CBX1

Protein-coding gene in the species Homo sapiens
CBX1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3Q6S, 2FMM, 3F2U

Identifiers
AliasesCBX1, CBX, HP1-BETA, HP1Hs-beta, HP1Hsbeta, M31, MOD1, p25beta, chromobox 1
External IDsOMIM: 604511; MGI: 105369; HomoloGene: 89116; GeneCards: CBX1; OMA:CBX1 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for CBX1
Genomic location for CBX1
Band17q21.32Start48,070,052 bp[1]
End48,101,478 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for CBX1
Genomic location for CBX1
Band11 D|11 60.11 cMStart96,679,953 bp[2]
End96,699,466 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ganglionic eminence

  • ventricular zone

  • secondary oocyte

  • tendon of biceps brachii

  • internal globus pallidus

  • C1 segment

  • endothelial cell

  • optic nerve

  • amniotic fluid

  • amygdala
Top expressed in
  • otic placode

  • saccule

  • Gonadal ridge

  • genital tubercle

  • mandibular prominence

  • tail of embryo

  • abdominal wall

  • maxillary prominence

  • otic vesicle

  • vas deferens
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • histone methyltransferase binding
  • enzyme binding
  • chromatin binding
  • protein binding
  • protein homodimerization activity
  • identical protein binding
Cellular component
  • chromocenter
  • pericentric heterochromatin
  • chromatin
  • spindle
  • chromosome, centromeric region
  • male pronucleus
  • female pronucleus
  • nucleoplasm
  • nucleus
  • site of DNA damage
Biological process
  • negative regulation of transcription, DNA-templated
  • cellular response to DNA damage stimulus
Sources:Amigo / QuickGO
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: 96.68 – 96.7 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]

Interactions

CBX1 has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000108468 – Ensembl, May 2017
  2. ^ a b c 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. S2CID 33460511.
  6. ^ a b "Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )".
  7. ^ 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. S2CID 18911371.
  8. ^ a b 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. hdl:10261/308369. PMID 11336697.
  9. ^ 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. doi:10.1182/blood.V91.4.1216. 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. S2CID 12381860.
  • 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. S2CID 4331863.
  • 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. S2CID 4334447.
  • 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. hdl:10261/308369. 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. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
  • 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. S2CID 36130549.
  • 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. Bibcode:2002Natur.416..103N. doi:10.1038/nature722. PMID 11882902. S2CID 4423019.
  • 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. Bibcode:2002PNAS...99.5919V. 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. S2CID 26016943.
  • 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. S2CID 16851984.
  • 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. Bibcode:2003Sci...299..719F. doi:10.1126/science.1078694. PMID 12560554. S2CID 26661977.

External links

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

  • v
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  • 1ap0: STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM MOUSE MODIFIER PROTEIN 1, NMR, 26 STRUCTURES
    1ap0: STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM MOUSE MODIFIER PROTEIN 1, NMR, 26 STRUCTURES
  • 1guw: STRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1BETA IN COMPLEX WITH THE LYSINE 9-METHYL HISTONE H3 N-TERMINAL PEPTIDE, NMR, 25 STRUCTURES
    1guw: STRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1BETA IN COMPLEX WITH THE LYSINE 9-METHYL HISTONE H3 N-TERMINAL PEPTIDE, NMR, 25 STRUCTURES
  • 1s4z: HP1 chromo shadow domain in complex with PXVXL motif of CAF-1
    1s4z: HP1 chromo shadow domain in complex with PXVXL motif of CAF-1
  • 2fmm: Crystal Structure of EMSY-HP1 complex
    2fmm: Crystal Structure of EMSY-HP1 complex
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(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies