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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Ubiquitin-like with PHD and ring finger domains 1

UHRF1, ICBP90, Np95, ubiquitin-like, containing PHD and RING finger domains 1
This gene encodes a member of a subfamily of RING-finger type E3 ubiquitin ligases. The protein binds to specific DNA sequences, and recruits a histone deacetylase to regulate gene expression. Its expression peaks at late G1 phase and continues during G2 and M phases of the cell cycle. It plays a major role in the G1/S transition by regulating topoisomerase IIalpha and retinoblastoma gene expression, and functions in the p53-dependent DNA damage checkpoint. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, DNA methyltransferase, Histone, V1a, CAN
Papers on UHRF1
Long noncoding RNA UPAT promotes colon tumorigenesis by inhibiting degradation of UHRF1.
Akiyama et al., Tokyo, Japan. In Proc Natl Acad Sci U S A, Feb 2016
Here we show that an lncRNA termed UPAT [ubiquitin-like plant homeodomain (PHD) and really interesting new gene (RING) finger domain-containing protein 1 (UHRF1) Protein Associated Transcript] is required for the survival and tumorigenicity of colorectal cancer cells.
The replication foci targeting sequence (RFTS) of DNMT1 functions as a potent histone H3 binding domain regulated by autoinhibition.
Nakanishi et al., Nagoya, Japan. In Biochem Biophys Res Commun, Feb 2016
The replication foci targeting sequence (RFTS) of DNMT1 is required for the recruitment of DNMT1 to DNA methylation sites through direct binding to ubiquitylated histone H3 mediated by UHRF1 (Ubiquitin-like containing PHD and RING finger domains 1).
Transcription factor ICBP90 regulates the MIF promoter and immune susceptibility locus.
Bucala et al., In J Clin Invest, Feb 2016
An analysis of monocyte nuclear lysates revealed that the transcription factor ICBP90 (also known as UHRF1) is the major protein interacting with the MIF microsatellite.
Gene expression profiling of lung adenocarcinoma in Xuanwei, China.
Zhang et al., Kunming, China. In Eur J Cancer Prev, Jan 2016
The tendency of changes in the expression of 12 selected DEGs (five downregulated genes, PIK3R1, RARB, HGF, MAPK11, and SESN1, and seven upregulated genes, PAK1, E2F1, CCNE1, EGF, CDC25A, PTTG1, and UHRF1) in RTq-PCR was consistent with the expression profiling data.
A cell cycle-dependent BRCA1-UHRF1 cascade regulates DNA double-strand break repair pathway choice.
Pei et al., Chongqing, China. In Nat Commun, Dec 2015
Here, we report that the E3 ubiquitin ligase UHRF1 (Ubiquitin-like, with PHD and RING finger domains 1) directly participates in the interplay between BRCA1 and 53BP1.
Conserved linker regions and their regulation determine multiple chromatin-binding modes of UHRF1.
Fischle et al., Göttingen, Germany. In Nucleus, 2014
Ubiquitin-like with PHD and RING Finger domains 1 (UHRF1) is an important nuclear protein that is mutated and aberrantly expressed in many tumors.
UHRF1 overexpression drives DNA hypomethylation and hepatocellular carcinoma.
Sadler et al., New York City, United States. In Cancer Cell, 2014
Ubiquitin-like with PHD and RING finger domains 1 (UHRF1) is an essential regulator of DNA methylation that is highly expressed in many cancers.
Increasing role of UHRF1 in the reading and inheritance of the epigenetic code as well as in tumorogenesis.
Mousli et al., Illkirch-Graffenstaden, France. In Biochem Pharmacol, 2014
UHRF1 plays a major role in the inheritance of some epigenetic marks from mother cells to daughter cells due to its particular structural domains.
Tudor: a versatile family of histone methylation 'readers'.
Wang et al., Chapel Hill, United States. In Trends Biochem Sci, 2013
Here, we discuss novel functions of a number of Tudor-containing proteins [including Jumonji domain-containing 2A (JMJD2A), p53-binding protein 1 (53BP1), SAGA-associated factor 29 (SGF29), Spindlin1, ubiquitin-like with PHD and RING finger domains 1 (UHRF1), PHD finger protein 1 (PHF1), PHD finger protein 19 (PHF19), and SAWADEE homeodomain homolog 1 (SHH1)] in 'reading' unique methylation events on histones in order to facilitate DNA damage repair or regulate transcription.
Uhrf1-dependent H3K23 ubiquitylation couples maintenance DNA methylation and replication.
Nakanishi et al., Nagoya, Japan. In Nature, 2013
Although it is well established that Uhrf1 (ubiquitin-like with PHD and ring finger domains 1; also known as Np95 and ICBP90) specifically binds to hemi-methylated DNA through its SRA (SET and RING finger associated) domain and has an essential role in maintenance of DNA methylation by recruiting Dnmt1 to hemi-methylated DNA sites, the mechanism by which Uhrf1 coordinates the maintenance of DNA methylation and DNA replication is largely unknown.
Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1.
Shirakawa et al., Kyoto, Japan. In Proc Natl Acad Sci U S A, 2012
UHRF1 contains linked two-histone reader modules tethered by a 17-aa linker, which plays a role as a functional switch involved in multiple regulatory pathways such as maintenance of DNA methylation and transcriptional repression.
Exogenous expression of UHRF1 promotes proliferation and metastasis of breast cancer cells.
Fan et al., Suzhou, China. In Oncol Rep, 2012
UHRF1 promoted the proliferation of breast cancer cells by apoptosis inhibition, G1 phase shortage and promotion of tumor vessel formation
Diverse epigenetic strategies interact to control epidermal differentiation.
Watt et al., Cambridge, United Kingdom. In Nat Cell Biol, 2012
We discovered a network of genetic interactions involving EZH2, UHRF1 (both known to regulate epidermal self-renewal), ING5 (a MORF complex component), BPTF and SMARCA5 (NURF complex components).
NIRF/UHRF2 occupies a central position in the cell cycle network and allows coupling with the epigenetic landscape.
NIRF Project et al., Fukushima, Japan. In Febs Lett, 2012
The NIRF gene is frequently lost in tumors and is a candidate tumor suppressor, while its paralog, the UHRF1 gene, is hardly altered.
M phase phosphorylation of the epigenetic regulator UHRF1 regulates its physical association with the deubiquitylase USP7 and stability.
Shi et al., Shanghai, China. In Proc Natl Acad Sci U S A, 2012
A cell cycle-specific signaling event that relieves UHRF1 from its interaction with USP7, is reported.
UHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tail.
Qian et al., Hong Kong, Hong Kong. In J Mol Biol, 2012
UHRF1 PHD finger (including the preceding zinc-Cys4 knuckle) acts together with the adjacent double Tudor domain to specifically recognize the H3K9me3 mark.
A possible 5'-NRIP1/UHRF1-3' fusion gene detected by array CGH analysis in a Ph+ ALL patient.
Lee et al., Oklahoma City, United States. In Cancer Genet, 2011
The fusion of NRIP1 with UHRF1 involved in the unbalanced translocation between chromosomes 19 and 21 in a patient with an ALL-positive for a t(9;22) translocation.
Epigenetics, development, and cancer: zebrafish make their mark..
Sadler et al., New York City, United States. In Birth Defects Res C Embryo Today, 2011
For instance, DNA methylation is an important epigenetic mark that is depleted in embryos lacking dnmt1 and uhrf1.
Genome-wide erasure of DNA methylation in mouse primordial germ cells is affected by AID deficiency.
Reik et al., Cambridge, United Kingdom. In Nature, 2010
Wild-type PGCs revealed marked genome-wide erasure of methylation to a level below that of methylation deficient (Np95(-/-), also called Uhrf1(-/-)) embryonic stem cells, with female PGCs being less methylated than male ones.
DNMT1 maintains progenitor function in self-renewing somatic tissue.
Khavari et al., Stanford, United States. In Nature, 2010
Furthermore, UHRF1 (refs 9, 10), a component of the DNA methylation machinery that targets DNMT1 to hemi-methylated DNA, is also necessary to suppress premature differentiation and sustain proliferation.
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