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IID00876
UniprotQ9H444
ProteinCharged multivesicular body protein 4b
GeneCHMP4B
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
224
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 23-97 Homo dimer :
 Evidence X-RAY 4abm A Reference
       Region 4abm A 23-97 order
 Evidence X-RAY 4abm B Reference
       Region 4abm B 23-97 order
Seq 23-97 Monomer :
 Evidence X-RAY 4abm C Reference
       Region 4abm C 23-96 order
       Region 4abm C 97-97 disorder
 Evidence X-RAY 4abm D Reference
       Region 4abm D 23-97 order
Seq 121-224 Hetero dimer : Q5VW32
 Evidence X-RAY 3um3 B Reference
       Region 3um3 B 121-206 disorder
       Region 3um3 B 207-224 order
Seq 205-224 Hetero trimer : Q9H3S7
 Evidence X-RAY 5mk2 C Reference
       Region 5mk2 C 205-211 disorder
       Region 5mk2 C 212-222 order
       Region 5mk2 C 223-224 disorder
Seq 207-224 Hetero dimer : IID00852Complex
 Evidence X-RAY 3c3q B Reference
       Region 3c3q B 207-224 order
SeqProS possible 207-224 Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950). Hetero dimer : IID00852Complex
       Region 3c3q B 207-224 order
SeqProS possible 207-224 Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950). Hetero dimer : Q5VW32
       Region 3um3 B 207-224 order
SeqProS possible 212-222 Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950). Hetero trimer : Q9H3S7
       Region 5mk2 C 212-222 order
Seqphosphorylation
    184-184 Phosphoserine
    223-223 Phosphoserine
Seqacetylation
    114-114 N6-acetyllysine
    6-6 N6-acetyllysine
    2-2 N-acetylserine
 
Prediction
NeProc
Disorder 1-21,131-137,150-224
Order 22-130,138-149
ProS 4-11,131-137,150-173,188-196,212-224
AlphaFold
Disorder 1-18,122-124,151-159,179-210,224-224
Order 19-121,125-150,160-178,211-223
Pfam Hmmer
PF03357 24-199 1e-82
SEG 4-19 ,60-74 ,157-182 ,205-216
Function
Function in SwissProt
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 (PubMed:12860994, PubMed:18209100). The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:21310966). Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). 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 (PubMed:22660413). Majority of the protein exists in a folded closed conformation (PubMed:33349255).
(Microbial infection) The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the budding of enveloped viruses (HIV-1 and other lentiviruses). Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release.
Biological Process
See also
Diagram with PDB data
CHMP4C/PDCD6IPALIX BRO1 CHMP4C complex