CHMP6_HUMAN - dbPTM
CHMP6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHMP6_HUMAN
UniProt AC Q96FZ7
Protein Name Charged multivesicular body protein 6
Gene Name CHMP6
Organism Homo sapiens (Human).
Sequence Length 201
Subcellular Localization Endomembrane system. Endosome membrane
Lipid-anchor. Late endosome membrane . Membrane
Lipid-anchor . Localizes to endosomal membranes.
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. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes..
Protein Sequence MGNLFGRKKQSRVTEQDKAILQLKQQRDKLRQYQKRIAQQLERERALARQLLRDGRKERAKLLLKKKRYQEQLLDRTENQISSLEAMVQSIEFTQIEMKVMEGLQFGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSFTQEDEDAILEELSAITQEQIELPEVPSEPLPEKIPENVPVKARPRQAELVAAS
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
2Myristoylation------MGNLFGRKK
------CCCCCCCCC
39.2815511219
18UbiquitinationSRVTEQDKAILQLKQ
CCCCHHHHHHHHHHH
36.7023000965
24UbiquitinationDKAILQLKQQRDKLR
HHHHHHHHHHHHHHH
31.2723000965
24MalonylationDKAILQLKQQRDKLR
HHHHHHHHHHHHHHH
31.2726320211
82PhosphorylationDRTENQISSLEAMVQ
HCCHHHHHHHHHHHH
21.0719053533
83PhosphorylationRTENQISSLEAMVQS
CCHHHHHHHHHHHHH
31.6819053533
101SulfoxidationTQIEMKVMEGLQFGN
HHHHHHHHHHHHHHH
2.5621406390
119PhosphorylationNKMHQVMSIEEVERI
HHHHHCCCHHHHHHH
28.1728450419
130PhosphorylationVERILDETQEAVEYQ
HHHHHHHHHHHHHHH
31.2321815630
136PhosphorylationETQEAVEYQRQIDEL
HHHHHHHHHHHHHHH
11.4629978859
189UbiquitinationIPENVPVKARPRQAE
CCCCCCCCCCCCHHH
32.3833845483

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 CHMP6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHMP6_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 CHMP6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NXN_HUMANNXNphysical
17353931
VPS25_HUMANVPS25physical
16371348
VPS25_HUMANVPS25physical
16973552
VPS25_HUMANVPS25physical
14505570
CHM4B_HUMANCHMP4Bphysical
14505570
CHM4B_HUMANCHMP4Bphysical
16730941
VPS25_HUMANVPS25physical
16730941
METL9_HUMANMETTL9physical
16730941
ELOF1_HUMANELOF1physical
16730941
CHM4B_HUMANCHMP4Bphysical
15511219
VPS25_HUMANVPS25physical
15511219

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 CHMP6_HUMAN

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Related Literatures of Post-Translational Modification

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