CHMP1A

CHMP1A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2JQ9, 2YMB, 4A5X
Identifiers
Aliases	CHMP1A, CHMP1, PCH8, PCOLN3, PRSM1, VPS46-1, VPS46A, charged multivesicular body protein 1A
External IDs	OMIM: 164010; MGI: 1920159; HomoloGene: 56240; GeneCards: CHMP1A; OMA:CHMP1A - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16q24.3 Start 89,640,816 bp End 89,657,738 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 E1 Start 123,931,003 bp End 123,939,502 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon left testis right testis granulocyte right uterine tube skin of leg skin of abdomen body of stomach right frontal lobe cingulate gyrus Top expressed in lip granulocyte esophagus transitional epithelium of urinary bladder right kidney interventricular septum stroma of bone marrow duodenum dentate gyrus of hippocampal formation granule cell intestinal villus More reference expression data BioGPS n/a
Gene ontology Molecular function protein homodimerization activity protein domain specific binding zinc ion binding protein binding identical protein binding metallopeptidase activity Cellular component cytoplasm endosome membrane microtubule organizing center condensed nuclear chromosome early endosome endosome membrane extracellular exosome endomembrane system nucleus nuclear matrix ESCRT III complex multivesicular body Biological process carbon catabolite repression of transcription by glucose regulation of centrosome duplication regulation of transcription, DNA-templated viral budding via host ESCRT complex nucleus organization multivesicular body assembly regulation of mitotic spindle assembly transcription, DNA-templated cell division protein transport cell cycle septum digestion after cytokinesis mitotic metaphase plate congression negative regulation of transcription, DNA-templated vacuolar transport ESCRT III complex disassembly proteolysis mitotic chromosome condensation vesicle-mediated transport transport endosome transport via multivesicular body sorting pathway late endosome to vacuole transport negative regulation of cell cycle midbody abscission Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5119 234852 Ensembl ENSG00000131165 ENSMUSG00000000743 UniProt Q9HD42 Q921W0 RefSeq (mRNA) NM_001083314 NM_002768 NM_145606 RefSeq (protein) NP_001076783 NP_002759 NP_663581 Location (UCSC) Chr 16: 89.64 – 89.66 Mb Chr 8: 123.93 – 123.94 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Charged multivesicular body protein 1a is a protein that in humans is encoded by the CHMP1A gene.

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.

Interactions

CHMP1A has been shown to interact with VPS4A.

External links

• Human CHMP1A genome location and CHMP1A gene details page in the UCSC Genome Browser.

Further reading

• Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, et al. (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, et al. (September 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 (December 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 (December 2002). "Physical interaction between hepatitis C virus NS4B protein and CREB-RP/ATF6beta" (PDF). Biochemical and Biophysical Research Communications. 299 (3): 366–72. doi:10.1016/S0006-291X(02)02638-4. PMID 12445808. Archived from the original (PDF) on 2020-07-12. Retrieved 2020-07-12.
• Strack B, Calistri A, Craig S, Popova E, Göttlinger HG (September 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, Ward DM, Chung HY, Morita E, et al. (September 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, Bieniasz PD, Yaravoy A (October 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. Bibcode:2003PNAS..10012414M. doi:10.1073/pnas.2133846100. PMC 218772. PMID 14519844.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (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, et al. (October 2007). "The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation" (PDF). The Journal of Biological Chemistry. 282 (42): 30929–37. doi:10.1074/jbc.M704009200. PMID 17711858. S2CID 28086824.