Q08345 (DDR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Epithelial discoidin domain-containing receptor 1
Short name=Epithelial discoidin domain receptor 1
EC=2.7.10.1

Alternative name(s):
CD167 antigen-like family member A
Cell adhesion kinase
Discoidin receptor tyrosine kinase
HGK2
Mammary carcinoma kinase 10
Short name=MCK-10
Protein-tyrosine kinase 3A
Protein-tyrosine kinase RTK-6
TRK E
Tyrosine kinase DDR
Tyrosine-protein kinase CAK
CD_antigen=CD167a

Gene names

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	913 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Homodimer. Interacts (via PPxY motif) with WWC1 (via WW domains) in a collagen-regulated manner. Forms a tripartite complex with WWC1 and PRKCZ, but predominantly in the absence of collagen. Interacts (tyrosine phosphorylated) with SHC1. Interacts with SRC. Interacts with MYH9. Interacts with CDH1. Interacts with PTPN11. Interacts with NCK2. Ref.18 Ref.20 Ref.22 Ref.23 Ref.25 Ref.26 Ref.29
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.18 Ref.23. Isoform 2: Cell membrane; Single-pass type I membrane protein Ref.18 Ref.23. Isoform 3: Secreted Potential Ref.18 Ref.23. Isoform 4: Cell membrane; Single-pass type I membrane protein Ref.18 Ref.23.
Tissue specificity	Detected in T-47D, MDA-MB-175 and HBL-100 breast carcinoma cells, A-431 epidermoid carcinoma cells, SW48 and SNU-C2B colon carcinoma cells and Hs 294T melanoma cells (at protein level). Expressed at low levels in most adult tissues and is highest in the brain, lung, placenta and kidney. Lower levels of expression are detected in melanocytes, heart, liver, skeletal muscle and pancreas. Abundant in breast carcinoma cell lines. In the colonic mucosa, expressed in epithelia but not in the connective tissue of the lamina propria. In the thyroid gland, expressed in the epithelium of the thyroid follicles. In pancreas, expressed in the islets of Langerhans cells, but not in the surrounding epithelial cells of the exocrine pancreas. In kidney, expressed in the epithelia of the distal tubules. Not expressed in connective tissue, endothelial cells, adipose tissue, muscle cells or cells of hematopoietic origin. Ref.3 Ref.15 Ref.17
Domain	The Gly/Pro-rich domains may be required for an unusual geometry of interaction with ligand or substrates.
Post-translational modification	Autophosphorylated in response to fibrillar collagen binding. Ref.18 Ref.20 Ref.23 Ref.28
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Contains 1 F5/8 type C domain. Contains 1 protein kinase domain.
Sequence caution	The sequence ACF47649.1 differs from that shown. Reason: Erroneous termination at position 287. Translated as Cys. The sequence BAE06103.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Lactation Pregnancy
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	branching involved in mammary gland duct morphogenesis Inferred from electronic annotation. Source: Compara ear development Inferred from electronic annotation. Source: Compara embryo implantation Inferred from electronic annotation. Source: Compara lactation Inferred from electronic annotation. Source: UniProtKB-KW mammary gland alveolus development Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara peptidyl-tyrosine autophosphorylation Inferred from direct assay Ref.28. Source: UniProtKB regulation of cell growth Inferred from electronic annotation. Source: Compara regulation of cell-matrix adhesion Inferred from electronic annotation. Source: Compara regulation of extracellular matrix disassembly Inferred from mutant phenotype Ref.19. Source: UniProtKB smooth muscle cell migration Inferred from mutant phenotype Ref.19. Source: UniProtKB smooth muscle cell-matrix adhesion Inferred from mutant phenotype Ref.19. Source: UniProtKB wound healing, spreading of cells Inferred from mutant phenotype Ref.19. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW collagen binding Inferred from direct assay Ref.18. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase collagen receptor activity Inferred from direct assay Ref.28Ref.18. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q08345-1)

Also known as: CAK I; DDR1b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q08345-2)

Also known as: CAK II; DDR1a; Short;

The sequence of this isoform differs from the canonical sequence as follows:
     506-542: Missing.

Isoform 3 (identifier: Q08345-4)

Also known as: DDR1d;

The sequence of this isoform differs from the canonical sequence as follows:
     190-243: GLLSYTAPVG...GVVGLDDFRK → CSMGVWASWQ...MWRWSLSLTG
     244-913: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 4 (identifier: Q08345-5)

The sequence of this isoform differs from the canonical sequence as follows:
     665-665: A → ASFSLFS

Isoform 5 (identifier: Q08345-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSLPRCCPHPLRPEGSGAM
     506-542: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Chain

19 – 913

895

Epithelial discoidin domain-containing receptor 1

PRO_0000016742

Regions

Topological domain

21 – 417

397

Extracellular Potential

Transmembrane

418 – 438

21

Helical; Potential

Topological domain

439 – 913

475

Cytoplasmic Potential

Domain

31 – 185

155

F5/8 type C

Domain

610 – 905

296

Protein kinase

Nucleotide binding

616 – 624

9

ATP By similarity

Region

192 – 367

176

DS-like domain

Motif

481 – 484

4

PPxY motif

Compositional bias

377 – 415

39

Gly/Pro-rich

Compositional bias

476 – 601

126

Gly/Pro-rich

Sites

Active site

766

1

Proton acceptor By similarity

Metal binding

211

1

Calcium 1; via carbonyl oxygen

Metal binding

230

1

Calcium 1

Metal binding

230

1

Calcium 2; via carbonyl oxygen

Metal binding

233

1

Calcium 2

Metal binding

235

1

Calcium 2; via carbonyl oxygen

Metal binding

253

1

Calcium 1; via carbonyl oxygen

Metal binding

255

1

Calcium 1; via carbonyl oxygen

Metal binding

360

1

Calcium 2; via carbonyl oxygen

Metal binding

361

1

Calcium 2

Binding site

655

1

ATP By similarity

Amino acid modifications

Modified residue

513

1

Phosphotyrosine; by autocatalysis Ref.18

Modified residue

631

1

Phosphoserine Ref.24

Modified residue

740

1

Phosphotyrosine; by autocatalysis Probable

Modified residue

792

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

796

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

797

1

Phosphotyrosine; by autocatalysis By similarity

Glycosylation

211

1

N-linked (GlcNAc...) Potential

Glycosylation

260

1

N-linked (GlcNAc...) Potential

Glycosylation

371

1

N-linked (GlcNAc...) Potential

Glycosylation

394

1

N-linked (GlcNAc...) Potential

Disulfide bond

31 ↔ 185

Ref.29

Disulfide bond

74 ↔ 177

Ref.29

Disulfide bond

303 ↔ 348

Ref.29

Natural variations

Alternative sequence

1

1

M → MSLPRCCPHPLRPEGSGAM in isoform 5.

VSP_043582

Alternative sequence

190 – 243

54

GLLSY…DDFRK → CSMGVWASWQMVWWGWMTLG RVRSCGSGQAMTMWDGATTA SPVAMWRWSLSLTG in isoform 3.

VSP_036916

Alternative sequence

244 – 913

670

Missing in isoform 3.

VSP_036917

Alternative sequence

506 – 542

37

Missing in isoform 2 and isoform 5.

VSP_002953

Alternative sequence

665

1

A → ASFSLFS in isoform 4.

VSP_038057

Natural variant

17

1

S → G. Ref.30
Corresponds to variant rs55901302 [ dbSNP | Ensembl ].

VAR_041492

Natural variant

100

1

V → A. Ref.30
Corresponds to variant rs34544756 [ dbSNP | Ensembl ].

VAR_041493

Natural variant

169

1

R → Q. Ref.30
Corresponds to variant rs55980643 [ dbSNP | Ensembl ].

VAR_041494

Natural variant

170

1

A → D. Ref.30
Corresponds to variant rs56231803 [ dbSNP | Ensembl ].

VAR_041495

Natural variant

306

1

R → W. Ref.30
Corresponds to variant rs56024191 [ dbSNP | Ensembl ].

VAR_041496

Natural variant

496

1

S → A in a lung squamous cell carcinoma sample; somatic mutation. Ref.30

VAR_041497

Natural variant

833

1

L → V. Ref.2 Ref.5
Corresponds to variant rs2524235 [ dbSNP | Ensembl ].

VAR_049716

Experimental info

Mutagenesis

740

1

Y → F: Abolishes interaction with PTPN11. Ref.20

Sequence conflict

94

1

L → V in AAA02866. Ref.2

Sequence conflict

94

1

L → V in AAC50917. Ref.5

Sequence conflict

165

1

R → H in AAH70070. Ref.14

Sequence conflict

285 – 286

2

VH → MW in ACF47649. Ref.8

Sequence conflict

741

1

P → Q in AAH70070. Ref.14

Sequence conflict

847 – 867

21

QLTDE…DQGRQ → SAHRRAGHRERGGVLPGPGP A in CAA66871. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

913

Helix Strand Turn

Details...

Turn

37 – 39

3

Helix

44 – 46

3

Beta strand

47 – 50

4

Helix

55 – 57

3

Helix

59 – 61

3

Turn

68 – 70

3

Beta strand

71 – 73

3

Beta strand

87 – 103

17

Helix

107 – 109

3

Beta strand

116 – 127

12

Beta strand

129 – 131

3

Beta strand

145 – 148

4

Beta strand

151 – 169

19

Beta strand

171 – 173

3

Beta strand

178 – 186

9

Beta strand

191 – 197

7

Beta strand

204 – 206

3

Beta strand

217 – 220

4

Beta strand

223 – 226

4

Helix

230 – 232

3

Beta strand

245 – 248

4

Turn

251 – 254

4

Beta strand

256 – 259

4

Helix

260 – 262

3

Beta strand

266 – 287

22

Helix

291 – 293

3

Beta strand

299 – 306

8

Beta strand

308 – 312

5

Beta strand

314 – 316

3

Beta strand

318 – 321

4

Beta strand

332 – 351

20

Beta strand

353 – 367

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CAK I) (DDR1b) [UniParc]. Last modified February 1, 1995. Version 1. Checksum: C96913EA906C481E	FASTA	913	101,128
	10 20 30 40 50 60 MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR 70 80 90 100 110 120 HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL 130 140 150 160 170 180 RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV 190 200 210 220 230 240 ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD 250 260 270 280 290 300 FRKSQELRVW PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG 310 320 330 340 350 360 VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF LFAGPWLLFS 370 380 390 400 410 420 EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL EPRGQQPVAK AEGSPTAILI 430 440 450 460 470 480 GCLVAIILLL LLIIALMLWR LHWRRLLSKA ERRVLEEELT VHLSVPGDTI LINNRPGPRE 490 500 510 520 530 540 PPPYQEPRPR GNPPHSAPCV PNGSALLLSN PAYRLLLATY ARPPRGPGPP TPAWAKPTNT 550 560 570 580 590 600 QAYSGDYMEP EKPGAPLLPP PPQNSVPHYA EADIVTLQGV TGGNTYAVPA LPPGAVGDGP 610 620 630 640 650 660 PRVDFPRSRL RFKEKLGEGQ FGEVHLCEVD SPQDLVSLDF PLNVRKGHPL LVAVKILRPD 670 680 690 700 710 720 ATKNARNDFL KEVKIMSRLK DPNIIRLLGV CVQDDPLCMI TDYMENGDLN QFLSAHQLED 730 740 750 760 770 780 KAAEGAPGDG QAAQGPTISY PMLLHVAAQI ASGMRYLATL NFVHRDLATR NCLVGENFTI 790 800 810 820 830 840 KIADFGMSRN LYAGDYYRVQ GRAVLPIRWM AWECILMGKF TTASDVWAFG VTLWEVLMLC 850 860 870 880 890 900 RAQPFGQLTD EQVIENAGEF FRDQGRQVYL SRPPACPQGL YELMLRCWSR ESEQRPPFSQ 910 LHRFLAEDAL NTV
	Isoform 2 (CAK II) (DDR1a) (Short) [UniParc]. Checksum: E02881598CC7CD0B	FASTA	876	97,174
	10 20 30 40 50 60 MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR 70 80 90 100 110 120 HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL 130 140 150 160 170 180 RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV 190 200 210 220 230 240 ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD 250 260 270 280 290 300 FRKSQELRVW PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG 310 320 330 340 350 360 VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF LFAGPWLLFS 370 380 390 400 410 420 EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL EPRGQQPVAK AEGSPTAILI 430 440 450 460 470 480 GCLVAIILLL LLIIALMLWR LHWRRLLSKA ERRVLEEELT VHLSVPGDTI LINNRPGPRE 490 500 510 520 530 540 PPPYQEPRPR GNPPHSAPCV PNGSAYSGDY MEPEKPGAPL LPPPPQNSVP HYAEADIVTL 550 560 570 580 590 600 QGVTGGNTYA VPALPPGAVG DGPPRVDFPR SRLRFKEKLG EGQFGEVHLC EVDSPQDLVS 610 620 630 640 650 660 LDFPLNVRKG HPLLVAVKIL RPDATKNARN DFLKEVKIMS RLKDPNIIRL LGVCVQDDPL 670 680 690 700 710 720 CMITDYMENG DLNQFLSAHQ LEDKAAEGAP GDGQAAQGPT ISYPMLLHVA AQIASGMRYL 730 740 750 760 770 780 ATLNFVHRDL ATRNCLVGEN FTIKIADFGM SRNLYAGDYY RVQGRAVLPI RWMAWECILM 790 800 810 820 830 840 GKFTTASDVW AFGVTLWEVL MLCRAQPFGQ LTDEQVIENA GEFFRDQGRQ VYLSRPPACP 850 860 870 QGLYELMLRC WSRESEQRPP FSQLHRFLAE DALNTV
	Isoform 3 (DDR1d) [UniParc]. Checksum: 36872B8FB29835D0	FASTA	243	27,130
	10 20 30 40 50 60 MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR 70 80 90 100 110 120 HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL 130 140 150 160 170 180 RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV 190 200 210 220 230 240 ELYGCLWRDC SMGVWASWQM VWWGWMTLGR VRSCGSGQAM TMWDGATTAS PVAMWRWSLS LTG
	Isoform 4 [UniParc]. Checksum: 2094224F6AE943F5	FASTA	919	101,796
	10 20 30 40 50 60 MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR 70 80 90 100 110 120 HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL 130 140 150 160 170 180 RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV 190 200 210 220 230 240 ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD 250 260 270 280 290 300 FRKSQELRVW PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG 310 320 330 340 350 360 VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF LFAGPWLLFS 370 380 390 400 410 420 EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL EPRGQQPVAK AEGSPTAILI 430 440 450 460 470 480 GCLVAIILLL LLIIALMLWR LHWRRLLSKA ERRVLEEELT VHLSVPGDTI LINNRPGPRE 490 500 510 520 530 540 PPPYQEPRPR GNPPHSAPCV PNGSALLLSN PAYRLLLATY ARPPRGPGPP TPAWAKPTNT 550 560 570 580 590 600 QAYSGDYMEP EKPGAPLLPP PPQNSVPHYA EADIVTLQGV TGGNTYAVPA LPPGAVGDGP 610 620 630 640 650 660 PRVDFPRSRL RFKEKLGEGQ FGEVHLCEVD SPQDLVSLDF PLNVRKGHPL LVAVKILRPD 670 680 690 700 710 720 ATKNASFSLF SRNDFLKEVK IMSRLKDPNI IRLLGVCVQD DPLCMITDYM ENGDLNQFLS 730 740 750 760 770 780 AHQLEDKAAE GAPGDGQAAQ GPTISYPMLL HVAAQIASGM RYLATLNFVH RDLATRNCLV 790 800 810 820 830 840 GENFTIKIAD FGMSRNLYAG DYYRVQGRAV LPIRWMAWEC ILMGKFTTAS DVWAFGVTLW 850 860 870 880 890 900 EVLMLCRAQP FGQLTDEQVI ENAGEFFRDQ GRQVYLSRPP ACPQGLYELM LRCWSRESEQ 910 RPPFSQLHRF LAEDALNTV
	Isoform 5 [UniParc]. Checksum: D46EECFC939B7585	FASTA	894	99,064
	10 20 30 40 50 60 MSLPRCCPHP LRPEGSGAMG PEALSSLLLL LLVASGDADM KGHFDPAKCR YALGMQDRTI 70 80 90 100 110 120 PDSDISASSS WSDSTAARHS RLESSDGDGA WCPAGSVFPK EEEYLQVDLQ RLHLVALVGT 130 140 150 160 170 180 QGRHAGGLGK EFSRSYRLRY SRDGRRWMGW KDRWGQEVIS GNEDPEGVVL KDLGPPMVAR 190 200 210 220 230 240 LVRFYPRADR VMSVCLRVEL YGCLWRDGLL SYTAPVGQTM YLSEAVYLND STYDGHTVGG 250 260 270 280 290 300 LQYGGLGQLA DGVVGLDDFR KSQELRVWPG YDYVGWSNHS FSSGYVEMEF EFDRLRAFQA 310 320 330 340 350 360 MQVHCNNMHT LGARLPGGVE CRFRRGPAMA WEGEPMRHNL GGNLGDPRAR AVSVPLGGRV 370 380 390 400 410 420 ARFLQCRFLF AGPWLLFSEI SFISDVVNNS SPALGGTFPP APWWPPGPPP TNFSSLELEP 430 440 450 460 470 480 RGQQPVAKAE GSPTAILIGC LVAIILLLLL IIALMLWRLH WRRLLSKAER RVLEEELTVH 490 500 510 520 530 540 LSVPGDTILI NNRPGPREPP PYQEPRPRGN PPHSAPCVPN GSAYSGDYME PEKPGAPLLP 550 560 570 580 590 600 PPPQNSVPHY AEADIVTLQG VTGGNTYAVP ALPPGAVGDG PPRVDFPRSR LRFKEKLGEG 610 620 630 640 650 660 QFGEVHLCEV DSPQDLVSLD FPLNVRKGHP LLVAVKILRP DATKNARNDF LKEVKIMSRL 670 680 690 700 710 720 KDPNIIRLLG VCVQDDPLCM ITDYMENGDL NQFLSAHQLE DKAAEGAPGD GQAAQGPTIS 730 740 750 760 770 780 YPMLLHVAAQ IASGMRYLAT LNFVHRDLAT RNCLVGENFT IKIADFGMSR NLYAGDYYRV 790 800 810 820 830 840 QGRAVLPIRW MAWECILMGK FTTASDVWAF GVTLWEVLML CRAQPFGQLT DEQVIENAGE 850 860 870 880 890 FFRDQGRQVY LSRPPACPQG LYELMLRCWS RESEQRPPFS QLHRFLAEDA LNTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of trkE, a novel trk-related putative tyrosine kinase receptor isolated from normal human keratinocytes and widely expressed by normal human tissues." di Marco E., Cutuli N., Guerra L., Cancedda R., de Luca M. J. Biol. Chem. 268:24290-24295(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Brain and Keratinocyte.
[2]	"A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain." Johnson J.D., Edman J.C., Rutter W.J. Proc. Natl. Acad. Sci. U.S.A. 90:5677-5681(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-833. Tissue: Placenta.
[3]	"Isolation and characterization of an epithelial-specific receptor tyrosine kinase from an ovarian cancer cell line." Laval S., Butler R., Shelling A.N., Hanby A.M., Poulsom R., Ganesan T.S. Cell Growth Differ. 5:1173-1183(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. Tissue: Ovary.
[4]	"Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain." Perez J.L., Shen X., Finkernagel S., Sciorra L., Jenkins N.A., Gilbert D.J., Copeland N.G., Wong T.W. Oncogene 9:211-219(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal liver.
[5]	"Receptor protein tyrosine kinase DDR is up-regulated by p53 protein." Sakuma S., Tada M., Saya H., Sawamura Y., Shinohe Y., Abe H. FEBS Lett. 398:165-169(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-833.
[6]	"The genomic structure of discoidin receptor tyrosine kinase." Playford M.P., Butler R.J., Wang X.C., Katso R.M., Cooke I.E., Ganesan T.S. Genome Res. 6:620-627(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Identification of two isoforms of the Cak receptor kinase that are coexpressed in breast tumor cell lines." Perez J.L., Jing S.Q., Wong T.W. Oncogene 12:1469-1477(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Lung.
[8]	"Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis." Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M. Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-286 (ISOFORMS 1/2/4).
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5). Tissue: Brain and Placenta.
[10]	"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method." Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[11]	"Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity." Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A. , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S. Genetics 173:1555-1570(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Tissue: Peripheral blood leukocyte.
[12]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain and Muscle.
[15]	"Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer." Alves F., Vogel W., Mossie K., Millauer B., Hoefler H., Ullrich A. Oncogene 10:609-618(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-550 (ISOFORMS 1/4), NUCLEOTIDE SEQUENCE [MRNA] OF 501-550 AND 651-694 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 651-694 (ISOFORM 4), ALTERNATIVE SPLICING, TISSUE SPECIFICITY. Tissue: Mammary carcinoma.
[16]	"Expression of growth factor receptors, the focal adhesion kinase, and other tyrosine kinases in human soft tissue tumors." Weiner T.M., Liu E.T., Craven R.J., Cance W.G. Ann. Surg. Oncol. 1:18-27(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 771-824 (ISOFORMS 1/2/4).
[17]	"A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes." Lee S.-T., Strunk K.M., Spritz R.A. Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 772-823 (ISOFORMS 1/2/4), TISSUE SPECIFICITY. Tissue: Melanocyte.
[18]	"The discoidin domain receptor tyrosine kinases are activated by collagen." Vogel W., Gish G.D., Alves F., Pawson T. Mol. Cell 1:13-23(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS COLLAGEN RECEPTOR, PHOSPHORYLATION AT TYR-513, INTERACTION WITH SHC1, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION.
[19]	"Tyrosine kinase activity of discoidin domain receptor 1 is necessary for smooth muscle cell migration and matrix metalloproteinase expression." Hou G., Vogel W.F., Bendeck M.P. Circ. Res. 90:1147-1149(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"Pinpointing phosphotyrosine-dependent interactions downstream of the collagen receptor DDR1." Koo D.H., McFadden C., Huang Y., Abdulhussein R., Friese-Hamim M., Vogel W.F. FEBS Lett. 580:15-22(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PTPN11 AND NCK2, PHOSPHORYLATION AT TYR-740, MUTAGENESIS OF TYR-740.
[21]	"Discoidin domain receptor-1a (DDR1a) promotes glioma cell invasion and adhesion in association with matrix metalloproteinase-2." Ram R., Lorente G., Nikolich K., Urfer R., Foehr E., Nagavarapu U. J. Neurooncol. 76:239-248(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[22]	"KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling." Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W., Daly R.J., Ormandy C.J. Biochim. Biophys. Acta 1783:383-393(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWC1 AND PRKCZ.
[23]	"The collagen receptor DDR1 regulates cell spreading and motility by associating with myosin IIA." Huang Y., Arora P., McCulloch C.A., Vogel W.F. J. Cell Sci. 122:1637-1646(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH MYH9.
[24]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, MASS SPECTROMETRY.
[25]	"DDR1 regulates the stabilization of cell surface E-cadherin and E-cadherin-mediated cell aggregation." Eswaramoorthy R., Wang C.K., Chen W.C., Tang M.J., Ho M.L., Hwang C.C., Wang H.M., Wang C.Z. J. Cell. Physiol. 224:387-397(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDH1.
[26]	"Collagen stimulates discoidin domain receptor 1-mediated migration of smooth muscle cells through Src." Lu K.K., Trcka D., Bendeck M.P. Cardiovasc. Pathol. 20:71-76(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SRC.
[27]	"Discoidin domain receptor 1 regulates bronchial epithelial repair and matrix metalloproteinase production." Roberts M.E., Magowan L., Hall I.P., Johnson S.R. Eur. Respir. J. 37:1482-1493(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[28]	"Collagen binding specificity of the discoidin domain receptors: binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1." Xu H., Raynal N., Stathopoulos S., Myllyharju J., Farndale R.W., Leitinger B. Matrix Biol. 30:16-26(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS COLLAGEN RECEPTOR, AUTOPHOSPHORYLATION.
[29]	"Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory Fab fragment reveals features important for signaling." Carafoli F., Mayer M.C., Shiraishi K., Pecheva M.A., Chan L.Y., Nan R., Leitinger B., Hohenester E. Structure 20:688-697(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 29-367 IN COMPLEX WITH INHIBITORY ANTIBODY, CALCIUM-BINDING SITES, DISULFIDE BONDS, SUBUNIT.
[30]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-17; ALA-100; GLN-169; ASP-170; TRP-306 AND ALA-496.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X74979 mRNA. Translation: CAA52915.1.
L11315 mRNA. Translation: AAA02866.1.
Z29093 mRNA. Translation: CAA82335.1.
L20817 mRNA. Translation: AAA18019.1.
U48705 Genomic DNA. Translation: AAC50917.1.
X98208 , X99023, X99024, X99025, X99026, X99027, X99028, X99029, X99030, X99031, X99032, X99033, X99034 Genomic DNA. Translation: CAA66871.1.
L57508 mRNA. Translation: AAB05208.1.
EU826613 mRNA. Translation: ACF47649.1. Sequence problems.
EU826614 mRNA. Translation: ACF47650.1.
AK291621 mRNA. Translation: BAF84310.1.
AK294793 mRNA. Translation: BAH11886.1.
AB210021 mRNA. Translation: BAE06103.1. Different initiation.
BA000025 Genomic DNA. Translation: BAB63318.1.
CR759747 Genomic DNA. Translation: CAQ06757.1.
CR759747 Genomic DNA. Translation: CAQ06756.1.
AB088102 Genomic DNA. Translation: BAC54935.1.
AB103608 Genomic DNA. Translation: BAF31270.1.
AL662854 Genomic DNA. Translation: CAI17434.1.
AL662870 Genomic DNA. Translation: CAI18441.1.
AL773541, AL773589 Genomic DNA. Translation: CAI18450.1.
AL773589, AL773541 Genomic DNA. Translation: CAI18534.1.
AL662854 Genomic DNA. Translation: CAI17433.1.
AL662870 Genomic DNA. Translation: CAI18442.1.
AL773541, AL773589 Genomic DNA. Translation: CAI18451.1.
AL773589, AL773541 Genomic DNA. Translation: CAI18533.1.
AB202100 Genomic DNA. Translation: BAE78621.1.
BX927194 Genomic DNA. Translation: CAQ09768.1.
BX927194 Genomic DNA. Translation: CAQ09767.1.
CH471081 Genomic DNA. Translation: EAX03335.1.
CH471081 Genomic DNA. Translation: EAX03338.1.
BC008716 mRNA. Translation: AAH08716.1.
BC013400 mRNA. Translation: AAH13400.1.
BC070070 mRNA. Translation: AAH70070.1.

IPI

IPI00001477.
IPI00219996.
IPI00657861.
IPI00910318.
IPI00965006.

PIR

A48280.
A49508.

RefSeq

NP_001189450.1. NM_001202521.1.
NP_001189451.1. NM_001202522.1.
NP_001189452.1. NM_001202523.1.
NP_001945.3. NM_001954.4.
NP_054699.2. NM_013993.2.
NP_054700.2. NM_013994.2.

UniGene

Hs.631988.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AG4	X-ray	2.80	A	29-367	[»]

ProteinModelPortal

Q08345.

SMR

Q08345. Positions 30-367, 603-909.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39698N.

IntAct

Q08345. 7 interactions.

MINT

MINT-1383336.

PTM databases

PhosphoSite

Q08345.

Polymorphism databases

DMDM

729008.

Proteomic databases

PaxDb

Q08345.

PRIDE

Q08345.

Protocols and materials databases

DNASU

780.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000259875; ENSP00000259875; ENSG00000137332.
ENST00000324771; ENSP00000318217; ENSG00000204580.
ENST00000376567; ENSP00000365751; ENSG00000204580.
ENST00000376568; ENSP00000365752; ENSG00000204580.
ENST00000376569; ENSP00000365753; ENSG00000204580.
ENST00000376570; ENSP00000365754; ENSG00000204580.
ENST00000376575; ENSP00000365759; ENSG00000204580.
ENST00000383377; ENSP00000372868; ENSG00000137332.
ENST00000400410; ENSP00000383261; ENSG00000137332.
ENST00000400411; ENSP00000383262; ENSG00000137332.
ENST00000400414; ENSP00000383265; ENSG00000137332.
ENST00000400486; ENSP00000383334; ENSG00000215522.
ENST00000400488; ENSP00000383336; ENSG00000215522.
ENST00000400489; ENSP00000383337; ENSG00000215522.
ENST00000400491; ENSP00000383338; ENSG00000215522.
ENST00000400492; ENSP00000383339; ENSG00000215522.
ENST00000412329; ENSP00000391805; ENSG00000230456.
ENST00000415092; ENSP00000405540; ENSG00000230456.
ENST00000418800; ENSP00000407699; ENSG00000204580.
ENST00000419412; ENSP00000416183; ENSG00000234078.
ENST00000421229; ENSP00000415730; ENSG00000234078.
ENST00000427053; ENSP00000416145; ENSG00000230456.
ENST00000429699; ENSP00000401397; ENSG00000234078.
ENST00000430933; ENSP00000397769; ENSG00000234078.
ENST00000446312; ENSP00000405998; ENSG00000204580.
ENST00000449518; ENSP00000414285; ENSG00000230456.
ENST00000452441; ENSP00000405039; ENSG00000204580.
ENST00000453510; ENSP00000401208; ENSG00000230456.
ENST00000454612; ENSP00000406091; ENSG00000204580.
ENST00000454774; ENSP00000400393; ENSG00000234078.
ENST00000482873; ENSP00000421978; ENSG00000204580.
ENST00000508312; ENSP00000422442; ENSG00000204580.
ENST00000513240; ENSP00000427552; ENSG00000204580.
ENST00000546507; ENSP00000447628; ENSG00000234078.
ENST00000546668; ENSP00000448546; ENSG00000230456.
ENST00000547742; ENSP00000449930; ENSG00000215522.
ENST00000548133; ENSP00000449611; ENSG00000230456.
ENST00000548962; ENSP00000448115; ENSG00000230456.
ENST00000549026; ENSP00000449238; ENSG00000215522.
ENST00000550384; ENSP00000447474; ENSG00000234078.
ENST00000550395; ENSP00000449255; ENSG00000215522.
ENST00000552068; ENSP00000449190; ENSG00000234078.
ENST00000552721; ENSP00000449307; ENSG00000137332.
ENST00000553015; ENSP00000448377; ENSG00000137332.
ENST00000553261; ENSP00000446713; ENSG00000137332.

GeneID

780.

KEGG

hsa:780.

UCSC

uc003nrq.3. human.
uc003nrr.3. human.
uc003nrv.3. human.
uc011dms.2. human.
uc011dmu.1. human.

Organism-specific databases

CTD

780.

GeneCards

GC06P030848.

HGNC

HGNC:2730. DDR1.

HPA

CAB010162.
CAB025656.

MIM

600408. gene.

neXtProt

NX_Q08345.

PharmGKB

PA24348.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000043102.

HOVERGEN

HBG005461.

InParanoid

Q08345.

KO

K05124.

OrthoDB

EOG4H19V5.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

SignaLink

Q08345.

Gene expression databases

ArrayExpress

Q08345.

Bgee

Q08345.

CleanEx

HS_DDR1.

Genevestigator

Q08345.

GermOnline

ENSG00000204580. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.260. 1 hit.

InterPro

IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008979. Galactose-bd-like.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]

Pfam

PF00754. F5_F8_type_C. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PRINTS

PR00109. TYRKINASE.

SMART

SM00231. FA58C. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF49785. Gal_bind_like. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q08345.

ChEMBL

CHEMBL5319.

ChiTaRS

DDR1. human.

DrugBank

DB00619. Imatinib.

GenomeRNAi

780.

NextBio

3152.

PMAP-CutDB

Q2L6H3.

SOURCE

Search...

Entry information

Entry name

DDR1_HUMAN

Accession

Primary (citable) accession number: Q08345
Secondary accession number(s): B5A975 , B5A976, B7Z2K0, Q14196, Q16562, Q2L6H3, Q4LE50, Q5ST11, Q5ST12, Q6NSK4, Q9UD35, Q9UD36, Q9UD37, Q9UD86, Q9UDL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 29, 2013
This is version 152 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.