SUV91_BOVIN
ID SUV91_BOVIN Reviewed; 412 AA.
AC Q2NL30;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Histone-lysine N-methyltransferase SUV39H1;
DE EC=2.1.1.355 {ECO:0000250|UniProtKB:O43463};
DE AltName: Full=Suppressor of variegation 3-9 homolog 1;
DE Short=Su(var)3-9 homolog 1;
GN Name=SUV39H1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3
CC 'Lys-9' trimethylation represents a specific tag for epigenetic
CC transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5)
CC proteins to methylated histones. Mainly functions in heterochromatin
CC regions, thereby playing a central role in the establishment of
CC constitutive heterochromatin at pericentric and telomere regions. H3
CC 'Lys-9' trimethylation is also required to direct DNA methylation at
CC pericentric repeats. SUV39H1 is targeted to histone H3 via its
CC interaction with RB1 and is involved in many processes, such as
CC repression of MYOD1-stimulated differentiation, regulation of the
CC control switch for exiting the cell cycle and entering differentiation,
CC repression by the PML-RARA fusion protein, BMP-induced repression,
CC repression of switch recombination to IgA and regulation of telomere
CC length. Component of the eNoSC (energy-dependent nucleolar silencing)
CC complex, a complex that mediates silencing of rDNA in response to
CC intracellular energy status and acts by recruiting histone-modifying
CC enzymes. The eNoSC complex is able to sense the energy status of cell:
CC upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates
CC SIRT1, leading to histone H3 deacetylation followed by dimethylation of
CC H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent
CC chromatin in the rDNA locus. Recruited by the large PER complex to the
CC E-box elements of the circadian target genes such as PER2 itself or
CC PER1, contributes to the conversion of local chromatin to a
CC heterochromatin-like repressive state through H3 'Lys-9' trimethylation
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000250|UniProtKB:O43463, ECO:0000255|PROSITE-
CC ProRule:PRU00912};
CC -!- ACTIVITY REGULATION: Negatively regulated by CCAR2. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with H3 and H4 histones. Interacts with GFI1B,
CC DNMT3B, CBX1, CBX4, CCAR2, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and RB1.
CC Interacts with SBF1 through the SET domain. Interacts with HDAC1 and
CC HDAC2 through the N-terminus and associates with the core histone
CC deacetylase complex composed of HDAC1, HDAC2, RBBP4 and RBBP7.
CC Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8 (By
CC similarity). Interacts (via SET domain) with MECOM; enhances MECOM
CC transcriptional repression activity. Interacts with LMNA; the
CC interaction increases stability of SUV39H1. The large PER complex
CC involved in the histone methylation is composed of at least PER2, CBX3,
CC TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus lamina
CC {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome,
CC centromere {ECO:0000250}. Note=Associates with centromeric constitutive
CC heterochromatin. {ECO:0000250}.
CC -!- DOMAIN: Although the SET domain contains the active site of enzymatic
CC activity, both pre-SET and post-SET domains are required for
CC methyltransferase activity. The SET domain also participates in stable
CC binding to heterochromatin (By similarity). {ECO:0000250}.
CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC arranged in a triangular cluster; some of these Cys residues contribute
CC to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine residues, and to a lesser degree, on
CC threonine residues. The phosphorylated form is stabilized by SBF1 and
CC is less active in its transcriptional repressor function (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylated at Lys-266, leading to inhibition of enzyme activity.
CC SIRT1-mediated deacetylation relieves this inhibition (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00912}.
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DR EMBL; BC111156; AAI11157.1; -; mRNA.
DR RefSeq; NP_001039729.1; NM_001046264.2.
DR AlphaFoldDB; Q2NL30; -.
DR SMR; Q2NL30; -.
DR STRING; 9913.ENSBTAP00000006178; -.
DR PaxDb; Q2NL30; -.
DR PRIDE; Q2NL30; -.
DR GeneID; 523047; -.
DR KEGG; bta:523047; -.
DR CTD; 6839; -.
DR eggNOG; KOG1082; Eukaryota.
DR InParanoid; Q2NL30; -.
DR OrthoDB; 753093at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0036123; P:histone H3-K9 dimethylation; ISS:UniProtKB.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; ISS:UniProtKB.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR011381; Histone_H3-K9_MeTrfase.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF009343; SUV39_SET; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS51579; SAM_MT43_SUVAR39_3; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Biological rhythms; Cell cycle; Centromere;
KW Chromatin regulator; Chromosome; Differentiation; Metal-binding;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW rRNA processing; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..412
FT /note="Histone-lysine N-methyltransferase SUV39H1"
FT /id="PRO_0000281809"
FT DOMAIN 43..101
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 179..240
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 243..366
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 396..412
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..89
FT /note="Interaction with SIRT1"
FT /evidence="ECO:0000250"
FT REGION 255..377
FT /note="Mediates interaction with MECOM"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 254..256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 323..324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 266
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43463"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43463"
SQ SEQUENCE 412 AA; 47846 MW; 723990F42CDFAFC2 CRC64;
MAESLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGISKRNL YDFEVEYLCD YKKIREQEYY
LVKWRGYPDS ESTWEPRQNL KCVRILKQFH KDLERELLRR HHRSKPPRHL DPSLANYLVQ
KAKQRRALRR WEQELNAKRS HLGRITVENE VDLDGPPRAF VYINEYRVGE GITLNQVAVG
CECQDCLWAP AGGCCPGASL HKFAYNDQGQ VRLRAGLPIY ECNSRCRCGY DCPNRVVQKG
IRYDLCIFRT DDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD
LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF ATRTIRAGEE
LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC KCGTESCRKY LF
