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Database: UniProt
Entry: Q22795
LinkDB: Q22795
Original site: Q22795 
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   10-APR-2019, entry version 131.
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   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
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).
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
RT   Histone H4K20 Demethylase.";
RL   Cell 171:E23-E23(2017).
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:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-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; EC=2.1.1.43;
CC         Evidence={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). RNAi-
CC       mediated knockdown leads to embryonic lethality in a mutant
CC       background of the dosage compensation proteins dpy-21 or dpy-28
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). Causes mitotic
CC       chromosome segregation defects and chromosome bridges resulting in
CC       delayed or arrested embryonic development and embryonic lethality
CC       (PubMed:28867287). {ECO:0000269|PubMed:22393255,
CC       ECO:0000269|PubMed:23028348, ECO:0000269|PubMed:23884442,
CC       ECO:0000269|PubMed:28867287}.
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}.
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   STRING; 6239.T26A5.7a; -.
DR   EPD; Q22795; -.
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; ENSGT00940000163293; -.
DR   HOGENOM; HOG000020818; -.
DR   InParanoid; Q22795; -.
DR   KO; K11428; -.
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 7 organ(s), highest expression level in multi-cellular organism.
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   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
//
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