Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15047

- SETB1_HUMAN

UniProt

Q15047 - SETB1_HUMAN

Protein

Histone-lysine N-methyltransferase SETDB1

Gene

SETDB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.4 Publications

    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 bindingi729 – 7291Zinc 1By similarity
    Metal bindingi729 – 7291Zinc 2By similarity
    Metal bindingi731 – 7311Zinc 1By similarity
    Metal bindingi735 – 7351Zinc 1By similarity
    Metal bindingi735 – 7351Zinc 3By similarity
    Metal bindingi741 – 7411Zinc 1By similarity
    Metal bindingi743 – 7431Zinc 2By similarity
    Metal bindingi781 – 7811Zinc 2By similarity
    Metal bindingi781 – 7811Zinc 3By similarity
    Metal bindingi785 – 7851Zinc 2By similarity
    Metal bindingi787 – 7871Zinc 3By similarity
    Metal bindingi792 – 7921Zinc 3By similarity
    Binding sitei851 – 8511S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei853 – 8531S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei1220 – 12201S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi1226 – 12261Zinc 4By similarity
    Metal bindingi1279 – 12791Zinc 4By similarity
    Metal bindingi1281 – 12811Zinc 4By similarity
    Metal bindingi1286 – 12861Zinc 4By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. bone development Source: Ensembl
    2. inner cell mass cell proliferation Source: Ensembl
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. 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):
    ERG-associated protein with SET domain
    Short name:
    ESET
    Histone H3-K9 methyltransferase 4
    Short name:
    H3-K9-HMTase 4
    Lysine N-methyltransferase 1E
    SET domain bifurcated 1
    Gene namesi
    Name:SETDB1
    Synonyms:KIAA0067, KMT1E
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10761. SETDB1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. Golgi apparatus Source: HPA
    4. nucleus Source: HPA
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi729 – 7313CDC → LDP: Abolishes methyltransferase activity.
    Mutagenesisi976 – 9761T → A: Abrogates interaction with CHD7, NLK and PPARG. Reduces phosphorylation by NLK. Reduces transcriptional repression. 1 Publication
    Mutagenesisi1224 – 12241H → K: Abolishes methyltransferase activity. 1 Publication
    Mutagenesisi1226 – 12261C → A: Abolishes methyltransferase activity. 1 Publication
    Mutagenesisi1279 – 12791C → Y: Abolishes methyltransferase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA35679.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12911291Histone-lysine N-methyltransferase SETDB1PRO_0000186064Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki182 – 182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei976 – 9761Phosphothreonine; by NLK1 Publication
    Modified residuei1066 – 10661Phosphoserine3 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15047.
    PaxDbiQ15047.
    PRIDEiQ15047.

    PTM databases

    PhosphoSiteiQ15047.

    Expressioni

    Tissue specificityi

    Widely expressed. High expression in testis.

    Gene expression databases

    ArrayExpressiQ15047.
    BgeeiQ15047.
    CleanExiHS_SETDB1.
    GenevestigatoriQ15047.

    Organism-specific databases

    HPAiHPA018142.

    Interactioni

    Subunit structurei

    Interacts with MBD1; interaction is abolished when MBD1 is sumoylated. Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP is required to stimulate histone methyltransferase activity and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9'. During DNA replication, it is recruited by SETDB1 to form a S phase-specific complex that facilitates methylation of H3 'Lys-9' during replication-coupled chromatin assembly and is at least composed of the CAF-1 subunit CHAF1A, MBD1 and SETDB1. Interacts with ERG, TRIM28/TIF1B, CBX1, CBX5, CHD7, DNMT3A, HDAC1, HDAC2, NLK, PPARG, SIN3A, SIN3B, DNMT3B and SUMO2. Interacts with MPHOSPH8. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT1P317499EBI-79691,EBI-296087
    DNMT3AQ9Y6K17EBI-79691,EBI-923653
    MBD1Q9UIS93EBI-79691,EBI-867196
    MPHOSPH8Q995492EBI-79691,EBI-2653928
    ZDHHC17Q8IUH53EBI-9090795,EBI-524753

    Protein-protein interaction databases

    BioGridi115202. 115 interactions.
    DIPiDIP-31029N.
    IntActiQ15047. 109 interactions.
    MINTiMINT-1184137.
    STRINGi9606.ENSP00000357965.

    Structurei

    Secondary structure

    1
    1291
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi203 – 2075
    Beta strandi213 – 22412
    Beta strandi227 – 23711
    Beta strandi239 – 2424
    Helixi244 – 2463
    Beta strandi247 – 2515
    Helixi255 – 2573
    Beta strandi263 – 2697
    Beta strandi274 – 28310
    Turni287 – 2904
    Beta strandi293 – 2975
    Beta strandi302 – 3054
    Helixi307 – 3093
    Beta strandi310 – 3156
    Helixi320 – 3234
    Helixi327 – 33913
    Beta strandi353 – 3586
    Beta strandi361 – 37111
    Beta strandi374 – 3796
    Turni380 – 3834
    Beta strandi384 – 3896

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DLMX-ray1.77A196-402[»]
    ProteinModelPortaliQ15047.
    SMRiQ15047. Positions 196-397, 605-662, 681-881, 1165-1290.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15047.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini257 – 32064Tudor 1Add
    BLAST
    Domaini347 – 40357Tudor 2Add
    BLAST
    Domaini594 – 66572MBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini727 – 80074Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini803 – 1266464SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1275 – 129117Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni813 – 8153S-adenosyl-L-methionine bindingBy similarity
    Regioni1223 – 12242S-adenosyl-L-methionine bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili18 – 6447Sequence AnalysisAdd
    BLAST

    Domaini

    The pre-SET, SET and post-SET domains are all required for methyltransferase activity. The 347-amino-acid insertion in the SET domain has no effect on the catalytic activity.
    Isoform 2 lacks all domains required for histone methyltransferase activity.
    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

    eggNOGiCOG2940.
    HOVERGENiHBG061013.
    InParanoidiQ15047.
    KOiK11421.
    OMAiGSVGSGH.
    OrthoDBiEOG7ZD1TG.
    PhylomeDBiQ15047.
    TreeFamiTF106411.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15047-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSSLPGCIGL DAATATVESE EIAELQQAVV EELGISMEEL RHFIDEELEK     50
    MDCVQQRKKQ LAELETWVIQ KESEVAHVDQ LFDDASRAVT NCESLVKDFY 100
    SKLGLQYRDS SSEDESSRPT EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL 150
    REAMAALRKS AQDVQKFMDA VNKKSSSQDL HKGTLSQMSG ELSKDGDLIV 200
    SMRILGKKRT KTWHKGTLIA IQTVGPGKKY KVKFDNKGKS LLSGNHIAYD 250
    YHPPADKLYV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG 300
    YASYVTQSEL YPICRPLKKT WEDIEDISCR DFIEEYVTAY PNRPMVLLKS 350
    GQLIKTEWEG TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS 400
    MKTSSASALE KKQGQLRTRP NMGAVRSKGP VVQYTQDLTG TGTQFKPVEP 450
    PQPTAPPAPP FPPAPPLSPQ AGDSDLESQL AQSRKQVAKK STSFRPGSVG 500
    SGHSSPTSPA LSENVSGGKP GINQTYRSPL GSTASAPAPS ALPAPPAPPV 550
    FHGMLERAPA EPSYRAPMEK LFYLPHVCSY TCLSRVRPMR NEQYRGKNPL 600
    LVPLLYDFRR MTARRRVNRK MGFHVIYKTP CGLCLRTMQE IERYLFETGC 650
    DFLFLEMFCL DPYVLVDRKF QPYKPFYYIL DITYGKEDVP LSCVNEIDTT 700
    PPPQVAYSKE RIPGKGVFIN TGPEFLVGCD CKDGCRDKSK CACHQLTIQA 750
    TACTPGGQIN PNSGYQYKRL EECLPTGVYE CNKRCKCDPN MCTNRLVQHG 800
    LQVRLQLFKT QNKGWGIRCL DDIAKGSFVC IYAGKILTDD FADKEGLEMG 850
    DEYFANLDHI ESVENFKEGY ESDAPCSSDS SGVDLKDQED GNSGTEDPEE 900
    SNDDSSDDNF CKDEDFSTSS VWRSYATRRQ TRGQKENGLS ETTSKDSHPP 950
    DLGPPHIPVP PSIPVGGCNP PSSEETPKNK VASWLSCNSV SEGGFADSDS 1000
    HSSFKTNEGG EGRAGGSRME AEKASTSGLG IKDEGDIKQA KKEDTDDRNK 1050
    MSVVTESSRN YGYNPSPVKP EGLRRPPSKT SMHQSRRLMA SAQSNPDDVL 1100
    TLSSSTESEG ESGTSRKPTA GQTSATAVDS DDIQTISSGS EGDDFEDKKN 1150
    MTGPMKRQVA VKSTRGFALK STHGIAIKST NMASVDKGES APVRKNTRQF 1200
    YDGEESCYII DAKLEGNLGR YLNHSCSPNL FVQNVFVDTH DLRFPWVAFF 1250
    ASKRIRAGTE LTWDYNYEVG SVEGKELLCC CGAIECRGRL L 1291
    Length:1,291
    Mass (Da):143,157
    Last modified:November 1, 1996 - v1
    Checksum:iD8841B4C41B911C5
    GO
    Isoform 2 (identifier: Q15047-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         381-397: DDKRCEWIYRGSTRLEP → VLFFSTILEAEVGGGGT
         398-1291: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:397
    Mass (Da):44,689
    Checksum:iA880C9152E11A900
    GO
    Isoform 3 (identifier: Q15047-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1254-1254: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,290
    Mass (Da):143,001
    Checksum:iBBF5516339BE6C17
    GO

    Sequence cautioni

    The sequence BAA06689.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI13325.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI13326.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti236 – 2361N → S.
    Corresponds to variant rs2271075 [ dbSNP | Ensembl ].
    VAR_014284
    Natural varianti506 – 5061P → S.1 Publication
    Corresponds to variant rs17852587 [ dbSNP | Ensembl ].
    VAR_031281
    Natural varianti824 – 8241A → G.
    Corresponds to variant rs2691551 [ dbSNP | Ensembl ].
    VAR_014286
    Natural varianti824 – 8241A → P.
    Corresponds to variant rs2814054 [ dbSNP | Ensembl ].
    VAR_014285

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei381 – 39717DDKRC…TRLEP → VLFFSTILEAEVGGGGT in isoform 2. 1 PublicationVSP_002217Add
    BLAST
    Alternative sequencei398 – 1291894Missing in isoform 2. 1 PublicationVSP_002218Add
    BLAST
    Alternative sequencei1254 – 12541Missing in isoform 3. 1 PublicationVSP_034600

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31891 mRNA. Translation: BAA06689.2. Different initiation.
    AL590133 Genomic DNA. Translation: CAI13325.1. Sequence problems.
    AL590133 Genomic DNA. Translation: CAI13326.1. Sequence problems.
    AL590133 Genomic DNA. Translation: CAI13327.1.
    AL590133 Genomic DNA. Translation: CAI13328.1.
    CH471121 Genomic DNA. Translation: EAW53506.1.
    BC009362 mRNA. Translation: AAH09362.1.
    BC028671 mRNA. Translation: AAH28671.1.
    CCDSiCCDS44217.1. [Q15047-1]
    CCDS58026.1. [Q15047-2]
    CCDS972.1. [Q15047-3]
    RefSeqiNP_001138887.1. NM_001145415.1. [Q15047-1]
    NP_001230420.1. NM_001243491.1. [Q15047-2]
    NP_036564.3. NM_012432.3. [Q15047-3]
    UniGeneiHs.643565.

    Genome annotation databases

    EnsembliENST00000271640; ENSP00000271640; ENSG00000143379. [Q15047-1]
    ENST00000368962; ENSP00000357958; ENSG00000143379. [Q15047-2]
    ENST00000368969; ENSP00000357965; ENSG00000143379. [Q15047-3]
    GeneIDi9869.
    KEGGihsa:9869.
    UCSCiuc001evu.2. human. [Q15047-1]
    uc001evv.2. human. [Q15047-3]
    uc001evw.4. human. [Q15047-2]

    Polymorphism databases

    DMDMi25091210.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31891 mRNA. Translation: BAA06689.2 . Different initiation.
    AL590133 Genomic DNA. Translation: CAI13325.1 . Sequence problems.
    AL590133 Genomic DNA. Translation: CAI13326.1 . Sequence problems.
    AL590133 Genomic DNA. Translation: CAI13327.1 .
    AL590133 Genomic DNA. Translation: CAI13328.1 .
    CH471121 Genomic DNA. Translation: EAW53506.1 .
    BC009362 mRNA. Translation: AAH09362.1 .
    BC028671 mRNA. Translation: AAH28671.1 .
    CCDSi CCDS44217.1. [Q15047-1 ]
    CCDS58026.1. [Q15047-2 ]
    CCDS972.1. [Q15047-3 ]
    RefSeqi NP_001138887.1. NM_001145415.1. [Q15047-1 ]
    NP_001230420.1. NM_001243491.1. [Q15047-2 ]
    NP_036564.3. NM_012432.3. [Q15047-3 ]
    UniGenei Hs.643565.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DLM X-ray 1.77 A 196-402 [» ]
    ProteinModelPortali Q15047.
    SMRi Q15047. Positions 196-397, 605-662, 681-881, 1165-1290.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115202. 115 interactions.
    DIPi DIP-31029N.
    IntActi Q15047. 109 interactions.
    MINTi MINT-1184137.
    STRINGi 9606.ENSP00000357965.

    Chemistry

    ChEMBLi CHEMBL2321646.

    PTM databases

    PhosphoSitei Q15047.

    Polymorphism databases

    DMDMi 25091210.

    Proteomic databases

    MaxQBi Q15047.
    PaxDbi Q15047.
    PRIDEi Q15047.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000271640 ; ENSP00000271640 ; ENSG00000143379 . [Q15047-1 ]
    ENST00000368962 ; ENSP00000357958 ; ENSG00000143379 . [Q15047-2 ]
    ENST00000368969 ; ENSP00000357965 ; ENSG00000143379 . [Q15047-3 ]
    GeneIDi 9869.
    KEGGi hsa:9869.
    UCSCi uc001evu.2. human. [Q15047-1 ]
    uc001evv.2. human. [Q15047-3 ]
    uc001evw.4. human. [Q15047-2 ]

    Organism-specific databases

    CTDi 9869.
    GeneCardsi GC01P150898.
    HGNCi HGNC:10761. SETDB1.
    HPAi HPA018142.
    MIMi 604396. gene.
    neXtProti NX_Q15047.
    PharmGKBi PA35679.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOVERGENi HBG061013.
    InParanoidi Q15047.
    KOi K11421.
    OMAi GSVGSGH.
    OrthoDBi EOG7ZD1TG.
    PhylomeDBi Q15047.
    TreeFami TF106411.

    Miscellaneous databases

    ChiTaRSi SETDB1. human.
    EvolutionaryTracei Q15047.
    GeneWikii SETDB1.
    GenomeRNAii 9869.
    NextBioi 37203.
    PROi Q15047.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15047.
    Bgeei Q15047.
    CleanExi HS_SETDB1.
    Genevestigatori Q15047.

    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. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANT SER-506.
      Tissue: Muscle and Uterus.
    5. "SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins."
      Schultz D.C., Ayyanathan K., Negorev D., Maul G.G., Rauscher F.J. III
      Genes Dev. 16:919-932(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF 729-CYS--CYS-731; HIS-1224; CYS-1226 AND CYS-1279, INTERACTION WITH TRIM28.
    6. "Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation."
      Ayyanathan K., Lechner M.S., Bell P., Maul G.G., Schultz D.C., Yamada Y., Tanaka K., Torigoe K., Rauscher F.J. III
      Genes Dev. 17:1855-1869(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression."
      Wang H., An W., Cao R., Xia L., Erdjument-Bromage H., Chatton B., Tempst P., Roeder R.G., Zhang Y.
      Mol. Cell 12:475-487(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH ATF7IP.
    8. "Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly."
      Sarraf S.A., Stancheva I.
      Mol. Cell 15:595-605(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MBD1 AND CHAF1A.
    9. "In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation."
      Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J., Carpenter A.E., Belmont A.S., van Driel R.
      Mol. Cell. Biol. 25:4552-4564(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX1 AND CBX5.
    10. "Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins."
      Lyst M.J., Nan X., Stancheva I.
      EMBO J. 25:5317-5328(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MBD1.
    11. "Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins."
      Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.
      J. Biol. Chem. 280:13928-13935(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF7IP AND ATF7IP2.
    12. "The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells."
      Li H., Rauch T., Chen Z.-X., Szabo P.E., Riggs A.D., Pfeifer G.P.
      J. Biol. Chem. 281:19489-19500(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNMT3A AND DNMT3B.
    13. "NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression."
      Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A., Shi Y., Shi Y., Gill G.
      Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUMO2.
    14. "ESET/SETDB1 gene expression and histone H3 (K9) trimethylation in Huntington's disease."
      Ryu H., Lee J., Hagerty S.W., Soh B.Y., McAlpin S.E., Cormier K.A., Smith K.M., Ferrante R.J.
      Proc. Natl. Acad. Sci. U.S.A. 103:19176-19181(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: EXPRESSION IN HUNTINGTON DISEASE.
    15. Cited for: FUNCTION, INTERACTION WITH CHD7; NLK1 AND PPARG, PHOSPHORYLATION AT THR-976, MUTAGENESIS OF THR-976.
    16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
      Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
      Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH REST; CDYL; WIZ; EHMT1 AND EHMT2.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and promotes tumour cell motility and invasion."
      Kokura K., Sun L., Bedford M.T., Fang J.
      EMBO J. 29:3673-3687(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MPHOSPH8.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "The crystal structure of Tudor domain of human histone-lysine N-methyltransferase SETDB1."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 196-402.

    Entry informationi

    Entry nameiSETB1_HUMAN
    AccessioniPrimary (citable) accession number: Q15047
    Secondary accession number(s): A6NEW2
    , Q5SZD8, Q5SZD9, Q5SZE0, Q5SZE7, Q96GM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 159 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Highly up-regulated in Huntington disease patients, suggesting that participates in the altered chromatin modulation and transcription dysfunction observed in Huntington disease. Its down-regulation has salubrious effects on patients, suggesting that it may be a promising treatment in Huntington disease patients.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3