http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID438425
Outgoing Links
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abstract | RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1). UHRF1, also known as inverted CCAAT box-binding protein of 90 kDa, nuclear protein 95, nuclear zinc finger protein Np95 (Np95), RING finger protein 106, transcription factor ICBP90, or E3 ubiquitin-protein ligase UHRF1, is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 can acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also a N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF1 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) domain, a SET and RING finger associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger. It specifically binds to hemimethylated DNA, double-stranded CpG dinucleotides, and recruits the maintenance methyltransferase DNMT1 to its hemimethylated DNA substrate through its SRA domain. UHRF1-dependent H3K23 ubiquitylation has an essential role in maintenance DNA methylation and replication. The tandem Tudor domain directs UHRF1 binding to the heterochromatin mark histone H3K9me3 and the PHD domain targets UHRF1 to unmodified histone H3 in euchromatic regions. The RING-HC finger exhibits both autocatalytic E3 ubiquitin (Ub) ligase activity and activity against histone H3 and DNMT1. |
title | RING-HC_UHRF1 |
isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17416075 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7207842 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12716281 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9997243 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20748278 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12716282 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27578904 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20762002 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7919988 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/33652312 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1776421 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27605516 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22732383 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3869075 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12747444 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8638669 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30831878 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/31851268 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3163469 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/31641856 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/473062 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18132138 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/441312 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6388207 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18047791 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27627443 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14727661 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16084628 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3812616 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13397380 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20096998 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24138545 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28267081 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7311311 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13398118 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9970449 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12596789 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8527994 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3192231 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24242917 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8693849 |
type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Predicate | Subject |
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has component | http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ96T88 http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCNP_001041666 http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCB6CHA3 |
Total number of triples: 47.