CHMP7_HUMAN - dbPTM
CHMP7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHMP7_HUMAN
UniProt AC Q8WUX9
Protein Name Charged multivesicular body protein 7
Gene Name CHMP7
Organism Homo sapiens (Human).
Sequence Length 453
Subcellular Localization Cytoplasm . Nucleus envelope . Diffused localization, with some punctate distribution, especially in the perinuclear area (PubMed:16856878). Localizes to the nucleus envelope during late anaphase (PubMed:26040712).
Protein Description ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase. [PubMed: 26040712 Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase]
Protein Sequence MWSPEREAEAPAGGDPAGLLPPEWEEDEERMSFLFSAFKRSREVNSTDWDSKMGFWAPLVLSHSRRQGVVRLRLRDLQEAFQRKGSVPLGLATVLQDLLRRGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDNKVPAEEVLVAVELLKEKAEEVYRLYQNSPLSSHPVVALSELSTLCANSCPDERTFYLVLLQLQKEKRVTVLEQNGEKIVKFARGPRAKVSPVNDVDVGVYQLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKEPLDLPDNPRNRHFTNSVPNPRISDAELEAELEKLSLSEGGLVPSSKSPKRQLEPTLKPL
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
3Phosphorylation-----MWSPEREAEA
-----CCCHHHHHCC		18.6528348404
46PhosphorylationKRSREVNSTDWDSKM
HHHCCCCCCCHHHCC		32.6827251275
84UbiquitinationLQEAFQRKGSVPLGL
HHHHHHHCCCCCHHH		44.76-
84UbiquitinationLQEAFQRKGSVPLGL
HHHHHHHCCCCCHHH		44.76-
86PhosphorylationEAFQRKGSVPLGLAT
HHHHHCCCCCHHHHH		24.4820873877
93PhosphorylationSVPLGLATVLQDLLR
CCCHHHHHHHHHHHH		27.1323403867
196PhosphorylationNSCPDERTFYLVLLQ
CCCCCHHHHHHHHHH		18.0023401153
198PhosphorylationCPDERTFYLVLLQLQ
CCCHHHHHHHHHHHH		8.6923401153
219UbiquitinationVLEQNGEKIVKFARG
EEEECCCEEEEECCC		54.95-
230UbiquitinationFARGPRAKVSPVNDV
ECCCCCCCCCCCCCC		44.52-
232PhosphorylationRGPRAKVSPVNDVDV
CCCCCCCCCCCCCCH		23.5622617229
242PhosphorylationNDVDVGVYQLMQSEQ
CCCCHHHHHHHHHHH		7.0425850435
245SulfoxidationDVGVYQLMQSEQLLS
CHHHHHHHHHHHHHH		2.1330846556
247PhosphorylationGVYQLMQSEQLLSRK
HHHHHHHHHHHHHHH		17.2224117733
252PhosphorylationMQSEQLLSRKVESLS
HHHHHHHHHHHHHHH		38.3524117733
254UbiquitinationSEQLLSRKVESLSQE
HHHHHHHHHHHHHHH		47.15-
257PhosphorylationLLSRKVESLSQEAER
HHHHHHHHHHHHHHH		35.9929507054
259PhosphorylationSRKVESLSQEAERCK
HHHHHHHHHHHHHHH		34.9429507054
337UbiquitinationGALKLSMKDVTVEKA
CCEECCCCCCCHHHH		45.75-
393UbiquitinationILLQDTTKEPLDLPD
HHHHCCCCCCCCCCC		60.47-
405MethylationLPDNPRNRHFTNSVP
CCCCCCCCCCCCCCC		27.81-
408PhosphorylationNPRNRHFTNSVPNPR
CCCCCCCCCCCCCCC		22.0625159151
410PhosphorylationRNRHFTNSVPNPRIS
CCCCCCCCCCCCCCC		35.5725159151
417PhosphorylationSVPNPRISDAELEAE
CCCCCCCCHHHHHHH		31.8629255136
427UbiquitinationELEAELEKLSLSEGG
HHHHHHHHCCCCCCC		56.87-
429PhosphorylationEAELEKLSLSEGGLV
HHHHHHCCCCCCCCC		40.7029255136
431PhosphorylationELEKLSLSEGGLVPS
HHHHCCCCCCCCCCC		30.7129255136
438PhosphorylationSEGGLVPSSKSPKRQ
CCCCCCCCCCCCCCC		42.8125159151
439PhosphorylationEGGLVPSSKSPKRQL
CCCCCCCCCCCCCCC		30.9625159151
441PhosphorylationGLVPSSKSPKRQLEP
CCCCCCCCCCCCCCC		37.2922617229
449PhosphorylationPKRQLEPTLKPL---
CCCCCCCCCCCC---		37.7326074081
451AcetylationRQLEPTLKPL-----
CCCCCCCCCC-----		46.9125953088
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 CHMP7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHMP7_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 CHMP7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHG17_HUMANARHGAP17physical
26344197
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 CHMP7_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-417, 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-417, 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-417, AND MASSSPECTROMETRY.

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