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Protein

Discoidin domain-containing receptor 2

Gene

DDR2

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 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.PROSITE-ProRule annotation2 Publications

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)DescriptionActionsGraphical viewLength
Binding sitei608ATPCurated1
Active sitei710Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi569 – 577ATPPROSITE-ProRule annotation9

GO - Molecular functioni

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

GO - Biological processi

  • biomineral tissue development Source: UniProtKB
  • cell adhesion Source: ProtInc
  • chondrocyte proliferation Source: UniProtKB
  • collagen-activated tyrosine kinase receptor signaling pathway Source: UniProtKB
  • collagen fibril organization Source: UniProtKB
  • endochondral bone growth Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • ossification Source: UniProtKB-KW
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of extracellular matrix disassembly Source: UniProtKB
  • positive regulation of fibroblast migration Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: UniProtKB
  • positive regulation of osteoblast differentiation Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of bone mineralization Source: UniProtKB
  • regulation of extracellular matrix disassembly Source: UniProtKB
  • 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

BioCyciZFISH:HS08729-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-3000171. Non-integrin membrane-ECM interactions.
SignaLinkiQ16832.
SIGNORiQ16832.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2731. DDR2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 399ExtracellularSequence analysisAdd BLAST378
Transmembranei400 – 421HelicalSequence analysisAdd BLAST22
Topological domaini422 – 855CytoplasmicSequence analysisAdd BLAST434

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • 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)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:271665
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065719113E → K in SEMD-SL; abolishes collagen binding. 1 PublicationCorresponds to variant rs397514747dbSNPEnsembl.1
Natural variantiVAR_075417124R → W in SEMD-SL. 1 Publication1
Natural variantiVAR_063050713T → I in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant rs121964865dbSNPEnsembl.1
Natural variantiVAR_063051726I → R in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant rs121964864dbSNPEnsembl.1
Natural variantiVAR_063052752R → C in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant rs121964863dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52W → A: Abolishes collagen binding. 2 Publications1
Mutagenesisi608K → A: Abolishes kinase activity. 1 Publication1
Mutagenesisi736Y → F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-740 and F-741. 1 Publication1
Mutagenesisi740Y → F: Promotes autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-741. 1 Publication1
Mutagenesisi741Y → F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-740. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi4921.
MalaCardsiDDR2.
MIMi271665. phenotype.
OpenTargetsiENSG00000162733.
Orphaneti93358. Spondyloepimetaphyseal dysplasia - short limb - abnormal calcification.
PharmGKBiPA27196.

Chemistry databases

ChEMBLiCHEMBL5122.
DrugBankiDB08896. Regorafenib.
GuidetoPHARMACOLOGYi1844.

Polymorphism and mutation databases

BioMutaiDDR2.
DMDMi215273969.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001674622 – 855Discoidin domain-containing receptor 2Add BLAST834

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 185
Disulfide bondi73 ↔ 177
Glycosylationi121N-linked (GlcNAc...)Sequence analysis1
Glycosylationi213N-linked (GlcNAc...)Sequence analysis1
Glycosylationi261N-linked (GlcNAc...)Sequence analysis1
Glycosylationi280N-linked (GlcNAc...)Sequence analysis1
Glycosylationi372N-linked (GlcNAc...)Sequence analysis1
Modified residuei471Phosphotyrosine; by SRC and autocatalysisBy similarity1
Modified residuei736Phosphotyrosine; by SRC and autocatalysis1 Publication1
Modified residuei740Phosphotyrosine; by SRC and autocatalysis1 Publication1
Modified residuei741Phosphotyrosine; by SRC and autocatalysis1 Publication1

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

EPDiQ16832.
MaxQBiQ16832.
PaxDbiQ16832.
PeptideAtlasiQ16832.
PRIDEiQ16832.

PTM databases

iPTMnetiQ16832.
PhosphoSitePlusiQ16832.
SwissPalmiQ16832.

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

BgeeiENSG00000162733.
CleanExiHS_DDR2.
HS_TKT.
ExpressionAtlasiQ16832. baseline and differential.
GenevisibleiQ16832. HS.

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

GO - Molecular functioni

  • collagen binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110975. 10 interactors.
DIPiDIP-39699N.
IntActiQ16832. 7 interactors.
MINTiMINT-233614.
STRINGi9606.ENSP00000356898.

Chemistry databases

BindingDBiQ16832.

Structurei

Secondary structure

1855
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni27 – 29Combined sources3
Beta strandi33 – 35Combined sources3
Turni36 – 38Combined sources3
Beta strandi39 – 41Combined sources3
Helixi43 – 45Combined sources3
Beta strandi46 – 49Combined sources4
Helixi54 – 56Combined sources3
Helixi58 – 60Combined sources3
Beta strandi70 – 72Combined sources3
Beta strandi87 – 103Combined sources17
Helixi107 – 109Combined sources3
Beta strandi116 – 128Combined sources13
Beta strandi139 – 142Combined sources4
Beta strandi145 – 149Combined sources5
Beta strandi151 – 169Combined sources19
Beta strandi171 – 174Combined sources4
Beta strandi178 – 186Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WUHX-ray1.60A26-190[»]
2Z4FNMR-A26-186[»]
ProteinModelPortaliQ16832.
SMRiQ16832.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16832.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 185F5/8 type CPROSITE-ProRule annotationAdd BLAST156
Domaini563 – 849Protein kinasePROSITE-ProRule annotationAdd BLAST287

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.
InParanoidiQ16832.
KOiK05125.
OMAiFPLGPDY.
OrthoDBiEOG091G05Y8.
PhylomeDBiQ16832.
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. 3 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]

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)DescriptionActionsGraphical viewLength
Sequence conflicti642A → S in CAA52777 (PubMed:8247548).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041498105R → S in a lung large cell carcinoma sample; somatic mutation. 2 Publications1
Natural variantiVAR_065719113E → K in SEMD-SL; abolishes collagen binding. 1 PublicationCorresponds to variant rs397514747dbSNPEnsembl.1
Natural variantiVAR_075417124R → W in SEMD-SL. 1 Publication1
Natural variantiVAR_041499441M → I.1 PublicationCorresponds to variant rs34722354dbSNPEnsembl.1
Natural variantiVAR_041500478R → C.1 PublicationCorresponds to variant rs34869543dbSNPEnsembl.1
Natural variantiVAR_041501543V → F.1 PublicationCorresponds to variant rs55973200dbSNPEnsembl.1
Natural variantiVAR_063050713T → I in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant rs121964865dbSNPEnsembl.1
Natural variantiVAR_063051726I → R in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant rs121964864dbSNPEnsembl.1
Natural variantiVAR_063052752R → C in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant rs121964863dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006711344.3.
XP_011507888.1. XM_011509586.2.
XP_011507889.1. XM_011509587.2.
UniGeneiHs.275757.
Hs.593833.

Genome annotation databases

EnsembliENST00000367921; ENSP00000356898; ENSG00000162733.
ENST00000367922; ENSP00000356899; ENSG00000162733.
GeneIDi4921.
KEGGihsa:4921.
UCSCiuc001gcg.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006711344.3.
XP_011507888.1. XM_011509586.2.
XP_011507889.1. XM_011509587.2.
UniGeneiHs.275757.
Hs.593833.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WUHX-ray1.60A26-190[»]
2Z4FNMR-A26-186[»]
ProteinModelPortaliQ16832.
SMRiQ16832.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110975. 10 interactors.
DIPiDIP-39699N.
IntActiQ16832. 7 interactors.
MINTiMINT-233614.
STRINGi9606.ENSP00000356898.

Chemistry databases

BindingDBiQ16832.
ChEMBLiCHEMBL5122.
DrugBankiDB08896. Regorafenib.
GuidetoPHARMACOLOGYi1844.

PTM databases

iPTMnetiQ16832.
PhosphoSitePlusiQ16832.
SwissPalmiQ16832.

Polymorphism and mutation databases

BioMutaiDDR2.
DMDMi215273969.

Proteomic databases

EPDiQ16832.
MaxQBiQ16832.
PaxDbiQ16832.
PeptideAtlasiQ16832.
PRIDEiQ16832.

Protocols and materials databases

DNASUi4921.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367921; ENSP00000356898; ENSG00000162733.
ENST00000367922; ENSP00000356899; ENSG00000162733.
GeneIDi4921.
KEGGihsa:4921.
UCSCiuc001gcg.4. human.

Organism-specific databases

CTDi4921.
DisGeNETi4921.
GeneCardsiDDR2.
HGNCiHGNC:2731. DDR2.
MalaCardsiDDR2.
MIMi191311. gene.
271665. phenotype.
neXtProtiNX_Q16832.
OpenTargetsiENSG00000162733.
Orphaneti93358. Spondyloepimetaphyseal dysplasia - short limb - abnormal calcification.
PharmGKBiPA27196.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1094. Eukaryota.
ENOG410XQAI. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000043102.
HOVERGENiHBG005461.
InParanoidiQ16832.
KOiK05125.
OMAiFPLGPDY.
OrthoDBiEOG091G05Y8.
PhylomeDBiQ16832.
TreeFamiTF317840.

Enzyme and pathway databases

BioCyciZFISH:HS08729-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-3000171. Non-integrin membrane-ECM interactions.
SignaLinkiQ16832.
SIGNORiQ16832.

Miscellaneous databases

EvolutionaryTraceiQ16832.
GeneWikiiDiscoidin_domain-containing_receptor_2.
GenomeRNAii4921.
PROiQ16832.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000162733.
CleanExiHS_DDR2.
HS_TKT.
ExpressionAtlasiQ16832. baseline and differential.
GenevisibleiQ16832. 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. 3 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 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: November 2, 2016
This is version 171 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

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.