| Tag |
Content |
| WERAM ID |
WERAM-Hos-0062 |
| Ensembl Protein ID |
ENSP00000365877.3 |
| Uniprot Accession |
O43463; SUV91_HUMAN; B2R6E8; B4DST0; Q53G60; Q6FHK6
|
| Genbank Protein ID |
NP_001269095.1; NP_003164.1
|
| Protein Name |
Histone-lysine N-methyltransferase SUV39H1 |
| Genbank Nucleotide ID |
NM_001282166.1; NM_003173.3
|
| Gene Name |
SUV39H1;MG44;KMT1A;H3-K9-HMTase1;SUV39H |
| Ensembl Information |
|
| Details |
|
| Status |
Reviewed |
| Classification |
| Type |
Family |
E-value |
Score |
Start |
End |
| HMT |
SUV39 |
2.00e-42 |
147 |
244 |
366 |
| HMT |
SET1 |
2.40e-27 |
97.7 |
248 |
366 |
| Me_Reader |
Chromodomain |
1.80e-19 |
71.8 |
43 |
98 |
|
| Organism |
Homo sapiens |
| NCBI Taxa ID |
9606 |
Functional Description
(View)Functional Description
Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. |
Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.
|
| Domain Profile |
HMT SUV39
SUV39.txt 2 rLqvfktenk.GwGvrclddiakgsFvciyaGeiltddeaekegl...eegdeyladldskes 60
L +f+t++ GwGvr+l++i+k sFv++y+Gei+t++eae++g+ ++g +yl+dld++e+
ENSP00000365877.3 244 DLCIFRTDDGrGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQiydRQGATYLFDLDYVED 306
699*****988********************************8889999*********9876 PP
SUV39.txt 89 eseyiidakkegnvgrflnHscspNlfvqnvfvdthdlrfprvafFaskrikagtELtwdYg 150
e++y++da+++gn+++f+nHsc+pNl v nvf+d+ d+r+pr+afFa+++i+ag+ELt+dY+
ENSP00000365877.3 305 EDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYN 366
789**********************************************************7 PP
HMT SET1
SET1.txt 5 vakskikglglvakkeiekeelviEYvGevirsevadkrekeyekkeigvylfrldedae.vvvdatkkgniarfinhscepNceakvvavd 95
+++++ +g+g+++ ++i+k+ +v+EYvGe+i se+a++r + y+++++ +ylf ld ++ + vda gni++f+nhsc+pN+++ v +d
ENSP00000365877.3 248 FRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA-TYLFDLDYVEDvYTVDAAYYGNISHFVNHSCDPNLQVYNVFID 338
6789999**************************************955.6******9888799**********************9999887 PP
SET1.txt 96 ge....kkiviyakraIekgeeltydYk 119
+ +i +a+r+I++geelt+dY+
ENSP00000365877.3 339 NLderlPRIAFFATRTIRAGEELTFDYN 366
64222369*******************7 PP
Me_Reader Chromodomain
Chromodomain.txt 1 FeverivdkkelrkgeveYlVrWkGynksddtWepeenLlckelleefekkkekkkk 57
Feve+++d+k++r++e+ YlV+W+Gy++s++tWep++nL+c+++l++f+k+ e++ +
ENSP00000365877.3 43 FEVEYLCDYKKIREQEY-YLVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELL 98
9****************.*********************************999865 PP
|
Protein Sequence
(Fasta) | MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGISKRNL YDFEVEYLCD YKKIREQEYY 60
LVKWRGYPDS ESTWEPRQNL KCVRILKQFH KDLERELLRR HHRSKTPRHL DPSLANYLVQ 120
KAKQRRALRR WEQELNAKRS HLGRITVENE VDLDGPPRAF VYINEYRVGE GITLNQVAVG 180
CECQDCLWAP TGGCCPGASL HKFAYNDQGQ VRLRAGLPIY ECNSRCRCGY DCPNRVVQKG 240
IRYDLCIFRT DDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD 300
LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF ATRTIRAGEE 360
LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC KCGTESCRKY LF 412Protein Fasta Sequence
>ENSP00000365877.3|SUV39H1;MG44;KMT1A;H3-K9-HMTase1;SUV39H|Homo sapiens
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKGIRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF |
Nucleotide Sequence
(Fasta) | GCGGCGAGCA CCCGCCTCCG GGACCGAGCC GGGCGGCAGG GAGGGGTTCG GTCACGGCTC 60
TCCGGTTGGT CCGCGCGGGT GCTGCGAGTC GGGAGCCGCG GCCAATAGGC TGCGCGTTCC 120
CGGCCACGCC CGCGCGAGCG CTCTTCTCGC GAGGCCGGCT AGGCCCGAAT GTCGTTAGCC 180
GTGGGGAAAG ATGGCGGAAA ATTTAAAAGG CTGCAGCGTG TGTTGCAAGT CTTCTTGGAA 240
TCAGCTGCAG GACCTGTGCC GCCTGGCCAA GCTCTCCTGC CCTGCCCTCG GTATCTCTAA 300
GAGGAACCTC TATGACTTTG AAGTCGAGTA CCTGTGCGAT TACAAGAAGA TCCGCGAACA 360
GGAATATTAC CTGGTGAAAT GGCGTGGATA TCCAGACTCA GAGAGCACCT GGGAGCCACG 420
GCAGAATCTC AAGTGTGTGC GTATCCTCAA GCAGTTCCAC AAGGACTTAG AAAGGGAGCT 480
GCTCCGGCGG CACCACCGGT CAAAGACCCC CCGGCACCTG GACCCAAGCT TGGCCAACTA 540
CCTGGTGCAG AAGGCCAAGC AGAGGCGGGC GCTCCGTCGC TGGGAGCAGG AGCTCAATGC 600
CAAGCGCAGC CATCTGGGAC GCATCACTGT AGAGAATGAG GTGGACCTGG ACGGCCCTCC 660
GCGGGCCTTC GTGTACATCA ATGAGTACCG TGTTGGTGAG GGCATCACCC TCAACCAGGT 720
GGCTGTGGGC TGCGAGTGCC AGGACTGTCT GTGGGCACCC ACTGGAGGCT GCTGCCCGGG 780
GGCGTCACTG CACAAGTTTG CCTACAATGA CCAGGGCCAG GTGCGGCTTC GAGCCGGGCT 840
GCCCATCTAC GAGTGCAACT CCCGCTGCCG CTGCGGCTAT GACTGCCCAA ATCGTGTGGT 900
ACAGAAGGGT ATCCGATATG ACCTCTGCAT CTTCCGCACG GATGATGGGC GTGGCTGGGG 960
CGTCCGCACC CTGGAGAAGA TTCGCAAGAA CAGCTTCGTC ATGGAGTACG TGGGAGAGAT 1020
CATTACCTCA GAGGAGGCAG AGCGGCGGGG CCAGATCTAC GACCGTCAGG GCGCCACCTA 1080
CCTCTTTGAC CTGGACTACG TGGAGGACGT GTACACCGTG GATGCCGCCT ACTATGGCAA 1140
CATCTCCCAC TTTGTCAACC ACAGTTGTGA CCCCAACCTG CAGGTGTACA ACGTCTTCAT 1200
AGACAACCTT GACGAGCGGC TGCCCCGCAT CGCTTTCTTT GCCACAAGAA CCATCCGGGC 1260
AGGCGAGGAG CTCACCTTTG ATTACAACAT GCAAGTGGAC CCCGTGGACA TGGAGAGCAC 1320
CCGCATGGAC TCCAACTTTG GCCTGGCTGG GCTCCCTGGC TCCCCTAAGA AGCGGGTCCG 1380
TATTGAATGC AAGTGTGGGA CTGAGTCCTG CCGCAAATAC CTCTTCTAGC CCTTAGAAGT 1440
CTGAGGCCAG ACTGACTGAG GGGGCCTGAA GCTACATGCA CCTCCCCCAC TGCTGCCCTC 1500
CTGTCGAGAA TGACTGCCAG GGCCTCGCCT GCCTCCACCT GCCCCCACCT GCTCCTACCT 1560
GCTCTACGTT CAGGGCTGTG GCCGTGGTGA GGACCGACTC CAGGAGTCCC CTTTCCCTGT 1620
CCCAGCCCCA TCTGTGGGTT GCACTTACAA ACCCCCACCC ACCTTCAGAA ATAGTTTTTC 1680
AACATCAAGA CTCTCTGTCG TTGGGATTCA TGGCCTATTA AGGAGGTCCA AGGGGTGAGT 1740
CCCAACCCAG CCCCAGAATA TATTTGTTTT TGCACCTGCT TCTGCCTGGA GATTGAGGGG 1800
TCTGCTGCAG GCCTCCTCCC TGCTGCCCCA AAGGTATGGG GAAGCAACCC CAGAGCAGGC 1860
AGACATCAGA GGCCAGAGTG CCTAGCCCGA CATGAAGCTG GTTCCCCAAC CACAGAAACT 1920
TTGTACTAGT GAAAGAAAGG GGGTCCCTGG GCTACGGGCT GAGGCTGGTT TCTGCTCGTG 1980
CTTACAGTGC TGGGTAGTGT TGGCCCTAAG AGCTGTAGGG TCTCTTCTTC AGGGCTGCAT 2040
ATCTGAGAAG TGGATGCCCA CATGCCACTG GAAGGGAAGT GGGTGTCCAT GGGCCACTGA 2100
GCAGTGAGAG GAAGGCAGTG CAGAGCTGGC CAGCCCTGGA GGTAGGCTGG GACCAAGCTC 2160
TGCCTTCACA GTGCAGTGAA GGTACCTAGG GCTCTTGGGA GCTCTGCGGT TGCTAGGGGC 2220
CCTGACCTGG GGTGTCATGA CCGCTGACAC CACTCAGAGC TGGAACCAAG ATCTAGATAG 2280
TCCGTAGATA GCACTTAGGA CAAGAATGTG CATTGATGGG GTGGTGATGA GGTGCCAGGC 2340
ACTGGGTAGA GCACCTGGTC CACGTGGATT GTCTCAGGGA AGCCTTGAAA ACCACGGAGG 2400
TGGATGCCAG GAAAGGGCCC ATGTGGCAGA AGGCAAAGTA CAGGCCAAGA ATTGGGGGTG 2460
GGGGAGATGG CTTCCCCACT ATGGGATGAC GAGGCGAGAG GGAAGCCCTT GCTGCCTGCC 2520
ATTCCCAGAC CCCAGCCCTT TGTGCTCACC CTGGTTCCAC TGGTCTCAAA AGTCACCTGC 2580
CTACAAATGT ACAAAAGGCG AAGGTTCTGA TGGCTGCCTT GCTCCTTGCT CCCCCACCCC 2640
CTGTGAGGAC TTCTCTAGGA AGTCCTTCCT GACTACCTGT GCCCAGAGTG CCCCTACATG 2700
AGACTGTATG CCCTGCTATC AGATGCCAGA TCTATGTGTC TGTCTGTGTG TCCATCCCGC 2760
CGGCCCCCCA GACTAACCTC CAGGCATGGA CTGAATCTGG TTCTCCTCTT GTACACCCCT 2820
CAACCCTATG CAGCCTGGAG TGGGCATCAA TAAAATGAAC TGTCGACTGA A
2872Nucleotide Fasta Sequence
>ENSP00000365877.3|Chromodomain|Homo sapiens
GCGGCGAGCACCCGCCTCCGGGACCGAGCCGGGCGGCAGGGAGGGGTTCGGTCACGGCTCTCCGGTTGGTCCGCGCGGGTGCTGCGAGTCGGGAGCCGCGGCCAATAGGCTGCGCGTTCCCGGCCACGCCCGCGCGAGCGCTCTTCTCGCGAGGCCGGCTAGGCCCGAATGTCGTTAGCCGTGGGGAAAGATGGCGGAAAATTTAAAAGGCTGCAGCGTGTGTTGCAAGTCTTCTTGGAATCAGCTGCAGGACCTGTGCCGCCTGGCCAAGCTCTCCTGCCCTGCCCTCGGTATCTCTAAGAGGAACCTCTATGACTTTGAAGTCGAGTACCTGTGCGATTACAAGAAGATCCGCGAACAGGAATATTACCTGGTGAAATGGCGTGGATATCCAGACTCAGAGAGCACCTGGGAGCCACGGCAGAATCTCAAGTGTGTGCGTATCCTCAAGCAGTTCCACAAGGACTTAGAAAGGGAGCTGCTCCGGCGGCACCACCGGTCAAAGACCCCCCGGCACCTGGACCCAAGCTTGGCCAACTACCTGGTGCAGAAGGCCAAGCAGAGGCGGGCGCTCCGTCGCTGGGAGCAGGAGCTCAATGCCAAGCGCAGCCATCTGGGACGCATCACTGTAGAGAATGAGGTGGACCTGGACGGCCCTCCGCGGGCCTTCGTGTACATCAATGAGTACCGTGTTGGTGAGGGCATCACCCTCAACCAGGTGGCTGTGGGCTGCGAGTGCCAGGACTGTCTGTGGGCACCCACTGGAGGCTGCTGCCCGGGGGCGTCACTGCACAAGTTTGCCTACAATGACCAGGGCCAGGTGCGGCTTCGAGCCGGGCTGCCCATCTACGAGTGCAACTCCCGCTGCCGCTGCGGCTATGACTGCCCAAATCGTGTGGTACAGAAGGGTATCCGATATGACCTCTGCATCTTCCGCACGGATGATGGGCGTGGCTGGGGCGTCCGCACCCTGGAGAAGATTCGCAAGAACAGCTTCGTCATGGAGTACGTGGGAGAGATCATTACCTCAGAGGAGGCAGAGCGGCGGGGCCAGATCTACGACCGTCAGGGCGCCACCTACCTCTTTGACCTGGACTACGTGGAGGACGTGTACACCGTGGATGCCGCCTACTATGGCAACATCTCCCACTTTGTCAACCACAGTTGTGACCCCAACCTGCAGGTGTACAACGTCTTCATAGACAACCTTGACGAGCGGCTGCCCCGCATCGCTTTCTTTGCCACAAGAACCATCCGGGCAGGCGAGGAGCTCACCTTTGATTACAACATGCAAGTGGACCCCGTGGACATGGAGAGCACCCGCATGGACTCCAACTTTGGCCTGGCTGGGCTCCCTGGCTCCCCTAAGAAGCGGGTCCGTATTGAATGCAAGTGTGGGACTGAGTCCTGCCGCAAATACCTCTTCTAGCCCTTAGAAGTCTGAGGCCAGACTGACTGAGGGGGCCTGAAGCTACATGCACCTCCCCCACTGCTGCCCTCCTGTCGAGAATGACTGCCAGGGCCTCGCCTGCCTCCACCTGCCCCCACCTGCTCCTACCTGCTCTACGTTCAGGGCTGTGGCCGTGGTGAGGACCGACTCCAGGAGTCCCCTTTCCCTGTCCCAGCCCCATCTGTGGGTTGCACTTACAAACCCCCACCCACCTTCAGAAATAGTTTTTCAACATCAAGACTCTCTGTCGTTGGGATTCATGGCCTATTAAGGAGGTCCAAGGGGTGAGTCCCAACCCAGCCCCAGAATATATTTGTTTTTGCACCTGCTTCTGCCTGGAGATTGAGGGGTCTGCTGCAGGCCTCCTCCCTGCTGCCCCAAAGGTATGGGGAAGCAACCCCAGAGCAGGCAGACATCAGAGGCCAGAGTGCCTAGCCCGACATGAAGCTGGTTCCCCAACCACAGAAACTTTGTACTAGTGAAAGAAAGGGGGTCCCTGGGCTACGGGCTGAGGCTGGTTTCTGCTCGTGCTTACAGTGCTGGGTAGTGTTGGCCCTAAGAGCTGTAGGGTCTCTTCTTCAGGGCTGCATATCTGAGAAGTGGATGCCCACATGCCACTGGAAGGGAAGTGGGTGTCCATGGGCCACTGAGCAGTGAGAGGAAGGCAGTGCAGAGCTGGCCAGCCCTGGAGGTAGGCTGGGACCAAGCTCTGCCTTCACAGTGCAGTGAAGGTACCTAGGGCTCTTGGGAGCTCTGCGGTTGCTAGGGGCCCTGACCTGGGGTGTCATGACCGCTGACACCACTCAGAGCTGGAACCAAGATCTAGATAGTCCGTAGATAGCACTTAGGACAAGAATGTGCATTGATGGGGTGGTGATGAGGTGCCAGGCACTGGGTAGAGCACCTGGTCCACGTGGATTGTCTCAGGGAAGCCTTGAAAACCACGGAGGTGGATGCCAGGAAAGGGCCCATGTGGCAGAAGGCAAAGTACAGGCCAAGAATTGGGGGTGGGGGAGATGGCTTCCCCACTATGGGATGACGAGGCGAGAGGGAAGCCCTTGCTGCCTGCCATTCCCAGACCCCAGCCCTTTGTGCTCACCCTGGTTCCACTGGTCTCAAAAGTCACCTGCCTACAAATGTACAAAAGGCGAAGGTTCTGATGGCTGCCTTGCTCCTTGCTCCCCCACCCCCTGTGAGGACTTCTCTAGGAAGTCCTTCCTGACTACCTGTGCCCAGAGTGCCCCTACATGAGACTGTATGCCCTGCTATCAGATGCCAGATCTATGTGTCTGTCTGTGTGTCCATCCCGCCGGCCCCCCAGACTAACCTCCAGGCATGGACTGAATCTGGTTCTCCTCTTGTACACCCCTCAACCCTATGCAGCCTGGAGTGGGCATCAATAAAATGAACTGTCGACTGAA
|
| Sequence Source |
Ensembl |
| Keyword |
KW-0002--3D-structure
KW-0007--Acetylation
KW-0025--Alternative splicing
KW-0090--Biological rhythms
KW-0131--Cell cycle
KW-0137--Centromere
KW-0156--Chromatin regulator
KW-0158--Chromosome
KW-0181--Complete proteome
KW-0221--Differentiation
KW-0945--Host-virus interaction
KW-0479--Metal-binding
KW-0489--Methyltransferase
KW-0539--Nucleus
KW-0597--Phosphoprotein
KW-1185--Reference proteome
KW-0678--Repressor
KW-0698--rRNA processing
KW-0949--S-adenosyl-L-methionine
KW-0804--Transcription
KW-0805--Transcription regulation
KW-0808--Transferase
KW-0862--Zinc
--
|
| Interpro |
IPR000953--Chromo/shadow_dom
IPR023780--Chromo_domain
IPR016197--Chromodomain-like
IPR023779--Chromodomain_CS
IPR011381--Histone_H3-K9_MeTrfase
IPR003616--Post-SET_dom
IPR007728--Pre-SET_dom
IPR001214--SET_dom
|
| PROSITE |
PS00598--CHROMO_1
PS50013--CHROMO_2
PS50868--POST_SET
PS50867--PRE_SET
PS51579--SAM_MT43_SUVAR39_3
PS50280--SET
|
| Pfam |
PF00385--Chromo
PF05033--Pre-SET
PF00856--SET
|
| Gene Ontology |
GO:0005677--C:chromatin silencing complex
GO:0000775--C:chromosome, centromeric region
GO:0000794--C:condensed nuclear chromosome
GO:0000792--C:heterochromatin
GO:0005652--C:nuclear lamina
GO:0005654--C:nucleoplasm
GO:0005634--C:nucleus
GO:0033553--C:rDNA heterochromatin
GO:0003682--F:chromatin binding
GO:0042054--F:histone methyltransferase activity
GO:0046974--F:histone methyltransferase activity (H3-K9 specific)
GO:0018024--F:histone-lysine N-methyltransferase activity
GO:0047485--F:protein N-terminus binding
GO:0008757--F:S-adenosylmethionine-dependent methyltransferase activity
GO:0000976--F:transcription regulatory region sequence-specific DNA binding
GO:0008270--F:zinc ion binding
GO:0007049--P:cell cycle
GO:0030154--P:cell differentiation
GO:0006974--P:cellular response to DNA damage stimulus
GO:0071456--P:cellular response to hypoxia
GO:0006325--P:chromatin organization
GO:0000183--P:chromatin silencing at rDNA
GO:0036123--P:histone H3-K9 dimethylation
GO:0036124--P:histone H3-K9 trimethylation
GO:0042754--P:negative regulation of circadian rhythm
GO:0000122--P:negative regulation of transcription from RNA polymerase II promoter
GO:0045892--P:negative regulation of transcription, DNA-templated
GO:0048511--P:rhythmic process
GO:0006364--P:rRNA processing
GO:0006351--P:transcription, DNA-templated
GO:0016032--P:viral process
|
| Orthology |
|
| Created Date |
25-Jun-2016 |
