CBX3

From Wikipedia, the free encyclopedia

Chromobox homolog 3 (HP1 gamma homolog, Drosophila)

Identifiers

CBX3; HECH; HP1-GAMMA; HP1Hs-gamma

External IDs

OMIM: 604477 MGI: 108515 HomoloGene: 40583

Gene ontology
Molecular Function:	• chromatin binding • protein binding
Cellular Component:	• chromatin • nucleus
Biological Process:	• chromatin assembly or disassembly • transcription • regulation of transcription, DNA-dependent • chromatin modification

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Entrez

11335

12417

Refseq

NM_007276 (mRNA)
NP_009207 (protein)

NM_001037798 (mRNA)
NP_001032887 (protein)

Pubmed search

[1]

[2]

Chromobox homolog 3 (HP1 gamma homolog, Drosophila), also known as CBX3, is a human gene.^[1]

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.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Heterochromatin protein 1

[edit] References

^ ^a ^b Entrez Gene: CBX3 chromobox homolog 3 (HP1 gamma homolog, Drosophila).

[edit] Further reading

Ye Q, Worman HJ (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. PMID 8663349.
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. 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. 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. 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. 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. 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. 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. PMID 10460410.
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. 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. PMID 10664448.
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. PMID 11124534.
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. doi:10.1038/35065132. PMID 11242053.
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. 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.
Vassallo MF, Tanese N (2002). "Isoform-specific interaction of HP1 with human TAFII130.". Proc. Natl. Acad. Sci. U.S.A. 99 (9): 5919–24. doi:10.1073/pnas.092025499. 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. doi:10.1126/science.1069861. PMID 12004135.
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. doi:10.1073/pnas.242603899. 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. PMID 12485163.
Cheutin T, McNairn AJ, Jenuwein T, et al. (2003). "Maintenance of stable heterochromatin domains by dynamic HP1 binding.". Science 299 (5607): 721–5. doi:10.1126/science.1078572. PMID 12560555.

[edit] External links

MeSH CBX3+protein,+human

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

v • d • e

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1

(1.3) bHLH-ZIP	MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)

(1.6) Basic helix-span-helix (bHSH)	AP-2

(2) Zinc finger
DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)

(2.3) Cys₂His₂	ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2

(3.6) TEA domain	transcriptional enhancer factor 1, 2

(4) β-Scaffold factors with
minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	Rb • RBL1 • RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 • EREBP • B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD