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Protein

Histone-lysine N-methyltransferase SUV39H1

Gene

SUV39H1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation2 Publications

Enzyme regulationi

Inhibited by S-adenosyl-L-homocysteine. Negatively regulated by CCAR2.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi181 – 1811Zinc 1By similarity
Metal bindingi181 – 1811Zinc 2By similarity
Metal bindingi183 – 1831Zinc 1By similarity
Metal bindingi186 – 1861Zinc 1By similarity
Metal bindingi186 – 1861Zinc 3By similarity
Metal bindingi194 – 1941Zinc 1By similarity
Metal bindingi195 – 1951Zinc 1By similarity
Metal bindingi195 – 1951Zinc 2By similarity
Metal bindingi222 – 2221Zinc 2By similarity
Metal bindingi222 – 2221Zinc 3By similarity
Metal bindingi226 – 2261Zinc 2By similarity
Metal bindingi228 – 2281Zinc 3By similarity
Metal bindingi232 – 2321Zinc 3By similarity
Binding sitei297 – 2971S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi326 – 3261Zinc 4By similarity
Metal bindingi400 – 4001Zinc 4By similarity
Metal bindingi402 – 4021Zinc 4By similarity
Metal bindingi407 – 4071Zinc 4By similarity

GO - Molecular functioni

  • chromatin binding Source: ProtInc
  • histone-lysine N-methyltransferase activity Source: UniProtKB
  • histone methyltransferase activity Source: UniProtKB
  • histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • S-adenosylmethionine-dependent methyltransferase activity Source: UniProtKB
  • transcription regulatory region sequence-specific DNA binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: MGI
  • cellular response to hypoxia Source: MGI
  • chromatin organization Source: ProtInc
  • chromatin silencing at rDNA Source: UniProtKB
  • histone H3-K9 dimethylation Source: UniProtKB
  • histone H3-K9 trimethylation Source: UniProtKB
  • negative regulation of circadian rhythm Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • rhythmic process Source: UniProtKB-KW
  • rRNA processing Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Differentiation, Host-virus interaction, rRNA processing, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SUV39H1 (EC:2.1.1.43)
Alternative name(s):
Histone H3-K9 methyltransferase 1
Short name:
H3-K9-HMTase 1
Lysine N-methyltransferase 1A
Position-effect variegation 3-9 homolog
Suppressor of variegation 3-9 homolog 1
Short name:
Su(var)3-9 homolog 1
Gene namesi
Name:SUV39H1
Synonyms:KMT1A, SUV39H
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11479. SUV39H1.

Subcellular locationi

GO - Cellular componenti

  • chromatin silencing complex Source: UniProtKB
  • chromosome, centromeric region Source: UniProtKB-SubCell
  • condensed nuclear chromosome Source: ProtInc
  • heterochromatin Source: UniProtKB
  • nuclear lamina Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • rDNA heterochromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641W → A: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi67 – 671Y → A: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi266 – 2661K → A: Loss of SIRT1-mediated up-regulation of enzymatic activity. 1 Publication
Mutagenesisi266 – 2661K → Q: Significant loss of enzymatic activity. 1 Publication
Mutagenesisi320 – 3201H → R: Strongly increases methylation of histone H3. 1 Publication
Mutagenesisi324 – 3241H → L or K: Abolishes methylation of histone H3. 1 Publication
Mutagenesisi326 – 3261C → A: Abolishes methylation of histone H3. 1 Publication

Organism-specific databases

PharmGKBiPA36264.

Chemistry

ChEMBLiCHEMBL1795118.
GuidetoPHARMACOLOGYi2715.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Histone-lysine N-methyltransferase SUV39H1PRO_0000186057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661N6-acetyllysine1 Publication
Modified residuei391 – 3911PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on serine residues, and to a lesser degree, on threonine residues. The phosphorylated form is stabilized by SBF1 and is less active in its transcriptional repressor function.1 Publication
Acetylated at Lys-266, leading to inhibition of enzyme activity. SIRT1-mediated deacetylation relieves this inhibition.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO43463.
MaxQBiO43463.
PaxDbiO43463.
PeptideAtlasiO43463.
PRIDEiO43463.

PTM databases

iPTMnetiO43463.
PhosphoSiteiO43463.

Expressioni

Developmental stagei

Accumulates during mitosis at centromeres during prometaphase, but dissociates from the centromere at the meta- to anaphase transition.

Gene expression databases

BgeeiO43463.
CleanExiHS_SUV39H1.
GenevisibleiO43463. HS.

Interactioni

Subunit structurei

Interacts with H3 and H4 histones. Interacts with GFI1B, DNMT3B, CBX1, CBX4, CCAR2, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and RB1. Interacts with SBF1 through the SET domain. Interacts with HDAC1 and HDAC2 through the N-terminus and associates with the core histone deacetylase complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. In case of infection, interacts with HTLV-1 Tax protein, leading to abrogate Tax transactivation of HTLV-1 LTR. Interacts (via SET domain) with MECOM; enhances MECOM transcriptional repression activity. Interacts with LMNA; the interaction increases stability of SUV39H1. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P684322EBI-349968,EBI-79764From a different organism.
ATE1O952602EBI-349968,EBI-1043378
BCL11BQ9C0K03EBI-349968,EBI-6597578
C8orf74Q6P0472EBI-349968,EBI-8466055
CBX5P459733EBI-349968,EBI-78219
CCDC151A5D8V72EBI-349968,EBI-8466445
CDCA4Q9BXL82EBI-349968,EBI-1773949
CEP70Q8NHQ13EBI-349968,EBI-739624
CLK3P497612EBI-349968,EBI-745579
DCAF8Q5TAQ92EBI-349968,EBI-740686
EZH2Q159102EBI-349968,EBI-530054
FGD5Q6ZNL62EBI-349968,EBI-7962481
GPATCH2LQ9NWQ42EBI-349968,EBI-5666657
GTPBP2Q9BX102EBI-349968,EBI-6115579
HDAC1Q135473EBI-349968,EBI-301834
HDAC2Q927693EBI-349968,EBI-301821
HEL25V9HWG03EBI-349968,EBI-10183977
HOOK2Q96ED94EBI-349968,EBI-743290
HOXA1P496392EBI-349968,EBI-740785
HOXC4P090172EBI-349968,EBI-3923226
KLHDC4Q8TBB52EBI-349968,EBI-8472352
KRTAP10-7P604093EBI-349968,EBI-10172290
LZTS2Q9BRK43EBI-349968,EBI-741037
MBD1Q9UIS95EBI-349968,EBI-867196
NR1H3Q131332EBI-349968,EBI-781356
PHF19Q5T6S32EBI-349968,EBI-2339674
PSMC1P621912EBI-349968,EBI-357598
RASSF1Q9NS232EBI-349968,EBI-367363
RASSF2P507492EBI-349968,EBI-960081
RRP8O431593EBI-349968,EBI-2008793
SPSB1Q96BD62EBI-349968,EBI-2659201
STX19Q8N4C72EBI-349968,EBI-8484990
U2AF1Q010812EBI-349968,EBI-632461
ZKSCAN5Q9Y2L82EBI-349968,EBI-2876965
ZNF436Q9C0F32EBI-349968,EBI-8489702
ZNF649Q9BS312EBI-349968,EBI-4395789
ZNF670Q9BS342EBI-349968,EBI-745276

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112706. 168 interactions.
DIPiDIP-32589N.
IntActiO43463. 106 interactions.
MINTiMINT-191763.
STRINGi9606.ENSP00000365877.

Chemistry

BindingDBiO43463.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 539Combined sources
Beta strandi58 – 647Combined sources
Helixi69 – 713Combined sources
Beta strandi73 – 764Combined sources
Helixi77 – 793Combined sources
Helixi83 – 10321Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MTSX-ray2.20A/B/C44-106[»]
ProteinModelPortaliO43463.
SMRiO43463. Positions 44-104, 115-411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 10159ChromoPROSITE-ProRule annotationAdd
BLAST
Domaini179 – 24062Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini243 – 366124SETPROSITE-ProRule annotationAdd
BLAST
Domaini396 – 41217Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8989Interaction with SIRT1Add
BLAST
Regioni254 – 2563S-adenosyl-L-methionine bindingBy similarity
Regioni255 – 377123Mediates interaction with MECOMBy similarityAdd
BLAST
Regioni323 – 3242S-adenosyl-L-methionine bindingBy similarity

Domaini

Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates to stable binding to heterochromatin.1 Publication
In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.1 Publication

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
Contains 1 chromo domain.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1082. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000231244.
HOVERGENiHBG055621.
InParanoidiO43463.
KOiK11419.
OMAiNTFVMEY.
PhylomeDBiO43463.
TreeFamiTF106452.

Family and domain databases

InterProiIPR000953. 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.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF009343. SUV39_SET. 1 hit.
SMARTiSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51579. SAM_MT43_SUVAR39_3. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43463-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGISKRNL YDFEVEYLCD
60 70 80 90 100
YKKIREQEYY LVKWRGYPDS ESTWEPRQNL KCVRILKQFH KDLERELLRR
110 120 130 140 150
HHRSKTPRHL DPSLANYLVQ KAKQRRALRR WEQELNAKRS HLGRITVENE
160 170 180 190 200
VDLDGPPRAF VYINEYRVGE GITLNQVAVG CECQDCLWAP TGGCCPGASL
210 220 230 240 250
HKFAYNDQGQ VRLRAGLPIY ECNSRCRCGY DCPNRVVQKG IRYDLCIFRT
260 270 280 290 300
DDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD
310 320 330 340 350
LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF
360 370 380 390 400
ATRTIRAGEE LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC
410
KCGTESCRKY LF
Length:412
Mass (Da):47,907
Last modified:June 1, 1998 - v1
Checksum:iAF6F959AD20C6C76
GO
Isoform 2 (identifier: O43463-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MAENLK → MVGMSRLRNDRLADPLT

Note: No experimental confirmation available.
Show »
Length:423
Mass (Da):49,148
Checksum:i67729933D3ABC7CF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131L → P in BAD96791 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MAENLK → MVGMSRLRNDRLADPLT in isoform 2. 1 PublicationVSP_054286

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019968 mRNA. Translation: AAB92224.1.
CR541746 mRNA. Translation: CAG46546.1.
AK223071 mRNA. Translation: BAD96791.1.
AK299900 mRNA. Translation: BAG61742.1.
AK312547 mRNA. Translation: BAG35445.1.
AF196970 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50756.1.
CH471224 Genomic DNA. Translation: EAW50757.1.
BC006238 mRNA. Translation: AAH06238.1.
CCDSiCCDS14304.1. [O43463-1]
CCDS65252.1. [O43463-2]
RefSeqiNP_001269095.1. NM_001282166.1. [O43463-2]
NP_003164.1. NM_003173.3. [O43463-1]
UniGeneiHs.522639.

Genome annotation databases

EnsembliENST00000337852; ENSP00000337976; ENSG00000101945. [O43463-2]
ENST00000376687; ENSP00000365877; ENSG00000101945. [O43463-1]
GeneIDi6839.
KEGGihsa:6839.
UCSCiuc004dkn.5. human. [O43463-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019968 mRNA. Translation: AAB92224.1.
CR541746 mRNA. Translation: CAG46546.1.
AK223071 mRNA. Translation: BAD96791.1.
AK299900 mRNA. Translation: BAG61742.1.
AK312547 mRNA. Translation: BAG35445.1.
AF196970 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50756.1.
CH471224 Genomic DNA. Translation: EAW50757.1.
BC006238 mRNA. Translation: AAH06238.1.
CCDSiCCDS14304.1. [O43463-1]
CCDS65252.1. [O43463-2]
RefSeqiNP_001269095.1. NM_001282166.1. [O43463-2]
NP_003164.1. NM_003173.3. [O43463-1]
UniGeneiHs.522639.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MTSX-ray2.20A/B/C44-106[»]
ProteinModelPortaliO43463.
SMRiO43463. Positions 44-104, 115-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112706. 168 interactions.
DIPiDIP-32589N.
IntActiO43463. 106 interactions.
MINTiMINT-191763.
STRINGi9606.ENSP00000365877.

Chemistry

BindingDBiO43463.
ChEMBLiCHEMBL1795118.
GuidetoPHARMACOLOGYi2715.

PTM databases

iPTMnetiO43463.
PhosphoSiteiO43463.

Proteomic databases

EPDiO43463.
MaxQBiO43463.
PaxDbiO43463.
PeptideAtlasiO43463.
PRIDEiO43463.

Protocols and materials databases

DNASUi6839.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337852; ENSP00000337976; ENSG00000101945. [O43463-2]
ENST00000376687; ENSP00000365877; ENSG00000101945. [O43463-1]
GeneIDi6839.
KEGGihsa:6839.
UCSCiuc004dkn.5. human. [O43463-1]

Organism-specific databases

CTDi6839.
GeneCardsiSUV39H1.
HGNCiHGNC:11479. SUV39H1.
MIMi300254. gene.
neXtProtiNX_O43463.
PharmGKBiPA36264.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1082. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000231244.
HOVERGENiHBG055621.
InParanoidiO43463.
KOiK11419.
OMAiNTFVMEY.
PhylomeDBiO43463.
TreeFamiTF106452.

Enzyme and pathway databases

ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.

Miscellaneous databases

ChiTaRSiSUV39H1. human.
GeneWikiiSUV39H1.
GenomeRNAii6839.
PROiO43463.
SOURCEiSearch...

Gene expression databases

BgeeiO43463.
CleanExiHS_SUV39H1.
GenevisibleiO43463. HS.

Family and domain databases

InterProiIPR000953. 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.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF009343. SUV39_SET. 1 hit.
SMARTiSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51579. SAM_MT43_SUVAR39_3. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31."
    Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G., Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T.
    EMBO J. 18:1923-1938(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CBX1.
    Tissue: B-cell.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Tongue.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  8. "Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres."
    Aagaard L., Schmid M., Warburton P., Jenuwein T.
    J. Cell Sci. 113:817-829(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
  9. "Regulation of chromatin structure by site-specific histone H3 methyltransferases."
    Rea S., Eisenhaber F., O'Carroll D., Strahl B.D., Sun Z.-W., Schmid M., Opravil S., Mechtler K., Ponting C.P., Allis C.D., Jenuwein T.
    Nature 406:593-599(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, MUTAGENESIS OF HIS-320; HIS-324 AND CYS-326.
  10. "Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9."
    Firestein R., Cui X., Huie P., Cleary M.L.
    Mol. Cell. Biol. 20:4900-4909(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SBF1.
  11. "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins."
    Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.
    Nature 410:116-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HISTONE H3 AND HISTONE H4.
  12. Cited for: INTERACTION WITH RB1.
  13. "Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression."
    Fujita N., Watanabe S., Ichimura T., Tsuruzoe S., Shinkai Y., Tachibana M., Chiba T., Nakao M.
    J. Biol. Chem. 278:24132-24138(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBD1.
  14. "Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins."
    Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L., Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.
    Mol. Cell. Biol. 22:5539-5553(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBX4.
  15. "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo."
    Chakraborty S., Sinha K.K., Senyuk V., Nucifora G.
    Oncogene 22:5229-5237(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RUNX1.
  16. "pRb2/p130-E2F4/5-HDAC1-SUV39H1-p300 and pRb2/p130-E2F4/5-HDAC1-SUV39H1-DNMT1 multimolecular complexes mediate the transcription of estrogen receptor-alpha in breast cancer."
    Macaluso M., Cinti C., Russo G., Russo A., Giordano A.
    Oncogene 22:3511-3517(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HDAC1.
  17. "A Suv39h-dependent mechanism for silencing S-phase genes in differentiating but not in cycling cells."
    Ait-Si-Ali S., Guasconi V., Fritsch L., Yahi H., Sekhri R., Naguibneva I., Robin P., Cabon F., Polesskaya A., Harel-Bellan A.
    EMBO J. 23:605-615(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Suv39h histone methyltransferases interact with Smads and cooperate in BMP-induced repression."
    Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M., Lechleider R.J.
    Oncogene 23:5242-5251(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAD5.
  19. "A glue for heterochromatin maintenance: stable SUV39H1 binding to heterochromatin is reinforced by the SET domain."
    Krouwels I.M., Wiesmeijer K., Abraham T.E., Molenaar C., Verwoerd N.P., Tanke H.J., Dirks R.W.
    J. Cell Biol. 170:537-549(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, INTERACTION WITH CBX1.
  20. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "Gfi1b alters histone methylation at target gene promoters and sites of gamma-satellite containing heterochromatin."
    Vassen L., Fiolka K., Moeroey T.
    EMBO J. 25:2409-2419(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GFI1B.
  22. "The histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA."
    Bradley S.P., Kaminski D.A., Peters A.H.F.M., Jenuwein T., Stavnezer J.
    J. Immunol. 177:1179-1188(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Catalytic properties and kinetic mechanism of human recombinant Lys-9 histone H3 methyltransferase SUV39H1: participation of the chromodomain in enzymatic catalysis."
    Chin H.G., Patnaik D., Esteve P.-O., Jacobsen S.E., Pradhan S.
    Biochemistry 45:3272-3284(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, MUTAGENESIS OF TRP-64 AND TYR-67.
  24. "Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic differentiation."
    Mal A.K.
    EMBO J. 25:3323-3334(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYOD1.
  25. "Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein."
    Carbone R., Botrugno O.A., Ronzoni S., Insinga A., Di Croce L., Pelicci P.G., Minucci S.
    Mol. Cell. Biol. 26:1288-1296(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. Cited for: INTERACTION WITH RUNX1 AND RUNX3.
  27. "SUV39H1 interacts with HTLV-1 Tax and abrogates Tax transactivation of HTLV-1 LTR."
    Kamoi K., Yamamoto K., Misawa A., Miyake A., Ishida T., Tanaka Y., Mochizuki M., Watanabe T.
    Retrovirology 3:5-5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX.
  28. "SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation."
    Vaquero A., Scher M., Erdjument-Bromage H., Tempst P., Serrano L., Reinberg D.
    Nature 450:440-444(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACETYLATION AT LYS-266, MUTAGENESIS OF LYS-266, SUBCELLULAR LOCATION.
  29. Cited for: IDENTIFICATION IN THE ENOSC COMPLEX, FUNCTION.
  30. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. "Inhibition of SUV39H1 methyltransferase activity by DBC1."
    Li Z., Chen L., Kabra N., Wang C., Fang J., Chen J.
    J. Biol. Chem. 284:10361-10366(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCAR2, ENZYME REGULATION.
  32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  33. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  36. "Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model."
    Liu B., Wang Z., Zhang L., Ghosh S., Zheng H., Zhou Z.
    Nat. Commun. 4:1868-1868(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LMNA, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSUV91_HUMAN
AccessioniPrimary (citable) accession number: O43463
Secondary accession number(s): B2R6E8
, B4DST0, Q53G60, Q6FHK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.