Histone-lysine N-methyltransferase SETDB2 - Xenopus laevis (African clawed frog)

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Q6YI93 (SETB2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 56. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	setdb2
Synonyms:	clld8

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	703 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subcellular location	Nucleus By similarity. Chromosome By similarity.
Sequence similarities	Belongs to the histone-lysine methyltransferase family. Contains 1 MBD (methyl-CpG-binding) domain. Contains 1 pre-SET domain. Contains 1 SET domain.
Sequence caution	The sequence AAN61106.1 differs from that shown. Reason: Frameshift at position 695.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Chromosome Nucleus
Ligand	Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Chromatin regulator Developmental protein Methyltransferase Transferase
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from sequence or structural similarity. Source: UniProtKB heart looping Inferred from sequence or structural similarity. Source: UniProtKB left/right axis specification Inferred from sequence or structural similarity. Source: UniProtKB mitosis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro histone methyltransferase activity (H3-K9 specific) Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 703

703

Histone-lysine N-methyltransferase SETDB2

PRO_0000281825

Regions

Domain

178 – 248

MBD

Domain

310 – 384

Pre-SET

Domain

386 – 682

297

SET

Sites

Metal binding

312

Zinc 1 By similarity

Metal binding

312

Zinc 2 By similarity

Metal binding

314

Zinc 1 By similarity

Metal binding

318

Zinc 1 By similarity

Metal binding

318

Zinc 3 By similarity

Metal binding

324

Zinc 1 By similarity

Metal binding

326

Zinc 2 By similarity

Metal binding

365

Zinc 2 By similarity

Metal binding

365

Zinc 3 By similarity

Metal binding

369

Zinc 2 By similarity

Metal binding

371

Zinc 3 By similarity

Metal binding

376

Zinc 3 By similarity

Experimental info

Sequence conflict

K → Q in AAN61106. Ref.1

Sequence conflict

175

S → P in AAN61106. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q6YI93 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 12D86C32892B5325
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FASTA

703

78,698

        10         20         30         40         50         60 
MEQSANARQS TLRSRTQELN TLSVLSKDVS LEDAKKYWKD RQADGKVDWI FEKVLNKLKI 

        70         80         90        100        110        120 
LWQKIKDGSA TNLEYVRAVI LVNEAGNLEE DLEEDLKEDT DTIHIDIHKE NEVQENTDCS 

       130        140        150        160        170        180 
PERKEDTCLN LNTDCGTDVS GSEPECNSTV SPPAAERVYF GNHSCGPSCL SGINSFLFTK 

       190        200        210        220        230        240 
GNPLQLPISC DFQRCHLKIN SPDDLSHILY KAPCGRSLRD YDEVHSYLTE TGCHFLAVDN 

       250        260        270        280        290        300 
FSFNNHVRLD SNSSFNQGIV QDCDISNDVE SVPVAFSNEI DNTRPSNFIY RKTSWPPGYS 

       310        320        330        340        350        360 
LNNFTDIFVK CCNCTDGCLD ILTCSCLQLT AQAFTKCMES SLGIGPLGYK HKRLQEPIPT 

       370        380        390        400        410        420 
GLYECNVSCK CDRMLCQNRV VQHGLKLRLQ VFKTNTKGWG VRCLDDVDKG TFVCIYAGRI 

       430        440        450        460        470        480 
LIRTADCTVK STPDDSVACG NEDHEDSTST CALILSKRKR KTSHSDSEVT VMHTNPYSMR 

       490        500        510        520        530        540 
SHGLSVHRLS NTFSPRQARS GEREFSLQPL RRPKTKTSML QKRRRQLIEE GACTVQNSSE 

       550        560        570        580        590        600 
EEGPTPPQSP EQKSSAGTKI QRNENSDETA SGYVSEESSS SVISGGHPLE KPISKFKSKL 

       610        620        630        640        650        660 
NKTTVYLSTS PEQTCEENLH FLDASKEGNV GRFLNHSCCP NLFVQQVFVD THQKCFPWVA 

       670        680        690        700 
FFTNSVVKAG TELTWDYSYD IGTAADQEIQ CLCGQKTCKN KVV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY145835 mRNA. Translation: AAN61106.1. Frameshift. BC170303 mRNA. Translation: AAI70303.1.
RefSeq	NP_001082765.1. NM_001089296.1.
UniGene	Xl.29790.
3D structure databases
HSSP	HSSP built from PDB template 1PEG based on UniProtKB Q8X225.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	398711.
KEGG	xla:398711.
Organism-specific databases
CTD	83852.
Xenbase	XB-GENE-1219036. setdb2.
Phylogenomic databases
HOVERGEN	HBG106688.
KO	K11421.
Family and domain databases
InterPro	IPR016177. DNA-bd_integrase-typ. IPR001739. Methyl_CpG_DNA-bd. IPR003616. Post-SET_dom. IPR007728. Pre-SET_dom. IPR001214. SET_dom. [Graphical view]
Pfam	PF01429. MBD. 1 hit. PF05033. Pre-SET. 1 hit. PF00856. SET. 1 hit. [Graphical view]
SMART	SM00317. SET. 1 hit. [Graphical view]
SUPFAM	SSF54171. DNA-binding_integrase-type. 1 hit.
PROSITE	PS50982. MBD. False negative. PS50868. POST_SET. 1 hit. PS50867. PRE_SET. 1 hit. PS50280. SET. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SETB2_XENLA

Accession

Primary (citable) accession number: Q6YI93
Secondary accession number(s): B7ZRV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	October 5, 2010
Last modified:	April 3, 2013
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents