ID I3KK98_ORENI Unreviewed; 435 AA.
AC I3KK98;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=[histone H3]-lysine(4) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012182};
DE EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182};
GN Name=LOC100698697 {ECO:0000313|Ensembl:ENSONIP00000021543.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000021543.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000021543.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Protein-lysine N-methyltransferase that methylates both
CC histones and non-histone proteins, including p53/TP53 and RB1.
CC Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The
CC activity requires interaction with HSP90alpha. Shows even higher
CC methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of
CC p53/TP53, leading to decreased DNA-binding activity and subsequent
CC transcriptional regulation activity of p53/TP53. Monomethylates RB1 at
CC 'Lys-860'. {ECO:0000256|ARBA:ARBA00024002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000256|ARBA:ARBA00000944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000256|ARBA:ARBA00000587};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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 RefSeq; XP_003454536.1; XM_003454488.4.
DR AlphaFoldDB; I3KK98; -.
DR STRING; 8128.ENSONIP00000021543; -.
DR Ensembl; ENSONIT00000021562.2; ENSONIP00000021543.1; ENSONIG00000017085.2.
DR GeneID; 100698697; -.
DR KEGG; onl:100698697; -.
DR CTD; 541423; -.
DR eggNOG; KOG2084; Eukaryota.
DR GeneTree; ENSGT00940000157082; -.
DR HOGENOM; CLU_018406_0_0_1; -.
DR InParanoid; I3KK98; -.
DR OMA; HRIMDYL; -.
DR OrthoDB; 166337at2759; -.
DR TreeFam; TF106487; -.
DR Proteomes; UP000005207; Linkage group LG1.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.160; -; 1.
DR Gene3D; 1.25.40.970; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR12197; HISTONE-LYSINE N-METHYLTRANSFERASE SMYD; 1.
DR PANTHER; PTHR12197:SF193; N-LYSINE METHYLTRANSFERASE SMYD2; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 7..242
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 52..90
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
SQ SEQUENCE 435 AA; 50100 MW; 63E0E74388BA680F CRC64;
MKNEGIEGTE RFLSPDKGRG LRAVRHFAVG ELVFACPAYS YVLTVNERGA HCEHCFTRRE
DLFKCGKCKQ AYYCNVDCQR GDWPMHKLEC VAMCSYGENW CPSETVRLVA RIIMKQRATT
ERTPSERLLL LKEFEAHLDK MDSEKEEMNQ TDIAALHHFY SRHISNLPDE QALTELFAQV
NCNGFTIEDE ELSHLGSAVF PDVALMNHSC SPNVIVTYKG TVAEVRAVKE INPGEEIFNS
YIDLLYPTED RKERLLDSYF FTCQCTECTS RSKDKAKMEI RKLNPPPEPE EIRSMVRYAK
NVIEEFRRAK HYKTPSELLE MCELSLEKMG AIFADTNVYM LHMMYQAMGV CLYMQDWDGA
MSYGEKIVQP YSVHYPAYSL NVASMYLKLG RLYLGLEKKT QGVKALKKAL AVMEVAHGKD
HHYVAEVKRE IEEQK
//
