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Protein

Histone-lysine N-methyltransferase SUV39H2

Gene

SUV39H2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. 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 cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. 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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi191 – 1911Zinc 1By similarity
Metal bindingi191 – 1911Zinc 2By similarity
Metal bindingi193 – 1931Zinc 1By similarity
Metal bindingi196 – 1961Zinc 1By similarity
Metal bindingi196 – 1961Zinc 3By similarity
Metal bindingi201 – 2011Zinc 1By similarity
Metal bindingi202 – 2021Zinc 1By similarity
Metal bindingi202 – 2021Zinc 2By similarity
Metal bindingi229 – 2291Zinc 2By similarity
Metal bindingi229 – 2291Zinc 3By similarity
Metal bindingi233 – 2331Zinc 2By similarity
Metal bindingi235 – 2351Zinc 3By similarity
Metal bindingi239 – 2391Zinc 3By similarity
Binding sitei304 – 3041S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi333 – 3331Zinc 4By similarity
Metal bindingi398 – 3981Zinc 4By similarity
Metal bindingi400 – 4001Zinc 4By similarity
Metal bindingi405 – 4051Zinc 4By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-BTA-3214841. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SUV39H2 (EC:2.1.1.43)
Alternative name(s):
Suppressor of variegation 3-9 homolog 2
Short name:
Su(var)3-9 homolog 2
Gene namesi
Name:SUV39H2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 13

Subcellular locationi

  • Nucleus By similarity
  • Chromosomecentromere By similarity

  • Note: Associates with centromeric constitutive heterochromatin.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410Histone-lysine N-methyltransferase SUV39H2PRO_0000281813Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei381 – 3811PhosphoserineBy similarity
Modified residuei384 – 3841PhosphoserineBy similarity
Modified residuei388 – 3881PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ32PH7.
PRIDEiQ32PH7.

Expressioni

Gene expression databases

BgeeiENSBTAG00000010210.

Interactioni

Subunit structurei

Interacts with SMAD5. 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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013472.

Structurei

3D structure databases

ProteinModelPortaliQ32PH7.
SMRiQ32PH7. Positions 124-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 10559ChromoPROSITE-ProRule annotationAdd
BLAST
Domaini189 – 24759Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini250 – 373124SETPROSITE-ProRule annotationAdd
BLAST
Domaini394 – 41017Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni261 – 2633S-adenosyl-L-methionine bindingBy similarity
Regioni330 – 3312S-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 (By similarity).By similarity
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.By similarity

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.
InParanoidiQ32PH7.
KOiK11419.
OMAiAWCVPCL.
OrthoDBiEOG091G0Y4N.
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]

Sequencei

Sequence statusi: Complete.

Q32PH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAGAEAPG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE
60 70 80 90 100
YLCDYKVVKD MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFFNDKHNY
110 120 130 140 150
LSQVKKGKAI TLKENHRALK PAVAEYIVKK AKQRIALQRW QDELNRRKTH
160 170 180 190 200
KGMIFVENTV DLEGPPSDFY YINEYKPAPG ISLVNEATFG CSCTDCFFEK
210 220 230 240 250
CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP NRIVQKGTQY
260 270 280 290 300
SLCIFRTSNG CGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQLYDNK
310 320 330 340 350
GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR
360 370 380 390 400
LPRIALFSTR TINAGEELTF DYQMKGSGDV SSDSIDHSPA KKRARTVCKC
410
GAVTCRGYLN
Length:410
Mass (Da):46,551
Last modified:December 6, 2005 - v1
Checksum:i421D0D42D385DBB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC108111 mRNA. Translation: AAI08112.1.
RefSeqiNP_001032556.1. NM_001037479.2.
UniGeneiBt.42320.

Genome annotation databases

EnsembliENSBTAT00000013472; ENSBTAP00000013472; ENSBTAG00000010210.
GeneIDi536936.
KEGGibta:536936.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC108111 mRNA. Translation: AAI08112.1.
RefSeqiNP_001032556.1. NM_001037479.2.
UniGeneiBt.42320.

3D structure databases

ProteinModelPortaliQ32PH7.
SMRiQ32PH7. Positions 124-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013472.

Proteomic databases

PaxDbiQ32PH7.
PRIDEiQ32PH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000013472; ENSBTAP00000013472; ENSBTAG00000010210.
GeneIDi536936.
KEGGibta:536936.

Organism-specific databases

CTDi79723.

Phylogenomic databases

eggNOGiKOG1082. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000231244.
HOVERGENiHBG055621.
InParanoidiQ32PH7.
KOiK11419.
OMAiAWCVPCL.
OrthoDBiEOG091G0Y4N.
TreeFamiTF106452.

Enzyme and pathway databases

ReactomeiR-BTA-3214841. PKMTs methylate histone lysines.

Gene expression databases

BgeeiENSBTAG00000010210.

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...

Entry informationi

Entry nameiSUV92_BOVIN
AccessioniPrimary (citable) accession number: Q32PH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 6, 2005
Last modified: September 7, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.