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Q9Z148

- EHMT2_MOUSE

UniProt

Q9Z148 - EHMT2_MOUSE

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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

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. 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
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).
REACT_235780. RNA Polymerase I Transcription Initiation.

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-KW
  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. 1 Publication
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 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

BgeeiQ9Z148.
CleanExiMM_EHMT2.
ExpressionAtlasiQ9Z148. baseline and differential.
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 658-961, 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.
GeneTreeiENSGT00760000118855.
HOGENOMiHOG000231216.
HOVERGENiHBG028394.
InParanoidiQ9Z148.
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

        10         20         30         40         50
MRGLPRGRGL MRARGRGRAA PTGGRGRGRG GAHRGRGRPR SLLSLPRAQA
60 70 80 90 100
SWAPQLPAGL TGPPVPCLPS QGEAPAEMGA LLLEKEPRGA AERVHSSLGD
110 120 130 140 150
TPQSEETLPK ANPDSLEPAG PSSPASVTVT VGDEGADTPV GAASLIGDEP
160 170 180 190 200
ESLEGDGGRI VLGHATKSFP SSPSKGGACP SRAKMSMTGA GKSPPSVQSL
210 220 230 240 250
AMRLLSMPGA QGAATAGPEP SPATTAAQEG QPKVHRARKT MSKPSNGQPP
260 270 280 290 300
IPEKRPPEVQ HFRMSDDMHL GKVTSDVAKR RKLNSGSLSE DLGSAGGSGD
310 320 330 340 350
IILEKGEPRP LEEWETVVGD DFSLYYDAYS VDERVDSDSK SEVEALAEQL
360 370 380 390 400
SEEEEEEEEE EEEEEEEEEE EEEEEEDEES GNQSDRSGSS GRRKAKKKWR
410 420 430 440 450
KDSPWVKPSR KRRKREPPRA KEPRGVNGVG SSGPSEYMEV PLGSLELPSE
460 470 480 490 500
GTLSPNHAGV SNDTSSLETE RGFEELPLCS CRMEAPKIDR ISERAGHKCM
510 520 530 540 550
ATESVDGELL GCNAAILKRE TMRPSSRVAL MVLCEAHRAR MVKHHCCPGC
560 570 580 590 600
GYFCTAGTFL ECHPDFRVAH RFHKACVSQL NGMVFCPHCG EDASEAQEVT
610 620 630 640 650
IPRGDGGTPP IGTAAPALPP LAHDAPGRAD TSQPSARMRG HGEPRRPPCD
660 670 680 690 700
PLADTIDSSG PSLTLPNGGC LSAVGLPPGP GREALEKALV IQESERRKKL
710 720 730 740 750
RFHPRQLYLS VKQGELQKVI LMLLDNLDPN FQSDQQSKRT PLHAAAQKGS
760 770 780 790 800
VEICHVLLQA GANINAVDKQ QRTPLMEAVV NNHLEVARYM VQLGGCVYSK
810 820 830 840 850
EEDGSTCLHH AAKIGNLEMV SLLLSTGQVD VNAQDSGGWT PIIWAAEHKH
860 870 880 890 900
IDVIRMLLTR GADVTLTDNE ENICLHWASF TGSAAIAEVL LNAQCDLHAV
910 920 930 940 950
NYHGDTPLHI AARESYHDCV LLFLSRGANP ELRNKEGDTA WDLTPERSDV
960 970 980 990 1000
WFALQLNRKL RLGVGNRAVR TEKIICRDVA RGYENVPIPC VNGVDGEPCP
1010 1020 1030 1040 1050
EDYKYISENC ETSTMNIDRN ITHLQHCTCV DDCSSSNCLC GQLSIRCWYD
1060 1070 1080 1090 1100
KDGRLLQEFN KIEPPLIFEC NQACSCWRSC KNRVVQSGIK VRLQLYRTAK
1110 1120 1130 1140 1150
MGWGVRALQT IPQGTFICEY VGELISDAEA DVREDDSYLF DLDNKDGEVY
1160 1170 1180 1190 1200
CIDARYYGNI SRFINHLCDP NIIPVRVFML HQDLRFPRIA FFSSRDIRTG
1210 1220 1230 1240 1250
EELGFDYGDR FWDIKSKYFT CQCGSEKCKH SAEAIALEQS RLARLDPHPE
1260
LLPDLSSLPP INT
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 AAC84164.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAC84165.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAH25539.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH58357.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 658-961, 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

BindingDBi Q9Z148.
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 ENSGT00760000118855.
HOGENOMi HOG000231216.
HOVERGENi HBG028394.
InParanoidi Q9Z148.
KOi K11420.
OMAi AQASWAP.
OrthoDBi EOG744T8D.
PhylomeDBi Q9Z148.
TreeFami TF106443.

Enzyme and pathway databases

Reactomei REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_235780. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

NextBioi 363413.
PROi Q9Z148.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z148.
CleanExi MM_EHMT2.
ExpressionAtlasi Q9Z148. baseline and differential.
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: November 26, 2014
This is version 142 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