ID SET1_CAEEL Reviewed; 242 AA. AC Q22795; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1999, sequence version 2. DT 07-JUN-2017, entry version 119. DE RecName: Full=Histone-lysine N-methyltransferase set-1; DE EC=2.1.1.43 {ECO:0000255|PROSITE-ProRule:PRU00904, ECO:0000269|PubMed:23028348}; GN Name=set-1; ORFNames=T26A5.7; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=12119097; DOI=10.1016/S0378-1119(02)00671-6; RA Terranova R., Pujol N., Fasano L., Djabali M.; RT "Characterisation of set-1, a conserved PR/SET domain gene in RT Caenorhabditis elegans."; RL Gene 292:33-41(2002). RN [3] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22393255; DOI=10.1128/MCB.06546-11; RA Wells M.B., Snyder M.J., Custer L.M., Csankovszki G.; RT "Caenorhabditis elegans dosage compensation regulates histone H4 RT chromatin state on X chromosomes."; RL Mol. Cell. Biol. 32:1710-1719(2012). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RX PubMed=23028348; DOI=10.1371/journal.pgen.1002933; RA Vielle A., Lang J., Dong Y., Ercan S., Kotwaliwale C., RA Rechtsteiner A., Appert A., Chen Q.B., Dose A., Egelhofer T., RA Kimura H., Stempor P., Dernburg A., Lieb J.D., Strome S., Ahringer J.; RT "H4K20me1 contributes to downregulation of X-linked genes for C. RT elegans dosage compensation."; RL PLoS Genet. 8:E1002933-E1002933(2012). RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=23884442; DOI=10.1242/dev.094292; RA Webster C.M., Wu L., Douglas D., Soukas A.A.; RT "A non-canonical role for the C. elegans dosage compensation complex RT in growth and metabolic regulation downstream of TOR complex 2."; RL Development 140:3601-3612(2013). CC -!- FUNCTION: Histone methyltransferase that specifically CC monomethylates 'Lys-20' of histone H4 (H4K20me1) CC (PubMed:23028348). H4K20me1 is enriched on hermaphrodite X CC chromosomes and during mitosis (PubMed:23028348, PubMed:22393255). CC Involved in dosage compensation by repression of X-linked gene CC expression in hermaphrodites (PubMed:23028348). Plays a role in CC growth and body fat regulation downstream of the TOR complex 2 CC pathway (PubMed:23884442). {ECO:0000269|PubMed:22393255, CC ECO:0000269|PubMed:23028348, ECO:0000269|PubMed:23884442}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] = CC S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. CC {ECO:0000255|PROSITE-ProRule:PRU00904, CC ECO:0000269|PubMed:23028348}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12119097}. CC Chromosome {ECO:0000305|PubMed:23028348}. CC -!- TISSUE SPECIFICITY: In embryos, it is expressed ubiquitously. In CC late embryos, it is expressed in hypodermal seam cells. In L3 and CC L4 larvae and thereafter, it is expressed in vulval precursor CC cells. In adult males, it is also expressed in 6 unidentified CC posterior cells. {ECO:0000269|PubMed:12119097}. CC -!- DEVELOPMENTAL STAGE: Highly expressed in eggs, then decreases. CC {ECO:0000269|PubMed:12119097}. CC -!- DISRUPTION PHENOTYPE: Mutant animals lack methylation of 'Lys-20' CC of histone H4 (H4K20me) (PubMed:23028348). In a glp-1(e2141) CC mutant background which lacks a germline, the X-linked genes aco- CC 1, ajm-1 and apl-1 are up-regulated (PubMed:23028348). In a mutant CC background of the dosage compensation proteins dpy-21 or dpy-28, CC RNAi-mediated knockdown leads to embryonic lethality CC (PubMed:23028348). Increases 'Lys-16' acetylation of histone H4 on CC hermaphrodite X chromosomes (PubMed:22393255). In the TOR complex CC 2 mutant background rict-1, suppresses the growth delay and CC elevated body fat index (PubMed:23884442). CC {ECO:0000269|PubMed:22393255, ECO:0000269|PubMed:23028348, CC ECO:0000269|PubMed:23884442}. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding CC methyltransferase superfamily. Histone-lysine methyltransferase CC family. PR/SET subfamily. {ECO:0000255|PROSITE-ProRule:PRU00904}. 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; FO080366; CCD63213.1; -; Genomic_DNA. DR PIR; T34384; T34384. DR RefSeq; NP_001022796.1; NM_001027625.3. DR UniGene; Cel.7462; -. DR ProteinModelPortal; Q22795; -. DR SMR; Q22795; -. DR BioGrid; 41136; 1. DR IntAct; Q22795; 12. DR MINT; MINT-252002; -. DR STRING; 6239.T26A5.7a.1; -. DR PaxDb; Q22795; -. DR EnsemblMetazoa; T26A5.7a; T26A5.7a; WBGene00004781. DR GeneID; 175918; -. DR KEGG; cel:CELE_T26A5.7; -. DR UCSC; T26A5.7b.1; c. elegans. DR CTD; 175918; -. DR WormBase; T26A5.7a; CE19602; WBGene00004781; set-1. DR eggNOG; KOG1085; Eukaryota. DR eggNOG; COG2940; LUCA. DR GeneTree; ENSGT00410000025501; -. DR HOGENOM; HOG000020818; -. DR InParanoid; Q22795; -. DR KO; K11428; -. DR OMA; KQFSRGE; -. DR OrthoDB; EOG091G0UBI; -. DR PhylomeDB; Q22795; -. DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-CEL-3214841; PKMTs methylate histone lysines. DR PRO; PR:Q22795; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00004781; -. DR ExpressionAtlas; Q22795; baseline. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR016858; Hist_H4-K20_MeTrfase. DR InterPro; IPR001214; SET_dom. DR Pfam; PF00856; SET; 1. DR PIRSF; PIRSF027717; Histone_H4-K20_mtfrase; 1. DR SMART; SM00317; SET; 1. DR PROSITE; PS51571; SAM_MT43_PR_SET; 1. DR PROSITE; PS50280; SET; 1. PE 1: Evidence at protein level; KW Chromatin regulator; Chromosome; Complete proteome; Methyltransferase; KW Nucleus; Reference proteome; S-adenosyl-L-methionine; Transcription; KW Transcription regulation; Transferase. FT CHAIN 1 242 Histone-lysine N-methyltransferase set-1. FT /FTId=PRO_0000097694. FT DOMAIN 104 226 SET. {ECO:0000255|PROSITE- FT ProRule:PRU00190}. FT REGION 114 116 S-adenosyl-L-methionine binding. FT {ECO:0000255|PROSITE-ProRule:PRU00904}. FT REGION 186 187 S-adenosyl-L-methionine binding. FT {ECO:0000255|PROSITE-ProRule:PRU00904}. FT COMPBIAS 18 21 Poly-Ala. FT COMPBIAS 38 43 Poly-Ser. FT BINDING 159 159 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00190, FT ECO:0000255|PROSITE-ProRule:PRU00904}. SQ SEQUENCE 242 AA; 27568 MW; 0F752B79505AFA99 CRC64; MKVAAKKLAT SRMRKDRAAA ASPSSDIENS ENPSSLASHS SSSGRMTPSK NTRSRKGVSV KDVSNHKITE FFQVRRSNRK TSKQISDEAK HALRDTVLKG TNERLLEVYK DVVKGRGIRT KVNFEKGDFV VEYRGVMMEY SEAKVIEEQY SNDEEIGSYM YFFEHNNKKW CIDATKESPW KGRLINHSVL RPNLKTKVVE IDGSHHLILV ARRQIAQGEE LLYDYGDRSA ETIAKNPWLV NT //