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Q6NRE8

- SUV91_XENLA

UniProt

Q6NRE8 - SUV91_XENLA

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Protein
Histone-lysine N-methyltransferase SUV39H1
Gene
suv39h1
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi191 – 1911Zinc 1 By similarity
Metal bindingi191 – 1911Zinc 2 By similarity
Metal bindingi193 – 1931Zinc 1 By similarity
Metal bindingi196 – 1961Zinc 1 By similarity
Metal bindingi196 – 1961Zinc 3 By similarity
Metal bindingi203 – 2031Zinc 1 By similarity
Metal bindingi204 – 2041Zinc 1 By similarity
Metal bindingi204 – 2041Zinc 2 By similarity
Metal bindingi231 – 2311Zinc 2 By similarity
Metal bindingi231 – 2311Zinc 3 By similarity
Metal bindingi235 – 2351Zinc 2 By similarity
Metal bindingi237 – 2371Zinc 3 By similarity
Metal bindingi241 – 2411Zinc 3 By similarity
Binding sitei306 – 3061S-adenosyl-L-methionine By similarity
Metal bindingi335 – 3351Zinc 4 By similarity
Metal bindingi409 – 4091Zinc 4 By similarity
Metal bindingi411 – 4111Zinc 4 By similarity
Metal bindingi416 – 4161Zinc 4 By 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 SUV39H1
PRO_0000281812Add
BLAST

Interactioni

Protein-protein interaction databases

BioGridi101309. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ6NRE8.
SMRiQ6NRE8. Positions 125-420.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 10459Chromo
Add
BLAST
Domaini189 – 24961Pre-SET
Add
BLAST
Domaini252 – 375124SET
Add
BLAST
Domaini405 – 42117Post-SET
Add
BLAST

Region

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

Contains 1 chromo domain.
Contains 1 post-SET domain.
Contains 1 pre-SET domain.
Contains 1 SET domain.

Phylogenomic databases

HOVERGENiHBG055621.
KOiK11419.

Family and domain databases

InterProiIPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
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

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MAENSNGALG CVVRCLSSES ELQELCREEQ LCCAELGVTR KNLSDFEVEY    50
LWNYKKVQDQ ELYLVKWKYY PDSESTWEPR HHLKCNNLLK QFHLDLEREL 100
LRRAKAAGTK KTAVRCPRRL DQSLSHYLVL KAKQRKRLRQ WAQQLNAKRS 150
HLGLILVENE VDLEGPPRDF VYINEYRVGE GVTINRISAG CKCRDCFSDE 200
GGCCPGAFQH KKAYNNEGQV KVKPGFPIYE CNSCCRCGPS CPNRVVQKGI 250
QYKFCIFRTS DGRGWGVRTL EKIRKNSFVM EYVGEIITSE EAERRGQIYD 300
RQGTTYLFDL DYVEDVYTVD AARYGNISHF VNHSCKPNLQ VYNVFIDNLD 350
ERLPRIAFFA TRTIRTGEEL TFDYNMQVDP VDVESSKMDS NFGIAGLPAS 400
PKKRVRVECK CGVSSCRKYL F 421
Length:421
Mass (Da):48,581
Last modified:July 5, 2004 - v1
Checksum:i776BD7633D03C069
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BC070805 mRNA. Translation: AAH70805.1 .
RefSeqi NP_001084892.1. NM_001091423.1.
UniGenei Xl.46583.

3D structure databases

ProteinModelPortali Q6NRE8.
SMRi Q6NRE8. Positions 125-420.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 101309. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 431943.
KEGGi xla:431943.

Organism-specific databases

CTDi 6839.
Xenbasei XB-GENE-6049313. suv39h1.

Phylogenomic databases

HOVERGENi HBG055621.
KOi K11419.

Family and domain databases

InterProi IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR011381. Histone_H3-K9_MeTrfase.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
PIRSFi PIRSF009343. SUV39_SET. 1 hit.
SMARTi SM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (MAY-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: May 14, 2014
This is version 61 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

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