ID A0A3Q1CUM6_AMPOC Unreviewed; 436 AA.
AC A0A3Q1CUM6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=[histone H3]-lysine(4) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012182};
DE EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000029493.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000029493.1}
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}.
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DR AlphaFoldDB; A0A3Q1CUM6; -.
DR STRING; 80972.ENSAOCP00000029493; -.
DR Ensembl; ENSAOCT00000023662.1; ENSAOCP00000029493.1; ENSAOCG00000019851.1.
DR GeneTree; ENSGT00940000157082; -.
DR Proteomes; UP000257160; Unplaced.
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; 6.10.140.2220; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 2.
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 SUPFAM; SSF48452; TPR-like; 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:UP000257160};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 7..240
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 436 AA; 50106 MW; 79FC0BF234C1799C CRC64;
MKNEGIEGTE RFLSPDRGRG LRAVRHFSVG ELVFACPAYS YVLTVNERGA HCENCFSRRD
DLFKCGKCKQ AYYCNVDCQR GDWPMHKLEC VAMCAYGENW CPSETVRLVA RIIMKQRVTT
ERTPSERVLL LREFESHGVA SCFIILLNPS VRCLCLFVSF LLFFSVLPCL TCFFCLQVNC
NGFTIEDEEL SHLGSAVFPD VALMNHSCSP NVIVTYKGTV AEVRAVKEIN PGEEIFNSYI
DLLYPTEDRK ERLLDSYFFT CQCTECTTKS KDKEKMEIRK LSSPPEPEEI KSMVRYAKNV
IEEFRRAKHY KNILFSCELL EMCELSQEKM GAIFADTNVY MLHMMYQAMG VCLYMQDWDG
AMSYGEKIIQ PYSVHYPAYS LNVASMYLKL GRLYLGLEKK TQGVKALKKA LAIMEVAHGE
DHHYVAEVKR EIEDHK
//
