CPLM-021696

Genbank Nucleotide ID

Charged multivesicular body protein 1a

Protein Synonyms/Alias

Chromatin-modifying protein 1a; CHMP1a; Vacuolar protein sorting-associated protein 46-1; Vps46-1; hVps46-1

CHMP1; KIAA0047; PCOLN3; PRSM1

Homo sapiens (Human)

Position	Peptide	Type	References
27	KKAEKDSKAEQAKVK	acetylation	[1]
40	VKKALLQKNVECARV	ubiquitination	[2]
55	YAENAIRKKNEGVNW	ubiquitination	[2, 3]
56	AENAIRKKNEGVNWL	ubiquitination	[2, 3, 4, 5, 6]
75	RVDAVASKVQTAVTM	ubiquitination	[2, 5]
83	VQTAVTMKGVTKNMA	ubiquitination	[3, 6]
87	VTMKGVTKNMAQVTK	ubiquitination	[2]
94	KNMAQVTKALDKALS	ubiquitination	[6]
98	QVTKALDKALSTMDL	ubiquitination	[4, 6]

[1] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[2] 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]
[3] 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]
[4] 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]
[5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[6] 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]

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 cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condensed chromatin. May play a role in stable cell cycle progression and in PcG gene silencing.

MOTIF 185 195 MIT-interacting motif.
MOD_RES 1 1 N-acetylmethionine.

3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Endosome; Membrane; Nucleus; Protein transport; Reference proteome; Repressor; Transcription; Transcription regulation; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
GO:0005769; C:early endosome; IDA:UniProtKB.
GO:0012505; C:endomembrane system; IDA:UniProtKB.
GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO:0000910; P:cytokinesis; IMP:UniProtKB.
GO:0016458; P:gene silencing; IDA:UniProtKB.
GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
GO:0045014; P:negative regulation of transcription by glucose; IDA:UniProtKB.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.