CHM1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHM1A_MOUSE
• UniProt AC: Q921W0
• Protein Name: Charged multivesicular body protein 1a
• Gene Name: Chmp1a
• Organism: Mus musculus (Mouse).
• Sequence Length: 196
• Subcellular Localization: Cytoplasm . Endosome membrane ; Peripheral membrane protein . Nucleus matrix . The cytoplasmic form is partially membrane-associated and localizes to early endosomes. The nuclear form remains associated with the chromosome scaffold during mitosis. On
• Protein 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. 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 (By similarity)..
• Protein Sequence: MDDTLFQLKFTAKQLEKLAKKAEKDSKAEQAKVKKALQQKNVECARVYAENAIRKKNEGVNWLRMASRVDAVASKVQTAVTMKGVTKNMAQVTKALDKALSAMDLQKVSAVMDRFEQQVQNLDVHTSVMEDSVSSATTLTTPQEQVDSLIVQIAEENGLEVLDQLSQLPEGASAVGESSVRSQEDQLSRRLAALRN

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	-------MDDTLFQL -------CCCHHHHH	10.70	-
13	Malonylation	FQLKFTAKQLEKLAK HHHHHHHHHHHHHHH	52.97	26320211
17	Acetylation	FTAKQLEKLAKKAEK HHHHHHHHHHHHHHH	63.44	23864654
20	Acetylation	KQLEKLAKKAEKDSK HHHHHHHHHHHHCCH	64.05	23864654
44	Glutathionylation	LQQKNVECARVYAEN HHHCCHHHHHHHHHH	2.26	24333276
48	Phosphorylation	NVECARVYAENAIRK CHHHHHHHHHHHHHH	11.57	29514104
55	Ubiquitination	YAENAIRKKNEGVNW HHHHHHHHHCCCCCH	54.56	22790023
56	Ubiquitination	AENAIRKKNEGVNWL HHHHHHHHCCCCCHH	50.84	22790023
67	Phosphorylation	VNWLRMASRVDAVAS CCHHHHHHHHHHHHH	24.40	29514104
74	Phosphorylation	SRVDAVASKVQTAVT HHHHHHHHHHHHHHH	27.10	23737553
83	Ubiquitination	VQTAVTMKGVTKNMA HHHHHHHCCCCCCHH	40.64	22790023
87	Malonylation	VTMKGVTKNMAQVTK HHHCCCCCCHHHHHH	42.17	26320211
98	Acetylation	QVTKALDKALSAMDL HHHHHHHHHHHHHCH	52.67	6568321
101	Phosphorylation	KALDKALSAMDLQKV HHHHHHHHHHCHHHH	26.80	27180971
107	Acetylation	LSAMDLQKVSAVMDR HHHHCHHHHHHHHHH	45.51	6567033
173	Phosphorylation	SQLPEGASAVGESSV HCCCCCCCCCCHHHC	34.05	-
182	Phosphorylation	VGESSVRSQEDQLSR CCHHHCCCHHHHHHH	35.45	28066266

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

Oops, there are no upstream regulatory protein records of CHM1A_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHM1A_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 CHM1A_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CHM1A_MOUSE !!

Drug and Disease Associations

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