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Protein

Histone-lysine N-methyltransferase SUV39H1

Gene

suv39h1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 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 (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 bindingi203 – 2031Zinc 1By similarity
Metal bindingi204 – 2041Zinc 1By similarity
Metal bindingi204 – 2041Zinc 2By similarity
Metal bindingi231 – 2311Zinc 2By similarity
Metal bindingi231 – 2311Zinc 3By similarity
Metal bindingi235 – 2351Zinc 2By similarity
Metal bindingi237 – 2371Zinc 3By similarity
Metal bindingi241 – 2411Zinc 3By similarity
Binding sitei306 – 3061S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi335 – 3351Zinc 4By similarity
Metal bindingi409 – 4091Zinc 4By similarity
Metal bindingi411 – 4111Zinc 4By similarity
Metal bindingi416 – 4161Zinc 4By similarity

GO - Molecular functioni

  1. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Cell cycle, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SUV39H1 (EC:2.1.1.43)
Alternative name(s):
Suppressor of variegation 3-9 homolog 1
Short name:
Su(var)3-9 homolog 1
Gene namesi
Name:suv39h1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6049313. suv39h1.

Subcellular locationi

Nucleus By similarity. Chromosomecentromere By similarity
Note: Associates with centromeric constitutive heterochromatin.By similarity

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Histone-lysine N-methyltransferase SUV39H1PRO_0000281812Add
BLAST

Interactioni

Protein-protein interaction databases

BioGridi101309. 1 interaction.

Structurei

3D structure databases

SMRiQ6NRE8. Positions 125-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 10459ChromoPROSITE-ProRule annotationAdd
BLAST
Domaini189 – 24961Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini252 – 375124SETPROSITE-ProRule annotationAdd
BLAST
Domaini405 – 42117Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni263 – 2653S-adenosyl-L-methionine bindingBy similarity
Regioni332 – 3332S-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

HOVERGENiHBG055621.
KOiK11419.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
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.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS50013. 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.

Q6NRE8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENSNGALG CVVRCLSSES ELQELCREEQ LCCAELGVTR KNLSDFEVEY
60 70 80 90 100
LWNYKKVQDQ ELYLVKWKYY PDSESTWEPR HHLKCNNLLK QFHLDLEREL
110 120 130 140 150
LRRAKAAGTK KTAVRCPRRL DQSLSHYLVL KAKQRKRLRQ WAQQLNAKRS
160 170 180 190 200
HLGLILVENE VDLEGPPRDF VYINEYRVGE GVTINRISAG CKCRDCFSDE
210 220 230 240 250
GGCCPGAFQH KKAYNNEGQV KVKPGFPIYE CNSCCRCGPS CPNRVVQKGI
260 270 280 290 300
QYKFCIFRTS DGRGWGVRTL EKIRKNSFVM EYVGEIITSE EAERRGQIYD
310 320 330 340 350
RQGTTYLFDL DYVEDVYTVD AARYGNISHF VNHSCKPNLQ VYNVFIDNLD
360 370 380 390 400
ERLPRIAFFA TRTIRTGEEL TFDYNMQVDP VDVESSKMDS NFGIAGLPAS
410 420
PKKRVRVECK CGVSSCRKYL F
Length:421
Mass (Da):48,581
Last modified:July 5, 2004 - v1
Checksum:i776BD7633D03C069
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC070805 mRNA. Translation: AAH70805.1.
RefSeqiNP_001084892.1. NM_001091423.1.
UniGeneiXl.46583.

Genome annotation databases

GeneIDi431943.
KEGGixla:431943.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC070805 mRNA. Translation: AAH70805.1.
RefSeqiNP_001084892.1. NM_001091423.1.
UniGeneiXl.46583.

3D structure databases

SMRiQ6NRE8. Positions 125-420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi101309. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi431943.
KEGGixla:431943.

Organism-specific databases

CTDi6839.
XenbaseiXB-GENE-6049313. suv39h1.

Phylogenomic databases

HOVERGENiHBG055621.
KOiK11419.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
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.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS50013. 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

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Oocyte.

Entry informationi

Entry nameiSUV91_XENLA
AccessioniPrimary (citable) accession number: Q6NRE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: April 1, 2015
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.