CHMP1A

Charged multivesicular body protein 1A
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2JQ9​, 2YMB​, 4A5X​
Identifiers
Symbols	CHMP1A ; CHMP1; PCH8; PCOLN3; PRSM1; VPS46-1; VPS46A
External IDs	OMIM: 164010 HomoloGene: 56240 GeneCards: CHMP1A Gene
Gene ontology Molecular function • protein binding • metallopeptidase activity • zinc ion binding • protein domain specific binding • protein homodimerization activity Cellular component • condensed nuclear chromosome • ESCRT III complex • early endosome • microtubule organizing center • endomembrane system • nuclear matrix • extracellular exosome Biological process • cell separation after cytokinesis • transcription, DNA-templated • proteolysis • nucleus organization • vacuolar transport • mitotic chromosome condensation • mitotic metaphase plate congression • regulation of centrosome duplication • protein transport • vesicle-mediated transport • gene silencing • negative regulation of transcription by glucose • negative regulation of transcription, DNA-templated • cell division • regulation of mitotic spindle assembly Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5119	234852
Ensembl	ENSG00000131165	ENSMUSG00000000743
UniProt	Q9HD42	Q921W0
RefSeq (mRNA)	NM_001083314	NM_145606
RefSeq (protein)	NP_001076783	NP_663581
Location (UCSC)	Chr 16: 89.64 – 89.66 Mb	Chr 8: 123.2 – 123.21 Mb
PubMed search

Charged multivesicular body protein 1a is a protein that in humans is encoded by the CHMP1A gene.^[1][2][3]

Function

This gene encodes a member of the CHMP/Chmp family of proteins which are involved in multivesicular body sorting of proteins to the interiors of lysosomes. The initial prediction of the protein sequence encoded by this gene suggested that the encoded protein was a metallopeptidase. The nomenclature has been updated recently to reflect the correct biological function of this encoded protein.^[3]

Interactions

CHMP1A has been shown to interact with VPS4A.^[1]

References

1. Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (Jul 2001). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". Journal of Cell Science 114 (Pt 13): 2395–404. PMID 11559748.
2. Stauffer DR, Howard TL, Nyun T, Hollenberg SM (Jul 2001). "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression". Journal of Cell Science 114 (Pt 13): 2383–93. PMID 11559747.
3. "Entrez Gene: PCOLN3 procollagen (type III) N-endopeptidase".

Further reading

• Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S (1995). "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research 1 (5): 223–9. doi:10.1093/dnares/1.5.223. PMID 7584044.
• Scott IC, Halila R, Jenkins JM, Mehan S, Apostolou S, Winqvist R, Callen DF, Prockop DJ, Peltonen L, Kadler KE (Sep 1996). "Molecular cloning, expression and chromosomal localization of a human gene encoding a 33 kDa putative metallopeptidase (PRSM1)". Gene 174 (1): 135–43. doi:10.1016/0378-1119(96)00510-0. PMID 8863740.
• Yoshida H, Haze K, Yanagi H, Yura T, Mori K (Dec 1998). "Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors". The Journal of Biological Chemistry 273 (50): 33741–9. doi:10.1074/jbc.273.50.33741. PMID 9837962.
• Tong WY, Nagano-Fujii M, Hidajat R, Deng L, Takigawa Y, Hotta H (Dec 2002). "Physical interaction between hepatitis C virus NS4B protein and CREB-RP/ATF6beta". Biochemical and Biophysical Research Communications 299 (3): 366–72. doi:10.1016/S0006-291X(02)02638-4. PMID 12445808.
• Strack B, Calistri A, Craig S, Popova E, Göttlinger HG (Sep 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.
• von Schwedler UK, Stuchell M, Müller B, Ward DM, Chung HY, Morita E, Wang HE, Davis T, He GP, Cimbora DM, Scott A, Kräusslich HG, Kaplan J, Morham SG, Sundquist WI (Sep 2003). "The protein network of HIV budding". Cell 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570.
• Martin-Serrano J, Yarovoy A, Perez-Caballero D, Bieniasz PD, Yaravoy A (Oct 2003). "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins". Proceedings of the National Academy of Sciences of the United States of America 100 (21): 12414–9. doi:10.1073/pnas.2133846100. PMC 218772. PMID 14519844.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Row PE, Liu H, Hayes S, Welchman R, Charalabous P, Hofmann K, Clague MJ, Sanderson CM, Urbé S (Oct 2007). "The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation". The Journal of Biological Chemistry 282 (42): 30929–37. doi:10.1074/jbc.M704009200. PMID 17711858.