CHM2B_HUMAN - dbPTM
CHM2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHM2B_HUMAN
UniProt AC Q9UQN3
Protein Name Charged multivesicular body protein 2b
Gene Name CHMP2B
Organism Homo sapiens (Human).
Sequence Length 213
Subcellular Localization Cytoplasm, cytosol . Late endosome membrane
Peripheral membrane protein .
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..
Protein Sequence MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACKVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD
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
2Acetylation------MASLFKKKT
------CCCCCCCCC		18.2322814378
3Phosphorylation-----MASLFKKKTV
-----CCCCCCCCCH		32.8024719451
6Methylation--MASLFKKKTVDDV
--CCCCCCCCCHHHH		59.67-
7Methylation-MASLFKKKTVDDVI
-CCCCCCCCCHHHHH		46.47-
9PhosphorylationASLFKKKTVDDVIKE
CCCCCCCCHHHHHHH		37.7423312004
15UbiquitinationKTVDDVIKEQNRELR
CCHHHHHHHHHHHCC		53.77-
22MethylationKEQNRELRGTQRAII
HHHHHHCCHHHHHHH		41.16-
24PhosphorylationQNRELRGTQRAIIRD
HHHHCCHHHHHHHHC		14.40-
63UbiquitinationEACKVLAKQLVHLRK
HHHHHHHHHHHHHHC		39.75-
63MalonylationEACKVLAKQLVHLRK
HHHHHHHHHHHHHHC		39.7526320211
75PhosphorylationLRKQKTRTFAVSSKV
HHCCCCCCEEECCCC		22.6028348404
79PhosphorylationKTRTFAVSSKVTSMS
CCCCEEECCCCCCCC		22.4728857561
80PhosphorylationTRTFAVSSKVTSMST
CCCEEECCCCCCCCH		25.2528857561
81AcetylationRTFAVSSKVTSMSTQ
CCEEECCCCCCCCHH		41.8625953088
81UbiquitinationRTFAVSSKVTSMSTQ
CCEEECCCCCCCCHH		41.86-
83PhosphorylationFAVSSKVTSMSTQTK
EEECCCCCCCCHHHH		23.5820068231
84PhosphorylationAVSSKVTSMSTQTKV
EECCCCCCCCHHHHH		17.4520068231
85SulfoxidationVSSKVTSMSTQTKVM
ECCCCCCCCHHHHHH		3.5230846556
86PhosphorylationSSKVTSMSTQTKVMN
CCCCCCCCHHHHHHH		19.6828348404
87PhosphorylationSKVTSMSTQTKVMNS
CCCCCCCHHHHHHHH		31.4530206219
89PhosphorylationVTSMSTQTKVMNSQM
CCCCCHHHHHHHHHH		26.2030206219
90UbiquitinationTSMSTQTKVMNSQMK
CCCCHHHHHHHHHHH		29.66-
94PhosphorylationTQTKVMNSQMKMAGA
HHHHHHHHHHHHCCC		17.3530206219
103PhosphorylationMKMAGAMSTTAKTMQ
HHHCCCCHHHHHHHH		23.2824719451
105PhosphorylationMAGAMSTTAKTMQAV
HCCCCHHHHHHHHHH		20.8922210691
107AcetylationGAMSTTAKTMQAVNK
CCCHHHHHHHHHHHH		42.3025953088
107UbiquitinationGAMSTTAKTMQAVNK
CCCHHHHHHHHHHHH		42.30-
114AcetylationKTMQAVNKKMDPQKT
HHHHHHHHCCCHHHH		42.7625953088
120UbiquitinationNKKMDPQKTLQTMQN
HHCCCHHHHHHHHHH		57.50-
121PhosphorylationKKMDPQKTLQTMQNF
HCCCHHHHHHHHHHH		20.8927470641
124PhosphorylationDPQKTLQTMQNFQKE
CHHHHHHHHHHHHHH		24.6827470641
125SulfoxidationPQKTLQTMQNFQKEN
HHHHHHHHHHHHHHH		1.6621406390
130UbiquitinationQTMQNFQKENMKMEM
HHHHHHHHHHHHHHH		47.09-
145PhosphorylationTEEMINDTLDDIFDG
HHHHHHHHHHHHHCC		27.8322210691
153PhosphorylationLDDIFDGSDDEEESQ
HHHHHCCCCCHHHHH		43.6720058876
159PhosphorylationGSDDEEESQDIVNQV
CCCCHHHHHHHHHHH		36.1124275569
175PhosphorylationDEIGIEISGKMAKAP
HHHCCEECCEECCCC		21.4122210691
183PhosphorylationGKMAKAPSAARSLPS
CEECCCCHHHHHCCC		39.1529514088
187PhosphorylationKAPSAARSLPSASTS
CCCHHHHHCCCCCCC		39.6525849741
190PhosphorylationSAARSLPSASTSKAT
HHHHHCCCCCCCCCC		39.9026657352
192PhosphorylationARSLPSASTSKATIS
HHHCCCCCCCCCCCC		37.2426657352
193PhosphorylationRSLPSASTSKATISD
HHCCCCCCCCCCCCH		33.6823403867
194PhosphorylationSLPSASTSKATISDE
HCCCCCCCCCCCCHH		20.1423403867
195UbiquitinationLPSASTSKATISDEE
CCCCCCCCCCCCHHH		50.03-
197PhosphorylationSASTSKATISDEEIE
CCCCCCCCCCHHHHH		25.4230266825
199PhosphorylationSTSKATISDEEIERQ
CCCCCCCCHHHHHHH		34.3219664994
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 CHM2B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHM2B_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 CHM2B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHM2B_HUMANCHMP2Bphysical
16730941
CHMP3_HUMANCHMP3physical
16730941
PNMA1_HUMANPNMA1physical
16730941
SERA_HUMANPHGDHphysical
16730941
MASU1_HUMANMALSU1physical
16730941
CHM2A_HUMANCHMP2Aphysical
26344197
CHM4B_HUMANCHMP4Bphysical
26344197
Drug and Disease Associations
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)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHM2B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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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