MIZF

HINFP

Identifiers

HINFP, HiNF-P, MIZF, ZNF743, histone H4 transcription factor

External IDs

MGI: 2429620 HomoloGene: 9174 GeneCards: HINFP

Gene ontology
Molecular function	• DNA binding • transcription factor activity, sequence-specific DNA binding • transcription coactivator activity • histone binding • chromatin binding • metal ion binding • RNA polymerase II core promoter proximal region sequence-specific DNA binding • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding • protein binding • nucleic acid binding • enzyme binding • transcription regulatory region DNA binding
Cellular component	• Cajal body • nucleoplasm • nucleolus • nucleus
Biological process	• regulation of transcription, DNA-templated • establishment of protein localization • G1/S transition of mitotic cell cycle • DNA damage checkpoint • in utero embryonic development • negative regulation of transcription from RNA polymerase II promoter • regulation of transcription involved in G1/S transition of mitotic cell cycle • negative regulation of gene expression • transcription, DNA-templated • positive regulation of transcription, DNA-templated • positive regulation of gene expression • regulation of gene expression • myoblast differentiation • negative regulation of transcription, DNA-templated • DNA repair
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


25988


102423

Ensembl


ENSG00000172273


ENSMUSG00000032119

UniProt


Q9BQA5


Q8K1K9

RefSeq (mRNA)


NM_001243259 NM_015517 NM_198971


NM_172162

RefSeq (protein)


NP_001230188.1 NP_056332.2 NP_945322.1


NP_751894.2

Location (UCSC)

Chr 11: 119.12 – 119.14 Mb

Chr 9: 44.3 – 44.31 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Histone H4 transcription factor is a protein that in humans is encoded by the HINFP gene.^[3]^[4]

Function

MIZF interacts with methyl-CpG-binding protein-2 (MBD2; MIM 603547), a component of the MeCP1 histone deacetylase (HDAC) complex, and plays a role in DNA methylation and transcription repression.[supplied by OMIM]^[4]

Interactions

MIZF has been shown to interact with Methyl-CpG-binding domain protein 2^[3] and DHX9.^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 Sekimata M, Takahashi A, Murakami-Sekimata A, Homma Y (Nov 2001). "Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2". J. Biol. Chem. 276 (46): 42632–8. doi:10.1074/jbc.M107048200. PMID 11553631.
1 2 "Entrez Gene: MIZF MBD2-interacting zinc finger".
↑ Fujita H, Fujii R, Aratani S, Amano T, Fukamizu A, Nakajima T (Apr 2003). "Antithetic effects of MBD2a on gene regulation". Mol. Cell. Biol. 23 (8): 2645–57. doi:10.1128/MCB.23.8.2645-2657.2003. PMC 152551. PMID 12665568.

Medina R, van der Deen M, Miele-Chamberland A, Xie RL, van Wijnen AJ, Stein JL, Stein GS (2007). "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone target genes". Cancer Res. 67 (21): 10334–42. doi:10.1158/0008-5472.CAN-07-1560. PMID 17974976.
Mitra P, Xie R, Harper JW, Stein JL, Stein GS, van Wijnen AJ (2007). "HiNF-P is a bifunctional regulator of cell cycle controlled histone H4 gene transcription". J. Cell. Biochem. 101 (1): 181–91. doi:10.1002/jcb.21157. PMID 17163457.
Fukushige S, Kondo E, Gu Z, Suzuki H, Horii A (2006). "RET finger protein enhances MBD2- and MBD4-dependent transcriptional repression". Biochem. Biophys. Res. Commun. 351 (1): 85–92. doi:10.1016/j.bbrc.2006.10.005. PMID 17049487.
Pulukuri SM, Rao JS (2006). "CpG island promoter methylation and silencing of 14-3-3sigma gene expression in LNCaP and Tramp-C1 prostate cancer cell lines is associated with methyl-CpG-binding protein MBD2". Oncogene. 25 (33): 4559–72. doi:10.1038/sj.onc.1209462. PMC 1526774. PMID 16786000.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Miele A, Braastad CD, Holmes WF, Mitra P, Medina R, Xie R, Zaidi SK, Ye X, Wei Y, Harper JW, van Wijnen AJ, Stein JL, Stein GS (2005). "HiNF-P directly links the cyclin E/CDK2/p220NPAT pathway to histone H4 gene regulation at the G1/S phase cell cycle transition". Mol. Cell. Biol. 25 (14): 6140–53. doi:10.1128/MCB.25.14.6140-6153.2005. PMC 1168814. PMID 15988025.
Sekimata M, Homma Y (2004). "Regulation of Rb gene expression by an MBD2-interacting zinc finger protein MIZF during myogenic differentiation". Biochem. Biophys. Res. Commun. 325 (3): 653–9. doi:10.1016/j.bbrc.2004.10.090. PMID 15541338.
Sekimata M, Homma Y (2004). "Sequence-specific transcriptional repression by an MBD2-interacting zinc finger protein MIZF". Nucleic Acids Res. 32 (2): 590–7. doi:10.1093/nar/gkh249. PMC 373363. PMID 14752047.
Mitra P, Xie RL, Medina R, Hovhannisyan H, Zaidi SK, Wei Y, Harper JW, Stein JL, van Wijnen AJ, Stein GS (2003). "Identification of HiNF-P, a key activator of cell cycle-controlled histone H4 genes at the onset of S phase". Mol. Cell. Biol. 23 (22): 8110–23. doi:10.1128/MCB.23.22.8110-8123.2003. PMC 262391. PMID 14585971.

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MIZF

Function

Interactions

References

Further reading