VPS18_HUMAN - dbPTM
VPS18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPS18_HUMAN
UniProt AC Q9P253
Protein Name Vacuolar protein sorting-associated protein 18 homolog
Gene Name VPS18
Organism Homo sapiens (Human).
Sequence Length 973
Subcellular Localization Late endosome membrane
Peripheral membrane protein
Cytoplasmic side . Lysosome membrane
Peripheral membrane protein
Cytoplasmic side . Early endosome . Cytoplasmic vesicle, autophagosome . Cytoplasmic vesicle, clathrin-coated vesicle . Cytopl
Protein Description Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. [PubMed: 11382755]
Protein Sequence MASILDEYENSLSRSAVLQPGCPSVGIPHSGYVNAQLEKEVPIFTKQRIDFTPSERITSLVVSSNQLCMSLGKDTLLRIDLGKANEPNHVELGRKDDAKVHKMFLDHTGSHLLIALSSTEVLYVNRNGQKVRPLARWKGQLVESVGWNKALGTESSTGPILVGTAQGHIFEAELSASEGGLFGPAPDLYFRPLYVLNEEGGPAPVCSLEAERGPDGRSFVIATTRQRLFQFIGRAAEGAEAQGFSGLFAAYTDHPPPFREFPSNLGYSELAFYTPKLRSAPRAFAWMMGDGVLYGALDCGRPDSLLSEERVWEYPEGVGPGASPPLAIVLTQFHFLLLLADRVEAVCTLTGQVVLRDHFLEKFGPLKHMVKDSSTGQLWAYTERAVFRYHVQREARDVWRTYLDMNRFDLAKEYCRERPDCLDTVLAREADFCFRQRRYLESARCYALTQSYFEEIALKFLEARQEEALAEFLQRKLASLKPAERTQATLLTTWLTELYLSRLGALQGDPEALTLYRETKECFRTFLSSPRHKEWLFASRASIHELLASHGDTEHMVYFAVIMQDYERVVAYHCQHEAYEEALAVLARHRDPQLFYKFSPILIRHIPRQLVDAWIEMGSRLDARQLIPALVNYSQGGEVQQVSQAIRYMEFCVNVLGETEQAIHNYLLSLYARGRPDSLLAYLEQAGASPHRVHYDLKYALRLCAEHGHHRACVHVYKVLELYEEAVDLALQVDVDLAKQCADLPEEDEELRKKLWLKIARHVVQEEEDVQTAMACLASCPLLKIEDVLPFFPDFVTIDHFKEAICSSLKAYNHHIQELQREMEEATASAQRIRRDLQELRGRYGTVEPQDKCATCDFPLLNRPFYLFLCGHMFHADCLLQAVRPGLPAYKQARLEELQRKLGAAPPPAKGSARAKEAEGGAATAGPSREQLKADLDELVAAECVYCGELMIRSIDRPFIDPQRYEEEQLSWL
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
2Acetylation------MASILDEYE
------CCCHHHHHH		12.7922223895
3Phosphorylation-----MASILDEYEN
-----CCCHHHHHHH		23.5328857561
8PhosphorylationMASILDEYENSLSRS
CCCHHHHHHHHCCHH		21.7825106551
11PhosphorylationILDEYENSLSRSAVL
HHHHHHHHCCHHHHC		18.7825849741
13PhosphorylationDEYENSLSRSAVLQP
HHHHHHCCHHHHCCC		24.8225849741
14MethylationEYENSLSRSAVLQPG
HHHHHCCHHHHCCCC		33.65115389081
15PhosphorylationYENSLSRSAVLQPGC
HHHHCCHHHHCCCCC		21.2521945579
24PhosphorylationVLQPGCPSVGIPHSG
HCCCCCCCCCCCCCC		36.7321945579
30PhosphorylationPSVGIPHSGYVNAQL
CCCCCCCCCCCCCEE		26.8521945579
32PhosphorylationVGIPHSGYVNAQLEK
CCCCCCCCCCCEEEE		8.1121945579
39UbiquitinationYVNAQLEKEVPIFTK
CCCCEEEEECCCEEC		73.02-
46UbiquitinationKEVPIFTKQRIDFTP
EECCCEECCCCCCCC		27.16-
83UbiquitinationLLRIDLGKANEPNHV
EEEEECCCCCCCCCC		56.17-
224PhosphorylationRSFVIATTRQRLFQF
CCEEEEEHHHHHHHH		18.7824719451
276UbiquitinationELAFYTPKLRSAPRA
HHHHCCHHHCCCCCH		49.05-
362AcetylationLRDHFLEKFGPLKHM
HCHHHHHHHCCCCCE		58.7419608861
367UbiquitinationLEKFGPLKHMVKDSS
HHHHCCCCCEEECCC		32.56-
412UbiquitinationMNRFDLAKEYCRERP
CCCHHHHHHHHHHCC		57.42-
476UbiquitinationLAEFLQRKLASLKPA
HHHHHHHHHHCCCHH		35.13-
479PhosphorylationFLQRKLASLKPAERT
HHHHHHHCCCHHHHH		47.57-
481UbiquitinationQRKLASLKPAERTQA
HHHHHCCCHHHHHHH		39.42-
528PhosphorylationECFRTFLSSPRHKEW
HHHHHHHCCHHHHHH		33.8223186163
529PhosphorylationCFRTFLSSPRHKEWL
HHHHHHCCHHHHHHH		28.2723186163
597UbiquitinationRDPQLFYKFSPILIR
CCHHHHHHCCHHHHH		31.84-
689PhosphorylationYLEQAGASPHRVHYD
HHHHCCCCCCCCCCC		21.9621712546
717PhosphorylationHRACVHVYKVLELYE
HHHHHHHHHHHHHHH		4.78-
758UbiquitinationLRKKLWLKIARHVVQ
HHHHHHHHHHHHHHC		23.80-
810UbiquitinationEAICSSLKAYNHHIQ
HHHHHHHHHHHHHHH		51.26-
810MalonylationEAICSSLKAYNHHIQ
HHHHHHHHHHHHHHH		51.2626320211
810AcetylationEAICSSLKAYNHHIQ
HHHHHHHHHHHHHHH		51.2625953088
827PhosphorylationQREMEEATASAQRIR
HHHHHHHHHHHHHHH		25.1525867546
829PhosphorylationEMEEATASAQRIRRD
HHHHHHHHHHHHHHH		22.1525159151
844PhosphorylationLQELRGRYGTVEPQD
HHHHHCCCCCCCCCC		21.7028152594
846PhosphorylationELRGRYGTVEPQDKC
HHHCCCCCCCCCCCC		16.8628152594
901UbiquitinationRLEELQRKLGAAPPP
HHHHHHHHHCCCCCC		38.01-
910UbiquitinationGAAPPPAKGSARAKE
CCCCCCCCCCCCHHH		60.20-
912PhosphorylationAPPPAKGSARAKEAE
CCCCCCCCCCHHHHC		17.5518785766
916UbiquitinationAKGSARAKEAEGGAA
CCCCCCHHHHCCCCC		52.48-
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 VPS18_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPS18_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 VPS18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS11_HUMANVPS11physical
11382755
VPS16_HUMANVPS16physical
11382755
STX7_HUMANSTX7physical
11382755
GGA3_HUMANGGA3physical
16996030
PLK2_RATPlk2physical
16203730
UVRAG_HUMANUVRAGphysical
18552835
UB2D2_HUMANUBE2D2physical
16996030
VPS41_HUMANVPS41physical
22939629
GAG_HV1H2gagphysical
21450827
VP33A_HUMANVPS33Aphysical
25783203
VPS16_HUMANVPS16physical
25783203
VPS11_HUMANVPS11physical
25783203
VPS41_HUMANVPS41physical
25783203
ALDOA_HUMANALDOAphysical
26496610
BIN1_HUMANBIN1physical
26496610
NDUV3_HUMANNDUFV3physical
26496610
TRY1_HUMANPRSS1physical
26496610
UPP1_HUMANUPP1physical
26496610
TERA_HUMANVCPphysical
26496610
MTA1_HUMANMTA1physical
26496610
TGFA1_HUMANTGFBRAP1physical
26496610
SRRM1_HUMANSRRM1physical
26496610
VPS8_HUMANVPS8physical
26496610
DNJB5_HUMANDNAJB5physical
26496610
VPS41_HUMANVPS41physical
26496610
RSRC1_HUMANRSRC1physical
26496610
SCLY_HUMANSCLYphysical
26496610
ZGRF1_HUMANZGRF1physical
26496610
VPS11_HUMANVPS11physical
26496610
SERC1_HUMANSERINC1physical
26496610
VPS16_HUMANVPS16physical
26496610
VP33A_HUMANVPS33Aphysical
26496610
ELMO3_HUMANELMO3physical
26496610
SEN2_HUMANTSEN2physical
26496610
OBSCN_HUMANOBSCNphysical
26496610
TJAP1_HUMANTJAP1physical
26496610
TGO1_HUMANMIA3physical
26496610
VPS16_HUMANVPS16physical
26463206
VP33A_HUMANVPS33Aphysical
26463206
VPS41_HUMANVPS41physical
26463206
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VPS18_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-362, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-529, ANDMASS SPECTROMETRY.

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