http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID438167

Outgoing Links

Predicate Object
abstract RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins. COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.
title RING-HC_COP1
isDiscussedBy http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18048163
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25124490
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13474462
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5012066
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8649229
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11401882
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13938639
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26974563
type http://purl.obolibrary.org/obo/SO_0000417

Incoming Links

Predicate Subject
has component http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ8NHY2
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9R1A8

Total number of triples: 13.