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Q6YI93

- SETB2_XENLA

UniProt

Q6YI93 - SETB2_XENLA

Protein

Histone-lysine N-methyltransferase SETDB2

Gene

setdb2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    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.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 1By similarity
    Metal bindingi312 – 3121Zinc 2By similarity
    Metal bindingi314 – 3141Zinc 1By similarity
    Metal bindingi318 – 3181Zinc 1By similarity
    Metal bindingi318 – 3181Zinc 3By similarity
    Metal bindingi324 – 3241Zinc 1By similarity
    Metal bindingi326 – 3261Zinc 2By similarity
    Metal bindingi365 – 3651Zinc 2By similarity
    Metal bindingi365 – 3651Zinc 3By similarity
    Metal bindingi369 – 3691Zinc 2By similarity
    Metal bindingi371 – 3711Zinc 3By similarity
    Metal bindingi376 – 3761Zinc 3By similarity
    Binding sitei632 – 6321S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi638 – 6381Zinc 4By similarity
    Metal bindingi691 – 6911Zinc 4By similarity
    Metal bindingi693 – 6931Zinc 4By similarity
    Metal bindingi698 – 6981Zinc 4By 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

    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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 703703Histone-lysine N-methyltransferase SETDB2PRO_0000281825Add
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini178 – 24871MBDAdd
    BLAST
    Domaini310 – 38475Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini387 – 678292SETPROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
    Contains 1 pre-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    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

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    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.

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 65 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