CHM2A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHM2A_MOUSE
• UniProt AC: Q9DB34
• Protein Name: Charged multivesicular body protein 2a
• Gene Name: Chmp2a
• Organism: Mus musculus (Mouse).
• Sequence Length: 222
• Subcellular Localization: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm . Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body.
• Protein 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. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4..
• Protein Sequence: MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEATASALADADADLEERLKNLRRD

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
1	Acetylation	-------MDLLFGRR -------CCCCCCCC	8.06	-
52	Ubiquitination	ADIKKMAKQGQMDAV HHHHHHHHCCCCHHH	52.00	27667366
52	Malonylation	ADIKKMAKQGQMDAV HHHHHHHHCCCCHHH	52.00	26320211
89	Ubiquitination	NIQAVSLKIQTLKSN HHHHHHHHHHHHHCC	25.84	22790023
94	Ubiquitination	SLKIQTLKSNNSMAQ HHHHHHHHCCCHHHH	55.30	22790023
104	Ubiquitination	NSMAQAMKGVTKAMG CHHHHHHHHHHHHHH	53.93	22790023
107	Phosphorylation	AQAMKGVTKAMGTMN HHHHHHHHHHHHHHH	23.04	22418434
108	Ubiquitination	QAMKGVTKAMGTMNR HHHHHHHHHHHHHHH	33.69	22790023
118	Ubiquitination	GTMNRQLKLPQIQKI HHHHHHCCCHHHHHH	50.19	27667366
124	Ubiquitination	LKLPQIQKIMMEFER CCCHHHHHHHHHHHH	33.91	22790023
184	Phosphorylation	DELSNLPSTGGSLSV HHHHCCCCCCCCEEE	42.73	-
185	Phosphorylation	ELSNLPSTGGSLSVA HHHCCCCCCCCEEEC	43.55	-
188	Phosphorylation	NLPSTGGSLSVAAGG CCCCCCCCEEECCCC	20.86	-
190	Phosphorylation	PSTGGSLSVAAGGKK CCCCCCEEECCCCCC	16.06	-
201	Phosphorylation	GGKKAEATASALADA CCCCHHHHHHHHHHC	16.79	28833060
203	Phosphorylation	KKAEATASALADADA CCHHHHHHHHHHCCC	21.33	28833060

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CHM2A_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHM2A_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CHM2A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VPS4B_MOUSE	Vps4b	physical	15173323
CLUS_HUMAN	CLU	physical	26496610
MEN1_HUMAN	MEN1	physical	26496610
CHM1A_HUMAN	CHMP1A	physical	26496610
NEST_HUMAN	NES	physical	26496610
IMA7_HUMAN	KPNA6	physical	26496610
CHMP3_HUMAN	CHMP3	physical	26496610
RBM26_HUMAN	RBM26	physical	26496610
CHM4B_HUMAN	CHMP4B	physical	26496610

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.