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Q08345

- DDR1_HUMAN

UniProt

Q08345 - DDR1_HUMAN

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Protein
Epithelial discoidin domain-containing receptor 1
Gene
DDR1, CAK, EDDR1, NEP, NTRK4, PTK3A, RTK6, TRKE
Organism
Homo sapiens (Human)
Status
Reviewed - 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 PTPN11.9 Publications

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi211 – 2111Calcium 1; via carbonyl oxygen
Metal bindingi230 – 2301Calcium 1
Metal bindingi230 – 2301Calcium 2; via carbonyl oxygen
Metal bindingi233 – 2331Calcium 2
Metal bindingi235 – 2351Calcium 2; via carbonyl oxygen
Metal bindingi253 – 2531Calcium 1; via carbonyl oxygen
Metal bindingi255 – 2551Calcium 1; via carbonyl oxygen
Metal bindingi360 – 3601Calcium 2; via carbonyl oxygen
Metal bindingi361 – 3611Calcium 2
Binding sitei655 – 6551ATP
Active sitei766 – 7661Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi616 – 6249ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. collagen binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: UniProtKB
  5. protein tyrosine kinase collagen receptor activity Source: UniProtKB
  6. transmembrane receptor protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

  1. branching involved in mammary gland duct morphogenesis Source: Ensembl
  2. cell adhesion Source: ProtInc
  3. collagen-activated tyrosine kinase receptor signaling pathway Source: UniProtKB
  4. ear development Source: Ensembl
  5. embryo implantation Source: Ensembl
  6. extracellular matrix organization Source: Reactome
  7. lactation Source: UniProtKB-KW
  8. mammary gland alveolus development Source: Ensembl
  9. negative regulation of cell proliferation Source: Ensembl
  10. peptidyl-tyrosine autophosphorylation Source: UniProtKB
  11. protein autophosphorylation Source: UniProtKB
  12. regulation of cell growth Source: Ensembl
  13. regulation of cell-matrix adhesion Source: Ensembl
  14. regulation of extracellular matrix disassembly Source: UniProtKB
  15. smooth muscle cell migration Source: UniProtKB
  16. smooth muscle cell-matrix adhesion Source: UniProtKB
  17. 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

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
SignaLinkiQ08345.

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
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:2730. DDR1.

Subcellular locationi

Isoform 1 : Cell membrane; Single-pass type I membrane protein 2 Publications
Isoform 2 : Cell membrane; Single-pass type I membrane protein 2 Publications
Isoform 3 : Secreted Reviewed prediction 2 Publications
Isoform 4 : Cell membrane; Single-pass type I membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 417397Extracellular Reviewed prediction
Add
BLAST
Transmembranei418 – 43821Helical; Reviewed prediction
Add
BLAST
Topological domaini439 – 913475Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. extracellular space Source: UniProt
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: Reactome
  5. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051R → A: Inhibits collagen-induced phosphorylation.
Mutagenesisi211 – 2111N → A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation.
Mutagenesisi211 – 2111N → 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.
Mutagenesisi213 – 2131S → A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation.
Mutagenesisi260 – 2601N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen.
Mutagenesisi371 – 3711N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen.
Mutagenesisi379 – 3791T → 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.
Mutagenesisi393 – 3931T → 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.
Mutagenesisi394 – 3941N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen.
Mutagenesisi655 – 6551K → A: Loss of kinase activity. Complete loss of the collagen-independent constitutive activation; when associated with Q-211.
Mutagenesisi707 – 7071G → A: Confers over 20-fold resistance to the ability of an inhibitor to inhibit autophosphorylation.
Mutagenesisi740 – 7401Y → F: Abolishes interaction with PTPN11. 1 Publication

Organism-specific databases

PharmGKBiPA24348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 913895Epithelial discoidin domain-containing receptor 1
PRO_0000016742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 1851 Publication
Disulfide bondi74 ↔ 1771 Publication
Glycosylationi211 – 2111N-linked (GlcNAc...)
Glycosylationi260 – 2601N-linked (GlcNAc...)
Disulfide bondi303 ↔ 3481 Publication
Glycosylationi370 – 3701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi371 – 3711N-linked (GlcNAc...) Reviewed prediction
Glycosylationi394 – 3941N-linked (GlcNAc...) Reviewed prediction
Modified residuei484 – 4841Phosphotyrosine; by autocatalysis
Modified residuei513 – 5131Phosphotyrosine; by autocatalysis1 Publication
Modified residuei520 – 5201Phosphotyrosine; by autocatalysis
Modified residuei631 – 6311Phosphoserine1 Publication
Modified residuei740 – 7401Phosphotyrosine; by autocatalysis Inferred
Modified residuei792 – 7921Phosphotyrosine; by autocatalysis
Modified residuei796 – 7961Phosphotyrosine; by autocatalysis
Modified residuei797 – 7971Phosphotyrosine; by autocatalysis

Post-translational modificationi

Autophosphorylated in response to fibrillar collagen binding.4 Publications
Glycosylation of Asn-211, but apparently not of Asn-260, Asn-371, or Asn-394, prevents autophosphorylation from occurring in the absence of collagen.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ08345.
PaxDbiQ08345.
PRIDEiQ08345.

PTM databases

PhosphoSiteiQ08345.

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

ArrayExpressiQ08345.
BgeeiQ08345.
CleanExiHS_DDR1.
GenevestigatoriQ08345.

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 NCK2.7 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi107234. 10 interactions.
DIPiDIP-39698N.
IntActiQ08345. 12 interactions.
MINTiMINT-1383336.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni37 – 393
Helixi44 – 463
Beta strandi47 – 504
Helixi55 – 573
Helixi59 – 613
Turni68 – 703
Beta strandi71 – 733
Beta strandi87 – 10317
Helixi107 – 1093
Beta strandi116 – 12712
Beta strandi129 – 1313
Beta strandi145 – 1484
Beta strandi151 – 16919
Beta strandi171 – 1733
Beta strandi178 – 1869
Beta strandi191 – 1977
Beta strandi204 – 2063
Beta strandi217 – 2204
Beta strandi223 – 2264
Helixi230 – 2323
Beta strandi245 – 2484
Turni251 – 2544
Beta strandi256 – 2594
Helixi260 – 2623
Beta strandi266 – 28722
Helixi291 – 2933
Beta strandi299 – 3068
Beta strandi308 – 3125
Beta strandi314 – 3163
Beta strandi318 – 3214
Beta strandi332 – 35120
Beta strandi353 – 36715
Helixi607 – 6093
Beta strandi610 – 61910
Beta strandi622 – 63110
Helixi632 – 6343
Beta strandi637 – 6393
Beta strandi651 – 6577
Helixi663 – 67816
Beta strandi687 – 6915
Beta strandi693 – 6964
Beta strandi698 – 7025
Helixi709 – 7146
Helixi740 – 75920
Helixi769 – 7713
Beta strandi772 – 7743
Helixi776 – 7783
Beta strandi780 – 7823
Helixi790 – 7956
Beta strandi797 – 8004
Beta strandi803 – 8053
Helixi807 – 8093
Helixi812 – 8176
Helixi822 – 83716
Turni838 – 8403
Turni844 – 8474
Helixi850 – 86213
Helixi878 – 88710
Helixi892 – 8943
Helixi898 – 9069
Turni907 – 9093
Helixi910 – 9123

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZOSX-ray1.92A/B601-913[»]
4AG4X-ray2.80A29-367[»]
4BKJX-ray1.70A/B601-913[»]
4CKRX-ray2.20A601-913[»]
ProteinModelPortaliQ08345.
SMRiQ08345. Positions 30-367, 602-913.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 185155F5/8 type C
Add
BLAST
Domaini610 – 905296Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 367176DS-like domain
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi481 – 4844PPxY motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi377 – 41539Gly/Pro-rich
Add
BLAST
Compositional biasi476 – 601126Gly/Pro-rich
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 F5/8 type C domain.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000043102.
HOVERGENiHBG005461.
InParanoidiQ08345.
KOiK05124.
OMAiCRFLFAG.
PhylomeDBiQ08345.
TreeFamiTF317840.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR029566. DDR1.
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:SF65. PTHR24416:SF65. 1 hit.
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. Align

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

MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS    50
SSWSDSTAAR HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV 100
GTQGRHAGGL GKEFSRSYRL RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV 150
VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV ELYGCLWRDG LLSYTAPVGQ 200
TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD FRKSQELRVW 250
PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG 300
VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF 350
LFAGPWLLFS EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL 400
EPRGQQPVAK AEGSPTAILI GCLVAIILLL LLIIALMLWR LHWRRLLSKA 450
ERRVLEEELT VHLSVPGDTI LINNRPGPRE PPPYQEPRPR GNPPHSAPCV 500
PNGSALLLSN PAYRLLLATY ARPPRGPGPP TPAWAKPTNT QAYSGDYMEP 550
EKPGAPLLPP PPQNSVPHYA EADIVTLQGV TGGNTYAVPA LPPGAVGDGP 600
PRVDFPRSRL RFKEKLGEGQ FGEVHLCEVD SPQDLVSLDF PLNVRKGHPL 650
LVAVKILRPD ATKNARNDFL KEVKIMSRLK DPNIIRLLGV CVQDDPLCMI 700
TDYMENGDLN QFLSAHQLED KAAEGAPGDG QAAQGPTISY PMLLHVAAQI 750
ASGMRYLATL NFVHRDLATR NCLVGENFTI KIADFGMSRN LYAGDYYRVQ 800
GRAVLPIRWM AWECILMGKF TTASDVWAFG VTLWEVLMLC RAQPFGQLTD 850
EQVIENAGEF FRDQGRQVYL SRPPACPQGL YELMLRCWSR ESEQRPPFSQ 900
LHRFLAEDAL NTV 913
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 BAE06103.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence ACF47649.1 differs from that shown. Reason: Erroneous termination at position 287. Translated as Cys.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171S → G.1 Publication
Corresponds to variant rs55901302 [ dbSNP | Ensembl ].
VAR_041492
Natural varianti100 – 1001V → A.1 Publication
Corresponds to variant rs34544756 [ dbSNP | Ensembl ].
VAR_041493
Natural varianti169 – 1691R → Q.1 Publication
Corresponds to variant rs55980643 [ dbSNP | Ensembl ].
VAR_041494
Natural varianti170 – 1701A → D.1 Publication
Corresponds to variant rs56231803 [ dbSNP | Ensembl ].
VAR_041495
Natural varianti306 – 3061R → W.1 Publication
Corresponds to variant rs56024191 [ dbSNP | Ensembl ].
VAR_041496
Natural varianti496 – 4961S → A in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_041497
Natural varianti833 – 8331L → V.2 Publications
Corresponds to variant rs2524235 [ dbSNP | Ensembl ].
VAR_049716

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MSLPRCCPHPLRPEGSGAM in isoform 5.
VSP_043582
Alternative sequencei190 – 24354GLLSY…DDFRK → CSMGVWASWQMVWWGWMTLG RVRSCGSGQAMTMWDGATTA SPVAMWRWSLSLTG in isoform 3.
VSP_036916Add
BLAST
Alternative sequencei244 – 913670Missing in isoform 3.
VSP_036917Add
BLAST
Alternative sequencei506 – 54237Missing in isoform 2 and isoform 5.
VSP_002953Add
BLAST
Alternative sequencei665 – 6651A → ASFSLFS in isoform 4.
VSP_038057

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → V in AAA02866. 1 Publication
Sequence conflicti94 – 941L → V in AAC50917. 1 Publication
Sequence conflicti165 – 1651R → H in AAH70070. 1 Publication
Sequence conflicti285 – 2862VH → MW in ACF47649. 1 Publication
Sequence conflicti741 – 7411P → Q in AAH70070. 1 Publication
Sequence conflicti847 – 86721QLTDE…DQGRQ → SAHRRAGHRERGGVLPGPGP A in CAA66871. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001945.3. NM_001954.4. [Q08345-2]
NP_054699.2. NM_013993.2. [Q08345-1]
NP_054700.2. NM_013994.2. [Q08345-5]
XP_005249443.1. XM_005249386.2. [Q08345-1]
XP_005249444.1. XM_005249387.2. [Q08345-2]
XP_005249446.1. XM_005249389.1. [Q08345-2]
XP_005272931.1. XM_005272874.2. [Q08345-1]
XP_005272932.1. XM_005272875.2. [Q08345-2]
XP_005272934.1. XM_005272877.1. [Q08345-2]
XP_005275085.1. XM_005275028.2. [Q08345-1]
XP_005275087.1. XM_005275030.2. [Q08345-2]
XP_005275088.1. XM_005275031.2. [Q08345-2]
XP_005275220.1. XM_005275163.2. [Q08345-1]
XP_005275221.1. XM_005275164.2. [Q08345-2]
XP_005275223.1. XM_005275166.1. [Q08345-2]
XP_005275515.1. XM_005275458.2. [Q08345-1]
XP_005275516.1. XM_005275459.2. [Q08345-2]
XP_005275518.1. XM_005275461.1. [Q08345-2]
XP_006715249.1. XM_006715186.1. [Q08345-1]
XP_006715250.1. XM_006715187.1. [Q08345-1]
XP_006715251.1. XM_006715188.1. [Q08345-1]
XP_006715252.1. XM_006715189.1. [Q08345-1]
XP_006725565.1. XM_006725502.1. [Q08345-1]
XP_006725566.1. XM_006725503.1. [Q08345-1]
XP_006725567.1. XM_006725504.1. [Q08345-1]
XP_006725568.1. XM_006725505.1. [Q08345-1]
XP_006725783.1. XM_006725720.1. [Q08345-1]
XP_006725891.1. XM_006725828.1. [Q08345-1]
XP_006725892.1. XM_006725829.1. [Q08345-1]
XP_006725893.1. XM_006725830.1. [Q08345-1]
XP_006725894.1. XM_006725831.1. [Q08345-1]
XP_006726081.1. XM_006726018.1. [Q08345-1]
XP_006726082.1. XM_006726019.1. [Q08345-1]
XP_006726083.1. XM_006726020.1. [Q08345-1]
XP_006726084.1. XM_006726021.1. [Q08345-1]
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. [Q08345-5]
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]
ENST00000446312; ENSP00000405998; ENSG00000204580. [Q08345-4]
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. [Q08345-5]
ENST00000548962; ENSP00000448115; ENSG00000230456. [Q08345-4]
ENST00000549026; ENSP00000449238; ENSG00000215522. [Q08345-4]
ENST00000550384; ENSP00000447474; ENSG00000234078. [Q08345-4]
ENST00000550395; ENSP00000449255; ENSG00000215522. [Q08345-5]
ENST00000552068; ENSP00000449190; ENSG00000234078. [Q08345-5]
ENST00000552721; ENSP00000449307; ENSG00000137332. [Q08345-4]
ENST00000553015; ENSP00000448377; ENSG00000137332. [Q08345-5]
GeneIDi780.
KEGGihsa:780.
UCSCiuc003nrq.3. human. [Q08345-2]
uc003nrr.3. human. [Q08345-1]
uc003nrv.3. human. [Q08345-5]
uc011dms.2. human. [Q08345-6]
uc011dmu.1. human. [Q08345-4]

Polymorphism databases

DMDMi729008.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS34385.1. [Q08345-1 ]
CCDS4690.1. [Q08345-2 ]
CCDS47396.1. [Q08345-5 ]
CCDS56411.1. [Q08345-6 ]
PIRi A48280.
A49508.
RefSeqi NP_001189450.1. NM_001202521.1.
NP_001189451.1. NM_001202522.1.
NP_001189452.1. NM_001202523.1. [Q08345-6 ]
NP_001945.3. NM_001954.4. [Q08345-2 ]
NP_054699.2. NM_013993.2. [Q08345-1 ]
NP_054700.2. NM_013994.2. [Q08345-5 ]
XP_005249443.1. XM_005249386.2. [Q08345-1 ]
XP_005249444.1. XM_005249387.2. [Q08345-2 ]
XP_005249446.1. XM_005249389.1. [Q08345-2 ]
XP_005272931.1. XM_005272874.2. [Q08345-1 ]
XP_005272932.1. XM_005272875.2. [Q08345-2 ]
XP_005272934.1. XM_005272877.1. [Q08345-2 ]
XP_005275085.1. XM_005275028.2. [Q08345-1 ]
XP_005275087.1. XM_005275030.2. [Q08345-2 ]
XP_005275088.1. XM_005275031.2. [Q08345-2 ]
XP_005275220.1. XM_005275163.2. [Q08345-1 ]
XP_005275221.1. XM_005275164.2. [Q08345-2 ]
XP_005275223.1. XM_005275166.1. [Q08345-2 ]
XP_005275515.1. XM_005275458.2. [Q08345-1 ]
XP_005275516.1. XM_005275459.2. [Q08345-2 ]
XP_005275518.1. XM_005275461.1. [Q08345-2 ]
XP_006715249.1. XM_006715186.1. [Q08345-1 ]
XP_006715250.1. XM_006715187.1. [Q08345-1 ]
XP_006715251.1. XM_006715188.1. [Q08345-1 ]
XP_006715252.1. XM_006715189.1. [Q08345-1 ]
XP_006725565.1. XM_006725502.1. [Q08345-1 ]
XP_006725566.1. XM_006725503.1. [Q08345-1 ]
XP_006725567.1. XM_006725504.1. [Q08345-1 ]
XP_006725568.1. XM_006725505.1. [Q08345-1 ]
XP_006725783.1. XM_006725720.1. [Q08345-1 ]
XP_006725891.1. XM_006725828.1. [Q08345-1 ]
XP_006725892.1. XM_006725829.1. [Q08345-1 ]
XP_006725893.1. XM_006725830.1. [Q08345-1 ]
XP_006725894.1. XM_006725831.1. [Q08345-1 ]
XP_006726081.1. XM_006726018.1. [Q08345-1 ]
XP_006726082.1. XM_006726019.1. [Q08345-1 ]
XP_006726083.1. XM_006726020.1. [Q08345-1 ]
XP_006726084.1. XM_006726021.1. [Q08345-1 ]
UniGenei Hs.631988.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZOS X-ray 1.92 A/B 601-913 [» ]
4AG4 X-ray 2.80 A 29-367 [» ]
4BKJ X-ray 1.70 A/B 601-913 [» ]
4CKR X-ray 2.20 A 601-913 [» ]
ProteinModelPortali Q08345.
SMRi Q08345. Positions 30-367, 602-913.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107234. 10 interactions.
DIPi DIP-39698N.
IntActi Q08345. 12 interactions.
MINTi MINT-1383336.

Chemistry

BindingDBi Q08345.
ChEMBLi CHEMBL5319.
DrugBanki DB00619. Imatinib.
GuidetoPHARMACOLOGYi 1843.

PTM databases

PhosphoSitei Q08345.

Polymorphism databases

DMDMi 729008.

Proteomic databases

MaxQBi Q08345.
PaxDbi Q08345.
PRIDEi Q08345.

Protocols and materials databases

DNASUi 780.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259875 ; 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 . [Q08345-5 ]
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 ]
ENST00000446312 ; ENSP00000405998 ; ENSG00000204580 . [Q08345-4 ]
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 . [Q08345-5 ]
ENST00000548962 ; ENSP00000448115 ; ENSG00000230456 . [Q08345-4 ]
ENST00000549026 ; ENSP00000449238 ; ENSG00000215522 . [Q08345-4 ]
ENST00000550384 ; ENSP00000447474 ; ENSG00000234078 . [Q08345-4 ]
ENST00000550395 ; ENSP00000449255 ; ENSG00000215522 . [Q08345-5 ]
ENST00000552068 ; ENSP00000449190 ; ENSG00000234078 . [Q08345-5 ]
ENST00000552721 ; ENSP00000449307 ; ENSG00000137332 . [Q08345-4 ]
ENST00000553015 ; ENSP00000448377 ; ENSG00000137332 . [Q08345-5 ]
GeneIDi 780.
KEGGi hsa:780.
UCSCi uc003nrq.3. human. [Q08345-2 ]
uc003nrr.3. human. [Q08345-1 ]
uc003nrv.3. human. [Q08345-5 ]
uc011dms.2. human. [Q08345-6 ]
uc011dmu.1. human. [Q08345-4 ]

Organism-specific databases

CTDi 780.
GeneCardsi GC06P030848.
GC06Pj30838.
GC06Pk30839.
GC06Pl30893.
GC06Pn30838.
HGNCi HGNC:2730. DDR1.
HPAi CAB010162.
CAB025656.
HPA057194.
MIMi 600408. gene.
neXtProti NX_Q08345.
PharmGKBi PA24348.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000043102.
HOVERGENi HBG005461.
InParanoidi Q08345.
KOi K05124.
OMAi CRFLFAG.
PhylomeDBi Q08345.
TreeFami TF317840.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
SignaLinki Q08345.

Miscellaneous databases

ChiTaRSi DDR1. human.
GeneWikii DDR1.
GenomeRNAii 780.
NextBioi 3152.
PMAP-CutDB Q2L6H3.
PROi Q08345.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q08345.
Bgeei Q08345.
CleanExi HS_DDR1.
Genevestigatori Q08345.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR029566. DDR1.
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 ]
PANTHERi PTHR24416:SF65. PTHR24416:SF65. 1 hit.
Pfami PF00754. F5_F8_type_C. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00231. FA58C. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS01285. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. "Glycosylation at Asn211 regulates the activation state of the discoidin domain receptor 1 (DDR1)."
    Fu H.L., Valiathan R.R., Payne L., Kumarasiri M., Mahasenan K.V., Mobashery S., Huang P., Fridman R.
    J. Biol. Chem. 289:9275-9287(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 480-490; 515-525 AND 790-798, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-484; TYR-513; TYR-520; TYR-792; TYR-796 AND TYR-797, GLYCOSYLATION AT ASN-211 AND ASN-260, MUTAGENESIS OF ARG-105; ASN-211; SER-213; ASN-260; ASN-371; THR-379; THR-393; ASN-394 AND LYS-655.
  16. "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.
  17. "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).
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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, SUBUNIT, CALCIUM-BINDING SITES, GLYCOSYLATION AT ASN-211 AND ASN-260, DISULFIDE BONDS.
  31. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 601-913 IN COMPLEX WITH INHIBITOR, AUTOPHOSPHORYLATION, MUTAGENESIS OF GLY-707.
  32. "Structural mechanisms determining inhibition of the collagen receptor DDR1 by selective and multi-targeted type II kinase inhibitors."
    Canning P., Tan L., Chu K., Lee S.W., Gray N.S., Bullock A.N.
    J. Mol. Biol. 426:2457-2470(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 601-913 IN COMPLEXES WITH INHIBITORS IMATINIB AND PONATINIB, ENZYME REGULATION, AUTOPHOSPHORYLATION.
  33. "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.

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: September 3, 2014
This is version 166 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

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

External Data

Dasty 3

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