CHM2A_HUMAN - dbPTM
CHM2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHM2A_HUMAN
UniProt AC O43633
Protein Name Charged multivesicular body protein 2a
Gene Name CHMP2A
Organism Homo sapiens (Human).
Sequence Length 222
Subcellular Localization Late endosome membrane
Peripheral membrane protein
Cytoplasmic side . 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. [PubMed: 21310966 Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase]
Protein Sequence MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEAAASALADADADLEERLKNLRRD
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 Orthologous
Protein Cluster
1Acetylation-------MDLLFGRR
-------CCCCCCCC		8.0612665801
9UbiquitinationDLLFGRRKTPEELLR
CCCCCCCCCHHHHHH		68.05-
10PhosphorylationLLFGRRKTPEELLRQ
CCCCCCCCHHHHHHH		33.8421815630
38PhosphorylationRERQKLETQEKKIIA
HHHHHHHHHHHHHHH		53.0920068231
48UbiquitinationKKIIADIKKMAKQGQ
HHHHHHHHHHHHCCC		36.7221890473
52AcetylationADIKKMAKQGQMDAV
HHHHHHHHCCCCHHH		52.0012435057
52UbiquitinationADIKKMAKQGQMDAV
HHHHHHHHCCCCHHH		52.0021906983
64UbiquitinationDAVRIMAKDLVRTRR
HHHHHHHHHHHHHHH		33.9321906983
87PhosphorylationRANIQAVSLKIQTLK
HCHHHHHHHHHHHHH		27.2828857561
89AcetylationNIQAVSLKIQTLKSN
HHHHHHHHHHHHHCC		25.8425953088
89UbiquitinationNIQAVSLKIQTLKSN
HHHHHHHHHHHHHCC		25.8421906983
92PhosphorylationAVSLKIQTLKSNNSM
HHHHHHHHHHCCCHH		39.36-
94UbiquitinationSLKIQTLKSNNSMAQ
HHHHHHHHCCCHHHH		55.3021906983
94AcetylationSLKIQTLKSNNSMAQ
HHHHHHHHCCCHHHH		55.3027452117
95PhosphorylationLKIQTLKSNNSMAQA
HHHHHHHCCCHHHHH		44.3425159151
98PhosphorylationQTLKSNNSMAQAMKG
HHHHCCCHHHHHHHH		21.5328857561
104UbiquitinationNSMAQAMKGVTKAMG
CHHHHHHHHHHHHHH		53.9321906983
108UbiquitinationQAMKGVTKAMGTMNR
HHHHHHHHHHHHHHH		33.6921906983
118UbiquitinationGTMNRQLKLPQIQKI
HHHHHHCCCHHHHHH		50.1921906983
118AcetylationGTMNRQLKLPQIQKI
HHHHHHCCCHHHHHH		50.1925038526
124UbiquitinationLKLPQIQKIMMEFER
CCCHHHHHHHHHHHH		33.9121906983
124AcetylationLKLPQIQKIMMEFER
CCCHHHHHHHHHHHH		33.9125038526
126SulfoxidationLPQIQKIMMEFERQA
CHHHHHHHHHHHHHH		2.4421406390
174PhosphorylationVLDELGLSLTDELSN
HHHHHCCCCCHHHHC		27.6824275569
180PhosphorylationLSLTDELSNLPSTGG
CCCCHHHHCCCCCCC		33.9824275569
184PhosphorylationDELSNLPSTGGSLSV
HHHHCCCCCCCCCEE		42.7329759185
185PhosphorylationELSNLPSTGGSLSVA
HHHCCCCCCCCCEEC		43.5529759185
188PhosphorylationNLPSTGGSLSVAAGG
CCCCCCCCCEECCCC		20.8629759185
190PhosphorylationPSTGGSLSVAAGGKK
CCCCCCCEECCCCHH		16.0629759185
197UbiquitinationSVAAGGKKAEAAASA
EECCCCHHHHHHHHH		55.5221906983
203PhosphorylationKKAEAAASALADADA
HHHHHHHHHHHHCCC		21.0622617229
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CHM2A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHM2A_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CHM2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STABP_HUMANSTAMBPphysical
17159328
CHMP3_HUMANCHMP3physical
17159328
VPS4A_HUMANVPS4Aphysical
16730941
CHM2A_HUMANCHMP2Aphysical
16730941
CHMP3_HUMANCHMP3physical
16730941
NOL4_HUMANNOL4physical
16730941
EI2BE_HUMANEIF2B5physical
16730941
MITD1_HUMANMITD1physical
16730941
RBP2_HUMANRANBP2physical
22939629
ERLN1_HUMANERLIN1physical
22939629
PP1A_HUMANPPP1CAphysical
22939629
RRBP1_HUMANRRBP1physical
22939629
E2F4_HUMANE2F4physical
21988832
TGFB3_HUMANTGFB3physical
21988832
DOCK8_HUMANDOCK8physical
25416956
4EBP1_HUMANEIF4EBP1physical
26344197
PARVA_HUMANPARVAphysical
26344197
TRI35_HUMANTRIM35physical
28514442
VTA1_HUMANVTA1physical
28514442
DECR_HUMANDECR1physical
28514442
CHMP5_HUMANCHMP5physical
28514442
Drug and Disease Associations
Kegg Disease
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.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHM2A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 1-7, AND ACETYLATION AT MET-1.
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.

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