CBX3

Protein-coding gene in the species Homo sapiens
CBX3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3TZD, 2L11, 3DM1, 3KUP

Identifiers
AliasesCBX3, HECH, HP1-GAMMA, HP1Hs-gamma, chromobox 3
External IDsOMIM: 604477; MGI: 108515; HomoloGene: 40583; GeneCards: CBX3; OMA:CBX3 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for CBX3
Genomic location for CBX3
Band7p15.2Start26,201,162 bp[1]
End26,213,607 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for CBX3
Genomic location for CBX3
Band6 B3|6 24.89 cMStart51,447,340 bp[2]
End51,460,684 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • ganglionic eminence

  • visceral pleura

  • ventricular zone

  • parietal pleura

  • germinal epithelium

  • tibia

  • epithelium of nasopharynx

  • trabecular bone

  • endometrium
Top expressed in
  • ventricular zone

  • genital tubercle

  • embryo

  • embryo

  • tail of embryo

  • morula

  • dentate gyrus of hippocampal formation granule cell

  • blastocyst

  • yolk sac

  • neural layer of retina
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein domain specific binding
  • histone methyltransferase binding
  • protein binding
  • identical protein binding
  • enzyme binding
Cellular component
  • nuclear envelope
  • spindle
  • nuclear inner membrane
  • chromatin
  • chromosome, centromeric region
  • nucleus
  • condensed chromosome, centromeric region
  • nucleoplasm
  • site of DNA damage
  • senescence-associated heterochromatin focus
Biological process
  • chromatin remodeling
  • regulation of transcription, DNA-templated
  • rhythmic process
  • transcription, DNA-templated
  • negative regulation of transcription, DNA-templated
  • negative regulation of G0 to G1 transition
  • chromatin organization
  • cellular response to DNA damage stimulus
  • cellular response to dexamethasone stimulus
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

11335

12417

Ensembl

ENSG00000122565

ENSMUSG00000029836

UniProt

Q13185

P23198

RefSeq (mRNA)

NM_007276
NM_016587

NM_001037798
NM_007624
NM_001355002

RefSeq (protein)

NP_009207
NP_057671

n/a

Location (UCSC)Chr 7: 26.2 – 26.21 MbChr 6: 51.45 – 51.46 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Chromobox protein homolog 3 is a protein that is encoded by the CBX3 gene in humans.[5][6]

At the nuclear envelope, the nuclear lamina and heterochromatin are adjacent to the inner nuclear membrane. The protein encoded by this gene binds DNA and is a component of heterochromatin. This protein also can bind lamin B receptor, an integral membrane protein found in the inner nuclear membrane. The dual binding functions of the encoded protein may explain the association of heterochromatin with the inner nuclear membrane. Two transcript variants encoding the same protein but differing in the 5' UTR, have been found for this gene.[6]

Interactions

CBX3 has been shown to interact with PIM1,[7] Ki-67,[8] Lamin B receptor,[9] CBX5[10] and CBX1.[10]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000122565 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029836 – 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. ^ Ye Q, Worman HJ (August 1996). "Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1". J Biol Chem. 271 (25): 14653–6. doi:10.1074/jbc.271.25.14653. PMID 8663349.
  6. ^ a b "Entrez Gene: CBX3 chromobox homolog 3 (HP1 gamma homolog, Drosophila)".
  7. ^ Koike N, Maita H, Taira T, Ariga H, Iguchi-Ariga S M (February 2000). "Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1(1)". FEBS Lett. 467 (1): 17–21. doi:10.1016/S0014-5793(00)01105-4. ISSN 0014-5793. PMID 10664448. S2CID 29392124.
  8. ^ Kametaka A, Takagi Masatoshi, Hayakawa Tomohiro, Haraguchi Tokuko, Hiraoka Yasushi, Yoneda Yoshihiro (December 2002). "Interaction of the chromatin compaction-inducing domain (LR domain) of Ki-67 antigen with HP1 proteins". Genes Cells. 7 (12): 1231–42. doi:10.1046/j.1365-2443.2002.00596.x. ISSN 1356-9597. PMID 12485163. S2CID 6802841.
  9. ^ Ye Q, Worman H J (June 1996). "Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1". J. Biol. Chem. 271 (25): 14653–6. doi:10.1074/jbc.271.25.14653. ISSN 0021-9258. PMID 8663349.
  10. ^ a b Nielsen AL, Oulad-Abdelghani M, Ortiz J A, Remboutsika E, Chambon P, Losson R (April 2001). "Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins". Mol. Cell. 7 (4): 729–39. doi:10.1016/S1097-2765(01)00218-0. hdl:10261/308369. ISSN 1097-2765. PMID 11336697.

Further reading

  • Ye Q, Callebaut I, Pezhman A, et al. (1997). "Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR". J. Biol. Chem. 272 (23): 14983–9. doi:10.1074/jbc.272.23.14983. PMID 9169472.
  • Lessard J, Baban S, Sauvageau G (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.
  • Seeler JS, Marchio A, Sitterlin D, et al. (1998). "Interaction of SP100 with HP1 proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment". Proc. Natl. Acad. Sci. U.S.A. 95 (13): 7316–21. Bibcode:1998PNAS...95.7316S. doi:10.1073/pnas.95.13.7316. PMC 22602. PMID 9636146.
  • Lehming N, Le Saux A, Schüller J, Ptashne M (1998). "Chromatin components as part of a putative transcriptional repressing complex". Proc. Natl. Acad. Sci. U.S.A. 95 (13): 7322–6. Bibcode:1998PNAS...95.7322L. doi:10.1073/pnas.95.13.7322. PMC 22604. PMID 9636147.
  • Ainsztein AM, Kandels-Lewis SE, Mackay AM, Earnshaw WC (1999). "INCENP Centromere and Spindle Targeting: Identification of Essential Conserved Motifs and Involvement of Heterochromatin Protein HP1". J. Cell Biol. 143 (7): 1763–74. doi:10.1083/jcb.143.7.1763. PMC 2175214. PMID 9864353.
  • Ryan RF, Schultz DC, Ayyanathan K, et al. (1999). "KAP-1 Corepressor Protein Interacts and Colocalizes with Heterochromatic and Euchromatic HP1 Proteins: a Potential Role for Krüppel-Associated Box–Zinc Finger Proteins in Heterochromatin-Mediated Gene Silencing". Mol. Cell. Biol. 19 (6): 4366–78. doi:10.1128/mcb.19.6.4366. PMC 104396. PMID 10330177.
  • Minc E, Allory Y, Worman HJ, et al. (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.
  • Nielsen AL, Ortiz JA, You J, et al. (2000). "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". EMBO J. 18 (22): 6385–95. doi:10.1093/emboj/18.22.6385. PMC 1171701. PMID 10562550.
  • Koike N, Maita H, Taira T, et al. (2000). "Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1(1)". FEBS Lett. 467 (1): 17–21. doi:10.1016/S0014-5793(00)01105-4. PMID 10664448. S2CID 29392124.
  • Minc E, Courvalin JC, Buendia B (2001). "HP1gamma associates with euchromatin and heterochromatin in mammalian nuclei and chromosomes". Cytogenet. Cell Genet. 90 (3–4): 279–84. doi:10.1159/000056789. PMID 11124534. S2CID 24349769.
  • Lachner M, O'Carroll D, Rea S, et al. (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature. 410 (6824): 116–20. Bibcode:2001Natur.410..116L. doi:10.1038/35065132. PMID 11242053. S2CID 4331863.
  • Nielsen AL, Oulad-Abdelghani M, Ortiz JA, et al. (2001). "Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins". Mol. Cell. 7 (4): 729–39. doi:10.1016/S1097-2765(01)00218-0. hdl:10261/308369. PMID 11336697.
  • Scholzen T, Endl E, Wohlenberg C, et al. (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". J. Pathol. 196 (2): 135–44. doi:10.1002/path.1016. PMID 11793364. S2CID 36130549.
  • Vassallo MF, Tanese N (2002). "Isoform-specific interaction of HP1 with human TAFII130". Proc. Natl. Acad. Sci. U.S.A. 99 (9): 5919–24. Bibcode:2002PNAS...99.5919V. doi:10.1073/pnas.092025499. PMC 122877. PMID 11959914.
  • Ogawa H, Ishiguro K, Gaubatz S, et al. (2002). "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells". Science. 296 (5570): 1132–6. Bibcode:2002Sci...296.1132O. doi:10.1126/science.1069861. PMID 12004135. S2CID 34863978.
  • Hwang KK, Worman HJ (2002). "Gene regulation by human orthologs of Drosophila heterochromatin protein 1". Biochem. Biophys. Res. Commun. 293 (4): 1217–22. doi:10.1016/S0006-291X(02)00377-7. PMID 12054505.
  • 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.
  • Kametaka A, Takagi M, Hayakawa T, et al. (2003). "Interaction of the chromatin compaction-inducing domain (LR domain) of Ki-67 antigen with HP1 proteins". Genes Cells. 7 (12): 1231–42. doi:10.1046/j.1365-2443.2002.00596.x. PMID 12485163. S2CID 6802841.
  • Cheutin T, McNairn AJ, Jenuwein T, et al. (2003). "Maintenance of stable heterochromatin domains by dynamic HP1 binding". Science. 299 (5607): 721–5. Bibcode:2003Sci...299..721C. doi:10.1126/science.1078572. PMID 12560555. S2CID 32776616.

External links

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

  • v
  • t
  • e
(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