Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Charged multivesicular body protein 2b  

UniProtKB / Swiss-Prot ID :  CHM2B_HUMAN

Gene Name (Synonyms) : 
CHMP2B CGI-84  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytosol. Late endosome membrane; Peripheral membrane protein (Probable). 

Protein Function :  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. 

Protein Sequence MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACKVLAKQLVHLRK...
Predicted Secondary Structure CCCHHCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
29I -> V. VAR_038373
148D -> Y (in FTD3). VAR_023383
206Q -> H (in amyotrophic lateral sclerosis;CHMP2B-related).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
153PhosphoserineIFDGSDDEE
CCCCCCHHH
43.67HPRD
Link-
153PhosphoserineIFDGSDDEE
CCCCCCHHH
43.67Phosphositeplus
Link-
187PhosphoserineSAARSLPSA
CCCCCCCCH
39.65Phosphositeplus
Link-
199PhosphoserineKATISDEEI
HCCCCHHHH
34.32HPRD
Link
199PhosphoserineKATISDEEI
HCCCCHHHH
34.32PhosphoELM
Link
199PhosphoserineKATISDEEI
HCCCCHHHH
34.32Phosphositeplus
Link
199PhosphoserineKATISDEEI
HCCCCHHHH
34.32SysPTM
Link
199Phosphoserine.KATISDEEI
HCCCCHHHH
34.32UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ATPG_HUMANphysical interactionMINT-63715MINT16169070
Q5T5T6_HUMANphysical interactionMINT-67299MINT16189514
TRAF2_HUMANphysical interactionEBI-756604
intact16189514
CENPF_HUMANyeast 2-hybridHPRD:13174HPRD16730941
PNMA1_HUMANyeast 2-hybridHPRD:13174HPRD16730941
SERA_HUMANyeast 2-hybridHPRD:13174HPRD16730941
CG030_HUMANyeast 2-hybridHPRD:13174HPRD16730941
CHM2B_HUMANyeast 2-hybridHPRD:13174HPRD16730941
CHMP3_HUMANyeast 2-hybridHPRD:13174HPRD16730941
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Disease Reference
Kegg disease
H00078 Frontotemporal lobar degeneration (FTLD), including: Pick disease of brain; Frontotemporal dementia
OMIM disease
600795Frontotemporal dementia, chromosome 3-linked (FTD3)
614696Amyotrophic lateral sclerosis 17 (ALS17)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
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-199, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASSSPECTROMETRY.
"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-199, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASSSPECTROMETRY.
"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-199, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures