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Reviewed, UniProtKB/Swiss-Prot Q9NZZ3 (CHMP5_HUMAN)

Last modified July 7, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Charged multivesicular body protein 5
Alternative name(s):
    Chromatin-modifying protein 5
    Vacuolar protein-sorting-associated protein 60
      Short name=Vps60
      Short name=hVps60
    SNF7 domain-containing protein 2
Gene names
Name: CHMP5
Synonyms: C9orf83, SNF7DC2
ORF Names: CGI-34, HSPC177, PNAS-2, PNAS-114
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Probable peripherally associated 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. Involved in HIV-1 p6- and p9-dependent virus release. Ref.6

Subunit structure

Probable peripherally associated 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 VTA1. Interacts with CHMP2A. Interacts with VTA1; the interaction involves soluble CHMP5. Ref.6 Ref.8 Ref.10

Subcellular location

Cytoplasmcytosol. Endosome membrane; Peripheral membrane protein Probable. Note: Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body.

Sequence similarities

Belongs to the SNF7 family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Endosome
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CAMK2AQ9UQM71EBI-751303,EBI-1383687
STAMBPO956301EBI-751303,EBI-396676

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 219219Charged multivesicular body protein 5
PRO_0000211500

Regions

Region121 – 15838Interaction with VTA1
Coiled coil26 – 179154 Potential

Amino acid modifications

Modified residue2191Phosphoserine Ref.11

Natural variations

Natural variant861S → P: dbSNP rs11540558.
VAR_052029

Experimental info

Sequence conflict141P → R in AAD27743. Ref.1
Sequence conflict191D → G in AAH16698. Ref.4
Sequence conflict84 – 9310QQSFNMEQAN → NSHSTWTGH in AAD27743. Ref.1
Sequence conflict1221Q → P in AAD27743. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NZZ3-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C99695F66FD7E126

FASTA21924,571
        10         20         30         40         50         60 
MNRLFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK KMREGPAKNM 

        70         80         90        100        110        120 
VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK DTKTTVDAMK LGVKEMKKAY 

       130        140        150        160        170        180 
KQVKIDQIED LQDQLEDMME DANEIQEALS RSYGTPELDE DDLEAELDAL GDELLADEDS 

       190        200        210 
SYLDEAASAP AIPEGVPTDT KNKDGVLVDE FGLPQIPAS 

« Hide

References

« Hide 'large scale' references
[1]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed: 10810093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow, Brain, Kidney and Urinary bladder.
[5]"Human acute promyelocytic leukemia cell line NB4's apoptosis related genes."
Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-219.
Tissue: Promyelocytic leukemia.
[6]"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: 14519844] [Abstract]
Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP2A.
[7]Erratum
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
[8]"The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells."
Ward D.M., Vaughn M.B., Shiflett S.L., White P.L., Pollock A.L., Hill J., Schnegelberger R., Sundquist W.I., Kaplan J.
J. Biol. Chem. 280:10548-10555(2005) [PubMed: 15644320] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VTA1.
[9]"Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
EMBO J. 26:4215-4227(2007) [PubMed: 17853893] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation."
Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G., Kirchhausen T.
J. Biol. Chem. 282:9805-9812(2007) [PubMed: 17261583] [Abstract]
Cited for: INTERACTION WITH VTA1, MASS SPECTROMETRY.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, MASS SPECTROMETRY.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

AF132968 mRNA. Translation: AAD27743.1.
AF161525 mRNA. Translation: AAF29140.1.
AL356472 Genomic DNA. Translation: CAH72744.1.
BC006974 mRNA. Translation: AAH06974.1.
BC007457 mRNA. Translation: AAH07457.1.
BC016698 mRNA. Translation: AAH16698.1.
BC020796 mRNA. Translation: AAH20796.1.
BC021168 mRNA. Translation: AAH21168.1.
AF275810 mRNA. Translation: AAG23821.1. Different initiation.
AF229832 mRNA. Translation: AAF42917.1.
IPIIPI00100796.
RefSeqNP_057494.3.
UniGeneHs.635313

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9NZZ3. 3 interactions.

PTM databases

PhosphoSiteQ9NZZ3.

Proteomic databases

PeptideAtlasQ9NZZ3.
PRIDEQ9NZZ3.

Genome annotation databases

EnsemblENSG00000086065. Homo sapiens. [Contig view]
GeneID51510.
KEGGhsa:51510.
UCSCuc003zsl.2. human.

Organism-specific databases

GeneCardsGC09P033257.
H-InvDBHIX0007979.
HGNCHGNC:26942. CHMP5.
MIM610900. gene.
PharmGKBPA134903143.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9NZZ3.
HOVERGENQ9NZZ3.
OMAQ9NZZ3. QADEVQE.

Gene expression databases

ArrayExpressQ9NZZ3.
BgeeQ9NZZ3.
CleanExHS_CHMP5.
GermOnlineENSG00000086065. Homo sapiens.

Family and domain databases

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

Other Resources

NextBio55198.
SOURCESearch...

Entry information

Entry nameCHMP5_HUMAN
AccessionPrimary (citable) accession number: Q9NZZ3
Secondary accession number(s): Q5VXW2 expand/collapse secondary AC list , Q96AV2, Q9HB68, Q9NYS4, Q9Y323
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: October 1, 2000
Last modified: July 7, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents