UniProt ID | CHM4B_MOUSE | |
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UniProt AC | Q9D8B3 | |
Protein Name | Charged multivesicular body protein 4b | |
Gene Name | Chmp4b | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 224 | |
Subcellular Localization |
Cytoplasm, cytosol . Late endosome membrane Peripheral membrane protein . Midbody . Nucleus envelope . Recruited to the nuclear envelope by CHMP7 during late anaphase. Localizes transiently to the midbody arms immediately before abscission. |
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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. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan.. | |
Protein Sequence | MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSVALPSKPAKKKEEEDDDMKELENWAGSM | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
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2 | Acetylation | ------MSVFGKLFG ------CCHHHHCCC | 26.59 | 23806337 | |
2 | Phosphorylation | ------MSVFGKLFG ------CCHHHHCCC | 26.59 | 29514104 | |
6 | Acetylation | --MSVFGKLFGAGGG --CCHHHHCCCCCCC | 29.22 | 23806337 | |
14 | Ubiquitination | LFGAGGGKAGKGGPT CCCCCCCCCCCCCCC | 58.18 | 27667366 | |
87 | Phosphorylation | AQIDGTLSTIEFQRE HHCCCCHHHHHHHHH | 27.46 | 26525534 | |
88 | Phosphorylation | QIDGTLSTIEFQREA HCCCCHHHHHHHHHH | 27.86 | 26525534 | |
107 | Ubiquitination | NTNTEVLKNMGYAAK CCCHHHHHHHHHHHH | 50.49 | 22790023 | |
114 | Acetylation | KNMGYAAKAMKAAHD HHHHHHHHHHHHHHH | 40.62 | 22826441 | |
184 | Phosphorylation | DKNLLEISGPETVPL HHHCHHHHCCCCCCC | 38.63 | 26239621 | |
188 | Phosphorylation | LEISGPETVPLPNVP HHHHCCCCCCCCCCC | 30.47 | 23984901 | |
196 | Phosphorylation | VPLPNVPSVALPSKP CCCCCCCCCCCCCCC | 18.75 | 29514104 | |
223 | Phosphorylation | ELENWAGSM------ HHHHHHHCC------ | 17.36 | 25521595 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of CHM4B_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of CHM4B_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of CHM4B_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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