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Protein

Charged multivesicular body protein 2b

Gene

CHMP2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. 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.

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB

GO - Biological processi

  • autophagy Source: ParkinsonsUK-UCL
  • cell separation after cytokinesis Source: UniProtKB
  • cognition Source: UniProtKB
  • endosomal transport Source: Reactome
  • endosome organization Source: UniProtKB
  • ESCRT III complex disassembly Source: ParkinsonsUK-UCL
  • macroautophagy Source: ParkinsonsUK-UCL
  • mitotic metaphase plate congression Source: UniProtKB
  • multivesicular body assembly Source: ParkinsonsUK-UCL
  • multivesicular body-lysosome fusion Source: ParkinsonsUK-UCL
  • neuron cellular homeostasis Source: UniProtKB
  • nucleus organization Source: UniProtKB
  • positive regulation of viral release from host cell Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of centrosome duplication Source: UniProtKB
  • regulation of mitotic spindle assembly Source: UniProtKB
  • viral budding via host ESCRT complex Source: UniProtKB
  • viral life cycle Source: Reactome

Keywordsi

Biological processProtein 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 2b
Alternative name(s):
CHMP2.5
Chromatin-modifying protein 2b
Short name:
CHMP2b
Vacuolar protein sorting-associated protein 2-2
Short name:
Vps2-2
Short name:
hVps2-2
Gene namesi
Name:CHMP2B
ORF Names:CGI-84
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000083937.8
HGNCiHGNC:24537 CHMP2B
MIMi609512 gene
neXtProtiNX_Q9UQN3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Frontotemporal dementia, chromosome 3-linked (FTD3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by an onset of dementia in the late 50's initially characterized by behavioral and personality changes including apathy, restlessness, disinhibition and hyperorality, progressing to stereotyped behaviors, non-fluent aphasia, mutism and dystonia, with a marked lack of insight. The brains of individuals with FTD3 have no distinctive neuropathological features. They show global cortical and central atrophy, but no beta-amyloid deposits.
See also OMIM:600795
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023383148D → Y in FTD3. 1 PublicationCorresponds to variant dbSNP:rs63750653EnsemblClinVar.1
Amyotrophic lateral sclerosis 17 (ALS17)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn adult-onset progressive neurodegenerative disorder with predominantly lower motor neuron involvement, manifest as muscle weakness and wasting of the upper and lower limbs, bulbar signs, and respiratory insufficiency.
See also OMIM:614696
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03837329I → V in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A1 overall indicating a defect in the autophagic pathway. 2 PublicationsCorresponds to variant dbSNP:rs63750818EnsemblClinVar.1
Natural variantiVAR_068689104T → N in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway. 1 PublicationCorresponds to variant dbSNP:rs281864934EnsemblClinVar.1
Natural variantiVAR_038374206Q → H in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway. 2 PublicationsCorresponds to variant dbSNP:rs63751126EnsemblClinVar.1

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi25978
GeneReviewsiCHMP2B
MalaCardsiCHMP2B
MIMi600795 phenotype
614696 phenotype
OpenTargetsiENSG00000083937
Orphaneti803 Amyotrophic lateral sclerosis
275864 Behavioral variant of frontotemporal dementia
100070 Progressive non-fluent aphasia
100069 Semantic dementia
PharmGKBiPA142672112

Polymorphism and mutation databases

BioMutaiCHMP2B
DMDMi73917746

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002114692 – 213Charged multivesicular body protein 2bAdd BLAST212

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei199PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UQN3
PaxDbiQ9UQN3
PeptideAtlasiQ9UQN3
PRIDEiQ9UQN3

PTM databases

iPTMnetiQ9UQN3
PhosphoSitePlusiQ9UQN3

Expressioni

Tissue specificityi

Widely expressed. Expressed in brain, heart, skeletal muscle, spleen, kidney, liver, small intestine, pancreas, lung, placenta and leukocytes. In brain, it is expressed in cerebellum, cerebral cortex, medulla, spinal chord, occipital lobe, frontal lobe, temporal lobe and putamen.1 Publication

Gene expression databases

BgeeiENSG00000083937
CleanExiHS_CHMP2B
ExpressionAtlasiQ9UQN3 baseline and differential
GenevisibleiQ9UQN3 HS

Organism-specific databases

HPAiHPA035069
HPA052754

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 sequentially. Interacts with CHMP2A. Interacts with VPS4A. Interacts with VPS4B; the interaction is direct.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117462, 47 interactors
CORUMiQ9UQN3
DIPiDIP-50766N
IntActiQ9UQN3, 45 interactors
MINTiQ9UQN3
STRINGi9606.ENSP00000263780

Structurei

Secondary structure

1213
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi201 – 210Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JQKNMR-B195-213[»]
ProteinModelPortaliQ9UQN3
SMRiQ9UQN3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UQN3

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili25 – 55Sequence analysisAdd BLAST31

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi201 – 211MIT-interacting motifAdd BLAST11

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3231 Eukaryota
ENOG4111QA0 LUCA
GeneTreeiENSGT00550000074737
HOGENOMiHOG000177218
HOVERGENiHBG102628
InParanoidiQ9UQN3
KOiK12192
OMAiENMKMGM
OrthoDBiEOG091G0S04
PhylomeDBiQ9UQN3
TreeFamiTF314163

Family and domain databases

InterProiView protein in InterPro
IPR005024 Snf7_fam
PfamiView protein in Pfam
PF03357 Snf7, 1 hit

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UQN3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA
60 70 80 90 100
KIGNKEACKV LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG
110 120 130 140 150
AMSTTAKTMQ AVNKKMDPQK TLQTMQNFQK ENMKMEMTEE MINDTLDDIF
160 170 180 190 200
DGSDDEEESQ DIVNQVLDEI GIEISGKMAK APSAARSLPS ASTSKATISD
210
EEIERQLKAL GVD
Length:213
Mass (Da):23,907
Last modified:May 1, 2000 - v1
Checksum:iBA192A0EAC45C19B
GO
Isoform 2 (identifier: Q9UQN3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQL → M

Show »
Length:172
Mass (Da):19,100
Checksum:i4F61A1400473D9F6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8K → R in CAB45721 (PubMed:11230166).Curated1
Sequence conflicti8K → R in CAG38487 (PubMed:14702039).Curated1
Sequence conflicti113N → S in BAD96374 (Ref. 5) Curated1
Sequence conflicti201E → V in CAB45721 (PubMed:11230166).Curated1
Sequence conflicti201E → V in CAG38487 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03837329I → V in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A1 overall indicating a defect in the autophagic pathway. 2 PublicationsCorresponds to variant dbSNP:rs63750818EnsemblClinVar.1
Natural variantiVAR_068689104T → N in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway. 1 PublicationCorresponds to variant dbSNP:rs281864934EnsemblClinVar.1
Natural variantiVAR_023383148D → Y in FTD3. 1 PublicationCorresponds to variant dbSNP:rs63750653EnsemblClinVar.1
Natural variantiVAR_038374206Q → H in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway. 2 PublicationsCorresponds to variant dbSNP:rs63751126EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0451421 – 42MASLF…QEKQL → M in isoform 2. CuratedAdd BLAST42

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151842 mRNA Translation: AAD34079.1
AL080122 mRNA Translation: CAB45721.1
AK296072 mRNA Translation: BAG58830.1
CR533456 mRNA Translation: CAG38487.1
AK222654 mRNA Translation: BAD96374.1
AC123511 Genomic DNA No translation available.
AC130885 Genomic DNA No translation available.
BC001553 mRNA Translation: AAH01553.1
CCDSiCCDS2918.1 [Q9UQN3-1]
CCDS58840.1 [Q9UQN3-2]
PIRiT12468
RefSeqiNP_001231573.1, NM_001244644.1 [Q9UQN3-2]
NP_054762.2, NM_014043.3 [Q9UQN3-1]
UniGeneiHs.476930

Genome annotation databases

EnsembliENST00000263780; ENSP00000263780; ENSG00000083937 [Q9UQN3-1]
ENST00000471660; ENSP00000419998; ENSG00000083937 [Q9UQN3-2]
GeneIDi25978
KEGGihsa:25978
UCSCiuc003dqp.5 human [Q9UQN3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiCHM2B_HUMAN
AccessioniPrimary (citable) accession number: Q9UQN3
Secondary accession number(s): B4DJG8, Q53HC7, Q9Y4U6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 152 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

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