CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011590
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Epithelial discoidin domain-containing receptor 1 
Protein Synonyms/Alias
 Epithelial discoidin domain receptor 1; CD167 antigen-like family member A; Cell adhesion kinase; Discoidin receptor tyrosine kinase; HGK2; Mammary carcinoma kinase 10; MCK-10; Protein-tyrosine kinase 3A; Protein-tyrosine kinase RTK-6; TRK E; Tyrosine kinase DDR; Tyrosine-protein kinase CAK; CD167a 
Gene Name
 DDR1 
Gene Synonyms/Alias
 CAK; EDDR1; NEP; NTRK4; PTK3A; RTK6; TRKE 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
153DPEGVVLKDLGPPMVubiquitination[1]
626ILRPDATKNARNDFLubiquitination[1]
634NARNDFLKEVKIMSRubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 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. 
Sequence Annotation
 DOMAIN 31 185 F5/8 type C.
 DOMAIN 610 905 Protein kinase.
 NP_BIND 616 624 ATP (By similarity).
 REGION 192 367 DS-like domain.
 MOTIF 481 484 PPxY motif.
 ACT_SITE 766 766 Proton acceptor (By similarity).
 METAL 211 211 Calcium 1; via carbonyl oxygen.
 METAL 230 230 Calcium 1.
 METAL 230 230 Calcium 2; via carbonyl oxygen.
 METAL 233 233 Calcium 2.
 METAL 235 235 Calcium 2; via carbonyl oxygen.
 METAL 253 253 Calcium 1; via carbonyl oxygen.
 METAL 255 255 Calcium 1; via carbonyl oxygen.
 METAL 360 360 Calcium 2; via carbonyl oxygen.
 METAL 361 361 Calcium 2.
 BINDING 655 655 ATP (By similarity).
 MOD_RES 513 513 Phosphotyrosine; by autocatalysis.
 MOD_RES 631 631 Phosphoserine.
 MOD_RES 740 740 Phosphotyrosine; by autocatalysis
 MOD_RES 792 792 Phosphotyrosine; by autocatalysis (By
 MOD_RES 796 796 Phosphotyrosine; by autocatalysis (By
 MOD_RES 797 797 Phosphotyrosine; by autocatalysis (By
 CARBOHYD 211 211 N-linked (GlcNAc...) (Potential).
 CARBOHYD 260 260 N-linked (GlcNAc...) (Potential).
 CARBOHYD 371 371 N-linked (GlcNAc...) (Potential).
 CARBOHYD 394 394 N-linked (GlcNAc...) (Potential).
 DISULFID 31 185
 DISULFID 74 177
 DISULFID 303 348  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Calcium; Cell membrane; Complete proteome; Disulfide bond; Glycoprotein; Kinase; Lactation; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Pregnancy; Receptor; Reference proteome; Secreted; Signal; Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 913 AA 
Protein Sequence
MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR 60
HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL 120
RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV 180
ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD 240
FRKSQELRVW PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG 300
VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF LFAGPWLLFS 360
EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL EPRGQQPVAK AEGSPTAILI 420
GCLVAIILLL LLIIALMLWR LHWRRLLSKA ERRVLEEELT VHLSVPGDTI LINNRPGPRE 480
PPPYQEPRPR GNPPHSAPCV PNGSAYSGDY MEPEKPGAPL LPPPPQNSVP HYAEADIVTL 540
QGVTGGNTYA VPALPPGAVG DGPPRVDFPR SRLRFKEKLG EGQFGEVHLC EVDSPQDLVS 600
LDFPLNVRKG HPLLVAVKIL RPDATKNARN DFLKEVKIMS RLKDPNIIRL LGVCVQDDPL 660
CMITDYMENG DLNQFLSAHQ LEDKAAEGAP GDGQAAQGPT ISYPMLLHVA AQIASGMRYL 720
ATLNFVHRDL ATRNCLVGEN FTIKIADFGM SRNLYAGDYY RVQGRAVLPI RWMAWECILM 780
GKFTTASDVW AFGVTLWEVL MLCRAQPFGQ LTDEQVIENA GEFFRDQGRQ VYLSRPPACP 840
QGLYELMLRC WSRESEQRPP FSQLHRFLAE DALNTV 876 
Gene Ontology
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005518; F:collagen binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0038062; F:protein tyrosine kinase collagen receptor activity; IDA:UniProtKB.
 GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Compara.
 GO:0043583; P:ear development; IEA:Compara.
 GO:0007566; P:embryo implantation; IEA:Compara.
 GO:0007595; P:lactation; IEA:UniProtKB-KW.
 GO:0060749; P:mammary gland alveolus development; IEA:Compara.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:UniProtKB.
 GO:0001558; P:regulation of cell growth; IEA:Compara.
 GO:0001952; P:regulation of cell-matrix adhesion; IEA:Compara.
 GO:0010715; P:regulation of extracellular matrix disassembly; IMP:UniProtKB.
 GO:0014909; P:smooth muscle cell migration; IMP:UniProtKB.
 GO:0061302; P:smooth muscle cell-matrix adhesion; IMP:UniProtKB.
 GO:0044319; P:wound healing, spreading of cells; IMP:UniProtKB. 
Interpro
 IPR000421; Coagulation_fac_5/8-C_type_dom.
 IPR008979; Galactose-bd-like.
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
 IPR008266; Tyr_kinase_AS.
 IPR020635; Tyr_kinase_cat_dom.
 IPR002011; Tyr_kinase_rcpt_2_CS. 
Pfam
 PF00754; F5_F8_type_C
 PF07714; Pkinase_Tyr 
SMART
 SM00231; FA58C
 SM00219; TyrKc 
PROSITE
 PS01285; FA58C_1
 PS01286; FA58C_2
 PS50022; FA58C_3
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00109; PROTEIN_KINASE_TYR
 PS00239; RECEPTOR_TYR_KIN_II 
PRINTS
 PR00109; TYRKINASE.