CPLM-015788

Genbank Nucleotide ID

Charged multivesicular body protein 1b

Protein Synonyms/Alias

CHMP1.5; Chromatin-modifying protein 1b; CHMP1b; Vacuolar protein sorting-associated protein 46-2; Vps46-2; hVps46-2

Homo sapiens (Human)

Position	Peptide	Type	References
6	**MSNMEKHLFNLKF	ubiquitination	[1, 2, 3, 4]
12	EKHLFNLKFAAKELS	ubiquitination	[1, 4]
16	FNLKFAAKELSRSAK	acetylation	[5]
16	FNLKFAAKELSRSAK	ubiquitination	[2]
42	KIKKAIQKGNMEVAR	ubiquitination	[2, 3]
59	AENAIRQKNQAVNFL	ubiquitination	[3]
87	QTAVTMGKVTKSMAG	ubiquitination	[2, 6]
90	VTMGKVTKSMAGVVK	ubiquitination	[3]
97	KSMAGVVKSMDATLK	ubiquitination	[2]
104	KSMDATLKTMNLEKI	ubiquitination	[1, 2, 3, 4, 6, 7, 8]
110	LKTMNLEKISALMDK	ubiquitination	[1, 2, 4]

[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] 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]
[3] 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]
[4] 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]
[5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[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]
[7] A data set of human endogenous protein ubiquitination sites.
Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
[8] 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]

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 and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.

REGION 132 156 Interaction with IST1.
REGION 174 199 Interaction with SPAST.
REGION 180 199 Interaction with VTA1.
REGION 180 196 Interaction with VPS4A, MITD1 and STAMBP.
REGION 183 199 Interaction with VPS4B.
MOTIF 186 196 MIT-interacting motif.

3D-structure; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Endosome; Membrane; Protein transport; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO:0000910; P:cytokinesis; IMP:UniProtKB.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.