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Q5DW34

- EHMT1_MOUSE

UniProt

Q5DW34 - EHMT1_MOUSE

Protein

Histone-lysine N-methyltransferase EHMT1

Gene

Ehmt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (08 Mar 2011)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Methyltransferase activity is inhibited by BIX-01294. Efficiently inhibited by compound E72, a BIX-01294 derivative in which the diazepane ring and the benzyl are replaced with a 3-dimethylaminopropyl and a 5-aminopentyl group at sites B and C, respectively By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1060 – 10601Zinc 1By similarity
    Metal bindingi1060 – 10601Zinc 2By similarity
    Metal bindingi1062 – 10621Zinc 1By similarity
    Metal bindingi1066 – 10661Zinc 1By similarity
    Metal bindingi1066 – 10661Zinc 3By similarity
    Metal bindingi1071 – 10711Zinc 1By similarity
    Metal bindingi1073 – 10731Zinc 2By similarity
    Metal bindingi1103 – 11031Zinc 2By similarity
    Metal bindingi1103 – 11031Zinc 3By similarity
    Metal bindingi1107 – 11071Zinc 2By similarity
    Metal bindingi1109 – 11091Zinc 3By similarity
    Metal bindingi1113 – 11131Zinc 3By similarity
    Binding sitei1153 – 11531Histone H3K9meBy similarity
    Binding sitei1171 – 11711S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi1201 – 12011Zinc 4By similarity
    Metal bindingi1254 – 12541Zinc 4By similarity
    Binding sitei1255 – 12551S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi1256 – 12561Zinc 4By similarity
    Metal bindingi1261 – 12611Zinc 4By similarity

    GO - Molecular functioni

    1. C2H2 zinc finger domain binding Source: UniProt
    2. histone methyltransferase activity (H3-K27 specific) Source: UniProtKB
    3. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. DNA methylation Source: UniProtKB
    2. embryo development Source: UniProtKB
    3. histone H3-K27 methylation Source: GOC
    4. histone H3-K9 methylation Source: GOC
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    7. peptidyl-lysine dimethylation Source: UniProtKB
    8. peptidyl-lysine monomethylation Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_206033. Senescence-Associated Secretory Phenotype (SASP).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase EHMT1 (EC:2.1.1.-, EC:2.1.1.43)
    Alternative name(s):
    Euchromatic histone-lysine N-methyltransferase 1
    Short name:
    Eu-HMTase1
    G9a-like protein 1
    Short name:
    GLP
    Short name:
    GLP1
    Lysine N-methyltransferase 1D
    Gene namesi
    Name:Ehmt1
    Synonyms:Euhmtase1, Glp, Kmt1d
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1924933. Ehmt1.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication
    Note: Associates with euchromatic regions.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Embryos die around E9.5. Levels of H3K9me1 and H3K9me2 are drastically reduced.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1153 – 11531Y → V in LM7; does not prevent methyltransferase activity; when associated with F-1240. 1 Publication
    Mutagenesisi1198 – 12014Missing in LM3; does not form heterodimer with EHMT2 and is defective in mediating both H3K9me and DNA methylation.
    Mutagenesisi1201 – 12011C → A in LM4; does not prevent methyltransferase activity. 1 Publication
    Mutagenesisi1240 – 12401Y → F in LM7; does not prevent methyltransferase activity; when associated with V-1153. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12961296Histone-lysine N-methyltransferase EHMT1PRO_0000405844Add
    BLAST

    Proteomic databases

    MaxQBiQ5DW34.
    PaxDbiQ5DW34.
    PRIDEiQ5DW34.

    PTM databases

    PhosphoSiteiQ5DW34.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiQ5DW34.
    GenevestigatoriQ5DW34.

    Interactioni

    Subunit structurei

    Interacts with WIZ. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts with MPHOSPH8 By similarity. Interacts with CDYL. Interacts with REST only in the presence of CDYL. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 By similarity. Heterodimer; heterodimerizes with EHMT2. Interacts (via ANK repeats) with RELA (when monomethylated at 'Lys-310').By similarity2 Publications

    Protein-protein interaction databases

    BioGridi218847. 6 interactions.
    DIPiDIP-49000N.
    DIP-59572N.
    IntActiQ5DW34. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5DW34.
    SMRiQ5DW34. Positions 714-1264.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati735 – 76430ANK 1Add
    BLAST
    Repeati770 – 79930ANK 2Add
    BLAST
    Repeati803 – 83230ANK 3Add
    BLAST
    Repeati836 – 86631ANK 4Add
    BLAST
    Repeati870 – 89930ANK 5Add
    BLAST
    Repeati903 – 93230ANK 6Add
    BLAST
    Repeati936 – 96530ANK 7Add
    BLAST
    Repeati969 – 100234ANK 8Add
    BLAST
    Domaini1058 – 112164Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1124 – 1241118SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni903 – 9053Histone H3K9me bindingBy similarity
    Regioni1134 – 11363S-adenosyl-L-methionine bindingBy similarity
    Regioni1160 – 117920Interaction with histone H3By similarityAdd
    BLAST
    Regioni1198 – 11992S-adenosyl-L-methionine bindingBy similarity
    Regioni1240 – 12434Interaction with histone H3By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi440 – 4478Poly-Arg
    Compositional biasi1290 – 12934Poly-Ala

    Domaini

    The ANK repeats specifically recognize and bind H3K9me1 and H3K9me2 By similarity. They also specifically recognize and bind RELA subunit of NF-kappa-B, when RELA is monomethylated at 'Lys-310'.By similarity1 Publication
    The SET domain mediates interaction with WIZ.By similarity
    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 8 ANK repeats.PROSITE-ProRule annotation
    Contains 1 pre-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    GeneTreeiENSGT00750000117632.
    HOGENOMiHOG000231216.
    HOVERGENiHBG028394.
    InParanoidiQ5DW34.
    KOiK11420.
    OMAiSDFGRQQ.
    OrthoDBiEOG744T8D.
    PhylomeDBiQ5DW34.
    TreeFamiTF106443.

    Family and domain databases

    Gene3Di1.25.40.20. 3 hits.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF00023. Ank. 1 hit.
    PF12796. Ank_2. 2 hits.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 7 hits.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS50867. PRE_SET. 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: Q5DW34-1) [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

    MAAADAEQAV LAKQETKQDC CMKTELLRED TPMAADEGST EKQEGETPMA     50
    ADGETNGSCE KSGDPSHLNA PKHTQENTRA SPQEGTNRVS RVAENGVSER 100
    DTEVGKQNHV TADDFMQTSV IGSNGYFLNK PALQGQPLRT PNILTSSLPG 150
    HAAKTLPGGA SKCRTLSALP QTPTTAPTVP GEGSADTEDR KPTASGTDVR 200
    VHRARKTMPK SILGLHAASK DHREVQDHKE PKEDINRNIS ECGRQQLLPT 250
    FPALHQSLPQ NQCYMATTKS QTACLPFVLA AAVSRKKKRR MGTYSLVPKK 300
    KTKVLKQRTV IEMFKSITHS TVGAKGEKAL DDSALHVNGE SLEMDSEDED 350
    SDELEDDEDH GAEQAAAFPT EDSRTSKESM SETDRAAKMD GDSEEEQESP 400
    DTGEDEDGGD ESDLSSESSI KKKFLKRRGK TDSPWIKPAR KRRRRSRKKP 450
    SSMLGSEACK SSPGSMEQAA LGDSAGYMEV SLDSLDLRVR GILSSQTENE 500
    GLASGPDVLG TDGLQEVPLC SCRMETPKSR EISTLANNQC MATESVDHEL 550
    GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF 600
    MECQPESSIS HRFHKDCASR VNNASYCPHC GEEASKAKEV TIAKADTTST 650
    VTLAPGQEKS LAAEGRADTT TGSIAGAPED ERSQSTAPQA PECFDPAGPA 700
    GLVRPTSGLS QGPGKETLES ALIALDSEKP KKLRFHPKQL YFSARQGELQ 750
    KVLLMLVDGI DPNFKMEHQS KRSPLHAAAE AGHVDICHML VQAGANIDTC 800
    SEDQRTPLME AAENNHLDAV KYLIKAGAQV DPKDAEGSTC LHLAAKKGHY 850
    DVVQYLLSNG QMDVNCQDDG GWTPMIWATE YKHVELVKLL LSKGSDINIR 900
    DNEENICLHW AAFSGCVDIA EILLAAKCDL HAVNIHGDSP LHIAARENRY 950
    DCVVLFLSRD SDVTLKNKEG ETPLQCASLS SQVWSALQMS KALRDSAPDK 1000
    PVAVEKTVSR DIARGYERIP IPCVNAVDSE LCPTNYKYVS QNCVTSPMNI 1050
    DRNITHLQYC VCVDDCSSST CMCGQLSMRC WYDKDGRLLP EFNMAEPPLI 1100
    FECNHACSCW RNCRNRVVQN GLRARLQLYR TQDMGWGVRS LQDIPLGTFV 1150
    CEYVGELISD SEADVREEDS YLFDLDNKDG EVYCIDARFY GNVSRFINHH 1200
    CEPNLVPVRV FMSHQDLRFP RIAFFSTRLI QAGEQLGFDY GERFWDVKGK 1250
    LFSCRCGSSK CRHSSAALAQ RQASAAQEPQ ENGLPDTSSA AAADPL 1296
    Length:1,296
    Mass (Da):141,999
    Last modified:March 8, 2011 - v2
    Checksum:iB7783B6F38D3C7CB
    GO
    Isoform 2 (identifier: Q5DW34-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         273-279: Missing.
         455-500: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,243
    Mass (Da):136,496
    Checksum:iAB666EE7F3CE9EC3
    GO
    Isoform 3 (identifier: Q5DW34-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         550-597: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,248
    Mass (Da):136,631
    Checksum:i6D881B82F181F36E
    GO

    Sequence cautioni

    The sequence CAM22112.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti411 – 4111E → D in BAD90007. (PubMed:15774718)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei273 – 2797Missing in isoform 2. 1 PublicationVSP_040724
    Alternative sequencei455 – 50046Missing in isoform 2. 1 PublicationVSP_040725Add
    BLAST
    Alternative sequencei550 – 59748Missing in isoform 3. 1 PublicationVSP_040726Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB205007 mRNA. Translation: BAD90007.1.
    AL732525 Genomic DNA. Translation: CAM22112.1. Different initiation.
    AL732525 Genomic DNA. Translation: CAM22113.1.
    AL732525 Genomic DNA. Translation: CAM22114.1.
    BC056938 mRNA. Translation: AAH56938.1.
    BC089302 mRNA. Translation: AAH89302.1.
    CCDSiCCDS15740.1. [Q5DW34-1]
    CCDS59634.1. [Q5DW34-2]
    CCDS59636.1. [Q5DW34-3]
    RefSeqiNP_001012536.2. NM_001012518.3. [Q5DW34-1]
    NP_001103156.1. NM_001109686.2. [Q5DW34-2]
    NP_001103157.1. NM_001109687.2. [Q5DW34-3]
    UniGeneiMm.24176.

    Genome annotation databases

    EnsembliENSMUST00000046227; ENSMUSP00000046077; ENSMUSG00000036893. [Q5DW34-3]
    ENSMUST00000102938; ENSMUSP00000100002; ENSMUSG00000036893. [Q5DW34-1]
    ENSMUST00000114432; ENSMUSP00000110075; ENSMUSG00000036893. [Q5DW34-2]
    ENSMUST00000147147; ENSMUSP00000119057; ENSMUSG00000036893.
    GeneIDi77683.
    KEGGimmu:77683.
    UCSCiuc008iph.3. mouse. [Q5DW34-3]
    uc008ipi.3. mouse. [Q5DW34-1]
    uc012brr.2. mouse. [Q5DW34-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB205007 mRNA. Translation: BAD90007.1 .
    AL732525 Genomic DNA. Translation: CAM22112.1 . Different initiation.
    AL732525 Genomic DNA. Translation: CAM22113.1 .
    AL732525 Genomic DNA. Translation: CAM22114.1 .
    BC056938 mRNA. Translation: AAH56938.1 .
    BC089302 mRNA. Translation: AAH89302.1 .
    CCDSi CCDS15740.1. [Q5DW34-1 ]
    CCDS59634.1. [Q5DW34-2 ]
    CCDS59636.1. [Q5DW34-3 ]
    RefSeqi NP_001012536.2. NM_001012518.3. [Q5DW34-1 ]
    NP_001103156.1. NM_001109686.2. [Q5DW34-2 ]
    NP_001103157.1. NM_001109687.2. [Q5DW34-3 ]
    UniGenei Mm.24176.

    3D structure databases

    ProteinModelPortali Q5DW34.
    SMRi Q5DW34. Positions 714-1264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 218847. 6 interactions.
    DIPi DIP-49000N.
    DIP-59572N.
    IntActi Q5DW34. 3 interactions.

    PTM databases

    PhosphoSitei Q5DW34.

    Proteomic databases

    MaxQBi Q5DW34.
    PaxDbi Q5DW34.
    PRIDEi Q5DW34.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000046227 ; ENSMUSP00000046077 ; ENSMUSG00000036893 . [Q5DW34-3 ]
    ENSMUST00000102938 ; ENSMUSP00000100002 ; ENSMUSG00000036893 . [Q5DW34-1 ]
    ENSMUST00000114432 ; ENSMUSP00000110075 ; ENSMUSG00000036893 . [Q5DW34-2 ]
    ENSMUST00000147147 ; ENSMUSP00000119057 ; ENSMUSG00000036893 .
    GeneIDi 77683.
    KEGGi mmu:77683.
    UCSCi uc008iph.3. mouse. [Q5DW34-3 ]
    uc008ipi.3. mouse. [Q5DW34-1 ]
    uc012brr.2. mouse. [Q5DW34-2 ]

    Organism-specific databases

    CTDi 79813.
    MGIi MGI:1924933. Ehmt1.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00750000117632.
    HOGENOMi HOG000231216.
    HOVERGENi HBG028394.
    InParanoidi Q5DW34.
    KOi K11420.
    OMAi SDFGRQQ.
    OrthoDBi EOG744T8D.
    PhylomeDBi Q5DW34.
    TreeFami TF106443.

    Enzyme and pathway databases

    Reactomei REACT_206033. Senescence-Associated Secretory Phenotype (SASP).

    Miscellaneous databases

    NextBioi 347359.
    PROi Q5DW34.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5DW34.
    Genevestigatori Q5DW34.

    Family and domain databases

    Gene3Di 1.25.40.20. 3 hits.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 1 hit.
    PF12796. Ank_2. 2 hits.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 7 hits.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS50867. PRE_SET. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9."
      Tachibana M., Ueda J., Fukuda M., Takeda N., Ohta T., Iwanari H., Sakihama T., Kodama T., Hamakubo T., Shinkai Y.
      Genes Dev. 19:815-826(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH EHMT2, TISSUE SPECIFICITY.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] OF 34-1296 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1296 (ISOFORM 3).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "G9a/GLP complexes independently mediate H3K9 and DNA methylation to silence transcription."
      Tachibana M., Matsumura Y., Fukuda M., Kimura H., Shinkai Y.
      EMBO J. 27:2681-2690(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-1153; 1198-ASN--CYS-1201; CYS-1201 AND TYR-1240.
    5. "Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kappaB signaling."
      Levy D., Kuo A.J., Chang Y., Schaefer U., Kitson C., Cheung P., Espejo A., Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I., Kuo A.Y., Tanjing S., Cheung R., Chua K.F., Utz P.J., Shi X., Prinjha R.K.
      , Lee K., Garcia B.A., Bedford M.T., Tarakhovsky A., Cheng X., Gozani O.
      Nat. Immunol. 12:29-36(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN ANK REPEATS, INTERACTION WITH RELA.

    Entry informationi

    Entry nameiEHMT1_MOUSE
    AccessioniPrimary (citable) accession number: Q5DW34
    Secondary accession number(s): A2AIS3
    , A2AIS4, Q5EBR1, Q6PGM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 8, 2011
    Last sequence update: March 8, 2011
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 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