SET1_CAEEL
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 03-AUG-2022, entry version 145.
DE RecName: Full=Histone-lysine N-methyltransferase set-1;
DE EC=2.1.1.361 {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 Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC 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 investigating
RT 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 chromatin
RT 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., Rechtsteiner A.,
RA Appert A., Chen Q.B., Dose A., Egelhofer T., Kimura H., Stempor P.,
RA Dernburg A., Lieb J.D., Strome S., Ahringer J.;
RT "H4K20me1 contributes to downregulation of X-linked genes for C. elegans
RT 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 in
RT growth and metabolic regulation downstream of TOR complex 2.";
RL Development 140:3601-3612(2013).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=28867287; DOI=10.1016/j.cell.2017.07.041;
RA Brejc K., Bian Q., Uzawa S., Wheeler B.S., Anderson E.C., King D.S.,
RA Kranzusch P.J., Preston C.G., Meyer B.J.;
RT "Dynamic Control of X Chromosome Conformation and Repression by a Histone
RT H4K20 Demethylase.";
RL Cell 171:E23-E23(2017).
CC -!- FUNCTION: Histone methyltransferase that specifically monomethylates
CC 'Lys-20' of histone H4 (H4K20me1) (PubMed:23028348). H4K20me1 is
CC enriched on hermaphrodite X chromosomes and during mitosis
CC (PubMed:23028348, PubMed:22393255). Involved in dosage compensation by
CC repression of X-linked gene expression in hermaphrodites
CC (PubMed:23028348). Plays a role in growth and body fat regulation
CC downstream of the TOR complex 2 pathway (PubMed:23884442).
CC {ECO:0000269|PubMed:22393255, ECO:0000269|PubMed:23028348,
CC ECO:0000269|PubMed:23884442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00904,
CC ECO:0000269|PubMed:23028348};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12119097}. Chromosome
CC {ECO:0000305|PubMed:23028348}.
CC -!- TISSUE SPECIFICITY: In embryos, it is expressed ubiquitously. In late
CC embryos, it is expressed in hypodermal seam cells. In L3 and L4 larvae
CC and thereafter, it is expressed in vulval precursor cells. In adult
CC males, it is also expressed in 6 unidentified posterior cells.
CC {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' of
CC histone H4 (H4K20me) (PubMed:23028348). In a glp-1(e2141) mutant
CC background which lacks a germline, the X-linked genes aco-1, ajm-1 and
CC apl-1 are up-regulated (PubMed:23028348). RNAi-mediated knockdown leads
CC to embryonic lethality in a mutant background of the dosage
CC compensation proteins dpy-21 or dpy-28 (PubMed:23028348). Increases
CC 'Lys-16' acetylation of histone H4 on hermaphrodite X chromosomes
CC (PubMed:22393255). In the TOR complex 2 mutant background rict-1,
CC suppresses the growth delay and elevated body fat index
CC (PubMed:23884442). Causes mitotic chromosome segregation defects and
CC chromosome bridges resulting in delayed or arrested embryonic
CC development and embryonic lethality (PubMed:28867287).
CC {ECO:0000269|PubMed:22393255, ECO:0000269|PubMed:23028348,
CC ECO:0000269|PubMed:23884442, ECO:0000269|PubMed:28867287}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. PR/SET subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00904}.
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DR EMBL; FO080366; CCD63213.1; -; Genomic_DNA.
DR PIR; T34384; T34384.
DR RefSeq; NP_001022796.1; NM_001027625.3.
DR AlphaFoldDB; Q22795; -.
DR SMR; Q22795; -.
DR BioGRID; 41136; 14.
DR IntAct; Q22795; 12.
DR STRING; 6239.T26A5.7a; -.
DR EPD; Q22795; -.
DR PaxDb; Q22795; -.
DR EnsemblMetazoa; T26A5.7a.1; T26A5.7a.1; 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 GeneTree; ENSGT00940000163293; -.
DR HOGENOM; CLU_047978_2_1_1; -.
DR InParanoid; Q22795; -.
DR OMA; KWCIDAT; -.
DR OrthoDB; 1460495at2759; -.
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; Expressed in embryo and 9 other tissues.
DR ExpressionAtlas; Q22795; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005700; C:polytene chromosome; IBA:GO_Central.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0034771; P:histone H4-K20 monomethylation; IBA:GO_Central.
DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016858; Hist_H4-K20_MeTrfase.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF027717; Histone_H4-K20_mtfrase; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51571; SAM_MT43_PR_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..242
FT /note="Histone-lysine N-methyltransferase set-1"
FT /id="PRO_0000097694"
FT DOMAIN 104..226
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00904"
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT ECO:0000255|PROSITE-ProRule:PRU00904"
FT BINDING 186..187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="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
