CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010713
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Very low-density lipoprotein receptor 
Protein Synonyms/Alias
 VLDL receptor; VLDL-R 
Gene Name
 VLDLR 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
828NWQHKNMKSMNFDNPubiquitination[1, 2, 3]
839FDNPVYLKTTEEDLSubiquitination[3, 4, 5, 6]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation (By similarity). 
Sequence Annotation
 DOMAIN 31 69 LDL-receptor class A 1.
 DOMAIN 70 110 LDL-receptor class A 2.
 DOMAIN 111 151 LDL-receptor class A 3.
 DOMAIN 152 190 LDL-receptor class A 4.
 DOMAIN 191 231 LDL-receptor class A 5.
 DOMAIN 237 275 LDL-receptor class A 6.
 DOMAIN 276 314 LDL-receptor class A 7.
 DOMAIN 316 355 LDL-receptor class A 8.
 DOMAIN 356 395 EGF-like 1.
 DOMAIN 396 435 EGF-like 2; calcium-binding (Potential).
 REPEAT 439 480 LDL-receptor class B 1.
 REPEAT 481 524 LDL-receptor class B 2.
 REPEAT 525 567 LDL-receptor class B 3.
 REPEAT 568 611 LDL-receptor class B 4.
 REPEAT 612 654 LDL-receptor class B 5.
 REPEAT 655 697 LDL-receptor class B 6.
 DOMAIN 702 750 EGF-like 3.
 REGION 751 790 Clustered O-linked oligosaccharides.
 MOTIF 832 837 Endocytosis signal (Potential).
 CARBOHYD 151 151 N-linked (GlcNAc...) (Potential).
 CARBOHYD 765 765 N-linked (GlcNAc...) (Potential).
 CARBOHYD 781 781 N-linked (GlcNAc...) (Potential).
 DISULFID 33 45 By similarity.
 DISULFID 40 58 By similarity.
 DISULFID 52 67 By similarity.
 DISULFID 72 84 By similarity.
 DISULFID 79 97 By similarity.
 DISULFID 91 108 By similarity.
 DISULFID 113 127
 DISULFID 120 140
 DISULFID 134 149
 DISULFID 154 166 By similarity.
 DISULFID 161 179 By similarity.
 DISULFID 173 188 By similarity.
 DISULFID 193 205 By similarity.
 DISULFID 200 218 By similarity.
 DISULFID 212 229 By similarity.
 DISULFID 239 251 By similarity.
 DISULFID 246 264 By similarity.
 DISULFID 258 273 By similarity.
 DISULFID 278 290 By similarity.
 DISULFID 285 303 By similarity.
 DISULFID 297 312 By similarity.
 DISULFID 318 331 By similarity.
 DISULFID 326 344 By similarity.
 DISULFID 338 355 By similarity.
 DISULFID 360 371 By similarity.
 DISULFID 367 380 By similarity.
 DISULFID 382 394 By similarity.
 DISULFID 400 410 By similarity.
 DISULFID 406 419 By similarity.
 DISULFID 421 434 By similarity.
 DISULFID 706 719 By similarity.
 DISULFID 715 734 By similarity.
 DISULFID 736 749 By similarity.
 CROSSLNK 839 839 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Cholesterol metabolism; Coated pit; Complete proteome; Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; Isopeptide bond; Lipid metabolism; Lipid transport; Membrane; Mental retardation; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix; Transport; Ubl conjugation; VLDL. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 873 AA 
Protein Sequence
MGTSALWALW LLLALCWAPR ESGATGTGRK AKCEPSQFQC TNGRCITLLW KCDGDEDCVD 60
GSDEKNCVKK TCAESDFVCN NGQCVPSRWK CDGDPDCEDG SDESPEQCHM RTCRIHEISC 120
GAHSTQCIPV SWRCDGENDC DSGEDEENCG NITCSPDEFT CSSGRCISRN FVCNGQDDCS 180
DGSDELDCAP PTCGAHEFQC STSSCIPISW VCDDDADCSD QSDESLEQCG RQPVIHTKCP 240
ASEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI 300
RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ EQDCRDWSDE PLKECHINEC 360
LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE 420
CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA 480
QKLFWADLSQ KAIFSASIDD KVGRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA 540
TLDGTKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTADIQ 600
WPNGITLDLI KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI 660
DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEEDM ENGGCEYLCL 720
PAPQINDHSP KYTCSCPSGY NVEENGRDCQ STATTVTYSE TKDTNTTEIS ATSGLVPGGI 780
NVTTAVSEVS VPPKGTSAAW AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT 840
TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA 873 
Gene Ontology
 GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; TAS:ProtInc.
 GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
 GO:0034185; F:apolipoprotein binding; IDA:BHF-UCL.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0034437; F:glycoprotein transporter activity; IDA:BHF-UCL.
 GO:0005041; F:low-density lipoprotein receptor activity; TAS:ProtInc.
 GO:0038025; F:reelin receptor activity; ISS:BHF-UCL.
 GO:0034189; F:very-low-density lipoprotein particle binding; IDA:BHF-UCL.
 GO:0030229; F:very-low-density lipoprotein particle receptor activity; IDA:BHF-UCL.
 GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
 GO:0034436; P:glycoprotein transport; IDA:BHF-UCL.
 GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
 GO:0007613; P:memory; TAS:ProtInc.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
 GO:1900006; P:positive regulation of dendrite development; ISS:BHF-UCL.
 GO:0045860; P:positive regulation of protein kinase activity; IEA:Compara.
 GO:0021517; P:ventral spinal cord development; IEA:Compara.
 GO:0034447; P:very-low-density lipoprotein particle clearance; IDA:BHF-UCL. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR000742; EG-like_dom.
 IPR001881; EGF-like_Ca-bd.
 IPR013032; EGF-like_CS.
 IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
 IPR018097; EGF_Ca-bd_CS.
 IPR009030; Growth_fac_rcpt_N_dom.
 IPR023415; LDLR_class-A_CS.
 IPR000033; LDLR_classB_rpt.
 IPR002172; LDrepeatLR_classA_rpt. 
Pfam
 PF07645; EGF_CA
 PF00057; Ldl_recept_a
 PF00058; Ldl_recept_b 
SMART
 SM00181; EGF
 SM00179; EGF_CA
 SM00192; LDLa
 SM00135; LY 
PROSITE
 PS00010; ASX_HYDROXYL
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01187; EGF_CA
 PS01209; LDLRA_1
 PS50068; LDLRA_2
 PS51120; LDLRB 
PRINTS