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Q9Z148

- EHMT2_MOUSE

UniProt

Q9Z148 - EHMT2_MOUSE

Protein

Histone-lysine N-methyltransferase EHMT2

Gene

Ehmt2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (15 Nov 2002)
      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 mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. 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. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.4 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1027 – 10271Zinc 1By similarity
    Metal bindingi1027 – 10271Zinc 2By similarity
    Metal bindingi1029 – 10291Zinc 1By similarity
    Metal bindingi1033 – 10331Zinc 1By similarity
    Metal bindingi1033 – 10331Zinc 3By similarity
    Metal bindingi1038 – 10381Zinc 1By similarity
    Metal bindingi1040 – 10401Zinc 2By similarity
    Metal bindingi1070 – 10701Zinc 2By similarity
    Metal bindingi1070 – 10701Zinc 3By similarity
    Metal bindingi1074 – 10741Zinc 2By similarity
    Metal bindingi1076 – 10761Zinc 3By similarity
    Metal bindingi1080 – 10801Zinc 3By similarity
    Binding sitei1120 – 11201Histone H3K9meBy similarity
    Binding sitei1138 – 11381S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi1168 – 11681Zinc 4By similarity
    Metal bindingi1221 – 12211Zinc 4By similarity
    Metal bindingi1223 – 12231Zinc 4By similarity
    Metal bindingi1228 – 12281Zinc 4By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. DNA methylation Source: UniProtKB
    2. DNA methylation on cytosine within a CG sequence Source: MGI
    3. fertilization Source: MGI
    4. germ cell development Source: MGI
    5. histone H3-K27 methylation Source: MGI
    6. histone H3-K9 methylation Source: MGI
    7. histone methylation Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    9. organ growth Source: MGI
    10. peptidyl-lysine dimethylation Source: UniProtKB
    11. regulation of DNA replication Source: UniProtKB
    12. regulation of transcription from RNA polymerase II promoter Source: MGI
    13. spermatid development Source: MGI
    14. synaptonemal complex assembly Source: MGI

    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 EHMT2 (EC:2.1.1.-, EC:2.1.1.43)
    Alternative name(s):
    Euchromatic histone-lysine N-methyltransferase 2
    HLA-B-associated transcript 8
    Histone H3-K9 methyltransferase 3
    Short name:
    H3-K9-HMTase 3
    Protein G9a
    Gene namesi
    Name:Ehmt2
    Synonyms:Bat8, G9a, Ng36
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:2148922. Ehmt2.

    Subcellular locationi

    Nucleus. Chromosome Curated
    Note: Almost excluded form nucleoli. Associates with euchromatic regions. Does not associate with heterochromatin. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 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. Interacts with UHRF1.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice show a higher level of histone H3 with acetylated 'Lys-9' (H3K9ac) and/or methylated 'Lys-4' (H3K4me), display severe developmental defects and die within E9.5-E12.5 stages.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1120 – 11201Y → V in GM7; defective in methyltransferase activity without affecting DNA methylation; when associated with F-1207. 2 Publications
    Mutagenesisi1162 – 11621R → H: Strongly reduces histone methyltransferase activity. 2 Publications
    Mutagenesisi1165 – 11684Missing: Abolishes histone methyltransferase activity and subsequent repression. 1 Publication
    Mutagenesisi1165 – 11684Missing in GM3; does not form heterodimer with EHMT1 and is defective in mediating both H3K9me and DNA methylation. 1 Publication
    Mutagenesisi1165 – 11662NH → LE in GM6; does not form heterodimer with EHMT1 and is defective in mediating H3K9me. 1 Publication
    Mutagenesisi1168 – 11681C → A in GM4; defective in methyltransferase activity without affecting DNA methylation. 2 Publications
    Mutagenesisi1207 – 12071Y → F in GM7; defective in methyltransferase activity without affecting DNA methylation; when associated with V-1120. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12631263Histone-lysine N-methyltransferase EHMT2PRO_0000186069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931PhosphoserineBy similarity
    Modified residuei239 – 2391N6,N6,N6-trimethyllysine; by EHMT2; alternateBy similarity
    Modified residuei239 – 2391N6,N6-dimethyllysine; by EHMT2; alternateBy similarity
    Modified residuei285 – 2851PhosphoserineBy similarity
    Modified residuei298 – 2981PhosphoserineBy similarity
    Modified residuei466 – 4661PhosphoserineBy similarity
    Modified residuei1257 – 12571PhosphoserineBy similarity
    Modified residuei1263 – 12631PhosphothreonineBy similarity

    Post-translational modificationi

    Methylated at Lys-239; automethylated.By similarity

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z148.
    PaxDbiQ9Z148.
    PRIDEiQ9Z148.

    PTM databases

    PhosphoSiteiQ9Z148.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9Z148.
    BgeeiQ9Z148.
    CleanExiMM_EHMT2.
    GenevestigatoriQ9Z148.

    Interactioni

    Subunit structurei

    Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, GFI1B, L3MBTL2 and YAF2 By similarity. Heterodimer; heterodimerizes with EHMT1. Interacts with WIZ.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Gfi1bO702372EBI-444966,EBI-4287943

    Protein-protein interaction databases

    BioGridi225335. 8 interactions.
    DIPiDIP-31916N.
    IntActiQ9Z148. 6 interactions.
    MINTiMINT-2736375.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z148.
    SMRiQ9Z148. Positions 685-961, 975-1245.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati702 – 73130ANK 1Add
    BLAST
    Repeati737 – 76630ANK 2Add
    BLAST
    Repeati770 – 79930ANK 3Add
    BLAST
    Repeati803 – 83331ANK 4Add
    BLAST
    Repeati837 – 86630ANK 5Add
    BLAST
    Repeati870 – 89930ANK 6Add
    BLAST
    Repeati903 – 93230ANK 7Add
    BLAST
    Domaini1025 – 108864Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1091 – 1208118SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1217 – 123317Post-SETAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni870 – 8723Histone H3K9me bindingBy similarity
    Regioni1101 – 11033S-adenosyl-L-methionine bindingBy similarity
    Regioni1127 – 114620Interaction with histone H3By similarityAdd
    BLAST
    Regioni1165 – 11662S-adenosyl-L-methionine bindingBy similarity
    Regioni1207 – 12104Interaction with histone H3By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi352 – 37928Poly-GluAdd
    BLAST

    Domaini

    The ANK repeats bind H3K9me1 and H3K9me2.By similarity
    The SET domain mediates interaction with WIZ.
    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 7 ANK repeats.PROSITE-ProRule annotation
    Contains 1 post-SET domain.Curated
    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.
    KOiK11420.
    OMAiAQASWAP.
    OrthoDBiEOG744T8D.
    PhylomeDBiQ9Z148.
    TreeFamiTF106443.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF12796. Ank_2. 3 hits.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 6 hits.
    SM00508. PostSET. 1 hit.
    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: Q9Z148-1) [UniParc]FASTAAdd to Basket

    Also known as: G9a-L

    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

    MRGLPRGRGL MRARGRGRAA PTGGRGRGRG GAHRGRGRPR SLLSLPRAQA     50
    SWAPQLPAGL TGPPVPCLPS QGEAPAEMGA LLLEKEPRGA AERVHSSLGD 100
    TPQSEETLPK ANPDSLEPAG PSSPASVTVT VGDEGADTPV GAASLIGDEP 150
    ESLEGDGGRI VLGHATKSFP SSPSKGGACP SRAKMSMTGA GKSPPSVQSL 200
    AMRLLSMPGA QGAATAGPEP SPATTAAQEG QPKVHRARKT MSKPSNGQPP 250
    IPEKRPPEVQ HFRMSDDMHL GKVTSDVAKR RKLNSGSLSE DLGSAGGSGD 300
    IILEKGEPRP LEEWETVVGD DFSLYYDAYS VDERVDSDSK SEVEALAEQL 350
    SEEEEEEEEE EEEEEEEEEE EEEEEEDEES GNQSDRSGSS GRRKAKKKWR 400
    KDSPWVKPSR KRRKREPPRA KEPRGVNGVG SSGPSEYMEV PLGSLELPSE 450
    GTLSPNHAGV SNDTSSLETE RGFEELPLCS CRMEAPKIDR ISERAGHKCM 500
    ATESVDGELL GCNAAILKRE TMRPSSRVAL MVLCEAHRAR MVKHHCCPGC 550
    GYFCTAGTFL ECHPDFRVAH RFHKACVSQL NGMVFCPHCG EDASEAQEVT 600
    IPRGDGGTPP IGTAAPALPP LAHDAPGRAD TSQPSARMRG HGEPRRPPCD 650
    PLADTIDSSG PSLTLPNGGC LSAVGLPPGP GREALEKALV IQESERRKKL 700
    RFHPRQLYLS VKQGELQKVI LMLLDNLDPN FQSDQQSKRT PLHAAAQKGS 750
    VEICHVLLQA GANINAVDKQ QRTPLMEAVV NNHLEVARYM VQLGGCVYSK 800
    EEDGSTCLHH AAKIGNLEMV SLLLSTGQVD VNAQDSGGWT PIIWAAEHKH 850
    IDVIRMLLTR GADVTLTDNE ENICLHWASF TGSAAIAEVL LNAQCDLHAV 900
    NYHGDTPLHI AARESYHDCV LLFLSRGANP ELRNKEGDTA WDLTPERSDV 950
    WFALQLNRKL RLGVGNRAVR TEKIICRDVA RGYENVPIPC VNGVDGEPCP 1000
    EDYKYISENC ETSTMNIDRN ITHLQHCTCV DDCSSSNCLC GQLSIRCWYD 1050
    KDGRLLQEFN KIEPPLIFEC NQACSCWRSC KNRVVQSGIK VRLQLYRTAK 1100
    MGWGVRALQT IPQGTFICEY VGELISDAEA DVREDDSYLF DLDNKDGEVY 1150
    CIDARYYGNI SRFINHLCDP NIIPVRVFML HQDLRFPRIA FFSSRDIRTG 1200
    EELGFDYGDR FWDIKSKYFT CQCGSEKCKH SAEAIALEQS RLARLDPHPE 1250
    LLPDLSSLPP INT 1263
    Length:1,263
    Mass (Da):138,039
    Last modified:November 15, 2002 - v2
    Checksum:i74DBFF9A36769589
    GO
    Isoform 2 (identifier: Q9Z148-2) [UniParc]FASTAAdd to Basket

    Also known as: G9a-S

    The sequence of this isoform differs from the canonical sequence as follows:
         1-57: Missing.
         58-71: AGLTGPPVPCLPSQ → MAAAAGAAAAAAAE
         426-459: Missing.

    Show »
    Length:1,172
    Mass (Da):128,420
    Checksum:i52D345057AFCF200
    GO
    Isoform 3 (identifier: Q9Z148-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-57: Missing.
         58-71: AGLTGPPVPCLPSQ → MAAAAGAAAAAAAE

    Show »
    Length:1,206
    Mass (Da):131,772
    Checksum:i5DFF4CBADB784977
    GO

    Sequence cautioni

    The sequence AAH25539.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH58357.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAC84164.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence AAC84165.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5757Missing in isoform 2 and isoform 3. 2 PublicationsVSP_002214Add
    BLAST
    Alternative sequencei58 – 7114AGLTG…CLPSQ → MAAAAGAAAAAAAE in isoform 2 and isoform 3. 2 PublicationsVSP_002215Add
    BLAST
    Alternative sequencei426 – 45934Missing in isoform 2. 1 PublicationVSP_002216Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF109906 Genomic DNA. Translation: AAC84164.1. Sequence problems.
    AF109906 Genomic DNA. Translation: AAC84165.1. Sequence problems.
    AB077209 mRNA. Translation: BAC05482.1.
    AB077210 mRNA. Translation: BAC05483.1.
    CT025759 Genomic DNA. Translation: CAM27791.1.
    BC025539 mRNA. Translation: AAH25539.1. Different initiation.
    BC058357 mRNA. Translation: AAH58357.1. Different initiation.
    CCDSiCCDS28666.1. [Q9Z148-2]
    CCDS28667.1. [Q9Z148-1]
    CCDS70797.1. [Q9Z148-3]
    RefSeqiNP_001273502.1. NM_001286573.1.
    NP_001273504.1. NM_001286575.1. [Q9Z148-3]
    NP_665829.1. NM_145830.2. [Q9Z148-1]
    NP_671493.1. NM_147151.2. [Q9Z148-2]
    UniGeneiMm.35345.

    Genome annotation databases

    EnsembliENSMUST00000013931; ENSMUSP00000013931; ENSMUSG00000013787. [Q9Z148-1]
    ENSMUST00000078061; ENSMUSP00000077208; ENSMUSG00000013787. [Q9Z148-2]
    ENSMUST00000114033; ENSMUSP00000109667; ENSMUSG00000013787. [Q9Z148-3]
    GeneIDi110147.
    KEGGimmu:110147.
    UCSCiuc008ced.2. mouse. [Q9Z148-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF109906 Genomic DNA. Translation: AAC84164.1 . Sequence problems.
    AF109906 Genomic DNA. Translation: AAC84165.1 . Sequence problems.
    AB077209 mRNA. Translation: BAC05482.1 .
    AB077210 mRNA. Translation: BAC05483.1 .
    CT025759 Genomic DNA. Translation: CAM27791.1 .
    BC025539 mRNA. Translation: AAH25539.1 . Different initiation.
    BC058357 mRNA. Translation: AAH58357.1 . Different initiation.
    CCDSi CCDS28666.1. [Q9Z148-2 ]
    CCDS28667.1. [Q9Z148-1 ]
    CCDS70797.1. [Q9Z148-3 ]
    RefSeqi NP_001273502.1. NM_001286573.1.
    NP_001273504.1. NM_001286575.1. [Q9Z148-3 ]
    NP_665829.1. NM_145830.2. [Q9Z148-1 ]
    NP_671493.1. NM_147151.2. [Q9Z148-2 ]
    UniGenei Mm.35345.

    3D structure databases

    ProteinModelPortali Q9Z148.
    SMRi Q9Z148. Positions 685-961, 975-1245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 225335. 8 interactions.
    DIPi DIP-31916N.
    IntActi Q9Z148. 6 interactions.
    MINTi MINT-2736375.

    Chemistry

    ChEMBLi CHEMBL2169718.

    PTM databases

    PhosphoSitei Q9Z148.

    Proteomic databases

    MaxQBi Q9Z148.
    PaxDbi Q9Z148.
    PRIDEi Q9Z148.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000013931 ; ENSMUSP00000013931 ; ENSMUSG00000013787 . [Q9Z148-1 ]
    ENSMUST00000078061 ; ENSMUSP00000077208 ; ENSMUSG00000013787 . [Q9Z148-2 ]
    ENSMUST00000114033 ; ENSMUSP00000109667 ; ENSMUSG00000013787 . [Q9Z148-3 ]
    GeneIDi 110147.
    KEGGi mmu:110147.
    UCSCi uc008ced.2. mouse. [Q9Z148-1 ]

    Organism-specific databases

    CTDi 10919.
    MGIi MGI:2148922. Ehmt2.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00750000117632.
    HOGENOMi HOG000231216.
    HOVERGENi HBG028394.
    KOi K11420.
    OMAi AQASWAP.
    OrthoDBi EOG744T8D.
    PhylomeDBi Q9Z148.
    TreeFami TF106443.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi EHMT2. mouse.
    NextBioi 363413.
    PROi Q9Z148.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z148.
    Bgeei Q9Z148.
    CleanExi MM_EHMT2.
    Genevestigatori Q9Z148.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF12796. Ank_2. 3 hits.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 6 hits.
    SM00508. PostSET. 1 hit.
    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. "G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis."
      Tachibana M., Sugimoto K., Nozaki M., Ueda J., Ohta T., Ohki M., Fukuda M., Takeda N., Niida H., Kato H., Shinkai Y.
      Genes Dev. 16:1779-1791(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF 1165-ASN--CYS-1168, DISRUPTION PHENOTYPE, FUNCTION.
    2. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
      Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
      Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 129.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] (ISOFORM 3).
      Tissue: Mammary tumor.
    5. "Novel NG36/G9a gene products encoded within the human and mouse MHC class III regions."
      Brown S.E., Campbell R.D., Sanderson C.M.
      Mamm. Genome 12:916-924(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
    6. "Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3."
      Tachibana M., Sugimoto K., Fukushima T., Shinkai Y.
      J. Biol. Chem. 276:25309-25317(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-1162.
    7. "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: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH EHMT1, TISSUE SPECIFICITY.
    8. "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP."
      Ueda J., Tachibana M., Ikura T., Shinkai Y.
      J. Biol. Chem. 281:20120-20128(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WIZ AND EHMT1.
    9. "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-1120; 1165-ASN--CYS-1168; 1165-ASN-HIS-1166; CYS-1168 AND TYR-1207.
    10. "UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells."
      Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.
      Nucleic Acids Res. 37:493-505(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UHRF1.
    11. "Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA."
      Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A., Carey M.F., Grunstein M.
      Mol. Cell 46:7-17(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiEHMT2_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z148
    Secondary accession number(s): A2CG75
    , Q6PE08, Q8K4R6, Q8K4R7, Q9Z149
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: November 15, 2002
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    NG36 and G9a were originally thought to derive from two separate genes.Curated

    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