VPS35_MOUSE - dbPTM
VPS35_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPS35_MOUSE
UniProt AC Q9EQH3
Protein Name Vacuolar protein sorting-associated protein 35
Gene Name Vps35
Organism Mus musculus (Mouse).
Sequence Length 796
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Endosome . Early endosome . Late endosome .
Protein Description Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for endosomal localization of WASHC2 and mediates the association of the CSC with the WASH complex (By similarity)..
Protein Sequence MPTTQQSPQDEQEKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDGPGIPAEIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPDPEDFADEQSLVGRFIHLLRSDDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYKENSQMDDKWEKKCQKIFSFAHQTISALIKAELAELPLRLFLQGALAAGEIGFENHETVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEPLRTQCALAASKLLKKPDQGRAVSTCAHLFWSGRNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQLFIEILNRYIYFYEKENDAVTIQVLNQLIQKIREDLPNLESSEETEQINKHFHNTLEHLRSRRESPESEGPIYEGLIL
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
3Phosphorylation-----MPTTQQSPQD
-----CCCCCCCCHH		35.6226160508
4Phosphorylation----MPTTQQSPQDE
----CCCCCCCCHHH		20.8126160508
7Phosphorylation-MPTTQQSPQDEQEK
-CCCCCCCCHHHHHH		18.0827087446
14UbiquitinationSPQDEQEKLLDEAIQ
CCHHHHHHHHHHHHH		54.78-
24UbiquitinationDEAIQAVKVQSFQMK
HHHHHHHHHCHHHHH		37.26-
44UbiquitinationNKLMDALKHASNMLG
HHHHHHHHHHHHHHH		38.55-
56PhosphorylationMLGELRTSMLSPKSY
HHHHHHHHCCCCHHH		15.9918779572
59PhosphorylationELRTSMLSPKSYYEL
HHHHHCCCCHHHHHH		22.9518779572
87UbiquitinationYLTDEFAKGRKVADL
EECHHHHCCCCHHHH		65.65-
131AcetylationQSRKDILKDLVEMCR
HHHHHHHHHHHHHHH		49.7222826441
239AcetylationGVNVERYKQIVLTGI
CCCHHHHHHHHHHHH		39.5122826441
396UbiquitinationATSSAVSKELTRLLK
HCCHHHHHHHHHHHC		50.58-
399PhosphorylationSAVSKELTRLLKIPV
HHHHHHHHHHHCCCH		21.9922817900
403UbiquitinationKELTRLLKIPVDTYN
HHHHHHHCCCHHHHH		49.94-
403AcetylationKELTRLLKIPVDTYN
HHHHHHHCCCHHHHH		49.9422826441
417UbiquitinationNNILTVLKLKHFHPL
HCHHHHHHHCCCCHH		51.67-
417AcetylationNNILTVLKLKHFHPL
HCHHHHHHHCCCCHH		51.6723954790
419AcetylationILTVLKLKHFHPLFE
HHHHHHHCCCCHHHH		42.5122826441
500PhosphorylationRFIHLLRSDDPDQQY
HHHHHHCCCCCCCCE		46.4620415495
507PhosphorylationSDDPDQQYLILNTAR
CCCCCCCEEEEEECH		7.0622817900
528PhosphorylationGNQRIRFTLPPLVFA
CCCCEEEECCHHHHH		28.62-
552AcetylationENSQMDDKWEKKCQK
HHCCCCHHHHHHHHH		53.6523954790
601PhosphorylationIGFENHETVAYEFMS
CCCCCCHHHHHHHHH		11.6825367039
604PhosphorylationENHETVAYEFMSQAF
CCCHHHHHHHHHHHH		12.8325367039
608PhosphorylationTVAYEFMSQAFSLYE
HHHHHHHHHHHHHHH		24.5525367039
612PhosphorylationEFMSQAFSLYEDEIS
HHHHHHHHHHHHHCC		32.8125367039
614PhosphorylationMSQAFSLYEDEISDS
HHHHHHHHHHHCCCC		21.8225367039
619PhosphorylationSLYEDEISDSKAQLA
HHHHHHCCCCHHHHH		33.5125367039
621PhosphorylationYEDEISDSKAQLAAI
HHHHCCCCHHHHHHH		24.0925367039
659AcetylationQCALAASKLLKKPDQ
HHHHHHHHHCCCCCC		53.7822826441
659UbiquitinationQCALAASKLLKKPDQ
HHHHHHHHHCCCCCC		53.78-
673GlutathionylationQGRAVSTCAHLFWSG
CCCCCHHHHHHHHCC		1.4224333276
694AcetylationGEELHGGKRVMECLK
CCCCCCCHHHHHHHH		46.547619353
749AcetylationVLNQLIQKIREDLPN
HHHHHHHHHHHHCCC		36.4223954790
759PhosphorylationEDLPNLESSEETEQI
HHCCCCCCHHHHHHH		46.3326525534
760PhosphorylationDLPNLESSEETEQIN
HCCCCCCHHHHHHHH		30.0330635358
763PhosphorylationNLESSEETEQINKHF
CCCCHHHHHHHHHHH		29.1930635358
779PhosphorylationNTLEHLRSRRESPES
HHHHHHHHCCCCCCC		41.8924925903
783PhosphorylationHLRSRRESPESEGPI
HHHHCCCCCCCCCCC		31.9625521595
786PhosphorylationSRRESPESEGPIYEG
HCCCCCCCCCCCCCC		51.7625521595
791PhosphorylationPESEGPIYEGLIL--
CCCCCCCCCCCCC--		13.6924925903
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 VPS35_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPS35_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 VPS35_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS29_MOUSEVps29physical
18656452
VP26A_MOUSEVps26aphysical
18656452
VP26B_MOUSEVps26bphysical
18656452
SNX1_MOUSESnx1physical
18656452
FKB15_HUMANFKBP15physical
24819384
WASC5_HUMANKIAA0196physical
24819384
WASH1_HUMANWASH1physical
24819384
VP26A_HUMANVPS26Aphysical
24819384
VPS29_HUMANVPS29physical
24819384
ATG9A_HUMANATG9Aphysical
24819384
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VPS35_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.
"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 TYR-791, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-791, AND MASSSPECTROMETRY.

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