LRP6_MOUSE - dbPTM
LRP6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRP6_MOUSE
UniProt AC O88572
Protein Name Low-density lipoprotein receptor-related protein 6
Gene Name Lrp6
Organism Mus musculus (Mouse).
Sequence Length 1613
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Endoplasmic reticulum. Membrane raft . On Wnt signaling, undergoes a cycle of caveolin- or clathrin-mediated endocytosis and plasma membrane location. Released from the endoplasmic reticulum on palm
Protein 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. Required for posterior patterning of the epiblast during gastrulation (By similarity)..
Protein Sequence MGAVLRSLLACSFCVLLRAAPLLLYANRRDLRLVDATNGKENATIVVGGLEDAAAVDFVFGHGLIYWSDVSEEAIKRTEFNKSESVQNVVVSGLLSPDGLACDWLGEKLYWTDSETNRIEVSNLDGSLRKVLFWQELDQPRAIALDPSSGFMYWTDWGEVPKIERAGMDGSSRFVIINTEIYWPNGLTLDYQERKLYWADAKLNFIHKSNLDGTNRQAVVKGSLPHPFALTLFEDTLYWTDWNTHSILACNKYTGEGLREIHSNIFSPMDIHAFSQQRQPNATNPCGIDNGGCSHLCLMSPVKPFYQCACPTGVKLMENGKTCKDGATELLLLARRTDLRRISLDTPDFTDIVLQLEDIRHAIAIDYDPVEGYIYWTDDEVRAIRRSFIDGSGSQFVVTAQIAHPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTMRKILISEDLEEPRAIVLDPMVGYMYWTDWGEIPKIERAALDGSDRVVLVNTSLGWPNGLALDYDEGTIYWGDAKTDKIEVMNTDGTGRRVLVEDKIPHIFGFTLLGDYVYWTDWQRRSIERVHKRSAEREVIIDQLPDLMGLKATSVHRVIGSNPCAEDNGGCSHLCLYRPQGLRCACPIGFELIGDMKTCIVPEAFLLFSRRADIRRISLETNNNNVAIPLTGVKEASALDFDVTDNRIYWTDISLKTISRAFMNGSALEHVVEFGLDYPEGMAVDWLGKNLYWADTGTNRIEVSKLDGQHRQVLVWKDLDSPRALALDPAEGFMYWTEWGGKPKIDRAAMDGSERTTLVPNVGRANGLTIDYAKRRLYWTDLDTNLIESSDMLGLNREVIADDLPHPFGLTQYQDYIYWTDWSRRSIERANKTSGQNRTIIQGHLDYVMDILVFHSSRQAGWNECASSNGHCSHLCLAVPVGGFVCGCPAHYSLNADNRTCSAPSTFLLFSQKSAINRMVIDEQQSPDIILPIHSLRNVRAIDYDPLDKQLYWIDSRQNSIRKAHEDGGQGFNVVANSVANQNLEIQPYDLSIDIYSRYIYWTCEATNVIDVTRLDGRSVGVVLKGEQDRPRAIVVNPEKGYMYFTNLQERSPKIERAALDGTEREVLFFSGLSKPIALALDSKLGKLFWADSDLRRIESSDLSGANRIVLEDSNILQPVGLTVFENWLYWIDKQQQMIEKIDMTGREGRTKVQARIAQLSDIHAVKELNLQEYRQHPCAQDNGGCSHICLVKGDGTTRCSCPMHLVLLQDELSCGEPPTCSPQQFTCFTGDIDCIPVAWRCDGFTECEDHSDELNCPVCSESQFQCASGQCIDGALRCNGDANCQDKSDEKNCEVLCLIDQFRCANGQCVGKHKKCDHSVDCSDRSDELDCYPTEEPAPQATNTVGSVIGVIVTIFVSGTIYFICQRMLCPRMKGDGETMTNDYVVHSPASVPLGYVPHPSSLSGSLPGMSRGKSMISSLSIMGGSSGPPYDRAHVTGASSSSSSSTKGTYFPAILNPPPSPATERSHYTMEFGYSSNSPSTHRSYSYRPYSYRHFAPPTTPCSTDVCDSDYAPSRRMTSVATAKGYTSDVNYDSEPVPPPPTPRSQYLSAEENYESCPPSPYTERSYSHHLYPPPPSPCTDSS
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
42N-linked_GlycosylationDATNGKENATIVVGG
ECCCCCCCEEEEECC
45.96-
81N-linked_GlycosylationAIKRTEFNKSESVQN
HHHHCCCCCCHHCCE
40.48-
281N-linked_GlycosylationFSQQRQPNATNPCGI
HCCCCCCCCCCCCCC
51.57-
433N-linked_GlycosylationRIEVTRLNGTMRKIL
EEEEEEECCCEEEEE
40.37-
486N-linked_GlycosylationSDRVVLVNTSLGWPN
CCEEEEEECCCCCCC
21.57-
539PhosphorylationIPHIFGFTLLGDYVY
CCEEEEEEEECCEEE
22.8125777480
544PhosphorylationGFTLLGDYVYWTDWQ
EEEEECCEEEECHHH
8.1425777480
546PhosphorylationTLLGDYVYWTDWQRR
EEECCEEEECHHHHH
9.0725777480
548PhosphorylationLGDYVYWTDWQRRSI
ECCEEEECHHHHHHH
15.0725777480
679PhosphorylationTDNRIYWTDISLKTI
CCCEEEEEECCHHHH
13.39-
692N-linked_GlycosylationTISRAFMNGSALEHV
HHHHHHHCCHHHHHH
34.51-
859N-linked_GlycosylationRRSIERANKTSGQNR
HHHHHHHHCCCCCCC
55.12-
865N-linked_GlycosylationANKTSGQNRTIIQGH
HHCCCCCCCEEEEHH
46.73-
926N-linked_GlycosylationHYSLNADNRTCSAPS
CEECCCCCCEECCCC
38.46-
1189PhosphorylationQARIAQLSDIHAVKE
HHHHHHHHHHHHHHC
23.5726026062
1394S-palmitoylationSGTIYFICQRMLCPR
CCHHHHHHHHHCCCC
1.18-
1399S-palmitoylationFICQRMLCPRMKGDG
HHHHHHCCCCCCCCC
1.15-
1420PhosphorylationYVVHSPASVPLGYVP
EEEECCCCCCCCCCC
27.87-
1430PhosphorylationLGYVPHPSSLSGSLP
CCCCCCHHHCCCCCC
40.66-
1444PhosphorylationPGMSRGKSMISSLSI
CCCCCCHHHHHHCEE
24.95-
1469PhosphorylationRAHVTGASSSSSSST
CCCCCCCCCCCCCCC
31.9023684622
1470PhosphorylationAHVTGASSSSSSSTK
CCCCCCCCCCCCCCC
33.4323684622
1471PhosphorylationHVTGASSSSSSSTKG
CCCCCCCCCCCCCCC
31.5723684622
1475PhosphorylationASSSSSSSTKGTYFP
CCCCCCCCCCCCCCC
35.7723684622
1479PhosphorylationSSSSTKGTYFPAILN
CCCCCCCCCCCEEEC
24.44-
1490PhosphorylationAILNPPPSPATERSH
EEECCCCCCCCCCCE
32.7026824392
1493PhosphorylationNPPPSPATERSHYTM
CCCCCCCCCCCEEEE
35.0026745281
1504PhosphorylationHYTMEFGYSSNSPST
EEEEEECCCCCCCCC
17.7829514104
1505PhosphorylationYTMEFGYSSNSPSTH
EEEEECCCCCCCCCC
24.3529550500
1506PhosphorylationTMEFGYSSNSPSTHR
EEEECCCCCCCCCCC
32.6123984901
1508PhosphorylationEFGYSSNSPSTHRSY
EECCCCCCCCCCCCC
23.3626643407
1510PhosphorylationGYSSNSPSTHRSYSY
CCCCCCCCCCCCCCC
36.3423984901
1511PhosphorylationYSSNSPSTHRSYSYR
CCCCCCCCCCCCCCC
25.3723984901
1515PhosphorylationSPSTHRSYSYRPYSY
CCCCCCCCCCCCCEE
15.0729514104
1517PhosphorylationSTHRSYSYRPYSYRH
CCCCCCCCCCCEECC
13.8429514104
1520PhosphorylationRSYSYRPYSYRHFAP
CCCCCCCCEECCCCC
14.8829514104
1539PhosphorylationCSTDVCDSDYAPSRR
CCCCCCCCCCCCCCC
27.6529514104
1541PhosphorylationTDVCDSDYAPSRRMT
CCCCCCCCCCCCCCC
25.1029514104
1562PhosphorylationGYTSDVNYDSEPVPP
CCCCCCCCCCCCCCC
22.2426032504
1564PhosphorylationTSDVNYDSEPVPPPP
CCCCCCCCCCCCCCC
33.1829514104
1572PhosphorylationEPVPPPPTPRSQYLS
CCCCCCCCCHHHCCC
36.7929514104
1579PhosphorylationTPRSQYLSAEENYES
CCHHHCCCHHHCCCC
28.80-
1590PhosphorylationNYESCPPSPYTERSY
CCCCCCCCCCCCCCC
18.7126745281
1593PhosphorylationSCPPSPYTERSYSHH
CCCCCCCCCCCCCCC
28.4526745281
1607PhosphorylationHLYPPPPSPCTDSS-
CCCCCCCCCCCCCC-
38.0826643407
1610PhosphorylationPPPPSPCTDSS----
CCCCCCCCCCC----
42.1526643407
1612PhosphorylationPPSPCTDSS------
CCCCCCCCC------
21.5726643407
1613PhosphorylationPSPCTDSS-------
CCCCCCCC-------
47.2326643407

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
1420SPhosphorylationKinaseCK1-Uniprot
1430SPhosphorylationKinaseCK1-Uniprot
1490SPhosphorylationKinaseCDK14O35495
Uniprot
1490SPhosphorylationKinaseGRK5Q8VEB1
Uniprot
1490SPhosphorylationKinaseGRK6O70293
Uniprot
1493TPhosphorylationKinaseCK1-Uniprot
1579SPhosphorylationKinaseCSNK2A1P68400
GPS
1579SPhosphorylationKinaseCK2A1Q60737
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1479TPhosphorylation

-
1490SPhosphorylation

-

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 LRP6_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WNT1_MOUSEWnt1physical
16126904
DKK1_MOUSEDkk1physical
16126904
KREM2_MOUSEKremen2physical
16126904
WNT5A_MOUSEWnt5aphysical
19056682
WNT5A_MOUSEWnt5agenetic
19056682
MESD_MOUSEMesdc2physical
16126904
MESD_MOUSEMesdc2physical
12581525

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRP6_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP