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Q6YI93

- SETB2_XENLA

UniProt

Q6YI93 - SETB2_XENLA

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Protein
Histone-lysine N-methyltransferase SETDB2
Gene
setdb2, clld8
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis 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 bindingi312 – 3121Zinc 1 By similarity
Metal bindingi312 – 3121Zinc 2 By similarity
Metal bindingi314 – 3141Zinc 1 By similarity
Metal bindingi318 – 3181Zinc 1 By similarity
Metal bindingi318 – 3181Zinc 3 By similarity
Metal bindingi324 – 3241Zinc 1 By similarity
Metal bindingi326 – 3261Zinc 2 By similarity
Metal bindingi365 – 3651Zinc 2 By similarity
Metal bindingi365 – 3651Zinc 3 By similarity
Metal bindingi369 – 3691Zinc 2 By similarity
Metal bindingi371 – 3711Zinc 3 By similarity
Metal bindingi376 – 3761Zinc 3 By similarity
Binding sitei632 – 6321S-adenosyl-L-methionine By similarity
Metal bindingi638 – 6381Zinc 4 By similarity
Metal bindingi691 – 6911Zinc 4 By similarity
Metal bindingi693 – 6931Zinc 4 By similarity
Metal bindingi698 – 6981Zinc 4 By similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromosome segregation Source: UniProtKB
  2. heart looping Source: UniProtKB
  3. histone H3-K9 methylation Source: UniProtKB
  4. left/right axis specification Source: UniProtKB
  5. mitotic nuclear division Source: UniProtKB
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Methyltransferase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SETDB2 (EC:2.1.1.43)
Alternative name(s):
Chronic lymphocytic leukemia deletion region gene 8 protein homolog
SET domain bifurcated 2
Gene namesi
Name:setdb2
Synonyms:clld8
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1219036. setdb2.

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 703703Histone-lysine N-methyltransferase SETDB2
PRO_0000281825Add
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 24871MBD
Add
BLAST
Domaini310 – 38475Pre-SET
Add
BLAST
Domaini387 – 678292SET
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni397 – 3993S-adenosyl-L-methionine binding By similarity
Regioni635 – 6362S-adenosyl-L-methionine binding By similarity

Domaini

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 pre-SET domain.
Contains 1 SET domain.

Phylogenomic databases

HOVERGENiHBG106688.
KOiK11421.

Family and domain databases

InterProiIPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6YI93-1 [UniParc]FASTAAdd to Basket

« Hide

MEQSANARQS TLRSRTQELN TLSVLSKDVS LEDAKKYWKD RQADGKVDWI    50
FEKVLNKLKI LWQKIKDGSA TNLEYVRAVI LVNEAGNLEE DLEEDLKEDT 100
DTIHIDIHKE NEVQENTDCS PERKEDTCLN LNTDCGTDVS GSEPECNSTV 150
SPPAAERVYF GNHSCGPSCL SGINSFLFTK GNPLQLPISC DFQRCHLKIN 200
SPDDLSHILY KAPCGRSLRD YDEVHSYLTE TGCHFLAVDN FSFNNHVRLD 250
SNSSFNQGIV QDCDISNDVE SVPVAFSNEI DNTRPSNFIY RKTSWPPGYS 300
LNNFTDIFVK CCNCTDGCLD ILTCSCLQLT AQAFTKCMES SLGIGPLGYK 350
HKRLQEPIPT GLYECNVSCK CDRMLCQNRV VQHGLKLRLQ VFKTNTKGWG 400
VRCLDDVDKG TFVCIYAGRI LIRTADCTVK STPDDSVACG NEDHEDSTST 450
CALILSKRKR KTSHSDSEVT VMHTNPYSMR SHGLSVHRLS NTFSPRQARS 500
GEREFSLQPL RRPKTKTSML QKRRRQLIEE GACTVQNSSE EEGPTPPQSP 550
EQKSSAGTKI QRNENSDETA SGYVSEESSS SVISGGHPLE KPISKFKSKL 600
NKTTVYLSTS PEQTCEENLH FLDASKEGNV GRFLNHSCCP NLFVQQVFVD 650
THQKCFPWVA FFTNSVVKAG TELTWDYSYD IGTAADQEIQ CLCGQKTCKN 700
KVV 703
Length:703
Mass (Da):78,698
Last modified:October 5, 2010 - v2
Checksum:i12D86C32892B5325
GO

Sequence cautioni

The sequence AAN61106.1 differs from that shown. Reason: Frameshift at position 695.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971K → Q in AAN61106. 1 Publication
Sequence conflicti175 – 1751S → P in AAN61106. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145835 mRNA. Translation: AAN61106.1. Frameshift.
BC170303 mRNA. Translation: AAI70303.1.
RefSeqiNP_001082765.1. NM_001089296.1.
UniGeneiXl.29790.

Genome annotation databases

GeneIDi398711.
KEGGixla:398711.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145835 mRNA. Translation: AAN61106.1 . Frameshift.
BC170303 mRNA. Translation: AAI70303.1 .
RefSeqi NP_001082765.1. NM_001089296.1.
UniGenei Xl.29790.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 398711.
KEGGi xla:398711.

Organism-specific databases

CTDi 83852.
Xenbasei XB-GENE-1219036. setdb2.

Phylogenomic databases

HOVERGENi HBG106688.
KOi K11421.

Family and domain databases

InterProi IPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF54171. SSF54171. 1 hit.
PROSITEi PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and analysis of the expression of SET-domain putative histone methyltransferase CLLD8 in Xenopus laevis."
    Ruzov A., Meehan R.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Oocyte.

Entry informationi

Entry nameiSETB2_XENLA
AccessioniPrimary (citable) accession number: Q6YI93
Secondary accession number(s): B7ZRV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 64 of the entry and version 2 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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