Family

Histone-lysine N-methyltransferase, H3 lysine-4 specific (IPR017111)

Short name: Hist_H3-K4_MeTrfase

Family relationships

None.

Description

This entry represents fungal-type histone H3-K4 methyltransferase Set1 (EC:2.1.1.43), which is the catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation [PMID: 18849979, PMID: 18838538, PMID: 18083099]. The COMPASS (Set1C) complex consists of SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1), and SWD3(1) [PMID: 9988274, PMID: 11687631, PMID: 12488447, PMID: 14617822].

Methyltransferases (EC 2.1.1.-) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as oxygen leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule [PMID: 16225687, PMID: 21858014, PMID: 12826405]. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM [PMID: 7897657]. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids [PMID: 16225687, PMID: 21858014, PMID: 7897657]. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing [PMID: 16225687, PMID: 21858014, PMID: 12826405]. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor.

GO terms

Biological Process

GO:0034968 histone lysine methylation

Molecular Function

GO:0018024 histone-lysine N-methyltransferase activity

Cellular Component

GO:0048188 Set1C/COMPASS complex

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles
PIRSF