Q9BY43 · CHM4A_HUMAN
- ProteinCharged multivesicular body protein 4a
- GeneCHMP4A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids222 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. When overexpressed, membrane-assembled circular arrays of CHMP4A filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCharged multivesicular body protein 4a
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BY43
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Late endosome membrane ; Peripheral membrane protein
Note: Membrane-associated. Localizes to large vesicle-like structures. Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_023384 | 153 | in dbSNP:rs2295322 | |||
Sequence: G → R | ||||||
Mutagenesis | 182-222 | Membrane association; releases autoinhibition. | ||||
Sequence: Missing | ||||||
Mutagenesis | 209 | Reduces interaction with PDCD6IP. | ||||
Sequence: E → A | ||||||
Mutagenesis | 214 | Abolishes interaction with PDCD6IP. | ||||
Sequence: L → A | ||||||
Mutagenesis | 217 | Abolishes interaction with PDCD6IP. | ||||
Sequence: L → A | ||||||
Mutagenesis | 220 | Abolishes interaction with PDCD6IP. | ||||
Sequence: W → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 360 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000211488 | 1-222 | UniProt | Charged multivesicular body protein 4a | |||
Sequence: MSGLGRLFGKGKKEKGPTPEEAIQKLKETEKILIKKQEFLEQKIQQELQTAKKYGTKNKRAALQALRRKKRFEQQLAQTDGTLSTLEFQREAIENATTNAEVLRTMELAAQSMKKAYQDMDIDKVDELMTDITEQQEVAQQISDAISRPMGFGDDVDEDELLEELEELEQEELAQELLNVGDKEEEPSVKLPSVPSTHLPAGPAPKVDEDEEALKQLAEWVS | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 196 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Expressed at higher level in heart, kidney, liver and skeletal muscle. Also expressed in brain, placenta, lung and pancreas.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Self-associates; overexpression leads to the assembly of filaments that curve and associate to create circular rings. Interacts with CHMP2A. Interacts with CHMP3; the interaction requires the release of CHMP4A autoinhibition. Interacts with CHMP4B. Interacts with CHMP4C. Interacts with CHMP6. Interacts with VPS4A. Interacts with PDCD6IP; the interaction is direct.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BY43 | CHMP4B Q9H444 | 4 | EBI-747981, EBI-749627 | |
BINARY | Q9BY43 | PDCD6IP Q8WUM4 | 3 | EBI-747981, EBI-310624 | |
BINARY | Q9BY43 | SYT17 Q9BSW7 | 6 | EBI-747981, EBI-745392 | |
BINARY | Q9BY43-2 | CHMP4B Q9H444 | 3 | EBI-12178895, EBI-749627 | |
BINARY | Q9BY43-2 | NTAQ1 Q96HA8 | 3 | EBI-12178895, EBI-741158 | |
BINARY | Q9BY43-2 | NUTF2 P61970 | 3 | EBI-12178895, EBI-591778 | |
BINARY | Q9BY43-2 | SYT17 Q9BSW7 | 3 | EBI-12178895, EBI-745392 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MSGLGRLFGKGKKEKGPTPEE | ||||||
Region | 1-116 | Interaction with phosphoinosides | ||||
Sequence: MSGLGRLFGKGKKEKGPTPEEAIQKLKETEKILIKKQEFLEQKIQQELQTAKKYGTKNKRAALQALRRKKRFEQQLAQTDGTLSTLEFQREAIENATTNAEVLRTMELAAQSMKKA | ||||||
Region | 1-150 | Intramolecular interaction with C-terminus | ||||
Sequence: MSGLGRLFGKGKKEKGPTPEEAIQKLKETEKILIKKQEFLEQKIQQELQTAKKYGTKNKRAALQALRRKKRFEQQLAQTDGTLSTLEFQREAIENATTNAEVLRTMELAAQSMKKAYQDMDIDKVDELMTDITEQQEVAQQISDAISRPM | ||||||
Coiled coil | 20-105 | |||||
Sequence: EEAIQKLKETEKILIKKQEFLEQKIQQELQTAKKYGTKNKRAALQALRRKKRFEQQLAQTDGTLSTLEFQREAIENATTNAEVLRT | ||||||
Region | 151-222 | Intramolecular interaction with N-terminus | ||||
Sequence: GFGDDVDEDELLEELEELEQEELAQELLNVGDKEEEPSVKLPSVPSTHLPAGPAPKVDEDEEALKQLAEWVS | ||||||
Coiled coil | 155-180 | |||||
Sequence: DVDEDELLEELEELEQEELAQELLNV | ||||||
Region | 180-211 | Disordered | ||||
Sequence: VGDKEEEPSVKLPSVPSTHLPAGPAPKVDEDE |
Domain
The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity).
Sequence similarities
Belongs to the SNF7 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9BY43-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length222
- Mass (Da)25,098
- Last updated2006-02-07 v3
- Checksum6712BA6AAA1D7CB7
Q9BY43-2
- Name2
- Differences from canonical
- 1-1: M → MSRRRPEDGLGKAGPCVMRHHPPRSKAEVWRTLRGGGGRGELAM
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056264 | 1 | in isoform 2 | |||
Sequence: M → MSRRRPEDGLGKAGPCVMRHHPPRSKAEVWRTLRGGGGRGELAM | ||||||
Sequence conflict | 16 | in Ref. 4; AAF29098 | ||||
Sequence: G → R | ||||||
Sequence conflict | 66 | in Ref. 4; AAF29098 | ||||
Sequence: L → S | ||||||
Sequence conflict | 152-153 | in Ref. 4; AAF29098 | ||||
Sequence: FG → LLE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB100262 EMBL· GenBank· DDBJ | BAC79376.2 EMBL· GenBank· DDBJ | mRNA | ||
AY329084 EMBL· GenBank· DDBJ | AAQ91193.1 EMBL· GenBank· DDBJ | mRNA | ||
AF212243 EMBL· GenBank· DDBJ | AAK14928.1 EMBL· GenBank· DDBJ | mRNA | ||
AF161483 EMBL· GenBank· DDBJ | AAF29098.1 EMBL· GenBank· DDBJ | mRNA | ||
BX161512 EMBL· GenBank· DDBJ | CAD61949.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL096870 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL136295 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC010893 EMBL· GenBank· DDBJ | AAH10893.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC107699 EMBL· GenBank· DDBJ | AAI07700.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC113533 EMBL· GenBank· DDBJ | AAI13534.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113535 EMBL· GenBank· DDBJ | AAI13536.1 EMBL· GenBank· DDBJ | mRNA |