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Q9Z148

- EHMT2_MOUSE

UniProt

Q9Z148 - EHMT2_MOUSE

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Protein
Histone-lysine N-methyltransferase EHMT2
Gene
Ehmt2, Bat8, G9a, Ng36
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1 By similarity
Metal bindingi1027 – 10271Zinc 2 By similarity
Metal bindingi1029 – 10291Zinc 1 By similarity
Metal bindingi1033 – 10331Zinc 1 By similarity
Metal bindingi1033 – 10331Zinc 3 By similarity
Metal bindingi1038 – 10381Zinc 1 By similarity
Metal bindingi1040 – 10401Zinc 2 By similarity
Metal bindingi1070 – 10701Zinc 2 By similarity
Metal bindingi1070 – 10701Zinc 3 By similarity
Metal bindingi1074 – 10741Zinc 2 By similarity
Metal bindingi1076 – 10761Zinc 3 By similarity
Metal bindingi1080 – 10801Zinc 3 By similarity
Binding sitei1120 – 11201Histone H3K9me By similarity
Binding sitei1138 – 11381S-adenosyl-L-methionine By similarity
Metal bindingi1168 – 11681Zinc 4 By similarity
Metal bindingi1221 – 12211Zinc 4 By similarity
Metal bindingi1223 – 12231Zinc 4 By similarity
Metal bindingi1228 – 12281Zinc 4 By 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. histone-lysine N-methyltransferase activity Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. zinc ion binding Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

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 Inferred
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 UHRF1.2 Publications

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB
Complete GO annotation...

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12631263Histone-lysine N-methyltransferase EHMT2
PRO_0000186069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931Phosphoserine By similarity
Modified residuei239 – 2391N6,N6,N6-trimethyllysine; by EHMT2; alternate By similarity
Modified residuei239 – 2391N6,N6-dimethyllysine; by EHMT2; alternate By similarity
Modified residuei285 – 2851Phosphoserine By similarity
Modified residuei298 – 2981Phosphoserine By similarity
Modified residuei466 – 4661Phosphoserine By similarity
Modified residuei1257 – 12571Phosphoserine By similarity
Modified residuei1263 – 12631Phosphothreonine By 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.3 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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni870 – 8723Histone H3K9me binding By similarity
Regioni1101 – 11033S-adenosyl-L-methionine binding By similarity
Regioni1127 – 114620Interaction with histone H3 By similarity
Add
BLAST
Regioni1165 – 11662S-adenosyl-L-methionine binding By similarity
Regioni1207 – 12104Interaction with histone H3 By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi352 – 37928Poly-Glu
Add
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

Contains 7 ANK repeats.
Contains 1 post-SET domain.
Contains 1 pre-SET domain.
Contains 1 SET domain.

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.
VSP_002214Add
BLAST
Alternative sequencei58 – 7114AGLTG…CLPSQ → MAAAAGAAAAAAAE in isoform 2 and isoform 3.
VSP_002215Add
BLAST
Alternative sequencei426 – 45934Missing in isoform 2.
VSP_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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 139 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.

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

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