LRP4_HUMAN - dbPTM
LRP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRP4_HUMAN
UniProt AC O75096
Protein Name Low-density lipoprotein receptor-related protein 4
Gene Name LRP4
Organism Homo sapiens (Human).
Sequence Length 1905
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein 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. May play an essential role in the process of digit differentiation (By similarity)..
Protein Sequence MRRQWGALLLGALLCAHGLASSPECACGRSHFTCAVSALGECTCIPAQWQCDGDNDCGDHSDEDGCILPTCSPLDFHCDNGKCIRRSWVCDGDNDCEDDSDEQDCPPRECEEDEFPCQNGYCIRSLWHCDGDNDCGDNSDEQCDMRKCSDKEFRCSDGSCIAEHWYCDGDTDCKDGSDEENCPSAVPAPPCNLEEFQCAYGRCILDIYHCDGDDDCGDWSDESDCSSHQPCRSGEFMCDSGLCINAGWRCDGDADCDDQSDERNCTTSMCTAEQFRCHSGRCVRLSWRCDGEDDCADNSDEENCENTGSPQCALDQFLCWNGRCIGQRKLCNGVNDCGDNSDESPQQNCRPRTGEENCNVNNGGCAQKCQMVRGAVQCTCHTGYRLTEDGHTCQDVNECAEEGYCSQGCTNSEGAFQCWCETGYELRPDRRSCKALGPEPVLLFANRIDIRQVLPHRSEYTLLLNNLENAIALDFHHRRELVFWSDVTLDRILRANLNGSNVEEVVSTGLESPGGLAVDWVHDKLYWTDSGTSRIEVANLDGAHRKVLLWQNLEKPRAIALHPMEGTIYWTDWGNTPRIEASSMDGSGRRIIADTHLFWPNGLTIDYAGRRMYWVDAKHHVIERANLDGSHRKAVISQGLPHPFAITVFEDSLYWTDWHTKSINSANKFTGKNQEIIRNKLHFPMDIHTLHPQRQPAGKNRCGDNNGGCTHLCLPSGQNYTCACPTGFRKISSHACAQSLDKFLLFARRMDIRRISFDTEDLSDDVIPLADVRSAVALDWDSRDDHVYWTDVSTDTISRAKWDGTGQEVVVDTSLESPAGLAIDWVTNKLYWTDAGTDRIEVANTDGSMRTVLIWENLDRPRDIVVEPMGGYMYWTDWGASPKIERAGMDASGRQVIISSNLTWPNGLAIDYGSQRLYWADAGMKTIEFAGLDGSKRKVLIGSQLPHPFGLTLYGERIYWTDWQTKSIQSADRLTGLDRETLQENLENLMDIHVFHRRRPPVSTPCAMENGGCSHLCLRSPNPSGFSCTCPTGINLLSDGKTCSPGMNSFLIFARRIDIRMVSLDIPYFADVVVPINITMKNTIAIGVDPQEGKVYWSDSTLHRISRANLDGSQHEDIITTGLQTTDGLAVDAIGRKVYWTDTGTNRIEVGNLDGSMRKVLVWQNLDSPRAIVLYHEMGFMYWTDWGENAKLERSGMDGSDRAVLINNNLGWPNGLTVDKASSQLLWADAHTERIEAADLNGANRHTLVSPVQHPYGLTLLDSYIYWTDWQTRSIHRADKGTGSNVILVRSNLPGLMDMQAVDRAQPLGFNKCGSRNGGCSHLCLPRPSGFSCACPTGIQLKGDGKTCDPSPETYLLFSSRGSIRRISLDTSDHTDVHVPVPELNNVISLDYDSVDGKVYYTDVFLDVIRRADLNGSNMETVIGRGLKTTDGLAVDWVARNLYWTDTGRNTIEASRLDGSCRKVLINNSLDEPRAIAVFPRKGYLFWTDWGHIAKIERANLDGSERKVLINTDLGWPNGLTLDYDTRRIYWVDAHLDRIESADLNGKLRQVLVSHVSHPFALTQQDRWIYWTDWQTKSIQRVDKYSGRNKETVLANVEGLMDIIVVSPQRQTGTNACGVNNGGCTHLCFARASDFVCACPDEPDSRPCSLVPGLVPPAPRATGMSEKSPVLPNTPPTTLYSSTTRTRTSLEEVEGRCSERDARLGLCARSNDAVPAAPGEGLHISYAIGGLLSILLILVVIAALMLYRHKKSKFTDPGMGNLTYSNPSYRTSTQEVKIEAIPKPAMYNQLCYKKEGGPDHNYTKEKIKIVEGICLLSGDDAEWDDLKQLRSSRGGLLRDHVCMKTDTVSIQASSGSLDDTETEQLLQEEQSECSSVHTAATPERRGSLPDTGWKHERKLSSESQV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
70O-linked_GlycosylationEDGCILPTCSPLDFH
CCCCEECCCCCCEEE		23.36OGP
184O-linked_GlycosylationSDEENCPSAVPAPPC
CCCCCCCCCCCCCCC		44.06OGP
264N-linked_GlycosylationDDQSDERNCTTSMCT
CCCCCCCCCCCCCHH		25.99UniProtKB CARBOHYD
286PhosphorylationSGRCVRLSWRCDGED
CCCEEEEEEECCCCC		11.2524719451
498N-linked_GlycosylationRILRANLNGSNVEEV
HHHHHHCCCCCHHHH		52.21UniProtKB CARBOHYD
604O-linked_GlycosylationLFWPNGLTIDYAGRR
EECCCCEEEECCCCE		17.1329351928
689PhosphorylationHFPMDIHTLHPQRQP
CCCCCHHHCCCCCCC		27.39-
719N-linked_GlycosylationLCLPSGQNYTCACPT
EECCCCCCEEEECCC		37.29UniProtKB CARBOHYD
733PhosphorylationTGFRKISSHACAQSL
CCCHHHCHHHHHHHH		20.6930631047
872PhosphorylationVVEPMGGYMYWTDWG
EEECCCCEEEEECCC		4.9423663014
874PhosphorylationEPMGGYMYWTDWGAS
ECCCCEEEEECCCCC		9.1823663014
876PhosphorylationMGGYMYWTDWGASPK
CCCEEEEECCCCCCC		12.3723663014
881PhosphorylationYWTDWGASPKIERAG
EEECCCCCCCCCCCC		23.8423663014
901N-linked_GlycosylationRQVIISSNLTWPNGL
CEEEECCCCCCCCCE		34.40UniProtKB CARBOHYD
918PhosphorylationDYGSQRLYWADAGMK
ECCCCEEEEECCCCC		10.7624719451
935PhosphorylationEFAGLDGSKRKVLIG
EEECCCCCCCEEEEE		29.0224719451
975PhosphorylationIQSADRLTGLDRETL
HHHHHHHHCCCHHHH		36.2724719451
1008UbiquitinationPVSTPCAMENGGCSH
CCCCCCEECCCCCCE		5.3921890473
1063PhosphorylationRIDIRMVSLDIPYFA
CCEEEEEECCCCCCC		15.8122210691
1068PhosphorylationMVSLDIPYFADVVVP
EEECCCCCCCCEEEE		16.2522210691
1077N-linked_GlycosylationADVVVPINITMKNTI
CCEEEEEEEEECCEE		20.01UniProtKB CARBOHYD
1113PhosphorylationSRANLDGSQHEDIIT
HHCCCCCCCCCCCHH		28.20-
1126PhosphorylationITTGLQTTDGLAVDA
HHCCCCCCCCEEEEC		18.34-
1156PhosphorylationEVGNLDGSMRKVLVW
EECCCCCCCEEEEEE		18.3227282143
1355PhosphorylationCDPSPETYLLFSSRG
CCCCCCEEEEEECCC		10.3518083107
1415N-linked_GlycosylationVIRRADLNGSNMETV
HHHHHHCCCCCCCEE		53.01UniProtKB CARBOHYD
1467N-linked_GlycosylationSCRKVLINNSLDEPR
CCCEEEECCCCCCCE		28.07UniProtKB CARBOHYD
1484PhosphorylationAVFPRKGYLFWTDWG
EEEECCCEEEEECHH		11.19-
1485UbiquitinationVFPRKGYLFWTDWGH
EEECCCEEEEECHHH		3.8321890473
1512PhosphorylationERKVLINTDLGWPNG
CCEEEEECCCCCCCC		26.13-
1674O-linked_GlycosylationKSPVLPNTPPTTLYS
CCCCCCCCCCCEECC		28.80OGP
1678PhosphorylationLPNTPPTTLYSSTTR
CCCCCCCEECCCCCC		29.4930387612
1681O-linked_GlycosylationTPPTTLYSSTTRTRT
CCCCEECCCCCCCCC		25.07OGP
1681PhosphorylationTPPTTLYSSTTRTRT
CCCCEECCCCCCCCC		25.0730387612
1682O-linked_GlycosylationPPTTLYSSTTRTRTS
CCCEECCCCCCCCCC		21.90OGP
1686O-linked_GlycosylationLYSSTTRTRTSLEEV
ECCCCCCCCCCHHHH		35.89OGP
1688O-linked_GlycosylationSSTTRTRTSLEEVEG
CCCCCCCCCHHHHCC		36.7355834835
1689O-linked_GlycosylationSTTRTRTSLEEVEGR
CCCCCCCCHHHHCCH		30.4155834841
1753UbiquitinationLYRHKKSKFTDPGMG
HHHHHCCCCCCCCCC		62.2521890473
1763PhosphorylationDPGMGNLTYSNPSYR
CCCCCCCCCCCCCCC		28.9821945579
1764PhosphorylationPGMGNLTYSNPSYRT
CCCCCCCCCCCCCCC		15.0421945579
1765PhosphorylationGMGNLTYSNPSYRTS
CCCCCCCCCCCCCCC		36.7121945579
1773PhosphorylationNPSYRTSTQEVKIEA
CCCCCCCCCEEEEEE		28.3028985074
1777UbiquitinationRTSTQEVKIEAIPKP
CCCCCEEEEEECCCC		33.7933845483
1787PhosphorylationAIPKPAMYNQLCYKK
ECCCCHHHCCCCCCC		11.2327642862
1792PhosphorylationAMYNQLCYKKEGGPD
HHHCCCCCCCCCCCC		33.42-
1833MethylationLKQLRSSRGGLLRDH
HHHHHHCCCCCCCCC		44.43-
1853PhosphorylationDTVSIQASSGSLDDT
CEEEEEECCCCCCHH		20.8928348404
1854PhosphorylationTVSIQASSGSLDDTE
EEEEEECCCCCCHHH		35.1028348404
1856PhosphorylationSIQASSGSLDDTETE
EEEECCCCCCHHHHH		30.4928348404
1860PhosphorylationSSGSLDDTETEQLLQ
CCCCCCHHHHHHHHH		44.4628348404
1871PhosphorylationQLLQEEQSECSSVHT
HHHHHHHHHHCCCCC		43.8028348404
1874PhosphorylationQEEQSECSSVHTAAT
HHHHHHHCCCCCCCC		31.2028348404
1875PhosphorylationEEQSECSSVHTAATP
HHHHHHCCCCCCCCC		29.5828348404
1878PhosphorylationSECSSVHTAATPERR
HHHCCCCCCCCCCCC		18.8128348404
1881PhosphorylationSSVHTAATPERRGSL
CCCCCCCCCCCCCCC		24.1828348404
1887PhosphorylationATPERRGSLPDTGWK
CCCCCCCCCCCCCCC		34.6125159151
1891PhosphorylationRRGSLPDTGWKHERK
CCCCCCCCCCCCCCC		42.9030108239
1900PhosphorylationWKHERKLSSESQV--
CCCCCCCCCCCCC--		34.7929255136
1901PhosphorylationKHERKLSSESQV---
CCCCCCCCCCCC---		52.2629255136
1903PhosphorylationERKLSSESQV-----
CCCCCCCCCC-----		37.8933259812
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of LRP4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRP4_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LRP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WHRN_HUMANDFNB31physical
12421765
PCLI1_HUMANPID1physical
20205790
Drug and Disease Associations
Kegg Disease
H00853 Cenani-Lenz syndactyly syndrome
OMIM Disease
212780Cenani-Lenz syndactyly syndrome (CLSS)
614305Sclerosteosis 2 (SOST2)
616304Myasthenic syndrome, congenital, 17 (CMS17)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRP4_HUMAN

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Related Literatures of Post-Translational Modification

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