CPLM-000741

Genbank Nucleotide ID

Charged multivesicular body protein 2a

Protein Synonyms/Alias

Chromatin-modifying protein 2a; CHMP2a; Putative breast adenocarcinoma marker BC-2; Vacuolar protein sorting-associated protein 2-1; Vps2-1; hVps2-1

Homo sapiens (Human)

Position	Peptide	Type	References
48	KKIIADIKKMAKQGQ	ubiquitination	[1, 2]
52	ADIKKMAKQGQMDAV	ubiquitination	[1, 2, 3, 4, 5, 6]
64	DAVRIMAKDLVRTRR	ubiquitination	[1, 2, 6]
89	NIQAVSLKIQTLKSN	ubiquitination	[1, 2, 5]
94	SLKIQTLKSNNSMAQ	ubiquitination	[1, 2, 6]
104	NSMAQAMKGVTKAMG	ubiquitination	[1, 2, 6]
108	QAMKGVTKAMGTMNR	ubiquitination	[1, 2, 6]
118	GTMNRQLKLPQIQKI	ubiquitination	[1, 2]
124	LKLPQIQKIMMEFER	ubiquitination	[1, 2]
197	SVAAGGKKAEAAASA	ubiquitination	[3]

[1] 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]
[2] 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]
[3] 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]
[4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[5] 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]
[6] 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]

Functional Description

Probable core 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 56 222 Interaction with VPS4B.
REGION 217 222 Interaction with VTA1.
MOTIF 210 220 MIT-interacting motif.
MOD_RES 1 1 N-acetylmethionine.

Acetylation; Coiled coil; Complete proteome; Direct protein sequencing; Endosome; Membrane; Protein transport; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO:0016044; P:cellular membrane organization; TAS:Reactome.
GO:0016197; P:endosomal transport; TAS:Reactome.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.