CHMP3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHMP3_MOUSE
• UniProt AC: Q9CQ10
• Protein Name: Charged multivesicular body protein 3
• Gene Name: Chmp3
• Organism: Mus musculus (Mouse).
• Sequence Length: 224
• Subcellular Localization: Cytoplasm, cytosol. Membrane; Lipid-anchor. Endosome. Late endosome membrane. Localizes to the midbody of dividing cells..
• 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. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor (By similarity)..
• Protein Sequence: MGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKEVCVVLAKEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEAAEMEIDRILFEITAGALGKAPSKVTDALPEPEPAGAMAASEEGEEEEDEEDLEAMQSRLATLRS

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
2	Myristoylation	------MGLFGKTQE ------CCCCCCCCC	29.70	-
20	Phosphorylation	KELVNEWSLKIRKEM HHHHHHHHHHHHHHH	17.38	29514104
60	Glutathionylation	KKGQKEVCVVLAKEM HCCCHHHHHHHHHHH	1.51	24333276
112	Ubiquitination	QKSTEVMKAMQSLVK HHHHHHHHHHHHHHC	45.97	22790023
185	Phosphorylation	GKAPSKVTDALPEPE CCCCCCCCCCCCCCC	21.20	25619855
200	Phosphorylation	PAGAMAASEEGEEEE CCCCCCCCCCCCCCC	27.00	27087446
217	Phosphorylation	EDLEAMQSRLATLRS HHHHHHHHHHHHHCC	19.04	25619855
221	Phosphorylation	AMQSRLATLRS---- HHHHHHHHHCC----	27.56	26643407
224	Phosphorylation	SRLATLRS------- HHHHHHCC-------	47.92	26643407

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

Oops, there are no upstream regulatory protein records of CHMP3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHMP3_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 CHMP3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CHM4B_HUMAN	CHMP4B	physical	20360068
ZEP1_HUMAN	HIVEP1	physical	26496610
NSF_HUMAN	NSF	physical	26496610
FUBP1_HUMAN	FUBP1	physical	26496610
BRE1B_HUMAN	RNF40	physical	26496610
DHRS2_HUMAN	DHRS2	physical	26496610
SNUT2_HUMAN	USP39	physical	26496610
B4GT7_HUMAN	B4GALT7	physical	26496610
DNJC8_HUMAN	DNAJC8	physical	26496610
MDN1_HUMAN	MDN1	physical	26496610
PRDX5_HUMAN	PRDX5	physical	26496610
FABD_HUMAN	MCAT	physical	26496610
PF21A_HUMAN	PHF21A	physical	26496610
DTL_HUMAN	DTL	physical	26496610
KDM3A_HUMAN	KDM3A	physical	26496610
IPO4_HUMAN	IPO4	physical	26496610
ZMYM1_HUMAN	ZMYM1	physical	26496610
MED25_HUMAN	MED25	physical	26496610

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.
PubMed: 15345747