
MGPEALSSLLLLLLVASGDADMKGHFDPAKCRYALGMQDRTIPDSDISASSSWSDSTAARHSRLESSDGDGAWCPAGSVFPKEEEYLQVDLQRLHLVALVGTQGRHAGGLGKEFSRSYRLRYSRDGRRWMGWKDRWGQEVISGNEDPEGVVLKDLGPPMVARLVRFYPRADRVMSVCLRVELYGCLWRDGLLSYTAPVGQTMYLSEAVYLNDSTYDGHTVGGLQYGGLGQLADGVVGLDDFRKSQELRVWPGYDYVGWSNHSFSSGYVEMEFEFDRLRAFQAMQVHCNNMHTLGARLPGGVECRFRRGPAMAWEGEPMRHNLGGNLGDPRARAVSVPLGGRVARFLQCRFLFAGPWLLFSEISFISDVVNNSSPALGGTFPPAPWWPPGPPPTNFSSLELEPRGQQPVAKAEGSPTAILIGCLVAIILLLLLIIALMLWRLHWRRLLSKAERRVLEEELTVHLSVPGDTILINNRPGPREPPPYQEPRPRGNPPHSAPCVPNGSALLLSNPAYRLLLATYARPPRGPGPPTPAWAKPTNTQAYSGDYMEPEKPGAPLLPPPPQNSVPHYAEADIVTLQGVTGGNTYAVPALPPGAVGDGPPRVDFPRSRLRFKEKLGEGQFGEVHLCEVDSPQDLVSLDFPLNVRKGHPLLVAVKILRPDATKNARNDFLKEVKIMSRLKDPNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLEDKAAEGAPGDGQAAQGPTISYPMLLHVAAQIASGMRYLATLNFVHRDLATRNCLVGENFTIKIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEVLMLCRAQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQGLYELMLRCWSRESEQRPPFSQLHRFLAEDALNTV
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine kinase that functions as a 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. {ECO:0000250, ECO:0000269|PubMed:12065315, ECO:0000269|PubMed:16234985, ECO:0000269|PubMed:16337946, ECO:0000269|PubMed:19401332, ECO:0000269|PubMed:20093046, ECO:0000269|PubMed:20432435, ECO:0000269|PubMed:20884741, ECO:0000269|PubMed:21044884, ECO:0000269|PubMed:9659899}.
uniprot
proteins
mass_dalton
101128
uniprot
proteins
mutagenesis
MUTAGEN 105; /note="R->A: Inhibits collagen-induced phosphorylation."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 211; /note="N->A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 211; /note="N->Q: Sustained phosphorylation regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. Located intracellularly and at the cell surface. Displays a reduced rate of receptor internalization, which is not altered in the presence of collagen. Able to bind collagen as wild-type. Exhibits enhanced collagen-independent receptor dimerization. Complete loss of the collagen-independent constitutive activation; when associated with A-655."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 213; /note="S->A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 260; /note="N->Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 371; /note="N->Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 379; /note="T->A: Phosphorylates in response to collagen, but at lower levels compared to wild-type. Phosphorylates in response to collagen, but at lower levels compared to wild-type; when associated with A-393."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 393; /note="T->A: Phosphorylates in response to collagen, but at lower levels compared to wild-type. Phosphorylates in response to collagen, but at lower levels compared to wild-type; when associated with A-379."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 394; /note="N->Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 655; /note="K->A: Loss of kinase activity. Complete loss of the collagen-independent constitutive activation; when associated with Q-211."; /evidence="ECO:0000269|PubMed:24509848"; MUTAGEN 707; /note="G->A: Confers over 20-fold resistance to the ability of an inhibitor to inhibit autophosphorylation."; /evidence="ECO:0000269|PubMed:23899692"; MUTAGEN 740; /note="Y->F: Abolishes interaction with PTPN11."; /evidence="ECO:0000269|PubMed:16337946
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated in response to fibrillar collagen binding.; PTM: Glycosylation of Asn-211, but apparently not of Asn-260 or Asn-394, prevents autophosphorylation from occurring in the absence of collagen. {ECO:0000269|PubMed:22483115, ECO:0000269|PubMed:24509848}.
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
12065315
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16234985
uniprot
proteins
pubmed
16337946
uniprot
proteins
pubmed
16702430
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18190796
uniprot
proteins
pubmed
18593464
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19401332
uniprot
proteins
pubmed
20093046
uniprot
proteins
pubmed
20432435
uniprot
proteins
pubmed
20884741
uniprot
proteins
pubmed
21044884
uniprot
proteins
pubmed
22483115
uniprot
proteins
pubmed
23899692
uniprot
proteins
pubmed
24509848
uniprot
proteins
pubmed
24768818
uniprot
proteins
pubmed
7834423
uniprot
proteins
pubmed
7845687
uniprot
proteins
pubmed
7848919
uniprot
proteins
pubmed
8226977
uniprot
proteins
pubmed
8247543
uniprot
proteins
pubmed
8302582
uniprot
proteins
pubmed
8390675
uniprot
proteins
pubmed
8622863
uniprot
proteins
pubmed
8796349
uniprot
proteins
pubmed
8977099
uniprot
proteins
pubmed
9659899
uniprot
proteins
sequence_length
913
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 418..438; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins