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Protein

Epithelial discoidin domain-containing receptor 1

Gene

DDR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity9 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

Inhibited by the multi-targeted cancer drugs imatinib and ponatinib.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi211Calcium 1; via carbonyl oxygen1
Metal bindingi230Calcium 11
Metal bindingi230Calcium 2; via carbonyl oxygen1
Metal bindingi233Calcium 21
Metal bindingi235Calcium 2; via carbonyl oxygen1
Metal bindingi253Calcium 1; via carbonyl oxygen1
Metal bindingi255Calcium 1; via carbonyl oxygen1
Metal bindingi360Calcium 2; via carbonyl oxygen1
Metal bindingi361Calcium 21
Binding sitei655ATP1
Active sitei766Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi616 – 624ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • collagen binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein tyrosine kinase collagen receptor activity Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

  • axon development Source: Ensembl
  • branching involved in mammary gland duct morphogenesis Source: Ensembl
  • cell adhesion Source: ProtInc
  • collagen-activated tyrosine kinase receptor signaling pathway Source: UniProtKB
  • ear development Source: Ensembl
  • embryo implantation Source: Ensembl
  • extracellular matrix organization Source: Reactome
  • lactation Source: UniProtKB-KW
  • mammary gland alveolus development Source: Ensembl
  • negative regulation of cell proliferation Source: Ensembl
  • neuron projection extension Source: Ensembl
  • peptidyl-tyrosine autophosphorylation Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of cell growth Source: Ensembl
  • regulation of cell-matrix adhesion Source: Ensembl
  • regulation of extracellular matrix disassembly Source: UniProtKB
  • smooth muscle cell-matrix adhesion Source: UniProtKB
  • smooth muscle cell migration Source: UniProtKB
  • wound healing, spreading of cells Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Lactation, Pregnancy

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS06318-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-3000171. Non-integrin membrane-ECM interactions.
SignaLinkiQ08345.
SIGNORiQ08345.

Names & Taxonomyi

Protein namesi
Recommended name:
Epithelial discoidin domain-containing receptor 1 (EC:2.7.10.1)
Short name:
Epithelial discoidin domain receptor 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 namesi
Name:DDR1
Synonyms:CAK, EDDR1, NEP, NTRK4, PTK3A, RTK6, TRKE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:2730. DDR1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 417ExtracellularSequence analysisAdd BLAST397
Transmembranei418 – 438HelicalSequence analysisAdd BLAST21
Topological domaini439 – 913CytoplasmicSequence analysisAdd BLAST475

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105R → A: Inhibits collagen-induced phosphorylation. 1 Publication1
Mutagenesisi211N → A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. 1 Publication1
Mutagenesisi211N → 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. 1 Publication1
Mutagenesisi213S → A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. 1 Publication1
Mutagenesisi260N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen. 1 Publication1
Mutagenesisi371N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen. 1 Publication1
Mutagenesisi379T → 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. 1 Publication1
Mutagenesisi393T → 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. 1 Publication1
Mutagenesisi394N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen. 1 Publication1
Mutagenesisi655K → A: Loss of kinase activity. Complete loss of the collagen-independent constitutive activation; when associated with Q-211. 1 Publication1
Mutagenesisi707G → A: Confers over 20-fold resistance to the ability of an inhibitor to inhibit autophosphorylation. 1 Publication1
Mutagenesisi740Y → F: Abolishes interaction with PTPN11. 1 Publication1

Organism-specific databases

DisGeNETi780.
OpenTargetsiENSG00000137332.
ENSG00000204580.
ENSG00000215522.
ENSG00000230456.
ENSG00000234078.
PharmGKBiPA24348.

Chemistry databases

ChEMBLiCHEMBL5319.
DrugBankiDB00619. Imatinib.
GuidetoPHARMACOLOGYi1843.

Polymorphism and mutation databases

BioMutaiDDR1.
DMDMi729008.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000001674219 – 913Epithelial discoidin domain-containing receptor 1Add BLAST895

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 185PROSITE-ProRule annotation1 Publication
Disulfide bondi74 ↔ 177PROSITE-ProRule annotation1 Publication
Glycosylationi211N-linked (GlcNAc...)2 Publications1
Glycosylationi260N-linked (GlcNAc...)2 Publications1
Disulfide bondi303 ↔ 348PROSITE-ProRule annotation1 Publication
Glycosylationi370N-linked (GlcNAc...)Sequence analysis1
Glycosylationi371N-linked (GlcNAc...)Sequence analysis1
Glycosylationi394N-linked (GlcNAc...)Sequence analysis1
Modified residuei484Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei513Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei520Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei631PhosphoserineCombined sources1
Modified residuei740Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei792Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei796Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei797Phosphotyrosine; by autocatalysis1 Publication1

Post-translational modificationi

Autophosphorylated in response to fibrillar collagen binding.
Glycosylation of Asn-211, but apparently not of Asn-260, Asn-371, or Asn-394, prevents autophosphorylation from occurring in the absence of collagen.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ08345.
PaxDbiQ08345.
PeptideAtlasiQ08345.
PRIDEiQ08345.

PTM databases

iPTMnetiQ08345.
PhosphoSitePlusiQ08345.

Miscellaneous databases

PMAP-CutDBQ2L6H3.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiENSG00000137332.
CleanExiHS_DDR1.
ExpressionAtlasiQ08345. baseline and differential.
GenevisibleiQ08345. HS.

Organism-specific databases

HPAiCAB010162.
CAB025656.
HPA057194.

Interactioni

Subunit structurei

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 NCK2.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK2O436393EBI-711879,EBI-713635
PTPN11Q061244EBI-711879,EBI-297779

GO - Molecular functioni

  • collagen binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107234. 15 interactors.
DIPiDIP-39698N.
IntActiQ08345. 13 interactors.
MINTiMINT-1383336.
STRINGi9606.ENSP00000365759.

Chemistry databases

BindingDBiQ08345.

Structurei

Secondary structure

1913
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni37 – 39Combined sources3
Helixi44 – 46Combined sources3
Beta strandi47 – 50Combined sources4
Helixi55 – 57Combined sources3
Helixi59 – 61Combined sources3
Turni68 – 70Combined sources3
Beta strandi71 – 73Combined sources3
Beta strandi87 – 103Combined sources17
Helixi107 – 109Combined sources3
Beta strandi116 – 127Combined sources12
Beta strandi129 – 131Combined sources3
Beta strandi145 – 148Combined sources4
Beta strandi151 – 169Combined sources19
Beta strandi171 – 173Combined sources3
Beta strandi178 – 186Combined sources9
Beta strandi191 – 197Combined sources7
Beta strandi204 – 206Combined sources3
Beta strandi217 – 220Combined sources4
Beta strandi223 – 226Combined sources4
Helixi230 – 232Combined sources3
Beta strandi245 – 248Combined sources4
Turni251 – 254Combined sources4
Beta strandi256 – 259Combined sources4
Helixi260 – 262Combined sources3
Beta strandi266 – 287Combined sources22
Helixi291 – 293Combined sources3
Beta strandi299 – 306Combined sources8
Beta strandi308 – 312Combined sources5
Beta strandi314 – 316Combined sources3
Beta strandi318 – 321Combined sources4
Beta strandi332 – 351Combined sources20
Beta strandi353 – 367Combined sources15
Helixi607 – 609Combined sources3
Beta strandi610 – 619Combined sources10
Beta strandi622 – 631Combined sources10
Helixi632 – 634Combined sources3
Beta strandi637 – 639Combined sources3
Beta strandi651 – 657Combined sources7
Helixi663 – 678Combined sources16
Beta strandi687 – 691Combined sources5
Beta strandi693 – 696Combined sources4
Beta strandi698 – 702Combined sources5
Helixi709 – 714Combined sources6
Helixi740 – 759Combined sources20
Helixi769 – 771Combined sources3
Beta strandi772 – 774Combined sources3
Helixi776 – 778Combined sources3
Beta strandi780 – 782Combined sources3
Helixi790 – 795Combined sources6
Beta strandi797 – 800Combined sources4
Beta strandi803 – 805Combined sources3
Helixi807 – 809Combined sources3
Helixi812 – 817Combined sources6
Helixi822 – 837Combined sources16
Turni838 – 840Combined sources3
Turni844 – 847Combined sources4
Helixi850 – 862Combined sources13
Helixi878 – 887Combined sources10
Helixi892 – 894Combined sources3
Helixi898 – 906Combined sources9
Turni907 – 909Combined sources3
Helixi910 – 912Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZOSX-ray1.92A/B601-913[»]
4AG4X-ray2.80A29-367[»]
4BKJX-ray1.70A/B601-913[»]
4CKRX-ray2.20A601-913[»]
5BVKX-ray2.29A595-913[»]
5BVNX-ray2.21A595-913[»]
5BVOX-ray1.98A595-913[»]
5BVWX-ray1.94A595-913[»]
5FDPX-ray2.25A601-913[»]
ProteinModelPortaliQ08345.
SMRiQ08345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 185F5/8 type CPROSITE-ProRule annotationAdd BLAST155
Domaini610 – 905Protein kinasePROSITE-ProRule annotationAdd BLAST296

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni192 – 367DS-like domainAdd BLAST176

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi481 – 484PPxY motif4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi377 – 415Gly/Pro-richAdd BLAST39
Compositional biasi476 – 601Gly/Pro-richAdd BLAST126

Domaini

The Gly/Pro-rich domains may be required for an unusual geometry of interaction with ligand or substrates.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 1 F5/8 type C domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1094. Eukaryota.
ENOG410XQAI. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000043102.
HOVERGENiHBG005461.
InParanoidiQ08345.
KOiK05124.
OMAiCEVENPQ.
OrthoDBiEOG091G05Y8.
PhylomeDBiQ08345.
TreeFamiTF317840.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR029553. DDR1/DDR2.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PANTHERiPTHR24416:SF295. PTHR24416:SF295. 5 hits.
PfamiPF00754. F5_F8_type_C. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00231. FA58C. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q08345-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS
60 70 80 90 100
SSWSDSTAAR HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV
110 120 130 140 150
GTQGRHAGGL GKEFSRSYRL RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV
160 170 180 190 200
VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV ELYGCLWRDG LLSYTAPVGQ
210 220 230 240 250
TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD FRKSQELRVW
260 270 280 290 300
PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG
310 320 330 340 350
VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF
360 370 380 390 400
LFAGPWLLFS EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL
410 420 430 440 450
EPRGQQPVAK AEGSPTAILI GCLVAIILLL LLIIALMLWR LHWRRLLSKA
460 470 480 490 500
ERRVLEEELT VHLSVPGDTI LINNRPGPRE PPPYQEPRPR GNPPHSAPCV
510 520 530 540 550
PNGSALLLSN PAYRLLLATY ARPPRGPGPP TPAWAKPTNT QAYSGDYMEP
560 570 580 590 600
EKPGAPLLPP PPQNSVPHYA EADIVTLQGV TGGNTYAVPA LPPGAVGDGP
610 620 630 640 650
PRVDFPRSRL RFKEKLGEGQ FGEVHLCEVD SPQDLVSLDF PLNVRKGHPL
660 670 680 690 700
LVAVKILRPD ATKNARNDFL KEVKIMSRLK DPNIIRLLGV CVQDDPLCMI
710 720 730 740 750
TDYMENGDLN QFLSAHQLED KAAEGAPGDG QAAQGPTISY PMLLHVAAQI
760 770 780 790 800
ASGMRYLATL NFVHRDLATR NCLVGENFTI KIADFGMSRN LYAGDYYRVQ
810 820 830 840 850
GRAVLPIRWM AWECILMGKF TTASDVWAFG VTLWEVLMLC RAQPFGQLTD
860 870 880 890 900
EQVIENAGEF FRDQGRQVYL SRPPACPQGL YELMLRCWSR ESEQRPPFSQ
910
LHRFLAEDAL NTV
Length:913
Mass (Da):101,128
Last modified:February 1, 1995 - v1
Checksum:iC96913EA906C481E
GO
Isoform 2 (identifier: Q08345-2) [UniParc]FASTAAdd to basket
Also known as: CAK II, DDR1a, Short

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

Show »
Length:876
Mass (Da):97,174
Checksum:iE02881598CC7CD0B
GO
Isoform 3 (identifier: Q08345-4) [UniParc]FASTAAdd to basket
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.
Show »
Length:243
Mass (Da):27,130
Checksum:i36872B8FB29835D0
GO
Isoform 4 (identifier: Q08345-5) [UniParc]FASTAAdd to basket

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

Show »
Length:919
Mass (Da):101,796
Checksum:i2094224F6AE943F5
GO
Isoform 5 (identifier: Q08345-6) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:894
Mass (Da):99,064
Checksum:iD46EECFC939B7585
GO

Sequence cautioni

The sequence ACF47649 differs from that shown. Reason: Erroneous termination at position 287. Translated as Cys.Curated
The sequence BAE06103 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti94L → V in AAA02866 (PubMed:8390675).Curated1
Sequence conflicti94L → V in AAC50917 (PubMed:8977099).Curated1
Sequence conflicti165R → H in AAH70070 (PubMed:15489334).Curated1
Sequence conflicti285 – 286VH → MW in ACF47649 (PubMed:18593464).Curated2
Sequence conflicti741P → Q in AAH70070 (PubMed:15489334).Curated1
Sequence conflicti847 – 867QLTDE…DQGRQ → SAHRRAGHRERGGVLPGPGP A in CAA66871 (PubMed:8796349).CuratedAdd BLAST21

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04149217S → G.1 PublicationCorresponds to variant rs55901302dbSNPEnsembl.1
Natural variantiVAR_041493100V → A.1 PublicationCorresponds to variant rs34544756dbSNPEnsembl.1
Natural variantiVAR_041494169R → Q.1 PublicationCorresponds to variant rs55980643dbSNPEnsembl.1
Natural variantiVAR_041495170A → D.1 PublicationCorresponds to variant rs56231803dbSNPEnsembl.1
Natural variantiVAR_041496306R → W.1 PublicationCorresponds to variant rs56024191dbSNPEnsembl.1
Natural variantiVAR_041497496S → A in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_049716833L → V.2 PublicationsCorresponds to variant rs2524235dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0435821M → MSLPRCCPHPLRPEGSGAM in isoform 5. 1 Publication1
Alternative sequenceiVSP_036916190 – 243GLLSY…DDFRK → CSMGVWASWQMVWWGWMTLG RVRSCGSGQAMTMWDGATTA SPVAMWRWSLSLTG in isoform 3. 1 PublicationAdd BLAST54
Alternative sequenceiVSP_036917244 – 913Missing in isoform 3. 1 PublicationAdd BLAST670
Alternative sequenceiVSP_002953506 – 542Missing in isoform 2 and isoform 5. 7 PublicationsAdd BLAST37
Alternative sequenceiVSP_038057665A → ASFSLFS in isoform 4. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34385.1. [Q08345-1]
CCDS4690.1. [Q08345-2]
CCDS47396.1. [Q08345-5]
CCDS56411.1. [Q08345-6]
PIRiA48280.
A49508.
RefSeqiNP_001189450.1. NM_001202521.1.
NP_001189451.1. NM_001202522.1.
NP_001189452.1. NM_001202523.1. [Q08345-6]
NP_001284581.1. NM_001297652.1. [Q08345-2]
NP_001284582.1. NM_001297653.1. [Q08345-2]
NP_001284583.1. NM_001297654.1. [Q08345-1]
NP_001945.3. NM_001954.4. [Q08345-2]
NP_054699.2. NM_013993.2. [Q08345-1]
NP_054700.2. NM_013994.2. [Q08345-5]
UniGeneiHs.631988.

Genome annotation databases

EnsembliENST00000259875; ENSP00000259875; ENSG00000137332. [Q08345-2]
ENST00000324771; ENSP00000318217; ENSG00000204580. [Q08345-1]
ENST00000376567; ENSP00000365751; ENSG00000204580. [Q08345-2]
ENST00000376568; ENSP00000365752; ENSG00000204580. [Q08345-1]
ENST00000376569; ENSP00000365753; ENSG00000204580. [Q08345-2]
ENST00000376570; ENSP00000365754; ENSG00000204580. [Q08345-2]
ENST00000376575; ENSP00000365759; ENSG00000204580. [Q08345-4]
ENST00000383377; ENSP00000372868; ENSG00000137332. [Q08345-1]
ENST00000400410; ENSP00000383261; ENSG00000137332. [Q08345-2]
ENST00000400411; ENSP00000383262; ENSG00000137332. [Q08345-2]
ENST00000400414; ENSP00000383265; ENSG00000137332. [Q08345-1]
ENST00000400486; ENSP00000383334; ENSG00000215522. [Q08345-2]
ENST00000400488; ENSP00000383336; ENSG00000215522. [Q08345-2]
ENST00000400489; ENSP00000383337; ENSG00000215522. [Q08345-2]
ENST00000400491; ENSP00000383338; ENSG00000215522. [Q08345-1]
ENST00000400492; ENSP00000383339; ENSG00000215522. [Q08345-1]
ENST00000412329; ENSP00000391805; ENSG00000230456. [Q08345-1]
ENST00000415092; ENSP00000405540; ENSG00000230456. [Q08345-2]
ENST00000418800; ENSP00000407699; ENSG00000204580. [Q08345-2]
ENST00000419412; ENSP00000416183; ENSG00000234078. [Q08345-2]
ENST00000421229; ENSP00000415730; ENSG00000234078. [Q08345-2]
ENST00000427053; ENSP00000416145; ENSG00000230456. [Q08345-2]
ENST00000429699; ENSP00000401397; ENSG00000234078. [Q08345-1]
ENST00000430933; ENSP00000397769; ENSG00000234078. [Q08345-1]
ENST00000449518; ENSP00000414285; ENSG00000230456. [Q08345-1]
ENST00000452441; ENSP00000405039; ENSG00000204580. [Q08345-1]
ENST00000453510; ENSP00000401208; ENSG00000230456. [Q08345-2]
ENST00000454612; ENSP00000406091; ENSG00000204580. [Q08345-2]
ENST00000454774; ENSP00000400393; ENSG00000234078. [Q08345-2]
ENST00000482873; ENSP00000421978; ENSG00000204580. [Q08345-4]
ENST00000508312; ENSP00000422442; ENSG00000204580. [Q08345-6]
ENST00000513240; ENSP00000427552; ENSG00000204580. [Q08345-5]
ENST00000548133; ENSP00000449611; ENSG00000230456. [Q08345-1]
ENST00000548962; ENSP00000448115; ENSG00000230456. [Q08345-6]
ENST00000549026; ENSP00000449238; ENSG00000215522. [Q08345-6]
ENST00000550384; ENSP00000447474; ENSG00000234078. [Q08345-6]
ENST00000550395; ENSP00000449255; ENSG00000215522. [Q08345-1]
ENST00000552068; ENSP00000449190; ENSG00000234078. [Q08345-1]
ENST00000552721; ENSP00000449307; ENSG00000137332. [Q08345-6]
ENST00000553015; ENSP00000448377; ENSG00000137332. [Q08345-1]
ENST00000617572; ENSP00000479195; ENSG00000215522. [Q08345-4]
ENST00000618059; ENSP00000479204; ENSG00000234078. [Q08345-4]
ENST00000620318; ENSP00000484588; ENSG00000137332. [Q08345-4]
ENST00000621544; ENSP00000484013; ENSG00000230456. [Q08345-4]
GeneIDi780.
KEGGihsa:780.
UCSCiuc003nrq.4. human. [Q08345-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34385.1. [Q08345-1]
CCDS4690.1. [Q08345-2]
CCDS47396.1. [Q08345-5]
CCDS56411.1. [Q08345-6]
PIRiA48280.
A49508.
RefSeqiNP_001189450.1. NM_001202521.1.
NP_001189451.1. NM_001202522.1.
NP_001189452.1. NM_001202523.1. [Q08345-6]
NP_001284581.1. NM_001297652.1. [Q08345-2]
NP_001284582.1. NM_001297653.1. [Q08345-2]
NP_001284583.1. NM_001297654.1. [Q08345-1]
NP_001945.3. NM_001954.4. [Q08345-2]
NP_054699.2. NM_013993.2. [Q08345-1]
NP_054700.2. NM_013994.2. [Q08345-5]
UniGeneiHs.631988.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZOSX-ray1.92A/B601-913[»]
4AG4X-ray2.80A29-367[»]
4BKJX-ray1.70A/B601-913[»]
4CKRX-ray2.20A601-913[»]
5BVKX-ray2.29A595-913[»]
5BVNX-ray2.21A595-913[»]
5BVOX-ray1.98A595-913[»]
5BVWX-ray1.94A595-913[»]
5FDPX-ray2.25A601-913[»]
ProteinModelPortaliQ08345.
SMRiQ08345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107234. 15 interactors.
DIPiDIP-39698N.
IntActiQ08345. 13 interactors.
MINTiMINT-1383336.
STRINGi9606.ENSP00000365759.

Chemistry databases

BindingDBiQ08345.
ChEMBLiCHEMBL5319.
DrugBankiDB00619. Imatinib.
GuidetoPHARMACOLOGYi1843.

PTM databases

iPTMnetiQ08345.
PhosphoSitePlusiQ08345.

Polymorphism and mutation databases

BioMutaiDDR1.
DMDMi729008.

Proteomic databases

MaxQBiQ08345.
PaxDbiQ08345.
PeptideAtlasiQ08345.
PRIDEiQ08345.

Protocols and materials databases

DNASUi780.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259875; ENSP00000259875; ENSG00000137332. [Q08345-2]
ENST00000324771; ENSP00000318217; ENSG00000204580. [Q08345-1]
ENST00000376567; ENSP00000365751; ENSG00000204580. [Q08345-2]
ENST00000376568; ENSP00000365752; ENSG00000204580. [Q08345-1]
ENST00000376569; ENSP00000365753; ENSG00000204580. [Q08345-2]
ENST00000376570; ENSP00000365754; ENSG00000204580. [Q08345-2]
ENST00000376575; ENSP00000365759; ENSG00000204580. [Q08345-4]
ENST00000383377; ENSP00000372868; ENSG00000137332. [Q08345-1]
ENST00000400410; ENSP00000383261; ENSG00000137332. [Q08345-2]
ENST00000400411; ENSP00000383262; ENSG00000137332. [Q08345-2]
ENST00000400414; ENSP00000383265; ENSG00000137332. [Q08345-1]
ENST00000400486; ENSP00000383334; ENSG00000215522. [Q08345-2]
ENST00000400488; ENSP00000383336; ENSG00000215522. [Q08345-2]
ENST00000400489; ENSP00000383337; ENSG00000215522. [Q08345-2]
ENST00000400491; ENSP00000383338; ENSG00000215522. [Q08345-1]
ENST00000400492; ENSP00000383339; ENSG00000215522. [Q08345-1]
ENST00000412329; ENSP00000391805; ENSG00000230456. [Q08345-1]
ENST00000415092; ENSP00000405540; ENSG00000230456. [Q08345-2]
ENST00000418800; ENSP00000407699; ENSG00000204580. [Q08345-2]
ENST00000419412; ENSP00000416183; ENSG00000234078. [Q08345-2]
ENST00000421229; ENSP00000415730; ENSG00000234078. [Q08345-2]
ENST00000427053; ENSP00000416145; ENSG00000230456. [Q08345-2]
ENST00000429699; ENSP00000401397; ENSG00000234078. [Q08345-1]
ENST00000430933; ENSP00000397769; ENSG00000234078. [Q08345-1]
ENST00000449518; ENSP00000414285; ENSG00000230456. [Q08345-1]
ENST00000452441; ENSP00000405039; ENSG00000204580. [Q08345-1]
ENST00000453510; ENSP00000401208; ENSG00000230456. [Q08345-2]
ENST00000454612; ENSP00000406091; ENSG00000204580. [Q08345-2]
ENST00000454774; ENSP00000400393; ENSG00000234078. [Q08345-2]
ENST00000482873; ENSP00000421978; ENSG00000204580. [Q08345-4]
ENST00000508312; ENSP00000422442; ENSG00000204580. [Q08345-6]
ENST00000513240; ENSP00000427552; ENSG00000204580. [Q08345-5]
ENST00000548133; ENSP00000449611; ENSG00000230456. [Q08345-1]
ENST00000548962; ENSP00000448115; ENSG00000230456. [Q08345-6]
ENST00000549026; ENSP00000449238; ENSG00000215522. [Q08345-6]
ENST00000550384; ENSP00000447474; ENSG00000234078. [Q08345-6]
ENST00000550395; ENSP00000449255; ENSG00000215522. [Q08345-1]
ENST00000552068; ENSP00000449190; ENSG00000234078. [Q08345-1]
ENST00000552721; ENSP00000449307; ENSG00000137332. [Q08345-6]
ENST00000553015; ENSP00000448377; ENSG00000137332. [Q08345-1]
ENST00000617572; ENSP00000479195; ENSG00000215522. [Q08345-4]
ENST00000618059; ENSP00000479204; ENSG00000234078. [Q08345-4]
ENST00000620318; ENSP00000484588; ENSG00000137332. [Q08345-4]
ENST00000621544; ENSP00000484013; ENSG00000230456. [Q08345-4]
GeneIDi780.
KEGGihsa:780.
UCSCiuc003nrq.4. human. [Q08345-1]

Organism-specific databases

CTDi780.
DisGeNETi780.
GeneCardsiDDR1.
HGNCiHGNC:2730. DDR1.
HPAiCAB010162.
CAB025656.
HPA057194.
MIMi600408. gene.
neXtProtiNX_Q08345.
OpenTargetsiENSG00000137332.
ENSG00000204580.
ENSG00000215522.
ENSG00000230456.
ENSG00000234078.
PharmGKBiPA24348.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1094. Eukaryota.
ENOG410XQAI. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000043102.
HOVERGENiHBG005461.
InParanoidiQ08345.
KOiK05124.
OMAiCEVENPQ.
OrthoDBiEOG091G05Y8.
PhylomeDBiQ08345.
TreeFamiTF317840.

Enzyme and pathway databases

BioCyciZFISH:HS06318-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-3000171. Non-integrin membrane-ECM interactions.
SignaLinkiQ08345.
SIGNORiQ08345.

Miscellaneous databases

ChiTaRSiDDR1. human.
GeneWikiiDDR1.
GenomeRNAii780.
PMAP-CutDBQ2L6H3.
PROiQ08345.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137332.
CleanExiHS_DDR1.
ExpressionAtlasiQ08345. baseline and differential.
GenevisibleiQ08345. HS.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR029553. DDR1/DDR2.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PANTHERiPTHR24416:SF295. PTHR24416:SF295. 5 hits.
PfamiPF00754. F5_F8_type_C. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00231. FA58C. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDDR1_HUMAN
AccessioniPrimary (citable) accession number: Q08345
Secondary accession number(s): B5A975
, B5A976, B7Z2K0, Q14196, Q16562, Q2L6H3, Q4LE50, Q5ST11, Q5ST12, Q6NSK4, Q9UD35, Q9UD36, Q9UD37, Q9UD86, Q9UDL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 189 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Caution

The mutant Gln-371 studied is still likely to be glycosylated at Asn-370, but study did not include mutagenesis of Asn-370.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  8. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.