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Protein

Charged multivesicular body protein 4b

Gene

CHMP4B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).5 Publications
(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.3 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • identical protein binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • autophagy Source: ParkinsonsUK-UCL
  • cell separation after cytokinesis Source: UniProtKB
  • endosomal transport Source: Reactome
  • exit from mitosis Source: UniProtKB
  • maintenance of lens transparency Source: UniProtKB
  • membrane fission Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • mitotic metaphase plate congression Source: UniProtKB
  • multivesicular body assembly Source: ParkinsonsUK-UCL
  • negative regulation of autophagosome assembly Source: UniProtKB
  • negative regulation of cell death Source: UniProtKB
  • negative regulation of neuron death Source: UniProtKB
  • nuclear envelope reassembly Source: UniProtKB
  • nucleus organization Source: UniProtKB
  • positive regulation of viral release from host cell Source: UniProtKB
  • posttranslational protein targeting to membrane Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • regulation of centrosome duplication Source: UniProtKB
  • regulation of mitotic spindle assembly Source: UniProtKB
  • regulation of viral process Source: UniProtKB
  • ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB
  • viral budding Source: UniProtKB
  • viral budding via host ESCRT complex Source: UniProtKB
  • viral life cycle Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-162588. Budding and maturation of HIV virion.
R-HSA-1632852. Macroautophagy.
R-HSA-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended name:
Charged multivesicular body protein 4b
Alternative name(s):
Chromatin-modifying protein 4b
Short name:
CHMP4b
SNF7 homolog associated with Alix 1
SNF7-2
Short name:
hSnf7-2
Vacuolar protein sorting-associated protein 32-2
Short name:
Vps32-2
Short name:
hVps32-2
Gene namesi
Name:CHMP4B
Synonyms:C20orf178, SHAX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16171. CHMP4B.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytoplasmic side of plasma membrane Source: UniProtKB
  • cytosol Source: Reactome
  • endosome Source: UniProtKB
  • ESCRT III complex Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • late endosome membrane Source: UniProtKB-SubCell
  • membrane coat Source: UniProtKB
  • midbody Source: UniProtKB
  • nuclear envelope Source: UniProtKB
  • nucleus Source: UniProtKB
  • vesicle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cataract 31, multiple types (CTRCT31)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT31 includes posterior polar, progressive posterior subcapsular, nuclear, and anterior subcapsular cataracts.
See also OMIM:605387
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037579129D → V in CTRCT31. 1 PublicationCorresponds to variant rs118203965dbSNPEnsembl.1
Natural variantiVAR_037580161E → K in CTRCT31. 1 PublicationCorresponds to variant rs118203966dbSNPEnsembl.1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNETi128866.
MalaCardsiCHMP4B.
MIMi605387. phenotype.
OpenTargetsiENSG00000101421.
Orphaneti98993. Posterior polar cataract.
PharmGKBiPA25721.

Polymorphism and mutation databases

BioMutaiCHMP4B.
DMDMi24636296.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002114892 – 224Charged multivesicular body protein 4bAdd BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei6N6-acetyllysineCombined sources1
Modified residuei114N6-acetyllysineCombined sources1
Modified residuei184PhosphoserineCombined sources1
Modified residuei223PhosphoserineCombined sources1

Post-translational modificationi

ISGylated. Isgylation weakens its interaction with VPS4A.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9H444.
MaxQBiQ9H444.
PaxDbiQ9H444.
PeptideAtlasiQ9H444.
PRIDEiQ9H444.

PTM databases

iPTMnetiQ9H444.
PhosphoSitePlusiQ9H444.

Expressioni

Tissue specificityi

Widely expressed. Expressed at higher level in heart and skeletal muscle. Also expressed in brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood lymphocytes.1 Publication

Gene expression databases

BgeeiENSG00000101421.
CleanExiHS_CHMP4B.
GenevisibleiQ9H444. HS.

Organism-specific databases

HPAiHPA041401.
HPA051751.

Interactioni

Subunit structurei

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 sequentally. Interacts with CHMP6 and CHMP4C. Interacts with PDCD6IP; the interaction is direct. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with CHMP7. Interacts with CFTR; the interaction requires misfolded CFTR. Interacts with PTPN23.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-749627,EBI-749627
CC2D1AQ6P1N03EBI-749627,EBI-7112364
CHMP2AO436333EBI-749627,EBI-2692789
CHMP2BQ9UQN32EBI-749627,EBI-718324
CHMP3Q9Y3E75EBI-749627,EBI-2118119
CHMP4AQ9BY434EBI-749627,EBI-747981
CHMP5Q9NZZ34EBI-749627,EBI-751303
CHMP7Q8WUX93EBI-749627,EBI-749253
PTPN23Q9H3S72EBI-749627,EBI-724478
STAMBPO956303EBI-749627,EBI-396676
UBE2IP632793EBI-749627,EBI-80168

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • identical protein binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi126170. 117 interactors.
DIPiDIP-29924N.
IntActiQ9H444. 109 interactors.
MINTiMINT-5000054.
STRINGi9606.ENSP00000217402.

Structurei

Secondary structure

1224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 57Combined sources35
Helixi62 – 96Combined sources35
Helixi209 – 212Combined sources4
Helixi215 – 222Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C3QX-ray2.10B207-224[»]
3UM3X-ray3.80B121-224[»]
4ABMX-ray1.80A/B/C/D23-97[»]
ProteinModelPortaliQ9H444.
SMRiQ9H444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H444.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili23 – 183Sequence analysisAdd BLAST161

Domaini

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.

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1656. Eukaryota.
ENOG410YE9I. LUCA.
GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
HOVERGENiHBG050928.
InParanoidiQ9H444.
KOiK12194.
OMAiMKELETW.
OrthoDBiEOG091G0V7X.
PhylomeDBiQ9H444.
TreeFamiTF314269.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9H444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVFGKLFGA GGGKAGKGGP TPQEAIQRLR DTEEMLSKKQ EFLEKKIEQE
60 70 80 90 100
LTAAKKHGTK NKRAALQALK RKKRYEKQLA QIDGTLSTIE FQREALENAN
110 120 130 140 150
TNTEVLKNMG YAAKAMKAAH DNMDIDKVDE LMQDIADQQE LAEEISTAIS
160 170 180 190 200
KPVGFGEEFD EDELMAELEE LEQEELDKNL LEISGPETVP LPNVPSIALP
210 220
SKPAKKKEEE DDDMKELENW AGSM
Length:224
Mass (Da):24,950
Last modified:March 1, 2001 - v1
Checksum:iDB1D79DD3803CB2F
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037579129D → V in CTRCT31. 1 PublicationCorresponds to variant rs118203965dbSNPEnsembl.1
Natural variantiVAR_037580161E → K in CTRCT31. 1 PublicationCorresponds to variant rs118203966dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB100261 mRNA. Translation: BAC79375.1.
AY329085 mRNA. Translation: AAQ91194.1.
AL050349 Genomic DNA. Translation: CAC14088.1.
CH471077 Genomic DNA. Translation: EAW76293.1.
CH471077 Genomic DNA. Translation: EAW76294.1.
BC033859 mRNA. Translation: AAH33859.1.
CCDSiCCDS13228.1.
RefSeqiNP_789782.1. NM_176812.4.
UniGeneiHs.472471.

Genome annotation databases

EnsembliENST00000217402; ENSP00000217402; ENSG00000101421.
GeneIDi128866.
KEGGihsa:128866.
UCSCiuc002xaa.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB100261 mRNA. Translation: BAC79375.1.
AY329085 mRNA. Translation: AAQ91194.1.
AL050349 Genomic DNA. Translation: CAC14088.1.
CH471077 Genomic DNA. Translation: EAW76293.1.
CH471077 Genomic DNA. Translation: EAW76294.1.
BC033859 mRNA. Translation: AAH33859.1.
CCDSiCCDS13228.1.
RefSeqiNP_789782.1. NM_176812.4.
UniGeneiHs.472471.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C3QX-ray2.10B207-224[»]
3UM3X-ray3.80B121-224[»]
4ABMX-ray1.80A/B/C/D23-97[»]
ProteinModelPortaliQ9H444.
SMRiQ9H444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126170. 117 interactors.
DIPiDIP-29924N.
IntActiQ9H444. 109 interactors.
MINTiMINT-5000054.
STRINGi9606.ENSP00000217402.

PTM databases

iPTMnetiQ9H444.
PhosphoSitePlusiQ9H444.

Polymorphism and mutation databases

BioMutaiCHMP4B.
DMDMi24636296.

Proteomic databases

EPDiQ9H444.
MaxQBiQ9H444.
PaxDbiQ9H444.
PeptideAtlasiQ9H444.
PRIDEiQ9H444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217402; ENSP00000217402; ENSG00000101421.
GeneIDi128866.
KEGGihsa:128866.
UCSCiuc002xaa.4. human.

Organism-specific databases

CTDi128866.
DisGeNETi128866.
GeneCardsiCHMP4B.
HGNCiHGNC:16171. CHMP4B.
HPAiHPA041401.
HPA051751.
MalaCardsiCHMP4B.
MIMi605387. phenotype.
610897. gene.
neXtProtiNX_Q9H444.
OpenTargetsiENSG00000101421.
Orphaneti98993. Posterior polar cataract.
PharmGKBiPA25721.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1656. Eukaryota.
ENOG410YE9I. LUCA.
GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
HOVERGENiHBG050928.
InParanoidiQ9H444.
KOiK12194.
OMAiMKELETW.
OrthoDBiEOG091G0V7X.
PhylomeDBiQ9H444.
TreeFamiTF314269.

Enzyme and pathway databases

ReactomeiR-HSA-162588. Budding and maturation of HIV virion.
R-HSA-1632852. Macroautophagy.
R-HSA-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

ChiTaRSiCHMP4B. human.
EvolutionaryTraceiQ9H444.
GeneWikiiCHMP4B.
GenomeRNAii128866.
PROiQ9H444.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101421.
CleanExiHS_CHMP4B.
GenevisibleiQ9H444. HS.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHM4B_HUMAN
AccessioniPrimary (citable) accession number: Q9H444
Secondary accession number(s): E1P5N4, Q53ZD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Its overexpression strongly inhibits HIV-1 release.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.