CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001140
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Low-density lipoprotein receptor-related protein 5 
Protein Synonyms/Alias
 LRP-5 
Gene Name
 LRP5 
Gene Synonyms/Alias
 LR3; LRP7 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
143NLNGTSRKVLFWQDLubiquitination[1]
592LPDLMGLKAVNVAKVubiquitination[1, 2]
802NCMTLVDKVGRANDLubiquitination[1]
1231CSHICIAKGDGTPRCubiquitination[1, 3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] 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]
 [3] 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] 
Functional Description
 Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor- ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3- mediated phosphorylation and destruction of beta-catenin. Appears be required for postnatal control of vascular regression in the eye. Required for posterior patterning of the epiblast during gastrulation. 
Sequence Annotation
 REPEAT 75 119 LDL-receptor class B 1.
 REPEAT 78 81 YWTD 1.
 REPEAT 120 162 LDL-receptor class B 2.
 REPEAT 123 126 YWTD 2.
 REPEAT 163 206 LDL-receptor class B 3.
 REPEAT 166 169 YWTD 3.
 REPEAT 207 247 LDL-receptor class B 4.
 REPEAT 248 290 LDL-receptor class B 5.
 REPEAT 251 254 YWTD 4.
 DOMAIN 295 337 EGF-like 1.
 REPEAT 385 427 LDL-receptor class B 6.
 REPEAT 388 391 YWTD 5.
 REPEAT 428 470 LDL-receptor class B 7.
 REPEAT 431 434 YWTD 6.
 REPEAT 471 514 LDL-receptor class B 8.
 REPEAT 474 477 YWTD 7.
 REPEAT 515 557 LDL-receptor class B 9.
 REPEAT 558 600 LDL-receptor class B 10.
 REPEAT 559 562 YWTD 8.
 DOMAIN 601 641 EGF-like 2.
 REPEAT 687 729 LDL-receptor class B 11.
 REPEAT 690 693 YWTD 9.
 REPEAT 730 772 LDL-receptor class B 12.
 REPEAT 773 815 LDL-receptor class B 13.
 REPEAT 816 855 LDL-receptor class B 14.
 REPEAT 819 822 YWTD 10.
 REPEAT 856 898 LDL-receptor class B 15.
 REPEAT 859 862 YWTD 11.
 DOMAIN 902 942 EGF-like 3.
 REPEAT 989 1035 LDL-receptor class B 16.
 REPEAT 1036 1078 LDL-receptor class B 17.
 REPEAT 1079 1123 LDL-receptor class B 18.
 REPEAT 1124 1164 LDL-receptor class B 19.
 REPEAT 1165 1207 LDL-receptor class B 20.
 DOMAIN 1213 1254 EGF-like 4.
 DOMAIN 1258 1296 LDL-receptor class A 1.
 DOMAIN 1297 1333 LDL-receptor class A 2.
 DOMAIN 1335 1371 LDL-receptor class A 3.
 REGION 32 288 Beta-propeller 1.
 REGION 341 602 Beta-propeller 2.
 REGION 644 903 Beta-propeller 3.
 REGION 945 1212 Beta-propeller 4.
 MOTIF 1500 1506 PPPSP motif A.
 MOTIF 1538 1545 PPPSP motif B.
 MOTIF 1574 1581 PPPSP motif C.
 MOTIF 1591 1596 PPPSP motif D.
 MOTIF 1605 1612 PPPSP motif E.
 CARBOHYD 93 93 N-linked (GlcNAc...) (Potential).
 CARBOHYD 138 138 N-linked (GlcNAc...) (Potential).
 CARBOHYD 446 446 N-linked (GlcNAc...) (Potential).
 CARBOHYD 499 499 N-linked (GlcNAc...) (Potential).
 CARBOHYD 705 705 N-linked (GlcNAc...) (Potential).
 CARBOHYD 878 878 N-linked (GlcNAc...) (Potential).
 DISULFID 299 310 By similarity.
 DISULFID 306 321 By similarity.
 DISULFID 323 336 By similarity.
 DISULFID 605 616 By similarity.
 DISULFID 612 625 By similarity.
 DISULFID 627 640 By similarity.
 DISULFID 906 917 By similarity.
 DISULFID 913 926 By similarity.
 DISULFID 928 941 By similarity.
 DISULFID 1217 1228 By similarity.
 DISULFID 1224 1238 By similarity.
 DISULFID 1240 1253 By similarity.
 DISULFID 1259 1273 By similarity.
 DISULFID 1266 1286 By similarity.
 DISULFID 1280 1295 By similarity.
 DISULFID 1298 1310 By similarity.
 DISULFID 1305 1323 By similarity.
 DISULFID 1317 1332 By similarity.
 DISULFID 1336 1348 By similarity.
 DISULFID 1343 1361 By similarity.
 DISULFID 1355 1370 By similarity.  
Keyword
 Complete proteome; Developmental protein; Disease mutation; Disulfide bond; EGF-like domain; Endocytosis; Endoplasmic reticulum; Glycoprotein; Membrane; Osteogenesis imperfecta; Osteopetrosis; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1615 AA 
Protein Sequence
MEAAPPGPPW PLLLLLLLLL ALCGCPAPAA ASPLLLFANR RDVRLVDAGG VKLESTIVVS 60
GLEDAAAVDF QFSKGAVYWT DVSEEAIKQT YLNQTGAAVQ NVVISGLVSP DGLACDWVGK 120
KLYWTDSETN RIEVANLNGT SRKVLFWQDL DQPRAIALDP AHGYMYWTDW GETPRIERAG 180
MDGSTRKIIV DSDIYWPNGL TIDLEEQKLY WADAKLSFIH RANLDGSFRQ KVVEGSLTHP 240
FALTLSGDTL YWTDWQTRSI HACNKRTGGK RKEILSALYS PMDIQVLSQE RQPFFHTRCE 300
EDNGGCSHLC LLSPSEPFYT CACPTGVQLQ DNGRTCKAGA EEVLLLARRT DLRRISLDTP 360
DFTDIVLQVD DIRHAIAIDY DPLEGYVYWT DDEVRAIRRA YLDGSGAQTL VNTEINDPDG 420
IAVDWVARNL YWTDTGTDRI EVTRLNGTSR KILVSEDLDE PRAIALHPVM GLMYWTDWGE 480
NPKIECANLD GQERRVLVNA SLGWPNGLAL DLQEGKLYWG DAKTDKIEVI NVDGTKRRTL 540
LEDKLPHIFG FTLLGDFIYW TDWQRRSIER VHKVKASRDV IIDQLPDLMG LKAVNVAKVV 600
GTNPCADRNG GCSHLCFFTP HATRCGCPIG LELLSDMKTC IVPEAFLVFT SRAAIHRISL 660
ETNNNDVAIP LTGVKEASAL DFDVSNNHIY WTDVSLKTIS RAFMNGSSVE HVVEFGLDYP 720
EGMAVDWMGK NLYWADTGTN RIEVARLDGQ FRQVLVWRDL DNPRSLALDP TKGYIYWTEW 780
GGKPRIVRAF MDGTNCMTLV DKVGRANDLT IDYADQRLYW TDLDTNMIES SNMLGQERVV 840
IADDLPHPFG LTQYSDYIYW TDWNLHSIER ADKTSGRNRT LIQGHLDFVM DILVFHSSRQ 900
DGLNDCMHNN GQCGQLCLAI PGGHRCGCAS HYTLDPSSRN CSPPTTFLLF SQKSAISRMI 960
PDDQHSPDLI LPLHGLRNVK AIDYDPLDKF IYWVDGRQNI KRAKDDGTQP FVLTSLSQGQ 1020
NPDRQPHDLS IDIYSRTLFW TCEATNTINV HRLSGEAMGV VLRGDRDKPR AIVVNAERGY 1080
LYFTNMQDRA AKIERAALDG TEREVLFTTG LIRPVALVVD NTLGKLFWVD ADLKRIESCD 1140
LSGANRLTLE DANIVQPLGL TILGKHLYWI DRQQQMIERV EKTTGDKRTR IQGRVAHLTG 1200
IHAVEEVSLE EFSAHPCARD NGGCSHICIA KGDGTPRCSC PVHLVLLQNL LTCGEPPTCS 1260
PDQFACATGE IDCIPGAWRC DGFPECDDQS DEEGCPVCSA AQFPCARGQC VDLRLRCDGE 1320
ADCQDRSDEA DCDAICLPNQ FRCASGQCVL IKQQCDSFPD CIDGSDELMC EITKPPSDDS 1380
PAHSSAIGPV IGIILSLFVM GGVYFVCQRV VCQRYAGANG PFPHEYVSGT PHVPLNFIAP 1440
GGSQHGPFTG IACGKSMMSS VSLMGGRGGV PLYDRNHVTG ASSSSSSSTK ATLYPPILNP 1500
PPSPATDPSL YNMDMFYSSN IPATARPYRP YIIRGMAPPT TPCSTDVCDS DYSASRWKAS 1560
KYYLDLNSDS DPYPPPPTPH SQYLSAEDSC PPSPATERSY FHLFPPPPSP CTDSS 1615 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IDA:BHF-UCL.
 GO:0043235; C:receptor complex; IDA:BHF-UCL.
 GO:0015026; F:coreceptor activity; IBA:RefGenome.
 GO:0042813; F:Wnt-activated receptor activity; IBA:RefGenome.
 GO:0017147; F:Wnt-protein binding; IBA:RefGenome.
 GO:0060612; P:adipose tissue development; IMP:BHF-UCL.
 GO:0009952; P:anterior/posterior pattern specification; IBA:RefGenome.
 GO:0048539; P:bone marrow development; IMP:BHF-UCL.
 GO:0060349; P:bone morphogenesis; IMP:BHF-UCL.
 GO:0046849; P:bone remodeling; IBA:RefGenome.
 GO:0060444; P:branching involved in mammary gland duct morphogenesis; IBA:RefGenome.
 GO:0060070; P:canonical Wnt receptor signaling pathway; IDA:BHF-UCL.
 GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
 GO:0048596; P:embryonic camera-type eye morphogenesis; IBA:RefGenome.
 GO:0030326; P:embryonic limb morphogenesis; IBA:RefGenome.
 GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IBA:RefGenome.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0001702; P:gastrulation with mouth forming second; IBA:RefGenome.
 GO:0006007; P:glucose catabolic process; IMP:BHF-UCL.
 GO:0045668; P:negative regulation of osteoblast differentiation; IMP:BHF-UCL.
 GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:BHF-UCL.
 GO:0002076; P:osteoblast development; IBA:RefGenome.
 GO:0045600; P:positive regulation of fat cell differentiation; IMP:BHF-UCL.
 GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:BHF-UCL.
 GO:0045840; P:positive regulation of mitosis; IDA:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0008217; P:regulation of blood pressure; IMP:BHF-UCL.
 GO:0060828; P:regulation of canonical Wnt receptor signaling pathway; IMP:BHF-UCL.
 GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IBA:RefGenome.
 GO:0061304; P:retinal blood vessel morphogenesis; IMP:BHF-UCL.
 GO:0044332; P:Wnt receptor signaling pathway involved in dorsal/ventral axis specification; IDA:BHF-UCL. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR000742; EG-like_dom.
 IPR023415; LDLR_class-A_CS.
 IPR000033; LDLR_classB_rpt.
 IPR002172; LDrepeatLR_classA_rpt.
 IPR017049; Low_density_Lipo_rcpt-rel_p5/6. 
Pfam
 PF00057; Ldl_recept_a
 PF00058; Ldl_recept_b 
SMART
 SM00181; EGF
 SM00192; LDLa
 SM00135; LY 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01187; EGF_CA
 PS01209; LDLRA_1
 PS50068; LDLRA_2
 PS51120; LDLRB 
PRINTS