CHMP5

Protein-coding gene in the species Homo sapiens
CHMP5
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2LXM, 3ULY, 3UM0, 3UM1, 3UM2, 4TXR

Identifiers
AliasesCHMP5, C9orf83, HSPC177, PNAS-2, SNF7DC2, Vps60, CGI-34, charged multivesicular body protein 5
External IDsOMIM: 610900; MGI: 1924209; HomoloGene: 5757; GeneCards: CHMP5; OMA:CHMP5 - orthologs
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[1]
Chromosome 4 (mouse)
Genomic location for CHMP5
Genomic location for CHMP5
Band4|4 A5Start40,948,407 bp[1]
End40,965,303 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • germinal epithelium

  • palpebral conjunctiva

  • amniotic fluid

  • visceral pleura

  • sperm

  • parietal pleura

  • bronchial epithelial cell

  • endothelial cell

  • jejunal mucosa

  • glomerulus
Top expressed in
  • transitional epithelium of urinary bladder

  • right lung lobe

  • vestibular membrane of cochlear duct

  • pineal gland

  • superior cervical ganglion

  • facial motor nucleus

  • medial ganglionic eminence

  • conjunctival fornix

  • anterior horn of spinal cord

  • gastric mucosa
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein binding
  • cadherin binding
Cellular component
  • cytoplasm
  • cytosol
  • endosome
  • membrane
  • endosome membrane
  • extracellular exosome
  • nucleus
Biological process
  • regulation of centrosome duplication
  • viral life cycle
  • nucleus organization
  • multivesicular body sorting pathway
  • endosome to lysosome transport
  • multivesicular body assembly
  • regulation of mitotic spindle assembly
  • endosomal transport
  • protein transport
  • septum digestion after cytokinesis
  • mitotic metaphase plate congression
  • regulation of receptor recycling
  • lysosome organization
  • vacuolar transport
  • ESCRT III complex disassembly
  • transport
  • midbody abscission
  • cellular response to lipopolysaccharide
  • cellular response to muramyl dipeptide
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51510

76959

Ensembl

n/a

ENSMUSG00000028419

UniProt

Q9NZZ3

Q9D7S9

RefSeq (mRNA)

NM_016410
NM_001195536

NM_029814

RefSeq (protein)

NP_001182465
NP_057494

NP_084090

Location (UCSC)n/aChr 4: 40.95 – 40.97 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Charged multivesicular body protein 5 is a protein that in humans is encoded by the CHMP5 gene.[4][5][6]

Function

CHMP5 belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A, is required for both MVB formation and regulation of cell cycle progression.[6][7]

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028419 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Ward DM, Vaughn MB, Shiflett SL, White PL, Pollock AL, Hill J, Schnegelberger R, Sundquist WI, Kaplan J (Mar 2005). "The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells". J Biol Chem. 280 (11): 10548–55. doi:10.1074/jbc.M413734200. PMID 15644320.
  5. ^ Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (Sep 2001). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". J Cell Sci. 114 (Pt 13): 2395–404. doi:10.1242/jcs.114.13.2395. PMID 11559748.
  6. ^ a b "Entrez Gene: CHMP5 chromatin modifying protein 5".
  7. ^ Tsang HT, Connell JW, Brown SE, Thompson A, Reid E, Sanderson CM (September 2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics. 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.

Further reading

  • Lai CH, Chou CY, Ch'ang LY, et al. (2000). "Identification of Novel Human Genes Evolutionarily Conserved in Caenorhabditis elegans by Comparative Proteomics". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
  • Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Strack B, Calistri A, Craig S, et al. (2003). "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding". Cell. 114 (6): 689–99. doi:10.1016/S0092-8674(03)00653-6. PMID 14505569. S2CID 10733770.
  • von Schwedler UK, Stuchell M, Müller B, et al. (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570. S2CID 16894972.
  • Martin-Serrano J, Yarovoy A, Perez-Caballero D, et al. (2003). "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins". Proc. Natl. Acad. Sci. U.S.A. 100 (21): 12414–9. Bibcode:2003PNAS..10012414M. doi:10.1073/pnas.2133846100. PMC 218772. PMID 14519844.
  • Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. Bibcode:2004Natur.429..369H. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


  • v
  • t
  • e