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Database: UniProt
Entry: Q4R3E0
LinkDB: Q4R3E0
Original site: Q4R3E0 
ID   SUV92_MACFA             Reviewed;         410 AA.
AC   Q4R3E0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   10-APR-2019, entry version 79.
DE   RecName: Full=Histone-lysine N-methyltransferase SUV39H2;
DE            EC=2.1.1.43;
DE   AltName: Full=Suppressor of variegation 3-9 homolog 2;
DE            Short=Su(var)3-9 homolog 2;
GN   Name=SUV39H2; ORFNames=QtsA-17663;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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 cell cycle regulation,
CC       transcriptional repression and regulation of telomere length. May
CC       participate in regulation of higher-order chromatin organization
CC       during spermatogenesis. Recruited by the large PER complex to the
CC       E-box elements of the circadian target genes such as PER2 itself
CC       or PER1, 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:
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU00912};
CC   -!- SUBUNIT: Interacts with SMAD5. The large PER complex involved in
CC       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}. Chromosome,
CC       centromere {ECO:0000250}. Note=Associates with centromeric
CC       constitutive heterochromatin. {ECO:0000250}.
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE02377.1; Type=Erroneous termination; Positions=411; Note=Translated as stop.; Evidence={ECO:0000305};
DR   EMBL; AB179326; BAE02377.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001306534.1; NM_001319605.1.
DR   RefSeq; XP_005564732.1; XM_005564675.2.
DR   UniGene; Mfa.7348; -.
DR   ProteinModelPortal; Q4R3E0; -.
DR   SMR; Q4R3E0; -.
DR   STRING; 9541.XP_005564730.1; -.
DR   Ensembl; ENSMFAT00000067200; ENSMFAP00000016665; ENSMFAG00000031495.
DR   GeneID; 102136014; -.
DR   KEGG; mcf:102136014; -.
DR   CTD; 79723; -.
DR   GeneTree; ENSGT00940000156788; -.
DR   HOVERGEN; HBG055621; -.
DR   KO; K11419; -.
DR   GO; GO:0000775; C:chromosome, centromeric region; 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: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   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   Biological rhythms; Cell cycle; Centromere; Chromatin regulator;
KW   Chromosome; Differentiation; Metal-binding; Methyltransferase;
KW   Nucleus; Phosphoprotein; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Zinc.
FT   CHAIN         1    410       Histone-lysine N-methyltransferase
FT                                SUV39H2.
FT                                /FTId=PRO_0000281814.
FT   DOMAIN       47    105       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      189    247       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      250    373       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      394    410       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      261    263       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      330    331       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       191    191       Zinc 1. {ECO:0000250}.
FT   METAL       191    191       Zinc 2. {ECO:0000250}.
FT   METAL       193    193       Zinc 1. {ECO:0000250}.
FT   METAL       196    196       Zinc 1. {ECO:0000250}.
FT   METAL       196    196       Zinc 3. {ECO:0000250}.
FT   METAL       201    201       Zinc 1. {ECO:0000250}.
FT   METAL       202    202       Zinc 1. {ECO:0000250}.
FT   METAL       202    202       Zinc 2. {ECO:0000250}.
FT   METAL       229    229       Zinc 2. {ECO:0000250}.
FT   METAL       229    229       Zinc 3. {ECO:0000250}.
FT   METAL       233    233       Zinc 2. {ECO:0000250}.
FT   METAL       235    235       Zinc 3. {ECO:0000250}.
FT   METAL       239    239       Zinc 3. {ECO:0000250}.
FT   METAL       333    333       Zinc 4. {ECO:0000250}.
FT   METAL       398    398       Zinc 4. {ECO:0000250}.
FT   METAL       400    400       Zinc 4. {ECO:0000250}.
FT   METAL       405    405       Zinc 4. {ECO:0000250}.
FT   BINDING     304    304       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES     381    381       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   MOD_RES     384    384       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   MOD_RES     388    388       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
SQ   SEQUENCE   410 AA;  46681 MW;  B5A91D08A1104350 CRC64;
     MAAVGAEARG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE YLCDYKVVKD
     MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY LSQVKKGKAI TPKNNNKTLK
     PAIAEYIVKK AKQRIALQRW QDELNRRKNH KGMIFVENTV DLEGPPSDFY YINEYKPAPG
     ISLVNEATFG CSCTDCFFQK CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP
     NRIVQKGTQY SLCIFRTSNG RGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQFYDNK
     GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR LPRIALFSTR
     TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC GAVTCRGYLN
//
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