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O88974

- SETB1_MOUSE

UniProt

O88974 - SETB1_MOUSE

Protein

Histone-lysine N-methyltransferase SETDB1

Gene

Setdb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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. 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 By similarity.By similarity

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi746 – 7461Zinc 1By similarity
    Metal bindingi746 – 7461Zinc 2By similarity
    Metal bindingi748 – 7481Zinc 1By similarity
    Metal bindingi752 – 7521Zinc 1By similarity
    Metal bindingi752 – 7521Zinc 3By similarity
    Metal bindingi758 – 7581Zinc 1By similarity
    Metal bindingi760 – 7601Zinc 2By similarity
    Metal bindingi798 – 7981Zinc 2By similarity
    Metal bindingi798 – 7981Zinc 3By similarity
    Metal bindingi802 – 8021Zinc 2By similarity
    Metal bindingi804 – 8041Zinc 3By similarity
    Metal bindingi809 – 8091Zinc 3By similarity
    Binding sitei868 – 8681S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei870 – 8701S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei1236 – 12361S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi1242 – 12421Zinc 4By similarity
    Metal bindingi1295 – 12951Zinc 4By similarity
    Metal bindingi1297 – 12971Zinc 4By similarity
    Metal bindingi1302 – 13021Zinc 4By similarity

    GO - Molecular functioni

    1. DNA binding Source: MGI
    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: MGI
    2. histone H3-K9 trimethylation Source: MGI
    3. inner cell mass cell proliferation Source: MGI
    4. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    5. 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
    SET domain bifurcated 1
    Gene namesi
    Name:Setdb1
    Synonyms:Eset, Kiaa0067
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1934229. Setdb1.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity
    Note: Associated with non-pericentromeric regions of chromatin.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi798 – 7981C → T: Abolishes methyltransferase activity. 1 Publication
    Mutagenesisi1242 – 12421C → T: Abolishes methyltransferase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13071307Histone-lysine N-methyltransferase SETDB1PRO_0000186065Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki182 – 182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei993 – 9931Phosphothreonine; by NLKBy similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO88974.
    PaxDbiO88974.
    PRIDEiO88974.

    PTM databases

    PhosphoSiteiO88974.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Strong expression in liver and testis.1 Publication

    Gene expression databases

    CleanExiMM_SETDB1.
    GenevestigatoriO88974.

    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 TRIM28/TIF1B, CBX1, CBX5, CHD7, DNMT3A, DNMT3B, NLK, PPARG and SUMO2. Interacts with MPHOSPH8 By similarity. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 By similarity. Interacts with ERG, HDAC1, HDAC2, SIN3A, SIN3B.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ErgP812703EBI-79658,EBI-79647

    Protein-protein interaction databases

    IntActiO88974. 9 interactions.
    MINTiMINT-1753431.
    STRINGi10090.ENSMUSP00000102788.

    Structurei

    3D structure databases

    ProteinModelPortaliO88974.
    SMRiO88974. Positions 196-397, 698-903, 1181-1306.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini257 – 32064Tudor 1Add
    BLAST
    Domaini347 – 40357Tudor 2Add
    BLAST
    Domaini611 – 68272MBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini744 – 81774Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini820 – 1282463SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1291 – 130717Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni830 – 8323S-adenosyl-L-methionine bindingBy similarity
    Regioni1239 – 12402S-adenosyl-L-methionine bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili30 – 6536Sequence 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.
    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.

    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 (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: O88974-1) [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

    MSSLPGCMSL AAAPAAADSA EIAELQQAVV EELGISMEEL RQYIDEELEK     50
    MDCIQQRKKQ LAELETWVLQ KESEVAYVDR LFDDASREVT NCESLVKDFY 100
    SKLGLQYHDS SSEDEASRPT EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL 150
    REAMAALRKS AQDVQKFMDA VNKKSSSQDL HKGTLGQVSG ELSKDGDLIV 200
    SMRILGKKRT KTWHKGTLIA IQTVGLGKKY KVKFDNKGKS LLSGNHIAYD 250
    YHPPADKLFV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG 300
    YASYVTQSEL YPICRPLKKT WEDIEDSSCR DFIEEYITAY PNRPMVLLKS 350
    GQLIKTEWEG TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS 400
    MKTSSASAME KKQGGQLRTR PNMGAVRSKG PVVQYTQDLT GTGIQFKPME 450
    PLQPIAPPAP LPIPPLSPQA ADTDLESQLA QSRKQVAKKS TSFRPGSVGS 500
    GHSSPTSSTL SENVSAGKLG INQTYRSPLA SVTSTPASAA PPVPPVPPGP 550
    PTPPGPPAPP GPLAPPAFHG MLERAPAEPS YRAPMEKLFY LPHVCSYTCL 600
    SRIRPMRNEQ YRGKNPLLVP LLYDFRRMTA RRRVNRKMGF HVIYKTPCGL 650
    CLRTMQEIER YLFETGCDFL FLEMFCLDPY VLVDRKFQPF KPFYYILDIT 700
    YGKEDVPLSC VNEIDTTPPP QVAYSKERIP GKGVFINTGP EFLVGCDCKD 750
    GCRDKSKCAC HQLTIQATAC TPGGQVNPNS GYQYKRLEEC LPTGVYECNK 800
    RCNCDPNMCT NRLVQHGLQV RLQLFKTQNK GWGIRCLDDI AKGSFVCIYA 850
    GKILTDDFAD KEGLEMGDEY FANLDHIESV ENFKEGYESD VPTSSDSSGV 900
    DMKDQEDGNS GSEDPEESND DSSDDNFCKD EDFSTSSVWR SYATRRQTRG 950
    QKENELSEMT SKDSRPPDLG PPHVPIPSSV SVGGCNPPSS EETPKNKVAS 1000
    WLSCNSVSEG GFADSDSRSS FKTSEGGDGR AGGGRGEAER ASTSGLSFKD 1050
    EGDNKQPKKE DPENRNKMPV VTEGSQNHGH NPPMKSEGLR RPASKMSVLQ 1100
    SQRVVTSTQS NPDDILTLSS STESEGESGT SRKPTAGHTS ATAVDSDDIQ 1150
    TISSGSDGDD FEDKKNLSGP TKRQVAVKST RGFALKSTHG IAIKSTNMAS 1200
    VDKGESAPVR KNTRQFYDGE ESCYIIDAKL EGNLGRYLNH SCSPNLFVQN 1250
    VFVDTHDLRF PWVAFFASKR IRAGTELTWD YNYEVGSVEG KELLCCCGAI 1300
    ECRGRLL 1307
    Length:1,307
    Mass (Da):144,549
    Last modified:November 1, 1998 - v1
    Checksum:i326AED6371D156C2
    GO
    Isoform 2 (identifier: O88974-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         482-486: SRKQV → AQSQK
         489-1307: Missing.

    Show »
    Length:488
    Mass (Da):54,696
    Checksum:i8874BF6A963B5415
    GO
    Isoform 3 (identifier: O88974-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-807: Missing.

    Show »
    Length:500
    Mass (Da):54,477
    Checksum:i164B400024020B2F
    GO
    Isoform 4 (identifier: O88974-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         474-474: D → ES

    Show »
    Length:1,308
    Mass (Da):144,650
    Checksum:iE224818F50D56E25
    GO
    Isoform 5 (identifier: O88974-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         527-1307: Missing.

    Show »
    Length:526
    Mass (Da):58,617
    Checksum:iF5B6903C06D91D11
    GO
    Isoform 6 (identifier: O88974-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         474-474: D → ES
         527-1307: Missing.

    Show »
    Length:527
    Mass (Da):58,719
    Checksum:iF2B3561EAA10EC06
    GO
    Isoform 7 (identifier: O88974-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         756-1307: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:755
    Mass (Da):84,400
    Checksum:i3AE0FFE5C3542A60
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti463 – 4631I → M in BAC40439. (PubMed:16141072)Curated
    Sequence conflicti1092 – 10921P → S in BAC65480. (PubMed:12693553)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 807807Missing in isoform 3. 1 PublicationVSP_002221Add
    BLAST
    Alternative sequencei474 – 4741D → ES in isoform 4 and isoform 6. 2 PublicationsVSP_024031
    Alternative sequencei482 – 4865SRKQV → AQSQK in isoform 2. 1 PublicationVSP_002219
    Alternative sequencei489 – 1307819Missing in isoform 2. 1 PublicationVSP_002220Add
    BLAST
    Alternative sequencei527 – 1307781Missing in isoform 5 and isoform 6. 1 PublicationVSP_024032Add
    BLAST
    Alternative sequencei756 – 1307552Missing in isoform 7. 1 PublicationVSP_024033Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091628 mRNA. Translation: AAC43039.1.
    AY091600 mRNA. Translation: AAM13922.1.
    AF546078 mRNA. Translation: AAN52358.1.
    AY226577 Genomic DNA. Translation: AAO73535.2.
    AY226577 Genomic DNA. Translation: AAO73536.2.
    BC007176 mRNA. Translation: AAH07176.1.
    BC079537 mRNA. Translation: AAH79537.1.
    AK122198 Transcribed RNA. Translation: BAC65480.3.
    AK088590 mRNA. Translation: BAC40439.1.
    CCDSiCCDS17613.1. [O88974-4]
    CCDS50991.1. [O88974-1]
    PIRiT17453.
    UniGeneiMm.490259.

    Genome annotation databases

    UCSCiuc008qjo.2. mouse. [O88974-5]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091628 mRNA. Translation: AAC43039.1 .
    AY091600 mRNA. Translation: AAM13922.1 .
    AF546078 mRNA. Translation: AAN52358.1 .
    AY226577 Genomic DNA. Translation: AAO73535.2 .
    AY226577 Genomic DNA. Translation: AAO73536.2 .
    BC007176 mRNA. Translation: AAH07176.1 .
    BC079537 mRNA. Translation: AAH79537.1 .
    AK122198 Transcribed RNA. Translation: BAC65480.3 .
    AK088590 mRNA. Translation: BAC40439.1 .
    CCDSi CCDS17613.1. [O88974-4 ]
    CCDS50991.1. [O88974-1 ]
    PIRi T17453.
    UniGenei Mm.490259.

    3D structure databases

    ProteinModelPortali O88974.
    SMRi O88974. Positions 196-397, 698-903, 1181-1306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O88974. 9 interactions.
    MINTi MINT-1753431.
    STRINGi 10090.ENSMUSP00000102788.

    PTM databases

    PhosphoSitei O88974.

    Proteomic databases

    MaxQBi O88974.
    PaxDbi O88974.
    PRIDEi O88974.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi uc008qjo.2. mouse. [O88974-5 ]

    Organism-specific databases

    MGIi MGI:1934229. Setdb1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOVERGENi HBG061013.

    Miscellaneous databases

    ChiTaRSi SETDB1. mouse.
    PROi O88974.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_SETDB1.
    Genevestigatori O88974.

    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. "Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor."
      Yang L., Xia L., Wu D.Y., Wang H., Chansky H.A., Schubach W.H., Hickstein D.D., Zhang Y.
      Oncogene 21:148-152(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME ACTIVITY, INTERACTION WITH ERG, MUTAGENESIS OF CYS-798 AND CYS-1242.
      Strain: BDF1.
      Tissue: Blood.
    2. "Genomic structure and expression of the mouse ESET gene encoding an ERG-associated histone methyltransferase with a SET domain."
      Blackburn M.L., Chansky H.A., Zielinska-Kwiatkowska A., Matsui Y., Yang L.
      Biochim. Biophys. Acta 1629:8-14(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 6), TISSUE SPECIFICITY.
      Strain: BDF1 and C57BL/6J X DBA/2.
    3. "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 3 AND 7).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
      DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-1307 (ISOFORM 4).
      Tissue: Brain.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1307 (ISOFORM 4).
      Strain: NOD.
      Tissue: Thymus.
    6. "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B."
      Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L., Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.
      Biochem. J. 369:651-657(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC1; HDAC2; SIN3A AND SIN3B.

    Entry informationi

    Entry nameiSETB1_MOUSE
    AccessioniPrimary (citable) accession number: O88974
    Secondary accession number(s): Q6AXH8
    , Q78N64, Q78N65, Q80U84, Q8BTV6, Q8CIX7, Q922K1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3