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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 B Reference
       Region 4abm B 23-97 order
 Evidence X-RAY 4abm A Reference
       Region 4abm A 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
(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