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Database: UniProt/SWISS-PROT
Entry: SUV91_PONAB
LinkDB: SUV91_PONAB
Original site: SUV91_PONAB 
ID   SUV91_PONAB             Reviewed;         412 AA.
AC   Q5RB81; Q5RAM0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   22-NOV-2017, entry version 84.
DE   RecName: Full=Histone-lysine N-methyltransferase SUV39H1;
DE            EC=2.1.1.43;
DE   AltName: Full=Suppressor of variegation 3-9 homolog 1;
DE            Short=Su(var)3-9 homolog 1;
GN   Name=SUV39H1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-
CC       9' as substrate. H3 'Lys-9' trimethylation represents a specific
CC       tag for epigenetic transcriptional repression by recruiting HP1
CC       (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly
CC       functions in heterochromatin regions, thereby playing a central
CC       role in the establishment of constitutive heterochromatin at
CC       pericentric and telomere regions. H3 'Lys-9' trimethylation is
CC       also required to direct DNA methylation at pericentric repeats.
CC       SUV39H1 is targeted to histone H3 via its interaction with RB1 and
CC       is involved in many processes, such as repression of MYOD1-
CC       stimulated differentiation, regulation of the control switch for
CC       exiting the cell cycle and entering differentiation, repression by
CC       the PML-RARA fusion protein, BMP-induced repression, repression of
CC       switch recombination to IgA and regulation of telomere length.
CC       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-
CC       modifying enzymes. The eNoSC complex is able to sense the energy
CC       status of cell: upon glucose starvation, elevation of
CC       NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3
CC       deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2)
CC       by SUV39H1 and the formation of silent chromatin in the rDNA
CC       locus. Recruited by the large PER complex to the E-box elements of
CC       the circadian target genes such as PER2 itself or PER1,
CC       contributes to the conversion of local chromatin to a
CC       heterochromatin-like repressive state through H3 'Lys-9'
CC       trimethylation (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00912}.
CC   -!- ENZYME 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
CC       RB1. Interacts with SBF1 through the SET domain. Interacts with
CC       HDAC1 and HDAC2 through the N-terminus and associates with the
CC       core histone deacetylase complex composed of HDAC1, HDAC2, RBBP4
CC       and RBBP7. Component of the eNoSC complex, composed of SIRT1,
CC       SUV39H1 and RRP8. Interacts (via SET domain) with MECOM; enhances
CC       MECOM transcriptional repression activity. Interacts with LMNA;
CC       the interaction increases stability of SUV39H1. The large PER
CC       complex involved in the histone methylation is composed of at
CC       least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates
CC       the formation of the 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
CC       constitutive heterochromatin. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5RB81-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5RB81-2; Sequence=VSP_024062;
CC         Note=No experimental confirmation available.;
CC   -!- DOMAIN: Although the SET domain contains the active site of
CC       enzymatic activity, both pre-SET and post-SET domains are required
CC       for methyltransferase activity. The SET domain also participates
CC       in stable binding to heterochromatin (By similarity).
CC       {ECO:0000250}.
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   -!- PTM: Phosphorylated on serine residues, and to a lesser degree, on
CC       threonine residues. The phosphorylated form is stabilized by SBF1
CC       and is less active in its transcriptional repressor function (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Acetylated at Lys-266, leading to inhibition of enzyme
CC       activity. SIRT1-mediated deacetylation relieves this inhibition
CC       (By similarity). {ECO:0000250}.
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:PRU00912}.
DR   EMBL; CR858772; CAH90979.1; -; mRNA.
DR   EMBL; CR858995; CAH91190.1; -; mRNA.
DR   RefSeq; NP_001125697.1; NM_001132225.1. [Q5RB81-2]
DR   ProteinModelPortal; Q5RB81; -.
DR   SMR; Q5RB81; -.
DR   STRING; 9601.ENSPPYP00000022743; -.
DR   GeneID; 100172621; -.
DR   KEGG; pon:100172621; -.
DR   CTD; 6839; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOVERGEN; HBG055621; -.
DR   InParanoid; Q5RB81; -.
DR   KO; K11419; -.
DR   Proteomes; UP000001595; 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 regulatory region sequence-specific DNA 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: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   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd00024; CHROMO; 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   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   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; Alternative splicing; Biological rhythms; Cell cycle;
KW   Centromere; Chromatin regulator; Chromosome; Complete proteome;
KW   Differentiation; Metal-binding; Methyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; rRNA processing;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc.
FT   CHAIN         1    412       Histone-lysine N-methyltransferase
FT                                SUV39H1.
FT                                /FTId=PRO_0000281810.
FT   DOMAIN       43    101       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      179    240       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      243    366       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      396    412       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION        1     89       Interaction with SIRT1. {ECO:0000250}.
FT   REGION      254    256       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      255    377       Mediates interaction with MECOM.
FT                                {ECO:0000250}.
FT   REGION      323    324       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       181    181       Zinc 1. {ECO:0000250}.
FT   METAL       181    181       Zinc 2. {ECO:0000250}.
FT   METAL       183    183       Zinc 1. {ECO:0000250}.
FT   METAL       186    186       Zinc 1. {ECO:0000250}.
FT   METAL       186    186       Zinc 3. {ECO:0000250}.
FT   METAL       194    194       Zinc 1. {ECO:0000250}.
FT   METAL       195    195       Zinc 1. {ECO:0000250}.
FT   METAL       195    195       Zinc 2. {ECO:0000250}.
FT   METAL       222    222       Zinc 2. {ECO:0000250}.
FT   METAL       222    222       Zinc 3. {ECO:0000250}.
FT   METAL       226    226       Zinc 2. {ECO:0000250}.
FT   METAL       228    228       Zinc 3. {ECO:0000250}.
FT   METAL       232    232       Zinc 3. {ECO:0000250}.
FT   METAL       326    326       Zinc 4. {ECO:0000250}.
FT   METAL       400    400       Zinc 4. {ECO:0000250}.
FT   METAL       402    402       Zinc 4. {ECO:0000250}.
FT   METAL       407    407       Zinc 4. {ECO:0000250}.
FT   BINDING     297    297       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES     266    266       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:O43463}.
FT   MOD_RES     391    391       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O43463}.
FT   VAR_SEQ       1      6       MAENLK -> MVGMSRLRNDRLADPLT (in isoform
FT                                2). {ECO:0000303|Ref.1}.
FT                                /FTId=VSP_024062.
SQ   SEQUENCE   412 AA;  47907 MW;  AF6F959AD20C6C76 CRC64;
     MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGISKRNL YDFEVEYLCD YKKIREQEYY
     LVKWRGYPDS ESTWEPRQNL KCVRILKQFH KDLERELLRR HHRSKTPRHL DPSLANYLVQ
     KAKQRRALRR WEQELNAKRS HLGRITVENE VDLDGPPRAF VYINEYRVGE GITLNQVAVG
     CECQDCLWAP TGGCCPGASL HKFAYNDQGQ VRLRAGLPIY ECNSRCRCGY DCPNRVVQKG
     IRYDLCIFRT DDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD
     LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF ATRTIRAGEE
     LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC KCGTESCRKY LF
//
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