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Q16832

- DDR2_HUMAN

UniProt

Q16832 - DDR2_HUMAN

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Protein

Discoidin domain-containing receptor 2

Gene

DDR2

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 differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing.8 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.2 PublicationsPROSITE-ProRule annotation

Enzyme regulationi

Present in an inactive state in the absence of collagen binding and phosphorylation by SRC. Tyrosine phosphorylation enhances the affinity for ATP and the catalytic activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei608 – 6081ATPCurated
Active sitei710 – 7101Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi569 – 5779ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. collagen binding Source: UniProtKB
  3. protein tyrosine kinase collagen receptor activity Source: UniProtKB
  4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB
  2. cell adhesion Source: ProtInc
  3. chondrocyte proliferation Source: UniProtKB
  4. collagen-activated tyrosine kinase receptor signaling pathway Source: UniProtKB
  5. collagen fibril organization Source: UniProtKB
  6. endochondral bone growth Source: UniProtKB
  7. extracellular matrix organization Source: Reactome
  8. ossification Source: UniProtKB-KW
  9. peptidyl-tyrosine phosphorylation Source: UniProtKB
  10. positive regulation of extracellular matrix disassembly Source: UniProtKB
  11. positive regulation of fibroblast migration Source: UniProtKB
  12. positive regulation of fibroblast proliferation Source: UniProtKB
  13. positive regulation of osteoblast differentiation Source: UniProtKB
  14. positive regulation of protein kinase activity Source: UniProtKB
  15. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  16. protein autophosphorylation Source: UniProtKB
  17. regulation of bone mineralization Source: UniProtKB
  18. regulation of extracellular matrix disassembly Source: UniProtKB
  19. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Osteogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
SignaLinkiQ16832.

Names & Taxonomyi

Protein namesi
Recommended name:
Discoidin domain-containing receptor 2 (EC:2.7.10.1)
Short name:
Discoidin domain receptor 2
Alternative name(s):
CD167 antigen-like family member B
Discoidin domain-containing receptor tyrosine kinase 2
Neurotrophic tyrosine kinase, receptor-related 3
Receptor protein-tyrosine kinase TKT
Tyrosine-protein kinase TYRO10
CD_antigen: CD167b
Gene namesi
Name:DDR2
Synonyms:NTRKR3, TKT, TYRO10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2731. DDR2.

Subcellular locationi

Cell membrane 3 Publications; Single-pass type I membrane protein 3 Publications

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. focal adhesion Source: UniProtKB
  4. integral component of plasma membrane Source: ProtInc
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Spondyloepimetaphyseal dysplasia short limb-hand type (SEMD-SL) [MIM:271665]: A bone disease characterized by short-limbed dwarfism, a narrow chest with pectus excavatum, brachydactyly in the hands and feet, a characteristic craniofacial appearance and premature calcifications. The radiological findings are distinctive and comprise short long bones throughout the skeleton with striking epiphyses that are stippled, flattened and fragmented and flared, irregular metaphyses. Platyspondyly in the spine with wide intervertebral spaces is observed and some vertebral bodies are pear-shaped with central humps, anterior protrusions and posterior scalloping.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti113 – 1131E → K in SEMD-SL; abolishes collagen binding. 1 Publication
VAR_065719
Natural varianti713 – 7131T → I in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
VAR_063050
Natural varianti726 – 7261I → R in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
VAR_063051
Natural varianti752 – 7521R → C in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
VAR_063052

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521W → A: Abolishes collagen binding. 2 Publications
Mutagenesisi608 – 6081K → A: Abolishes kinase activity. 1 Publication
Mutagenesisi736 – 7361Y → F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-740 and F-741. 1 Publication
Mutagenesisi740 – 7401Y → F: Promotes autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-741. 1 Publication
Mutagenesisi741 – 7411Y → F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-740. 1 Publication

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi271665. phenotype.
Orphaneti93358. Spondyloepimetaphyseal dysplasia - short limb - abnormal calcification.
PharmGKBiPA27196.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 855834Discoidin domain-containing receptor 2PRO_0000016746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 185
Disulfide bondi73 ↔ 177
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis
Modified residuei461 – 4611Phosphoserine
Modified residuei471 – 4711Phosphotyrosine; by SRC and autocatalysisBy similarity
Modified residuei674 – 6741Phosphoserine
Modified residuei736 – 7361Phosphotyrosine; by SRC and autocatalysis1 Publication
Modified residuei740 – 7401Phosphotyrosine; by SRC and autocatalysis1 Publication
Modified residuei741 – 7411Phosphotyrosine; by SRC and autocatalysis1 Publication

Post-translational modificationi

N-glycosylated.1 Publication
Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues.5 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ16832.
PaxDbiQ16832.
PRIDEiQ16832.

PTM databases

PhosphoSiteiQ16832.

Expressioni

Tissue specificityi

Detected in osteocytes, osteoblastic cells in subchondral bone, bone lining cells, tibia and cartilage (at protein level). Detected at high levels in heart and lung, and at low levels in brain, placenta, liver, skeletal muscle, pancreas, and kidney.3 Publications

Inductioni

Up-regulated during osteoblast differentiation (in vitro). Up-regulated in cartilage from osteoarthritis patients.2 Publications

Gene expression databases

BgeeiQ16832.
CleanExiHS_DDR2.
HS_TKT.
ExpressionAtlasiQ16832. baseline and differential.
GenevestigatoriQ16832.

Interactioni

Subunit structurei

Binds hydroxyproline-rich sequence motifs in fibrillar, glycosylated collagen, such as the GQOGVMGFO motif, where O stands for hydroxyproline. Interacts with SRC. Interacts (tyrosine phosphorylated) with SHC1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COL11A2P139422EBI-1381484,EBI-2515504
HSP90AB1P082382EBI-1381484,EBI-352572

Protein-protein interaction databases

BioGridi110975. 6 interactions.
DIPiDIP-39699N.
IntActiQ16832. 4 interactions.
MINTiMINT-233614.
STRINGi9606.ENSP00000356898.

Structurei

Secondary structure

1
855
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni27 – 293
Beta strandi33 – 353
Turni36 – 383
Beta strandi39 – 413
Helixi43 – 453
Beta strandi46 – 494
Helixi54 – 563
Helixi58 – 603
Beta strandi70 – 723
Beta strandi87 – 10317
Helixi107 – 1093
Beta strandi116 – 12813
Beta strandi139 – 1424
Beta strandi145 – 1495
Beta strandi151 – 16919
Beta strandi171 – 1744
Beta strandi178 – 1869

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WUHX-ray1.60A26-190[»]
2Z4FNMR-A26-186[»]
ProteinModelPortaliQ16832.
SMRiQ16832. Positions 26-369, 459-851.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16832.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 399378ExtracellularSequence AnalysisAdd
BLAST
Topological domaini422 – 855434CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei400 – 42122HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 185156F5/8 type CPROSITE-ProRule annotationAdd
BLAST
Domaini563 – 849287Protein kinasePROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000043102.
HOVERGENiHBG005461.
InParanoidiQ16832.
KOiK05125.
OMAiASAIKCQ.
OrthoDBiEOG77Q4W2.
PhylomeDBiQ16832.
TreeFamiTF317840.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR029553. DDR2.
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:SF297. PTHR24416:SF297. 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]

Sequencei

Sequence statusi: Complete.

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

Q16832-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MILIPRMLLV LFLLLPILSS AKAQVNPAIC RYPLGMSGGQ IPDEDITASS
60 70 80 90 100
QWSESTAAKY GRLDSEEGDG AWCPEIPVEP DDLKEFLQID LHTLHFITLV
110 120 130 140 150
GTQGRHAGGH GIEFAPMYKI NYSRDGTRWI SWRNRHGKQV LDGNSNPYDI
160 170 180 190 200
FLKDLEPPIV ARFVRFIPVT DHSMNVCMRV ELYGCVWLDG LVSYNAPAGQ
210 220 230 240 250
QFVLPGGSII YLNDSVYDGA VGYSMTEGLG QLTDGVSGLD DFTQTHEYHV
260 270 280 290 300
WPGYDYVGWR NESATNGYIE IMFEFDRIRN FTTMKVHCNN MFAKGVKIFK
310 320 330 340 350
EVQCYFRSEA SEWEPNAISF PLVLDDVNPS ARFVTVPLHH RMASAIKCQY
360 370 380 390 400
HFADTWMMFS EITFQSDAAM YNNSEALPTS PMAPTTYDPM LKVDDSNTRI
410 420 430 440 450
LIGCLVAIIF ILLAIIVIIL WRQFWQKMLE KASRRMLDDE MTVSLSLPSD
460 470 480 490 500
SSMFNNNRSS SPSEQGSNST YDRIFPLRPD YQEPSRLIRK LPEFAPGEEE
510 520 530 540 550
SGCSGVVKPV QPSGPEGVPH YAEADIVNLQ GVTGGNTYSV PAVTMDLLSG
560 570 580 590 600
KDVAVEEFPR KLLTFKEKLG EGQFGEVHLC EVEGMEKFKD KDFALDVSAN
610 620 630 640 650
QPVLVAVKML RADANKNARN DFLKEIKIMS RLKDPNIIHL LAVCITDDPL
660 670 680 690 700
CMITEYMENG DLNQFLSRHE PPNSSSSDVR TVSYTNLKFM ATQIASGMKY
710 720 730 740 750
LSSLNFVHRD LATRNCLVGK NYTIKIADFG MSRNLYSGDY YRIQGRAVLP
760 770 780 790 800
IRWMSWESIL LGKFTTASDV WAFGVTLWET FTFCQEQPYS QLSDEQVIEN
810 820 830 840 850
TGEFFRDQGR QTYLPQPAIC PDSVYKLMLS CWRRDTKNRP SFQEIHLLLL

QQGDE
Length:855
Mass (Da):96,736
Last modified:November 25, 2008 - v2
Checksum:i78662021BC53E1A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti642 – 6421A → S in CAA52777. (PubMed:8247548)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051R → S in a lung large cell carcinoma sample; somatic mutation. 2 Publications
VAR_041498
Natural varianti113 – 1131E → K in SEMD-SL; abolishes collagen binding. 1 Publication
VAR_065719
Natural varianti441 – 4411M → I.1 Publication
Corresponds to variant rs34722354 [ dbSNP | Ensembl ].
VAR_041499
Natural varianti478 – 4781R → C.1 Publication
Corresponds to variant rs34869543 [ dbSNP | Ensembl ].
VAR_041500
Natural varianti543 – 5431V → F.1 Publication
Corresponds to variant rs55973200 [ dbSNP | Ensembl ].
VAR_041501
Natural varianti713 – 7131T → I in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
VAR_063050
Natural varianti726 – 7261I → R in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
VAR_063051
Natural varianti752 – 7521R → C in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 1 Publication
VAR_063052

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74764 mRNA. Translation: CAA52777.1.
AK314388 mRNA. Translation: BAG37013.1.
AK095975 mRNA. Translation: BAG53183.1.
AL445197 Genomic DNA. Translation: CAI15941.1.
CH471067 Genomic DNA. Translation: EAW90713.1.
BC052998 mRNA. Translation: AAH52998.1.
CCDSiCCDS1241.1.
PIRiS42621.
RefSeqiNP_001014796.1. NM_001014796.1.
NP_006173.2. NM_006182.2.
XP_006711407.1. XM_006711344.1.
UniGeneiHs.275757.
Hs.593833.

Genome annotation databases

EnsembliENST00000367921; ENSP00000356898; ENSG00000162733.
ENST00000367922; ENSP00000356899; ENSG00000162733.
GeneIDi4921.
KEGGihsa:4921.
UCSCiuc001gcf.3. human.

Polymorphism databases

DMDMi215273969.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74764 mRNA. Translation: CAA52777.1 .
AK314388 mRNA. Translation: BAG37013.1 .
AK095975 mRNA. Translation: BAG53183.1 .
AL445197 Genomic DNA. Translation: CAI15941.1 .
CH471067 Genomic DNA. Translation: EAW90713.1 .
BC052998 mRNA. Translation: AAH52998.1 .
CCDSi CCDS1241.1.
PIRi S42621.
RefSeqi NP_001014796.1. NM_001014796.1.
NP_006173.2. NM_006182.2.
XP_006711407.1. XM_006711344.1.
UniGenei Hs.275757.
Hs.593833.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WUH X-ray 1.60 A 26-190 [» ]
2Z4F NMR - A 26-186 [» ]
ProteinModelPortali Q16832.
SMRi Q16832. Positions 26-369, 459-851.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110975. 6 interactions.
DIPi DIP-39699N.
IntActi Q16832. 4 interactions.
MINTi MINT-233614.
STRINGi 9606.ENSP00000356898.

Chemistry

BindingDBi Q16832.
ChEMBLi CHEMBL5122.
DrugBanki DB08896. Regorafenib.
GuidetoPHARMACOLOGYi 1844.

PTM databases

PhosphoSitei Q16832.

Polymorphism databases

DMDMi 215273969.

Proteomic databases

MaxQBi Q16832.
PaxDbi Q16832.
PRIDEi Q16832.

Protocols and materials databases

DNASUi 4921.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367921 ; ENSP00000356898 ; ENSG00000162733 .
ENST00000367922 ; ENSP00000356899 ; ENSG00000162733 .
GeneIDi 4921.
KEGGi hsa:4921.
UCSCi uc001gcf.3. human.

Organism-specific databases

CTDi 4921.
GeneCardsi GC01P162601.
HGNCi HGNC:2731. DDR2.
MIMi 191311. gene.
271665. phenotype.
neXtProti NX_Q16832.
Orphaneti 93358. Spondyloepimetaphyseal dysplasia - short limb - abnormal calcification.
PharmGKBi PA27196.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118818.
HOGENOMi HOG000043102.
HOVERGENi HBG005461.
InParanoidi Q16832.
KOi K05125.
OMAi ASAIKCQ.
OrthoDBi EOG77Q4W2.
PhylomeDBi Q16832.
TreeFami TF317840.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
SignaLinki Q16832.

Miscellaneous databases

EvolutionaryTracei Q16832.
GeneWikii Discoidin_domain-containing_receptor_2.
GenomeRNAii 4921.
NextBioi 18949.
PROi Q16832.
SOURCEi Search...

Gene expression databases

Bgeei Q16832.
CleanExi HS_DDR2.
HS_TKT.
ExpressionAtlasi Q16832. baseline and differential.
Genevestigatori Q16832.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR029553. DDR2.
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:SF297. PTHR24416:SF297. 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. "Structure, expression and chromosomal mapping of TKT from man and mouse: a new subclass of receptor tyrosine kinases with a factor VIII-like domain."
    Karn T., Holtrich U., Braeuninger A., Boehme B., Wolf G., Ruebsamen-Waigmann H., Strebhardt K.
    Oncogene 8:3433-3440(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Heart and Thymus.
  2. "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].
    Tissue: Hair follicle dermal papilla and Uterus.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Skin.
  6. "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 AND IN UP-REGULATION OF MMP1, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  7. "Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src stimulates intramolecular autophosphorylation and Shc signaling complex formation."
    Yang K., Kim J.H., Kim H.J., Park I.S., Kim I.Y., Yang B.S.
    J. Biol. Chem. 280:39058-39066(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF MMP1 AND MMP2, PHOSPHORYLATION AT TYR-736; TYR-740 AND TYR-741, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH SHC1, MUTAGENESIS OF LYS-608; TYR-736; TYR-740 AND TYR-741.
  8. "Discoidin domain receptor 2 mediates tumor cell cycle arrest induced by fibrillar collagen."
    Wall S.J., Werner E., Werb Z., DeClerck Y.A.
    J. Biol. Chem. 280:40187-40194(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS COLLAGEN RECEPTOR, PHOSPHORYLATION.
  9. "Increased expression of the collagen receptor discoidin domain receptor 2 in articular cartilage as a key event in the pathogenesis of osteoarthritis."
    Xu L., Peng H., Glasson S., Lee P.L., Hu K., Ijiri K., Olsen B.R., Goldring M.B., Li Y.
    Arthritis Rheum. 56:2663-2673(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UP-REGULATION OF MMP13, INDUCTION, TISSUE SPECIFICITY.
  10. "Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen."
    Konitsiotis A.D., Raynal N., Bihan D., Hohenester E., Farndale R.W., Leitinger B.
    J. Biol. Chem. 283:6861-6868(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS COLLAGEN RECEPTOR, SUBCELLULAR LOCATION, PHOSPHORYLATION, SUBUNIT.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Transcriptional upregulation of DDR2 by ATF4 facilitates osteoblastic differentiation through p38 MAPK-mediated Runx2 activation."
    Lin K.L., Chou C.H., Hsieh S.C., Hwa S.Y., Lee M.T., Wang F.F.
    J. Bone Miner. Res. 25:2489-2503(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION VIA ACTIVATION OF RUNX2, INDUCTION, TISSUE SPECIFICITY.
  14. "An essential role of discoidin domain receptor 2 (DDR2) in osteoblast differentiation and chondrocyte maturation via modulation of Runx2 activation."
    Zhang Y., Su J., Yu J., Bu X., Ren T., Liu X., Yao L.
    J. Bone Miner. Res. 26:604-617(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION AND CHONDROCYTE MATURATION VIA ACTIVATION OF RUNX2.
  15. "Sensing extracellular matrix: an update on discoidin domain receptor function."
    Vogel W.F., Abdulhussein R., Ford C.E.
    Cell. Signal. 18:1108-1116(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. Cited for: REVIEW.
  17. "Structural basis of the collagen-binding mode of discoidin domain receptor 2."
    Ichikawa O., Osawa M., Nishida N., Goshima N., Nomura N., Shimada I.
    EMBO J. 26:4168-4176(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 22-186, INTERACTION WITH COLLAGEN, DISULFIDE BONDS.
  18. "Crystallographic insight into collagen recognition by discoidin domain receptor 2."
    Carafoli F., Bihan D., Stathopoulos S., Konitsiotis A.D., Kvansakul M., Farndale R.W., Leitinger B., Hohenester E.
    Structure 17:1573-1581(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 26-190 IN COMPLEX WITH COLLAGEN PEPTIDE, DISULFIDE BONDS, MUTAGENESIS OF TRP-52, FUNCTION IN COLLAGEN BINDING, CATALYTIC ACTIVITY, PHOSPHORYLATION.
  19. "Somatic mutations of the protein kinase gene family in human lung cancer."
    Davies H., Hunter C., Smith R., Stephens P., Greenman C., Bignell G., Teague J., Butler A., Edkins S., Stevens C., Parker A., O'Meara S., Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J.
    , Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R., Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R., Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A., West S., Widaa S., Yates A., Brasseur F., Cooper C.S., Flanagan A.M., Green A., Knowles M., Leung S.Y., Looijenga L.H., Malkowicz B., Pierotti M.A., Teh B.T., Yuen S.T., Lakhani S.R., Easton D.F., Weber B.L., Goldstraw P., Nicholson A.G., Wooster R., Stratton M.R., Futreal P.A.
    Cancer Res. 65:7591-7595(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-105.
  20. "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] SER-105; ILE-441; CYS-478 AND PHE-543.
  21. Cited for: VARIANTS SEMD-SL ILE-713; ARG-726 AND CYS-752.
  22. "Trafficking defects and loss of ligand binding are the underlying causes of all reported DDR2 missense mutations found in SMED-SL patients."
    Ali B.R., Xu H., Akawi N.A., John A., Karuvantevida N.S., Langer R., Al-Gazali L., Leitinger B.
    Hum. Mol. Genet. 19:2239-2250(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SEMD-SL LYS-113, CHARACTERIZATION OF VARIANTS SEMD-SL LYS-113; ILE-713; ARG-726 AND CYS-752, MUTAGENESIS OF TRP-52, GLYCOSYLATION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDDR2_HUMAN
AccessioniPrimary (citable) accession number: Q16832
Secondary accession number(s): Q7Z730
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 149 of the entry and version 2 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, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: 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