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Protein

Charged multivesicular body protein 6

Gene

CHMP6

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. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes.

GO - Molecular functioni

  • protein-containing complex binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB

GO - Biological processi

  • cell separation after cytokinesis Source: UniProtKB
  • endosomal transport Source: Reactome
  • ESCRT III complex assembly Source: ParkinsonsUK-UCL
  • macroautophagy Source: ParkinsonsUK-UCL
  • mitotic metaphase plate congression Source: UniProtKB
  • multivesicular body assembly Source: ParkinsonsUK-UCL
  • negative regulation of epidermal growth factor-activated receptor activity Source: UniProtKB
  • nucleus organization Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • vacuolar transport Source: InterPro
  • 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 6
Alternative name(s):
Chromatin-modifying protein 6
Vacuolar protein sorting-associated protein 20
Short name:
Vps20
Short name:
hVps20
Gene namesi
Name:CHMP6
Synonyms:VPS20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000176108.9
HGNCiHGNC:25675 CHMP6
MIMi610901 gene
neXtProtiNX_Q96FZ7

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

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Abolishes myristoylation. 1 Publication1
Mutagenesisi49R → E: Does not affect the subcellular location. 1 Publication1
Mutagenesisi168 – 201Missing : Membrane association; releases autoinhibition. 1 PublicationAdd BLAST34
Mutagenesisi170L → D: Abolishes interaction with VPS4A. 1 Publication1
Mutagenesisi173V → D: Abolishes interaction with VPS4A. 1 Publication1
Mutagenesisi178L → D: Reduces interaction with VPS4A. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000176108
PharmGKBiPA142672114

Polymorphism and mutation databases

BioMutaiCHMP6
DMDMi73917777

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002115082 – 201Charged multivesicular body protein 6Add BLAST200

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1 Publication1
Modified residuei119PhosphoserineBy similarity1
Modified residuei130PhosphothreonineCombined sources1

Post-translational modificationi

ISGylated in a CHMP5-dependent manner. Isgylation weakens its interaction with VPS4A.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96FZ7
MaxQBiQ96FZ7
PaxDbiQ96FZ7
PeptideAtlasiQ96FZ7
PRIDEiQ96FZ7
ProteomicsDBi76576

PTM databases

iPTMnetiQ96FZ7
PhosphoSitePlusiQ96FZ7

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000176108
CleanExiHS_CHMP6
ExpressionAtlasiQ96FZ7 baseline and differential
GenevisibleiQ96FZ7 HS

Organism-specific databases

HPAiHPA023001
HPA024460

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 VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with CHMP4A, CHMP4B and CHMP4C. Interacts with SNF8, VPS25 and VPS36.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VPS25Q9BRG16EBI-1049648,EBI-741945

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122771, 14 interactors
ComplexPortaliCPX-329 ESCRT-III complex
CORUMiQ96FZ7
IntActiQ96FZ7, 13 interactors
MINTiQ96FZ7
STRINGi9606.ENSP00000317468

Structurei

Secondary structure

1201
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 43Combined sources29

3D structure databases

ProteinModelPortaliQ96FZ7
SMRiQ96FZ7
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96FZ7

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni170 – 181Interaction with VPS4AAdd BLAST12

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili10 – 145Sequence analysisAdd BLAST136

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi168 – 179Type-2 MIT-interacting motifAdd BLAST12

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

eggNOGiKOG2910 Eukaryota
ENOG4111HN3 LUCA
GeneTreeiENSGT00720000108863
HOGENOMiHOG000208642
HOVERGENiHBG080510
InParanoidiQ96FZ7
KOiK12195
OMAiYQKRITQ
PhylomeDBiQ96FZ7
TreeFamiTF105929

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

Q96FZ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNLFGRKKQ SRVTEQDKAI LQLKQQRDKL RQYQKRIAQQ LERERALARQ
60 70 80 90 100
LLRDGRKERA KLLLKKKRYQ EQLLDRTENQ ISSLEAMVQS IEFTQIEMKV
110 120 130 140 150
MEGLQFGNEC LNKMHQVMSI EEVERILDET QEAVEYQRQI DELLAGSFTQ
160 170 180 190 200
EDEDAILEEL SAITQEQIEL PEVPSEPLPE KIPENVPVKA RPRQAELVAA

S
Length:201
Mass (Da):23,485
Last modified:January 23, 2007 - v3
Checksum:i0D490C4DE047DC02
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17D → G in BAD96907 (Ref. 4) Curated1
Sequence conflicti106F → L in BAB13901 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06180755G → S. Corresponds to variant dbSNP:rs61037507Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY329087 mRNA Translation: AAQ91196.1
AK021811 mRNA Translation: BAB13901.1
CR457284 mRNA Translation: CAG33565.1
AK223187 mRNA Translation: BAD96907.1
AK292105 mRNA Translation: BAF84794.1
BC010108 mRNA Translation: AAH10108.1
CCDSiCCDS11774.1
RefSeqiNP_078867.2, NM_024591.4
UniGeneiHs.514560

Genome annotation databases

EnsembliENST00000325167; ENSP00000317468; ENSG00000176108
GeneIDi79643
KEGGihsa:79643
UCSCiuc002jyw.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCHMP6_HUMAN
AccessioniPrimary (citable) accession number: Q96FZ7
Secondary accession number(s): A8K7U0, Q53FU4, Q9HAE8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 145 of the entry and version 3 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 17
    Human chromosome 17: 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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