CHMP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHMP3_HUMAN
• UniProt AC: Q9Y3E7
• Protein Name: Charged multivesicular body protein 3
• Gene Name: CHMP3
• Organism: Homo sapiens (Human).
• Sequence Length: 222
• 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 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. 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. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells..
• Protein Sequence: MGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKDVCIVLAKEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEEAEMEIDRILFEITAGALGKAPSKVTDALPEPEPPGAMAASEDEEEEEEALEAMQSRLATLRS

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	-
6	Phosphorylation	--MGLFGKTQEKPPK --CCCCCCCCCCCCH	39.44	27642862
6	Ubiquitination	--MGLFGKTQEKPPK --CCCCCCCCCCCCH	39.44	29967540
20	Phosphorylation	KELVNEWSLKIRKEM HHHHHHHHHHHHHHH	17.38	27499020
40	Ubiquitination	QIRDIQREEEKVKRS HHHHHHHHHHHHHHH	54.88	33845483
66	Ubiquitination	VCIVLAKEMIRSRKA HHHHHHHHHHHHHHH	33.95	29967540
75	Phosphorylation	IRSRKAVSKLYASKA HHHHHHHHHHHHCHH	23.08	29083192
76	Acetylation	RSRKAVSKLYASKAH HHHHHHHHHHHCHHH	38.63	25953088
78	Phosphorylation	RKAVSKLYASKAHMN HHHHHHHHHCHHHHH	16.74	29083192
80	Phosphorylation	AVSKLYASKAHMNSV HHHHHHHCHHHHHHH	19.47	29083192
92	Ubiquitination	NSVLMGMKNQLAVLR HHHHHHHHHHHHHHH	35.49	29967540
106	Ubiquitination	RVAGSLQKSTEVMKA HHHHHHHHHHHHHHH	65.72	33845483
113	Ubiquitination	KSTEVMKAMQSLVKI HHHHHHHHHHHHHCH	5.33	18781797
116	Phosphorylation	EVMKAMQSLVKIPEI HHHHHHHHHHCHHHH	23.26	-
126	Phosphorylation	KIPEIQATMRELSKE CHHHHHHHHHHHHHH	10.61	19060867
127	Sulfoxidation	IPEIQATMRELSKEM HHHHHHHHHHHHHHH	3.34	21406390
132	Ubiquitination	ATMRELSKEMMKAGI HHHHHHHHHHHHHCH	63.35	29967540
134	Phosphorylation	MRELSKEMMKAGIIE HHHHHHHHHHHCHHH	3.72	32142685
135	Ubiquitination	RELSKEMMKAGIIEE HHHHHHHHHHCHHHH	2.56	33845483
139	Ubiquitination	KEMMKAGIIEEMLED HHHHHHCHHHHHHHH	4.24	18781797
160	Phosphorylation	DQEEMEEEAEMEIDR CHHHHHHHHHHHHHH	36.30	32142685
161	Ubiquitination	QEEMEEEAEMEIDRI HHHHHHHHHHHHHHH	25.39	29967540
179	Ubiquitination	ITAGALGKAPSKVTD HHHHHCCCCCCCCCC	58.96	18781797
182	Phosphorylation	GALGKAPSKVTDALP HHCCCCCCCCCCCCC	44.62	26270265
183	Ubiquitination	ALGKAPSKVTDALPE HCCCCCCCCCCCCCC	48.36	-
185	Phosphorylation	GKAPSKVTDALPEPE CCCCCCCCCCCCCCC	21.20	23927012
200	Phosphorylation	PPGAMAASEDEEEEE CCCCCCCCCCHHHHH	35.72	29255136
208	Ubiquitination	EDEEEEEEALEAMQS CCHHHHHHHHHHHHH	62.93	18781797
215	Phosphorylation	EALEAMQSRLATLRS HHHHHHHHHHHHHCC	19.04	23927012
219	Phosphorylation	AMQSRLATLRS---- HHHHHHHHHCC----	27.56	-
222	Phosphorylation	SRLATLRS------- HHHHHHCC-------	47.92	24719451
229	Phosphorylation	S-------------- C--------------		32142685
251	Phosphorylation	------------------------------------ ------------------------------------		24719451

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

Oops, there are no upstream regulatory protein records of CHMP3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHMP3_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IBP7_HUMAN	IGFBP7	physical	11549700
STABP_HUMAN	STAMBP	physical	17159328
STABP_HUMAN	STAMBP	physical	17261583
CHMP3_HUMAN	CHMP3	physical	17146056
STABP_HUMAN	STAMBP	physical	17146056
CHM4B_HUMAN	CHMP4B	physical	16730941
CHMP3_HUMAN	CHMP3	physical	16730941
STABP_HUMAN	STAMBP	physical	16730941
TNPO3_HUMAN	TNPO3	physical	16730941
RB11A_HUMAN	RAB11A	physical	16730941
A4_HUMAN	APP	physical	21832049
STABP_HUMAN	STAMBP	physical	18395747
CHM1B_HUMAN	CHMP1B	physical	26344197
CHM4B_HUMAN	CHMP4B	physical	26344197

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.
PubMed: 19690332

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.
PubMed: 17081983

Ubiquitylation

"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-179, AND MASSSPECTROMETRY.
PubMed: 18781797