CHMP1B

Charged multivesicular body protein 1b is a protein that in humans is encoded by the CHMP1B gene.^[5][6]

CHMP1B
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3EAB, 4TXQ, 4TXR, 3JC1
Identifiers
Aliases	CHMP1B, C10orf2, C18-ORF2, C18orf2, CHMP1.5, Vps46-2, Vps46B, hVps46-2, charged multivesicular body protein 1B
External IDs	OMIM: 606486; MGI: 1914314; HomoloGene: 41374; GeneCards: CHMP1B; OMA:CHMP1B - orthologs
Gene location (Human) Chr. Chromosome 18 (human)[1] Band 18p11.21 Start 11,851,413 bp[1] End 11,854,444 bp[1]
Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18|18 E1 Start 67,338,437 bp[2] End 67,340,960 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle beta cell tibialis anterior muscle muscle of thigh glutes mucosa of sigmoid colon popliteal artery tibial arteries biceps brachii monocyte Top expressed in transitional epithelium of urinary bladder left colon conjunctival fornix decidua medial ganglionic eminence blood granulocyte thymus duodenum jejunum More reference expression data BioGPS n/a
Gene ontology Molecular function protein domain specific binding protein binding identical protein binding Cellular component cytoplasm ESCRT III complex cytosol endosome late endosome membrane membrane membrane coat endosome membrane extracellular exosome nucleus midbody multivesicular body Biological process regulation of centrosome duplication nucleus organization establishment of protein localization multivesicular body assembly regulation of mitotic spindle assembly cell division protein transport cell cycle septum digestion after cytokinesis mitotic metaphase plate congression vacuolar transport ESCRT III complex disassembly transport viral budding via host ESCRT complex endosome transport via multivesicular body sorting pathway late endosome to vacuole transport midbody abscission Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 57132 67064 Ensembl ENSG00000255112 ENSMUSG00000109901 UniProt Q7LBR1 Q99LU0 RefSeq (mRNA) NM_020412 NM_024190 RefSeq (protein) NP_065145 NP_077152 Location (UCSC) Chr 18: 11.85 – 11.85 Mb Chr 18: 67.34 – 67.34 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000255112 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000109901 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Reid E, Connell J, Edwards TL, Duley S, Brown SE, Sanderson CM (Dec 2004). "The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B". Hum Mol Genet. 14 (1): 19–38. doi:10.1093/hmg/ddi003. PMID 15537668.
6. "Entrez Gene: CHMP1B chromatin modifying protein 1B".

External links

• Human C10orf2 genome location and C10orf2 gene details page in the UCSC Genome Browser.
• Human CHMP1B genome location and CHMP1B gene details page in the UCSC Genome Browser.
• Overview of all the structural information available in the PDB for UniProt: Q7LBR1 (Charged multivesicular body protein 1b) at the PDBe-KB.

Further reading

• Vuoristo JT, Berrettini WH, Ala-Kokko L (2001). "C18orf2, a novel, highly conserved intronless gene within intron 5 of the GNAL gene on chromosome 18p11". Cytogenet. Cell Genet. 93 (1–2): 19–22. doi:10.1159/000056940. PMID 11474171. S2CID 42139322.
• Stauffer DR, Howard TL, Nyun T, Hollenberg SM (2002). "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression". J. Cell Sci. 114 (Pt 13): 2383–93. doi:10.1242/jcs.114.13.2383. PMID 11559747.
• Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (2002). "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.
• 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.
• 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.
• Scott A, Gaspar J, Stuchell-Brereton MD, et al. (2005). "Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A". Proc. Natl. Acad. Sci. U.S.A. 102 (39): 13813–8. Bibcode:2005PNAS..10213813S. doi:10.1073/pnas.0502165102. PMC 1236530. PMID 16174732.
• Tsang HT, Connell JW, Brown SE, et al. (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.
• Row PE, Liu H, Hayes S, et al. (2007). "The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation" (PDF). J. Biol. Chem. 282 (42): 30929–37. doi:10.1074/jbc.M704009200. PMID 17711858.