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Q96FZ7 (CHMP6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CHMP6
Synonyms:VPS20
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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 VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with CHMP4A, CHMP4B and CHMP4C. Interacts with SNF8, VPS25 and VPS36. Ref.6 Ref.7 Ref.9 Ref.10 Ref.12

Subcellular location

Endomembrane system. Endosome membrane; Lipid-anchor. Late endosome membrane Probable. Note: Localizes to endosomal membranes. Ref.1 Ref.9

Tissue specificity

Ubiquitously expressed. Ref.9

Domain

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.

Post-translational modification

ISGylated in a CHMP5-dependent manner. Isgylation weakens its interaction with VPS4A. Ref.12

Sequence similarities

Belongs to the SNF7 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 201200Charged multivesicular body protein 6
PRO_0000211508

Regions

Region170 – 18112Interaction with VPS4A
Coiled coil10 – 145136 Potential
Motif168 – 17912Type-2 MIT-interacting motif

Amino acid modifications

Lipidation21N-myristoyl glycine Probable

Natural variations

Natural variant551G → S.
Corresponds to variant rs61037507 [ dbSNP | Ensembl ].
VAR_061807

Experimental info

Mutagenesis21G → A: Abolishes myristoylation. Ref.9
Mutagenesis491R → E: Does not affect the subcellular location. Ref.9
Mutagenesis168 – 20134Missing: Membrane association; releases autoinhibition. Ref.10
Mutagenesis1701L → D: Abolishes interaction with VPS4A. Ref.13
Mutagenesis1731V → D: Abolishes interaction with VPS4A. Ref.13
Mutagenesis1781L → D: Reduces interaction with VPS4A. Ref.13
Sequence conflict171D → G in BAD96907. Ref.4
Sequence conflict1061F → L in BAB13901. Ref.2

Secondary structure

... 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96FZ7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0D490C4DE047DC02

FASTA20123,485
        10         20         30         40         50         60 
MGNLFGRKKQ SRVTEQDKAI LQLKQQRDKL RQYQKRIAQQ LERERALARQ LLRDGRKERA 

        70         80         90        100        110        120 
KLLLKKKRYQ EQLLDRTENQ ISSLEAMVQS IEFTQIEMKV MEGLQFGNEC LNKMHQVMSI 

       130        140        150        160        170        180 
EEVERILDET QEAVEYQRQI DELLAGSFTQ EDEDAILEEL SAITQEQIEL PEVPSEPLPE 

       190        200 
KIPENVPVKA RPRQAELVAA S 

« Hide

References

« Hide 'large scale' references
[1]"Structure and function of human Vps20 and Snf7 proteins."
Peck J.W., Bowden E.T., Burbelo P.D.
Biochem. J. 377:693-700(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo and Synovial cell.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney proximal tubule.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[6]"The protein network of HIV budding."
von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y., Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A., Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.
Cell 114:701-713(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VPS25; CHMP4B; VPS4A AND VPS4B.
[7]"Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHMP4A; CHMP4B; CHMP4C; VPS25; SNF8 AND VPS36.
[8]Erratum
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
[9]"Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting."
Yorikawa C., Shibata H., Waguri S., Hatta K., Horii M., Katoh K., Kobayashi T., Uchiyama Y., Maki M.
Biochem. J. 387:17-26(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-2, INTERACTION WITH CHMP4B AND VPS25, MUTAGENESIS OF GLY-2 AND ARG-49.
[10]"Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain."
Shim S., Kimpler L.A., Hanson P.I.
Traffic 8:1068-1079(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOINHIBITORY MECHANISM, INTERACTION, MUTAGENESIS OF 168-ILE--SER-201.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15."
Kuang Z., Seo E.J., Leis J.
J. Virol. 85:7153-7161(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION, INTERACTION WITH VPS4A.
[13]"Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding."
Kieffer C., Skalicky J.J., Morita E., De Domenico I., Ward D.M., Kaplan J., Sundquist W.I.
Dev. Cell 15:62-73(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 168-179 IN COMPLEX WITH VPS4A, MUTAGENESIS OF LEU-170; VAL-173 AND LEU-178.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11774.1.
RefSeqNP_078867.2. NM_024591.4.
UniGeneHs.514560.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K3WNMR-B166-181[»]
3HTUX-ray2.00B/D/F/H11-48[»]
ProteinModelPortalQ96FZ7.
SMRQ96FZ7. Positions 17-92, 118-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122771. 9 interactions.
IntActQ96FZ7. 3 interactions.
MINTMINT-5003442.
STRING9606.ENSP00000317468.

PTM databases

PhosphoSiteQ96FZ7.

Polymorphism databases

DMDM73917777.

Proteomic databases

MaxQBQ96FZ7.
PaxDbQ96FZ7.
PRIDEQ96FZ7.

Protocols and materials databases

DNASU79643.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325167; ENSP00000317468; ENSG00000176108.
GeneID79643.
KEGGhsa:79643.
UCSCuc002jyw.4. human.

Organism-specific databases

CTD79643.
GeneCardsGC17P078965.
HGNCHGNC:25675. CHMP6.
HPAHPA023001.
HPA024460.
MIM610901. gene.
neXtProtNX_Q96FZ7.
PharmGKBPA142672114.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291677.
HOGENOMHOG000208642.
HOVERGENHBG080510.
InParanoidQ96FZ7.
KOK12195.
OMAECLARDD.
PhylomeDBQ96FZ7.
TreeFamTF105929.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ96FZ7.
BgeeQ96FZ7.
CleanExHS_CHMP6.
GenevestigatorQ96FZ7.

Family and domain databases

InterProIPR005024. Snf7.
[Graphical view]
PfamPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ96FZ7.
GeneWikiCHMP6.
GenomeRNAi79643.
NextBio68773.
PROQ96FZ7.
SOURCESearch...

Entry information

Entry nameCHMP6_HUMAN
AccessionPrimary (citable) accession number: Q96FZ7
Secondary accession number(s): A8K7U0, Q53FU4, Q9HAE8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM