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Database: UniProt
Entry: Q95Y12
LinkDB: Q95Y12
Original site: Q95Y12 
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   16-JAN-2019, entry version 107.
DE   RecName: Full=Probable histone-lysine N-methyltransferase set-23;
DE            EC=2.1.1.43;
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
RP   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
RT   investigating 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
RT   transcription to inhibit vulval development.";
RL   Development 134:2991-2999(2007).
CC   -!- FUNCTION: Probable histone methyltransferase (By similarity).
CC       Required for embryonic development. {ECO:0000250,
CC       ECO:0000269|PubMed:17634190}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {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         Note=No experimental confirmation available.;
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal.
CC       {ECO:0000269|PubMed:17634190}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
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   UniGene; Cel.32662; -.
DR   ProteinModelPortal; Q95Y12; -.
DR   SMR; Q95Y12; -.
DR   IntAct; Q95Y12; 1.
DR   STRING; 6239.Y41D4B.12a; -.
DR   PaxDb; Q95Y12; -.
DR   PRIDE; Q95Y12; -.
DR   EnsemblMetazoa; Y41D4B.12a; Y41D4B.12a; WBGene00021515. [Q95Y12-1]
DR   EnsemblMetazoa; Y41D4B.12b; Y41D4B.12b; WBGene00021515. [Q95Y12-2]
DR   GeneID; 176969; -.
DR   KEGG; cel:CELE_Y41D4B.12; -.
DR   CTD; 176969; -.
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   eggNOG; COG2940; LUCA.
DR   InParanoid; Q95Y12; -.
DR   KO; K11433; -.
DR   OMA; NCHIAAV; -.
DR   OrthoDB; 753093at2759; -.
DR   PhylomeDB; Q95Y12; -.
DR   PRO; PR:Q95Y12; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00021515; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 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   Complete proteome; Developmental protein; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    244       Probable histone-lysine N-
FT                                methyltransferase set-23.
FT                                /FTId=PRO_0000287565.
FT   DOMAIN       25     86       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN       89    213       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      221    237       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      101    103       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      173    174       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL        27     27       Zinc 1. {ECO:0000250}.
FT   METAL        27     27       Zinc 2. {ECO:0000250}.
FT   METAL        29     29       Zinc 1. {ECO:0000250}.
FT   METAL        33     33       Zinc 1. {ECO:0000250}.
FT   METAL        33     33       Zinc 3. {ECO:0000250}.
FT   METAL        39     39       Zinc 1. {ECO:0000250}.
FT   METAL        41     41       Zinc 2. {ECO:0000250}.
FT   METAL        65     65       Zinc 2. {ECO:0000250}.
FT   METAL        65     65       Zinc 3. {ECO:0000250}.
FT   METAL        69     69       Zinc 2. {ECO:0000250}.
FT   METAL        71     71       Zinc 3. {ECO:0000250}.
FT   METAL        78     78       Zinc 3. {ECO:0000250}.
FT   METAL       176    176       Zinc 4. {ECO:0000250}.
FT   METAL       225    225       Zinc 4. {ECO:0000250}.
FT   METAL       227    227       Zinc 4. {ECO:0000250}.
FT   METAL       232    232       Zinc 4. {ECO:0000250}.
FT   BINDING     141    141       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     143    143       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     170    170       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   VAR_SEQ       1     85       Missing (in isoform b). {ECO:0000305}.
FT                                /FTId=VSP_025564.
FT   VAR_SEQ      86     95       GPQKKLEIFS -> MCLHTAPNFI (in isoform b).
FT                                {ECO:0000305}.
FT                                /FTId=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
//
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