CBX1

Chromobox homolog 1
PDB rendering based on 1ap0.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2FMM​, 3F2U​, 3Q6S​
Identifiers
Symbols	CBX1 ; CBX; HP1-BETA; HP1Hs-beta; HP1Hsbeta; M31; MOD1; p25beta
External IDs	OMIM: 604511 MGI: 105369 HomoloGene: 89116 ChEMBL: 1741193 GeneCards: CBX1 Gene
Gene ontology Molecular function • chromatin binding • protein binding • enzyme binding • protein homodimerization activity • histone methyltransferase binding Cellular component • chromosome, centromeric region • chromatin • female pronucleus • male pronucleus • nucleoplasm • nuclear heterochromatin • pericentric heterochromatin • spindle • chromocenter Biological process • negative regulation of transcription, DNA-templated Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10951	12412
Ensembl	ENSG00000108468	ENSMUSG00000018666
UniProt	P83916	P83917
RefSeq (mRNA)	NM_001127228	NM_007622
RefSeq (protein)	NP_001120700	NP_031648
Location (UCSC)	Chr 17: 48.07 – 48.1 Mb	Chr 11: 96.79 – 96.81 Mb
PubMed search

Chromobox protein homolog 1 is a protein that in humans is encoded by the CBX1 gene.^[1][2]

Function

The protein is localized at heterochromatin sites, where it mediates gene silencing.^[2]

Model organisms

Cbx1 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Abnormal[3]
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Eye Histopathology	Normal
All tests and analysis from[4][5]

Model organisms have been used in the study of CBX1 function. A conditional knockout mouse line, called Cbx1^{tm1a(EUCOMM)Wtsi[6][7]} 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.^[8][9][10]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[4][11] 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.^[4]

Interactions

CBX1 has been shown to interact with:

• C11orf30,^[12]
• CBX3^[13] and
• CBX5,^[13] and
• SUV39H1.^[14]

See also

• Heterochromatin protein 1

References

1. 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.
2. "Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )".
3. "Indirect calorimetry data for Cbx1". Wellcome Trust Sanger Institute.
4. 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.
5. Mouse Resources Portal, Wellcome Trust Sanger Institute.
6. "International Knockout Mouse Consortium".
7. "Mouse Genome Informatics".
8. 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.
9. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
10. 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.
11. 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.
12. 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.
13. 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.
14. 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.

External links

• CBX1 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

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