CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001107
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Low-density lipoprotein receptor-related protein 4 
Protein Synonyms/Alias
 LRP-4; Multiple epidermal growth factor-like domains 7 
Gene Name
 LRP4 
Gene Synonyms/Alias
 KIAA0816; LRP10; MEGF7 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1753LYRHKKSKFTDPGMGubiquitination[1, 2]
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] 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] 
Functional Description
 Mediates SOST-dependent inhibition of bone formation. Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling. Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN- induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes. 
Sequence Annotation
 DOMAIN 26 67 LDL-receptor class A 1.
 DOMAIN 70 106 LDL-receptor class A 2.
 DOMAIN 109 144 LDL-receptor class A 3.
 DOMAIN 147 183 LDL-receptor class A 4.
 DOMAIN 190 226 LDL-receptor class A 5.
 DOMAIN 230 266 LDL-receptor class A 6.
 DOMAIN 269 305 LDL-receptor class A 7.
 DOMAIN 311 350 LDL-receptor class A 8.
 DOMAIN 354 394 EGF-like 1; calcium-binding (Potential).
 DOMAIN 395 434 EGF-like 2; calcium-binding (Potential).
 REPEAT 480 522 LDL-receptor class B 1.
 REPEAT 523 565 LDL-receptor class B 2.
 REPEAT 566 609 LDL-receptor class B 3.
 REPEAT 610 652 LDL-receptor class B 4.
 REPEAT 653 693 LDL-receptor class B 5.
 DOMAIN 698 737 EGF-like 3.
 REPEAT 785 827 LDL-receptor class B 6.
 REPEAT 828 870 LDL-receptor class B 7.
 REPEAT 871 914 LDL-receptor class B 8.
 REPEAT 915 956 LDL-receptor class B 9.
 REPEAT 957 998 LDL-receptor class B 10.
 REPEAT 1093 1135 LDL-receptor class B 11.
 REPEAT 1136 1178 LDL-receptor class B 12.
 REPEAT 1179 1222 LDL-receptor class B 13.
 REPEAT 1223 1263 LDL-receptor class B 14.
 REPEAT 1264 1306 LDL-receptor class B 15.
 REPEAT 1397 1439 LDL-receptor class B 16.
 REPEAT 1440 1482 LDL-receptor class B 17.
 REPEAT 1483 1526 LDL-receptor class B 18.
 REPEAT 1527 1568 LDL-receptor class B 19.
 REPEAT 1569 1610 LDL-receptor class B 20.
 MOTIF 1766 1769 Endocytosis signal (Potential).
 MOD_RES 1887 1887 Phosphoserine (By similarity).
 CARBOHYD 264 264 N-linked (GlcNAc...) (Potential).
 CARBOHYD 498 498 N-linked (GlcNAc...) (Potential).
 CARBOHYD 719 719 N-linked (GlcNAc...) (Potential).
 CARBOHYD 901 901 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1077 1077 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1415 1415 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1467 1467 N-linked (GlcNAc...) (Potential).
 DISULFID 27 44 By similarity.
 DISULFID 34 57 By similarity.
 DISULFID 51 66 By similarity.
 DISULFID 71 83 By similarity.
 DISULFID 78 96 By similarity.
 DISULFID 90 105 By similarity.
 DISULFID 110 122 By similarity.
 DISULFID 117 135 By similarity.
 DISULFID 129 143 By similarity.
 DISULFID 148 160 By similarity.
 DISULFID 155 173 By similarity.
 DISULFID 167 182 By similarity.
 DISULFID 191 203 By similarity.
 DISULFID 198 216 By similarity.
 DISULFID 210 225 By similarity.
 DISULFID 231 243 By similarity.
 DISULFID 238 256 By similarity.
 DISULFID 250 265 By similarity.
 DISULFID 270 282 By similarity.
 DISULFID 277 295 By similarity.
 DISULFID 289 304 By similarity.
 DISULFID 312 324 By similarity.
 DISULFID 319 337 By similarity.
 DISULFID 331 349 By similarity.
 DISULFID 358 369 By similarity.
 DISULFID 365 378 By similarity.
 DISULFID 380 393 By similarity.
 DISULFID 399 409 By similarity.
 DISULFID 405 418 By similarity.
 DISULFID 420 433 By similarity.
 DISULFID 702 713 By similarity.
 DISULFID 709 722 By similarity.
 DISULFID 724 736 By similarity.  
Keyword
 Calcium; Complete proteome; Developmental protein; Differentiation; Disease mutation; Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1905 AA 
Protein Sequence
MRRQWGALLL GALLCAHGLA SSPECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH 60
SDEDGCILPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS DEQDCPPREC EEDEFPCQNG 120
YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE 180
NCPSAVPAPP CNLEEFQCAY GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS 240
GLCINAGWRC DGDADCDDQS DERNCTTSMC TAEQFRCHSG RCVRLSWRCD GEDDCADNSD 300
EENCENTGSP QCALDQFLCW NGRCIGQRKL CNGVNDCGDN SDESPQQNCR PRTGEENCNV 360
NNGGCAQKCQ MVRGAVQCTC HTGYRLTEDG HTCQDVNECA EEGYCSQGCT NSEGAFQCWC 420
ETGYELRPDR RSCKALGPEP VLLFANRIDI RQVLPHRSEY TLLLNNLENA IALDFHHRRE 480
LVFWSDVTLD RILRANLNGS NVEEVVSTGL ESPGGLAVDW VHDKLYWTDS GTSRIEVANL 540
DGAHRKVLLW QNLEKPRAIA LHPMEGTIYW TDWGNTPRIE ASSMDGSGRR IIADTHLFWP 600
NGLTIDYAGR RMYWVDAKHH VIERANLDGS HRKAVISQGL PHPFAITVFE DSLYWTDWHT 660
KSINSANKFT GKNQEIIRNK LHFPMDIHTL HPQRQPAGKN RCGDNNGGCT HLCLPSGQNY 720
TCACPTGFRK ISSHACAQSL DKFLLFARRM DIRRISFDTE DLSDDVIPLA DVRSAVALDW 780
DSRDDHVYWT DVSTDTISRA KWDGTGQEVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI 840
EVANTDGSMR TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGMD ASGRQVIISS 900
NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG LTLYGERIYW 960
TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRRRP PVSTPCAMEN GGCSHLCLRS 1020
PNPSGFSCTC PTGINLLSDG KTCSPGMNSF LIFARRIDIR MVSLDIPYFA DVVVPINITM 1080
KNTIAIGVDP QEGKVYWSDS TLHRISRANL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW 1140
TDTGTNRIEV GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS 1200
DRAVLINNNL GWPNGLTVDK ASSQLLWADA HTERIEAADL NGANRHTLVS PVQHPYGLTL 1260
LDSYIYWTDW QTRSIHRADK GTGSNVILVR SNLPGLMDMQ AVDRAQPLGF NKCGSRNGGC 1320
SHLCLPRPSG FSCACPTGIQ LKGDGKTCDP SPETYLLFSS RGSIRRISLD TSDHTDVHVP 1380
VPELNNVISL DYDSVDGKVY YTDVFLDVIR RADLNGSNME TVIGRGLKTT DGLAVDWVAR 1440
NLYWTDTGRN TIEASRLDGS CRKVLINNSL DEPRAIAVFP RKGYLFWTDW GHIAKIERAN 1500
LDGSERKVLI NTDLGWPNGL TLDYDTRRIY WVDAHLDRIE SADLNGKLRQ VLVSHVSHPF 1560
ALTQQDRWIY WTDWQTKSIQ RVDKYSGRNK ETVLANVEGL MDIIVVSPQR QTGTNACGVN 1620
NGGCTHLCFA RASDFVCACP DEPDSRPCSL VPGLVPPAPR ATGMSEKSPV LPNTPPTTLY 1680
SSTTRTRTSL EEVEGRCSER DARLGLCARS NDAVPAAPGE GLHISYAIGG LLSILLILVV 1740
IAALMLYRHK KSKFTDPGMG NLTYSNPSYR TSTQEVKIEA IPKPAMYNQL CYKKEGGPDH 1800
NYTKEKIKIV EGICLLSGDD AEWDDLKQLR SSRGGLLRDH VCMKTDTVSI QASSGSLDDT 1860
ETEQLLQEEQ SECSSVHTAA TPERRGSLPD TGWKHERKLS SESQV 1905 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0005509; F:calcium ion binding; NAS:UniProtKB.
 GO:0009953; P:dorsal/ventral pattern formation; IEA:Compara.
 GO:0042733; P:embryonic digit morphogenesis; IEA:Compara.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0001942; P:hair follicle development; IEA:Compara.
 GO:0001822; P:kidney development; IEA:Compara.
 GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IDA:UniProtKB.
 GO:0030279; P:negative regulation of ossification; IMP:UniProtKB.
 GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Compara.
 GO:0009954; P:proximal/distal pattern formation; IEA:Compara.
 GO:0043113; P:receptor clustering; IEA:Compara.
 GO:0001932; P:regulation of protein phosphorylation; IEA:Compara.
 GO:0051124; P:synaptic growth at neuromuscular junction; IEA:Compara.
 GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR026823; cEGF.
 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
 PF12662; cEGF
 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