CBX1

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

CBX1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3Q6S, 2FMM, 3F2U
Identifiers
Aliases	CBX1, CBX, HP1-BETA, HP1Hs-beta, HP1Hsbeta, M31, MOD1, p25beta, chromobox 1
External IDs	OMIM: 604511 MGI: 105369 HomoloGene: 89116 GeneCards: CBX1
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q21.32 Start 48,070,052 bp[1] End 48,101,478 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 D|11 60.11 cM Start 96,789,127 bp[2] End 96,808,640 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • histone methyltransferase binding • enzyme binding • chromatin binding • GO:0001948 protein binding • protein homodimerization activity • identical protein binding Cellular component • nuclear heterochromatin • chromocenter • pericentric heterochromatin • chromatin • spindle • chromosome, centromeric region • male pronucleus • female pronucleus • nuclear chromosome, telomeric region • nucleoplasm • cell nucleus • site of DNA damage Biological process • negative regulation of transcription, DNA-templated • cellular response to DNA damage stimulus Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
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 Mb	Chr 11: 96.79 – 96.81 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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

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[7]
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[8][9]

Model organisms have been used in the study of CBX1 function. A conditional knockout mouse line, called Cbx1^{tm1a(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:

• C11orf30,[16]
• CBX3[17] and
• CBX5,[17] and
• SUV39H1.[18]

See also

• Heterochromatin protein 1

References

1. GRCh38: Ensembl release 89: ENSG00000108468 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000018666 - 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. 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. "Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )".
7. "Indirect calorimetry data for Cbx1". Wellcome Trust Sanger Institute.
8. 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". Archived from the original on 2012-03-20. Retrieved 2012-01-05.
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. 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.

External links

• CBX1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
• Human CBX1 genome location and CBX1 gene details page in the UCSC Genome Browser.

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