MPRI_MOUSE - dbPTM
MPRI_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPRI_MOUSE
UniProt AC Q07113
Protein Name Cation-independent mannose-6-phosphate receptor
Gene Name Igf2r
Organism Mus musculus (Mouse).
Sequence Length 2483
Subcellular Localization Lysosome membrane
Single-pass type I membrane protein.
Protein Description Acts as a positive regulator of T-cell coactivation, by binding DPP4 (By similarity). Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2..
Protein Sequence MRAVQLGPVPSGPRVALLPPLLLLLLLAAAGSAQAQAVDLDALCSYTWEAVDSKNNAVYKINVCGNVGISSCGPTSAICMCDLKTENCRSVGDSLLRSSARSLLEFNTTMGCQPSDSQHRIQTSITFLCGKTLGTPEFVTATDCVHYFEWRTTAACKKDIFKADKEVPCYAFDDKLQKHDLNPLIKLNGGYLVDDSDPDTSLFINVCRDIDSLRDPSTQLRVCPAGTAACLLKGNQAFDVGRPKEGLKLLSKDRLVLTYVKEEGEKPDFCNGHSPAVTVTFVCPSERREGTIPKLTAKSNCRYEVEWITEYACHRDYLQSESCSLSSEQHDITIDLSPLAQYGGSPYVSDGREYTFFINVCGDTKVSLCNNKEAAVCQEKKADSTQVKIAGRHQNQTLRYSDGDLTLIYSGGDECSSGFQRMSVINFECNKTAGKDGRGEPVFTGEVDCTYFFTWDTKYACIKEKEDLLCGAINGKKRYDLSVLARHSESEQNWEAVDGSQAESEKYFFINVCHRVLQEGKARNCPEDAAVCAVDKNGSKNLGKFVSSPTKEKGHIQLSYTDGDDCGSDKKISTNITLVCKPGDLESAPVLRAARSDGCFYEFEWHTAAACVLSKTEGENCTVLDAQAGFSFDLSLLTKKNGAYKVETEKYDFYINVCGPVSMDPCQSNSGACQVAKSGKSWNLGLSSTKLTYYDGMIQLSYRNGTPYNNEKHTPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPEEPLECMVTDPSMMEQYDLSSLVKSEGGSGGNWYAMENSREHVTRRKYYLNVCRPLNPVPGCDRYASACQMKYENHEGSLAETVSISNLGVAKIGPVVEESGSLLLEYVNGSACTTSDGQLTTYSTRIHLVCGRGFMNSHPIFTFNWECVVSFLWNTEAACPIQTITETDQACSIRDPSSGFVFNLSPLNDSAQGHVVLGIGKTFVFNICGAMPACGTVAGKPAYGCEAETQIEDIKDLRPQRPVGMERSLQLSAEGFLTLTYKGSSPSDRGTAFIIRFICNDDIYPGAPKFLHQDIDSTRGIRNTYFEFETALACTPSLVDCQVTDPAGNEYDLSALSMVRKPWTAVDTSAYGKRRHFYLSVCNPLPYIPGCHGIALGSCMVSEDNSFNLGVVQISPQATGNGSLSILYVNGDRCGDQRFSTRIVFECAQTSGSPMFQFVNNCEYVFVWRTVEACPVIREEGDNCQVKDPRHGNLYDLKPLGLNDTIVSVGEYTYYLRVCGKLSSDVCSAHDGSKAVSSCQEKKGPQGFQKVAGLLSQKLTFENGLLKMNYTGGDTCHKVYQRSTTIYFYCDRTTQKPVFLKETSDCSYMFEWRTQYACPPFNVTECSVQDAAGNSIDLSSLSRYSDNWEAVTRTGATEHYLINVCKSLSPHAGTEPCPPEAAVCLLNGSKPVNLGKVRDGPQWTDGVTVLQYVDGDLCPDKIRRRSTIIRFTCSDNQVNSRPLFISAVQDCEYTFSWPTPSACPVKSNTHDDCQVTNPSTGHLFDLSSLSGRAGINASYSEKGLVFMSICEENENCGPGVGACFGQTRISVGKASKRLSYKDQVLQLVYENGSPCPSLSDLRYKSVISFVCRPEAGPTNRPMLISLDKQTCTLFFSWHTPLACEQATECTVRNGSSIIDLSPLIHRTGGYEAYDESEDDTSDTTPDFYINICQPLNPMHGVPCPAGASVCKVPVDGPPIDIGRVTGPPIFNPVANEVYLNFESSTHCLADRYMNYTSLITFHCKRGVSMGTPKLIRTNDCDFVFEWETPIVCPDEVKTQGCAVTDEQLLYSFNLTSLSTSTFKVTRDARTYSIGVCTAAAGLGQEGCKDGGVCLLSGNKGASFGRLASMQLDYRHQDEAVILSYVNGDPCPPETDDGEPCVFPFIYKGKSYDECVLEGRAKLWCSKTANYDRDHEWGFCRQTNSYRMSAIIFTCDESEDIGRPQVFSEDRGCEVTFEWKTKVVCPPKKMECKFVQKHKTYDLRLLSSLTGSWDFVHEGNSYFINLCQRVYKGPLDCSERASICKKSATGQVQVLGLVHTQKLEVIDETVIVTYSKGYPCGGNKTASSVIELTCAKTVGRPAFKRFDSVSCTYYFYWYSRAACAVRPQEVTMVNGTLTNPVTGKSFSLGEIYFKLFSASGDMRTNGDNYLYEIQLSSITSSSYPACAGANICQVKPNDQHFSRKVGTSDMTKYYVQDGDLDVVFTSSSKCGKDKTKSVSSTIFFHCDPLVKDGIPEFSHETADCQYLFSWYTSAVCPLGVDFEDESAGPEYKGLSERSQAVGAVLSLLLVALTGCLLALLLHKKERRETVINKLTSCCRRSSGVSYKYSKVSKEEETDENETEWLMEEIQVPAPRLGKDGQENGHITTKAVKAEALSSLHGDDQDSEDEVLTVPEVKVHSGRGAEVESSQPLRNPQRKVLKEREGERLGLVRGEKARKGKFRPGQRKPTAPAKLVSFHDDSDEDLLHI
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
107N-linked_GlycosylationARSLLEFNTTMGCQP
HHHHHHHCCCCCCCC		25.84-
212PhosphorylationNVCRDIDSLRDPSTQ
EEECCHHHCCCCCCC		26.1624719451
218PhosphorylationDSLRDPSTQLRVCPA
HHCCCCCCCEEECCC		36.6924719451
227PhosphorylationLRVCPAGTAACLLKG
EEECCCCHHHHHEEC		17.1224719451
395N-linked_GlycosylationKIAGRHQNQTLRYSD
EECEECCCCEEEECC		30.58-
430N-linked_GlycosylationSVINFECNKTAGKDG
EEEEEEECCCCCCCC		37.20-
537N-linked_GlycosylationAVCAVDKNGSKNLGK
EEEEECCCCCCCCCC		56.35-
575N-linked_GlycosylationSDKKISTNITLVCKP
CCCEEECCEEEEECC		20.61-
620N-linked_GlycosylationLSKTEGENCTVLDAQ
HHCCCCCCCEEEECC		37.30-
724S-palmitoylationATLITFLCDRDAGVG
EEEEEHHHCCCCCCC		3.3528526873
724GlutathionylationATLITFLCDRDAGVG
EEEEEHHHCCCCCCC		3.3524333276
740N-linked_GlycosylationPEYQEEDNSTYNFRW
CCCCCCCCCEEEEEE		39.2619349973
864N-linked_GlycosylationSLLLEYVNGSACTTS
CEEEEEECCCEEECC		37.49-
944N-linked_GlycosylationVFNLSPLNDSAQGHV
EEEECCCCCCCCCEE		44.57-
1157N-linked_GlycosylationISPQATGNGSLSILY
ECCCCCCCCCEEEEE		32.31-
1239N-linked_GlycosylationDLKPLGLNDTIVSVG
CCCCCCCCCEEEECC		42.45-
1275GlutathionylationGSKAVSSCQEKKGPQ
CCHHHHHHHHHCCCC		4.7624333276
1279AcetylationVSSCQEKKGPQGFQK
HHHHHHHCCCCHHHH		75.076566751
1305N-linked_GlycosylationENGLLKMNYTGGDTC
CCCCEEEEECCCCCC		29.63-
1358N-linked_GlycosylationQYACPPFNVTECSVQ
CCCCCCCCEEEEEEE		45.64-
1390PhosphorylationNWEAVTRTGATEHYL
CCEEECCCCCCHHHH		23.0822817900
1393PhosphorylationAVTRTGATEHYLINV
EECCCCCCHHHHHHH		25.3322817900
1423N-linked_GlycosylationEAAVCLLNGSKPVNL
HHEEEEECCCCCCCC		39.48-
1454GlutathionylationQYVDGDLCPDKIRRR
EECCCCCCCHHHHCC		4.9524333276
1532N-linked_GlycosylationLSGRAGINASYSEKG
CCCCCCCCCCCCCCC		23.1619656770
1601PhosphorylationLSDLRYKSVISFVCR
HHHHHCCEEEEEEEC		18.75-
1604PhosphorylationLRYKSVISFVCRPEA
HHCCEEEEEEECCCC		14.96-
1649N-linked_GlycosylationATECTVRNGSSIIDL
CCCCEEECCCEEEEC		50.81-
1750N-linked_GlycosylationCLADRYMNYTSLITF
HHHHHHCCCEEEEEE		28.1719349973
1809N-linked_GlycosylationEQLLYSFNLTSLSTS
HHEEEEEECCCCCCC		36.15-
2078N-linked_GlycosylationKGYPCGGNKTASSVI
CCCCCCCCCCHHHHH		24.64-
2103PhosphorylationPAFKRFDSVSCTYYF
CHHHCCCEEECEEEE		17.1427149854
2105PhosphorylationFKRFDSVSCTYYFYW
HHCCCEEECEEEEEE		12.5127149854
2107PhosphorylationRFDSVSCTYYFYWYS
CCCEEECEEEEEEEE		17.4727149854
2108PhosphorylationFDSVSCTYYFYWYSR
CCEEECEEEEEEEEC		8.9027149854
2109PhosphorylationDSVSCTYYFYWYSRA
CEEECEEEEEEEECC		3.3627149854
2111PhosphorylationVSCTYYFYWYSRAAC
EECEEEEEEEECCEE		6.3127149854
2113PhosphorylationCTYYFYWYSRAACAV
CEEEEEEEECCEEEE		4.1227149854
2114PhosphorylationTYYFYWYSRAACAVR
EEEEEEEECCEEEEC		10.9927149854
2129N-linked_GlycosylationPQEVTMVNGTLTNPV
CCEEEEEECEEECCC		27.23-
2328UbiquitinationRRETVINKLTSCCRR
HHHHHHHHHHHHHHH		41.85-
2336PhosphorylationLTSCCRRSSGVSYKY
HHHHHHHCCCCCCEE		16.4624453211
2337PhosphorylationTSCCRRSSGVSYKYS
HHHHHHCCCCCCEEE		41.2126824392
2340PhosphorylationCRRSSGVSYKYSKVS
HHHCCCCCCEEEECC		21.3127717184
2342AcetylationRSSGVSYKYSKVSKE
HCCCCCCEEEECCCC		35.23-
2344PhosphorylationSGVSYKYSKVSKEEE
CCCCCEEEECCCCCC		23.5628418008
2347PhosphorylationSYKYSKVSKEEETDE
CCEEEECCCCCCCCC		37.7821183079
2352PhosphorylationKVSKEEETDENETEW
ECCCCCCCCCCHHHH		52.4726824392
2357PhosphorylationEETDENETEWLMEEI
CCCCCCHHHHHHHHC		44.0019060867
2373UbiquitinationVPAPRLGKDGQENGH
CCCCCCCCCCCCCCC		64.38-
2384UbiquitinationENGHITTKAVKAEAL
CCCCCCHHHHHHHHH		42.40-
2392PhosphorylationAVKAEALSSLHGDDQ
HHHHHHHHHCCCCCC		37.5924925903
2393PhosphorylationVKAEALSSLHGDDQD
HHHHHHHHCCCCCCC		25.8224925903
2401PhosphorylationLHGDDQDSEDEVLTV
CCCCCCCCCCCEEEC		41.1224925903
2407PhosphorylationDSEDEVLTVPEVKVH
CCCCCEEECCEEEEE		38.9124925903
2415PhosphorylationVPEVKVHSGRGAEVE
CCEEEEECCCCCCCC		32.9223335269
2417MethylationEVKVHSGRGAEVESS
EEEEECCCCCCCCCC		44.1324129315
2423PhosphorylationGRGAEVESSQPLRNP
CCCCCCCCCCCCCCC		39.1823335269
2424PhosphorylationRGAEVESSQPLRNPQ
CCCCCCCCCCCCCCC		23.4723335269
2471PhosphorylationTAPAKLVSFHDDSDE
CCCCEEEEECCCCCC		27.5724925903
2476PhosphorylationLVSFHDDSDEDLLHI
EEEECCCCCCCCCCC		49.2924925903
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 MPRI_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPRI_MOUSE !!
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 MPRI_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MPRI_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPRI_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-740; ASN-1532 ANDASN-1750, AND MASS SPECTROMETRY.
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation.";
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.;
Mol. Cell. Proteomics 8:2555-2569(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1532, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, ANDMASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2393; SER-2401; SER-2471AND SER-2476, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2476, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2476, AND MASSSPECTROMETRY.

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