http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID277167

Outgoing Links

Predicate Object
abstract Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.
title ePHD2_KMT2C
isDiscussedBy http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32766645
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6503818
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27490384
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16321086
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13861751
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24223300
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32923228
type http://purl.obolibrary.org/obo/SO_0000417

Incoming Links

Predicate Subject
has component http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ8NEZ4
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ8BRH4

Total number of triples: 12.