CBX1

CBX1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCBX1, CBX, HP1-BETA, HP1Hs-beta, HP1Hsbeta, M31, MOD1, p25beta, chromobox 1
External IDsOMIM: 604511 MGI: 105369 HomoloGene: 89116 GeneCards: CBX1
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17q21.32Start48,070,052 bp[1]
End48,101,521 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

10951

12412

Ensembl

ENSG00000108468

ENSMUSG00000018666

UniProt

P83916

P83917

RefSeq (mRNA)

NM_006807
NM_001127228

NM_007622
NM_001362560
NM_001362561
NM_001362563
NM_001362564

RefSeq (protein)

NP_001120700
NP_006798

NP_031648
NP_001349489
NP_001349490
NP_001349492
NP_001349493

Location (UCSC)Chr 17: 48.07 – 48.1 MbChr 11: 96.79 – 96.81 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Chromobox protein homolog 1 is a protein that in humans is encoded by the CBX1 gene.[5][6]

Function

The protein is localized at heterochromatin sites, where it mediates gene silencing.[6]

Model organisms

Model organisms have been used in the study of CBX1 function. A conditional knockout mouse line, called Cbx1tm1a(EUCOMM)Wtsi[10][11] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[12][13][14]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[8][15] Twenty two tests were carried out and two phenotypes were reported. No homozygous mutant animals survived until two weeks of age, therefore the remaining tests were carried out on heterozygous mutant mice. Male heterozygotes showed increased VO2, rate of elimination of carbon dioxide, and energy expenditure as determined by indirect calorimetry.[8]

Interactions

CBX1 has been shown to interact with:

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000108468 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000018666 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Furuta K, Chan EK, Kiyosawa K, Reimer G, Luderschmidt C, Tan EM (Jun 1997). "Heterochromatin protein HP1Hsbeta (p25beta) and its localization with centromeres in mitosis". Chromosoma. 106 (1): 11–9. doi:10.1007/s004120050219. PMID 9169582.
  6. 1 2 "Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )".
  7. ↑ "Indirect calorimetry data for Cbx1". Wellcome Trust Sanger Institute.
  8. 1 2 3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
  9. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  10. ↑ "International Knockout Mouse Consortium".
  11. ↑ "Mouse Genome Informatics".
  12. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  13. ↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  14. ↑ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  15. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  16. ↑ Hughes-Davies L, Huntsman D, Ruas M, Fuks F, Bye J, Chin SF, Milner J, Brown LA, Hsu F, Gilks B, Nielsen T, Schulzer M, Chia S, Ragaz J, Cahn A, Linger L, Ozdag H, Cattaneo E, Jordanova ES, Schuuring E, Yu DS, Venkitaraman A, Ponder B, Doherty A, Aparicio S, Bentley D, Theillet C, Ponting CP, Caldas C, Kouzarides T (Nov 2003). "EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer". Cell. 115 (5): 523–35. doi:10.1016/s0092-8674(03)00930-9. PMID 14651845.
  17. 1 2 Nielsen AL, Oulad-Abdelghani M, Ortiz JA, Remboutsika E, Chambon P, Losson R (Apr 2001). "Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins". Molecular Cell. 7 (4): 729–39. doi:10.1016/S1097-2765(01)00218-0. PMID 11336697.
  18. ↑ Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T (Apr 1999). "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31". The EMBO Journal. 18 (7): 1923–38. doi:10.1093/emboj/18.7.1923. PMC 1171278. PMID 10202156.

Further reading

  • Lessard J, Baban S, Sauvageau G (Feb 1998). "Stage-specific expression of polycomb group genes in human bone marrow cells". Blood. 91 (4): 1216–24. PMID 9454751.
  • Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T (Apr 1999). "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31". The EMBO Journal. 18 (7): 1923–38. doi:10.1093/emboj/18.7.1923. PMC 1171278. PMID 10202156.
  • Minc E, Allory Y, Worman HJ, Courvalin JC, Buendia B (Aug 1999). "Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells". Chromosoma. 108 (4): 220–34. doi:10.1007/s004120050372. PMID 10460410.
  • Murzina N, Verreault A, Laue E, Stillman B (Oct 1999). "Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins". Molecular Cell. 4 (4): 529–40. doi:10.1016/S1097-2765(00)80204-X. PMID 10549285.
  • Nielsen AL, Ortiz JA, You J, Oulad-Abdelghani M, Khechumian R, Gansmuller A, Chambon P, Losson R (Nov 1999). "Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family". The EMBO Journal. 18 (22): 6385–95. doi:10.1093/emboj/18.22.6385. PMC 1171701. PMID 10562550.
  • Brasher SV, Smith BO, Fogh RH, Nietlispach D, Thiru A, Nielsen PR, Broadhurst RW, Ball LJ, Murzina NV, Laue ED (Apr 2000). "The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer". The EMBO Journal. 19 (7): 1587–97. doi:10.1093/emboj/19.7.1587. PMC 310228. PMID 10747027.
  • Zhao T, Heyduk T, Allis CD, Eissenberg JC (Sep 2000). "Heterochromatin protein 1 binds to nucleosomes and DNA in vitro". The Journal of Biological Chemistry. 275 (36): 28332–8. doi:10.1074/jbc.M003493200. PMID 10882726.
  • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T (Mar 2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature. 410 (6824): 116–20. doi:10.1038/35065132. PMID 11242053.
  • Bannister AJ, Zegerman P, Partridge JF, Miska EA, Thomas JO, Allshire RC, Kouzarides T (Mar 2001). "Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain". Nature. 410 (6824): 120–4. doi:10.1038/35065138. PMID 11242054.
  • Nielsen AL, Oulad-Abdelghani M, Ortiz JA, Remboutsika E, Chambon P, Losson R (Apr 2001). "Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins". Molecular Cell. 7 (4): 729–39. doi:10.1016/S1097-2765(01)00218-0. PMID 11336697.
  • Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (Jan 2002). "Directed proteomic analysis of the human nucleolus". Current Biology. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
  • Scholzen T, Endl E, Wohlenberg C, van der Sar S, Cowell IG, Gerdes J, Singh PB (Feb 2002). "The Ki-67 protein interacts with members of the heterochromatin protein 1 (HP1) family: a potential role in the regulation of higher-order chromatin structure". The Journal of Pathology. 196 (2): 135–44. doi:10.1002/path.1016. PMID 11793364.
  • Nielsen PR, Nietlispach D, Mott HR, Callaghan J, Bannister A, Kouzarides T, Murzin AG, Murzina NV, Laue ED (Mar 2002). "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9". Nature. 416 (6876): 103–7. doi:10.1038/nature722. PMID 11882902.
  • Vassallo MF, Tanese N (Apr 2002). "Isoform-specific interaction of HP1 with human TAFII130". Proceedings of the National Academy of Sciences of the United States of America. 99 (9): 5919–24. doi:10.1073/pnas.092025499. PMC 122877. PMID 11959914.
  • Hwang KK, Worman HJ (May 2002). "Gene regulation by human orthologs of Drosophila heterochromatin protein 1". Biochemical and Biophysical Research Communications. 293 (4): 1217–22. doi:10.1016/S0006-291X(02)00377-7. PMID 12054505.
  • Bhattacharya N, Wang Z, Davitt C, McKenzie IF, Xing PX, Magnuson NS (Jul 2002). "Pim-1 associates with protein complexes necessary for mitosis". Chromosoma. 111 (2): 80–95. doi:10.1007/s00412-002-0192-6. PMID 12111331.
  • Lin CY, Li CC, Huang PH, Lee FJ (Dec 2002). "A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1". Journal of Cell Science. 115 (Pt 23): 4433–45. doi:10.1242/jcs.00123. PMID 12414990.
  • Festenstein R, Pagakis SN, Hiragami K, Lyon D, Verreault A, Sekkali B, Kioussis D (Jan 2003). "Modulation of heterochromatin protein 1 dynamics in primary Mammalian cells". Science. 299 (5607): 719–21. doi:10.1126/science.1078694. PMID 12560554.

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