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Q6INA9

- SETB1_XENLA

UniProt

Q6INA9 - SETB1_XENLA

Protein

Histone-lysine N-methyltransferase SETDB1

Gene

setdb1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. 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 euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation 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 bindingi755 – 7551Zinc 1By similarity
    Metal bindingi755 – 7551Zinc 2By similarity
    Metal bindingi757 – 7571Zinc 1By similarity
    Metal bindingi761 – 7611Zinc 1By similarity
    Metal bindingi761 – 7611Zinc 3By similarity
    Metal bindingi767 – 7671Zinc 1By similarity
    Metal bindingi769 – 7691Zinc 2By similarity
    Metal bindingi807 – 8071Zinc 2By similarity
    Metal bindingi807 – 8071Zinc 3By similarity
    Metal bindingi811 – 8111Zinc 2By similarity
    Metal bindingi813 – 8131Zinc 3By similarity
    Metal bindingi818 – 8181Zinc 3By similarity
    Binding sitei877 – 8771S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei879 – 8791S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei1198 – 11981S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi1204 – 12041Zinc 4By similarity
    Metal bindingi1257 – 12571Zinc 4By similarity
    Metal bindingi1259 – 12591Zinc 4By similarity
    Metal bindingi1264 – 12641Zinc 4By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase SETDB1 (EC:2.1.1.43)
    Alternative name(s):
    SET domain bifurcated 1
    Gene namesi
    Name:setdb1
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-866480. setdb1.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity
    Note: Associated with non-pericentromeric regions of chromatin. Excluded from nucleoli and islands of condensed chromatin By similarity.By similarity

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12691269Histone-lysine N-methyltransferase SETDB1PRO_0000281821Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ6INA9.
    SMRiQ6INA9. Positions 190-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini250 – 31263Tudor 1Add
    BLAST
    Domaini340 – 39556Tudor 2Add
    BLAST
    Domaini620 – 69172MBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini753 – 82674Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini829 – 1244416SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1253 – 126917Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni839 – 8413S-adenosyl-L-methionine bindingBy similarity
    Regioni1201 – 12022S-adenosyl-L-methionine bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili9 – 6355Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi508 – 58073Gln-richAdd
    BLAST

    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. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
    Contains 1 MBD (methyl-CpG-binding) 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
    Contains 2 Tudor domains.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    HOVERGENiHBG061013.
    KOiK11421.

    Family and domain databases

    InterProiIPR016177. DNA-bd_dom.
    IPR025796. Hist-Lys_N-MeTrfase_SETDB1.
    IPR001739. Methyl_CpG_DNA-bd.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    IPR002999. Tudor.
    [Graphical view]
    PfamiPF01429. MBD. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    SMARTiSM00391. MBD. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    SM00333. TUDOR. 2 hits.
    [Graphical view]
    SUPFAMiSSF54171. SSF54171. 1 hit.
    PROSITEiPS50982. MBD. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS51573. SAM_MT43_SUVAR39_1. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6INA9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELEQMVVKE LGISMDDLRE LIDRELEKIE FVKQRKAQLL EMEQLVKQKE     50
    AEVDHVDKLF DNATRAVDDC ETLVKSLYDQ IGMTYKESSS EDEGSSKPTE 100
    VIEIPDEDDD DVMSVGSGEA VSKIPKEKHL LREAMAAMKR SRQDVQSIVE 150
    AIQKKSDGPQ TRFSSHPSSP TSSVGGSNQA SASNDMSKDG DLVVGMRILG 200
    KKRTKTWHKG TLISIQCVGT GKKFKVKFDN KGKSLLSGNH IAYDYHPPPE 250
    NLTVGSRVVA KYKDGNQVWL YAGIVAEPPS SKNKMRYLIF FDDGYASYVT 300
    HAELYPVCRP WSKSWEDIED VSCRDFIQEY VNAYPNRPMV LLKSGQLIKT 350
    EWEGTWWKSK VEEVDGSLVK ILFLDDKRCE WIYRGSTRLE PMFSMKTSNA 400
    STQEKQQAGQ QRTRPNVGAI RSKGPVVQFT HDLTGNEPEH NPAAPPSPQS 450
    MPSPQLIDTD SDSQQAQSKK QVAKKSTSFR PGSAGSGQSS PIPTESVPQP 500
    PAAPRPFQSN QSVQPVQSIQ PIQPIHNIQT IQTIQGIQTI QAIQPIQSIQ 550
    TLQPIQTIQP LQTIQTLQGN RIVTSIQQFQ IIRTENIPAE STYKAPKEKL 600
    FYLPHVCNYT CLSRIRPLSH RGKNPLLVPL LYDFRRMTAR RRVNRKMGFH 650
    VIYKSPCGLS LRTMPEIERY LFETQCKMLF LEMFCLDPYV LVDRKFQPQK 700
    PFYYIPDITY GKEDVMLSCV NEIDRTPPPQ VAYSKERIPG KGVFINTGAD 750
    YLVGCDCTDG CRDKSKCACH QLTIQATACT PGAQSNPMAG YQHKRLEECL 800
    PTGVYECNKR CKCSANMCNN RLVQHGLQVR LQLFKTQNKG WGIRGLDDIA 850
    KGSFVCIYAG KILTDDFADK EGLEMGDEYF ANLDHIESVE NFKEGYESDA 900
    KSSSDSSGVD LKEDHEENSG SEDQEESNDS SDDNFGKNED ITTSSVWRSY 950
    ATRRTTRGQK ENGTSETASK DSRTRDETTD CKLPEETSKN KVASWLSSNT 1000
    MADSVMDSDS RSSLKMGEAL ETDKPKESEE ASKYPRFAEG NRAYGYNPTP 1050
    TKKDGVRRPV TKTALHQIKR QSSSAQPTEE VLTLSSSSDS EVGSGTNGSK 1100
    KPAAQATAND SDDIQTISSG SDEEEEKKNV AASAGPVKRQ VAVKSTRGFA 1150
    LKSTHGITVK SNMASGEGGP GRRNTRQFFD GEESCYIIDA KLEGNLGRYL 1200
    NHSCSPNLFV QNVFVDTHDL RFPWVAFFAS KRIRAGTELT WDYNYEVGSV 1250
    EGKKLLCCCG STECRGRLL 1269
    Length:1,269
    Mass (Da):141,777
    Last modified:July 5, 2004 - v1
    Checksum:i6241910CB4266FAC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC072374 mRNA. Translation: AAH72374.1.
    RefSeqiNP_001085076.2. NM_001091607.1.
    UniGeneiXl.54988.

    Genome annotation databases

    GeneIDi432147.
    KEGGixla:432147.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC072374 mRNA. Translation: AAH72374.1 .
    RefSeqi NP_001085076.2. NM_001091607.1.
    UniGenei Xl.54988.

    3D structure databases

    ProteinModelPortali Q6INA9.
    SMRi Q6INA9. Positions 190-391.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 432147.
    KEGGi xla:432147.

    Organism-specific databases

    CTDi 9869.
    Xenbasei XB-GENE-866480. setdb1.

    Phylogenomic databases

    HOVERGENi HBG061013.
    KOi K11421.

    Family and domain databases

    InterProi IPR016177. DNA-bd_dom.
    IPR025796. Hist-Lys_N-MeTrfase_SETDB1.
    IPR001739. Methyl_CpG_DNA-bd.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    IPR002999. Tudor.
    [Graphical view ]
    Pfami PF01429. MBD. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    SMARTi SM00391. MBD. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    SM00333. TUDOR. 2 hits.
    [Graphical view ]
    SUPFAMi SSF54171. SSF54171. 1 hit.
    PROSITEi PS50982. MBD. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS51573. SAM_MT43_SUVAR39_1. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiSETB1_XENLA
    AccessioniPrimary (citable) accession number: Q6INA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 73 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