CPLM-022471

Genbank Nucleotide ID

Charged multivesicular body protein 5

Protein Synonyms/Alias

Chromatin-modifying protein 5; SNF7 domain-containing protein 2; Vacuolar protein sorting-associated protein 60; Vps60; hVps60

C9orf83; SNF7DC2; CGI-34; HSPC177; PNAS-114; PNAS-2

Homo sapiens (Human)

Position	Peptide	Type	References
7	*MNRLFGKAKPKAPP	ubiquitination	[1]
44	RLDAELVKYKDQIKK	acetylation	[2]
44	RLDAELVKYKDQIKK	ubiquitination	[3, 4, 5]
100	NYTIQSLKDTKTTVD	ubiquitination	[3, 5, 6]
110	KTTVDAMKLGVKEMK	ubiquitination	[1]

[1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]

Functional Description

Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT- III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release.

REGION 121 158 Interaction with VTA1.
MOD_RES 86 86 Phosphoserine.

3D-structure; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Endosome; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IEA:Compara.
GO:0016044; P:cellular membrane organization; TAS:Reactome.
GO:0016197; P:endosomal transport; TAS:Reactome.
GO:0008333; P:endosome to lysosome transport; IEA:Compara.
GO:0007040; P:lysosome organization; IEA:Compara.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0001919; P:regulation of receptor recycling; IEA:Compara.