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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 + N6-methyl-L-lysine-[histone].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi191Zinc 1By similarity1
Metal bindingi191Zinc 2By similarity1
Metal bindingi193Zinc 1By similarity1
Metal bindingi196Zinc 1By similarity1
Metal bindingi196Zinc 3By similarity1
Metal bindingi201Zinc 1By similarity1
Metal bindingi202Zinc 1By similarity1
Metal bindingi202Zinc 2By similarity1
Metal bindingi229Zinc 2By similarity1
Metal bindingi229Zinc 3By similarity1
Metal bindingi233Zinc 2By similarity1
Metal bindingi235Zinc 3By similarity1
Metal bindingi239Zinc 3By similarity1
Binding sitei304S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi333Zinc 4By similarity1
Metal bindingi398Zinc 4By similarity1
Metal bindingi400Zinc 4By similarity1
Metal bindingi405Zinc 4By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, Methyltransferase, Repressor, Transferase
Biological processBiological rhythms, Cell cycle, Differentiation, Transcription, Transcription regulation
LigandMetal-binding, S-adenosyl-L-methionine, Zinc

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002818131 – 410Histone-lysine N-methyltransferase SUV39H2Add BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei381PhosphoserineBy similarity1
Modified residuei384PhosphoserineBy similarity1
Modified residuei388PhosphoserineBy similarity1

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 105ChromoPROSITE-ProRule annotationAdd BLAST59
Domaini189 – 247Pre-SETPROSITE-ProRule annotationAdd BLAST59
Domaini250 – 373SETPROSITE-ProRule annotationAdd BLAST124
Domaini394 – 410Post-SETPROSITE-ProRule annotationAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni261 – 263S-adenosyl-L-methionine bindingBy similarity3
Regioni330 – 331S-adenosyl-L-methionine bindingBy similarity2

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 in 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

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR000953. Chromo/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.
PfamiView protein in Pfam
PF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
PIRSFiPIRSF009343. SUV39_SET. 1 hit.
SMARTiView protein in SMART
SM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiView protein in PROSITE
PS00598. 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.

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.

Similar proteinsi

Entry informationi

Entry nameiSUV92_BOVIN
AccessioniPrimary (citable) accession number: Q32PH7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 6, 2005
Last modified: September 27, 2017
This is version 96 of the entry and version 1 of the sequence. See 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