ID SET23_CAEEL Reviewed; 244 AA. AC Q95Y12; Q8MXT0; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Probable histone-lysine N-methyltransferase set-23; DE EC=2.1.1.-; DE AltName: Full=SET-domain containing protein 23; GN Name=set-23; ORFNames=Y41D4B.12; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17634190; DOI=10.1242/dev.009373; RA Andersen E.C., Horvitz H.R.; RT "Two C. elegans histone methyltransferases repress lin-3 EGF transcription RT to inhibit vulval development."; RL Development 134:2991-2999(2007). CC -!- FUNCTION: Probable histone methyltransferase (By similarity). Required CC for embryonic development. {ECO:0000250, ECO:0000269|PubMed:17634190}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; CC IsoId=Q95Y12-1; Sequence=Displayed; CC Name=b; CC IsoId=Q95Y12-2; Sequence=VSP_025564, VSP_025565; CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are CC arranged in a triangular cluster; some of these Cys residues contribute CC to the binding of two zinc ions within the cluster. {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:17634190}. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. Suvar3-9 CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FO080782; CCD66712.1; -; Genomic_DNA. DR EMBL; FO080782; CCD66713.1; -; Genomic_DNA. DR RefSeq; NP_741320.1; NM_171270.1. [Q95Y12-1] DR RefSeq; NP_741321.1; NM_171271.3. [Q95Y12-2] DR AlphaFoldDB; Q95Y12; -. DR SMR; Q95Y12; -. DR BioGRID; 42125; 1. DR IntAct; Q95Y12; 1. DR STRING; 6239.Y41D4B.12a.1; -. DR PaxDb; 6239-Y41D4B-12a; -. DR EnsemblMetazoa; Y41D4B.12a.1; Y41D4B.12a.1; WBGene00021515. [Q95Y12-1] DR EnsemblMetazoa; Y41D4B.12a.2; Y41D4B.12a.2; WBGene00021515. [Q95Y12-1] DR EnsemblMetazoa; Y41D4B.12b.1; Y41D4B.12b.1; WBGene00021515. [Q95Y12-2] DR GeneID; 176969; -. DR KEGG; cel:CELE_Y41D4B.12; -. DR AGR; WB:WBGene00021515; -. DR WormBase; Y41D4B.12a; CE27623; WBGene00021515; set-23. [Q95Y12-1] DR WormBase; Y41D4B.12b; CE31647; WBGene00021515; set-23. [Q95Y12-2] DR eggNOG; KOG1082; Eukaryota. DR InParanoid; Q95Y12; -. DR OMA; QNGPLNC; -. DR OrthoDB; 2879726at2759; -. DR PhylomeDB; Q95Y12; -. DR PRO; PR:Q95Y12; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00021515; Expressed in germ line (C elegans) and 5 other cell types or tissues. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt. DR GO; GO:0042054; F:histone methyltransferase activity; IBA:GO_Central. DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProt. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR Gene3D; 2.170.270.10; SET domain; 1. DR InterPro; IPR003616; Post-SET_dom. DR InterPro; IPR007728; Pre-SET_dom. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR PANTHER; PTHR46223:SF3; HISTONE H3 (LYS9) METHYLTRANSFERASE-RELATED; 1. DR PANTHER; PTHR46223; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H; 1. DR Pfam; PF00856; SET; 1. DR SMART; SM00317; SET; 1. DR SUPFAM; SSF82199; SET domain; 1. DR PROSITE; PS50868; POST_SET; 1. DR PROSITE; PS50867; PRE_SET; 1. DR PROSITE; PS50280; SET; 1. PE 3: Inferred from homology; KW Alternative splicing; Chromatin regulator; Chromosome; KW Developmental protein; Metal-binding; Methyltransferase; Nucleus; KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1..244 FT /note="Probable histone-lysine N-methyltransferase set-23" FT /id="PRO_0000287565" FT DOMAIN 25..86 FT /note="Pre-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157" FT DOMAIN 89..213 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT DOMAIN 221..237 FT /note="Post-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155" FT BINDING 27 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 27 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 41 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 101..103 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 141 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 143 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 170 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 173..174 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 176 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 225 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 227 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 232 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250" FT VAR_SEQ 1..85 FT /note="Missing (in isoform b)" FT /evidence="ECO:0000305" FT /id="VSP_025564" FT VAR_SEQ 86..95 FT /note="GPQKKLEIFS -> MCLHTAPNFI (in isoform b)" FT /evidence="ECO:0000305" FT /id="VSP_025565" SQ SEQUENCE 244 AA; 27108 MW; AB291915D129C2A3 CRC64; MNYEKIDSTI PGPGISETDW NDVFEGCNCE AECSSAAGCS CLINKIDNYT VDGKINKSSE LLIECSDQCA CILLPTSCRN RVVQCGPQKK LEIFSTCEMA KGFGVRAGEQ IAAGEFVCEY AGECIGEQEV ERRCREFRGD DNYTLTLKEF FGGKPVKTFV DPRLRGNIGR FLNHSCEPNC EIILARLGRM IPAAGIFAKR DIVRGEELCY DYGHSAIEGE NRKLCLCKSE KCRKYLPMSA TPIE //