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 13-JUL-2010, entry version 70. DE RecName: Full=Probable histone-lysine N-methyltransferase set-1; DE EC=2.1.1.43; GN Name=set-1; ORFNames=T26A5.7; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; 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 MEDLINE=22114964; 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). CC -!- FUNCTION: Probable histone methyltransferase involved in chromatin CC modification and/or regulation (By similarity). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] = CC S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. CC -!- SUBCELLULAR LOCATION: Nucleus. 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. CC -!- DEVELOPMENTAL STAGE: Highly expressed in eggs, then decreases. CC -!- SIMILARITY: Belongs to the histone-lysine methyltransferase CC family. PR/SET subfamily. CC -!- SIMILARITY: Contains 1 SET domain. 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; U00043; AAC77512.1; -; Genomic_DNA. DR PIR; T34384; T34384. DR RefSeq; NP_001022796.1; -. DR UniGene; Cel.7462; -. DR SMR; Q22795; 80-240. DR IntAct; Q22795; 1. DR MINT; MINT-252002; -. DR PRIDE; Q22795; -. DR EnsemblMetazoa; T26A5.7a; T26A5.7a; T26A5.7. DR GeneID; 175918; -. DR KEGG; cel:T26A5.7; -. DR NMPDR; fig|6239.3.peg.10206; -. DR UCSC; T26A5.7b.1; c. elegans. DR CTD; 175918; -. DR WormBase; T26A5.7a; CE19602; WBGene00004781; set-1. DR eggNOG; meNOG11471; -. DR HOGENOM; HBG388866; -. DR InParanoid; Q22795; -. DR OMA; RRSNRKT; -. DR PhylomeDB; Q22795; -. DR BRENDA; 2.1.1.43; 672. DR NextBio; 890302; -. DR ArrayExpress; Q22795; -. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:EC. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase. DR GO; GO:0040007; P:growth; IMP:WormBase. DR GO; GO:0040011; P:locomotion; IMP:WormBase. DR GO; GO:0002119; P:nematode larval development; IMP:WormBase. DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase. DR GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW. DR GO; GO:0000003; P:reproduction; IMP:WormBase. DR GO; GO:0006350; P:transcription; 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; PS50280; SET; 1. PE 2: Evidence at transcript level; KW Chromatin regulator; Chromosomal protein; Complete proteome; KW Methyltransferase; Nucleus; S-adenosyl-L-methionine; Transcription; KW Transcription regulation; Transferase. FT CHAIN 1 242 Probable histone-lysine N- FT methyltransferase set-1. FT /FTId=PRO_0000097694. FT DOMAIN 103 230 SET. FT REGION 114 116 S-adenosyl-L-methionine binding (By FT similarity). FT REGION 186 187 S-adenosyl-L-methionine binding (By FT similarity). FT COMPBIAS 18 21 Poly-Ala. FT COMPBIAS 38 43 Poly-Ser. FT BINDING 159 159 S-adenosyl-L-methionine (By similarity). 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 //