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Protein

Histone-lysine N-methyltransferase EHMT2

Gene

Ehmt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi1027Zinc 1By similarity1
Metal bindingi1027Zinc 2By similarity1
Metal bindingi1029Zinc 1By similarity1
Metal bindingi1033Zinc 1By similarity1
Metal bindingi1033Zinc 3By similarity1
Metal bindingi1038Zinc 1By similarity1
Metal bindingi1040Zinc 2By similarity1
Metal bindingi1070Zinc 2By similarity1
Metal bindingi1070Zinc 3By similarity1
Metal bindingi1074Zinc 2By similarity1
Metal bindingi1076Zinc 3By similarity1
Metal bindingi1080Zinc 3By similarity1
Binding sitei1120Histone H3K9meBy similarity1
Binding sitei1138S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi1168Zinc 4By similarity1
Metal bindingi1221Zinc 4By similarity1
Metal bindingi1223Zinc 4By similarity1
Metal bindingi1228Zinc 4By similarity1

GO - Molecular functioni

  • C2H2 zinc finger domain binding Source: UniProtKB
  • histone-lysine N-methyltransferase activity Source: UniProtKB
  • histone methyltransferase activity (H3-K27 specific) Source: UniProtKB
  • histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  • p53 binding Source: MGI
  • promoter-specific chromatin binding Source: MGI
  • protein-lysine N-methyltransferase activity Source: MGI
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • behavioral response to cocaine Source: MGI
  • cellular response to cocaine Source: MGI
  • cellular response to drug Source: Ensembl
  • cellular response to starvation Source: MGI
  • DNA methylation Source: UniProtKB
  • DNA methylation on cytosine within a CG sequence Source: MGI
  • fertilization Source: MGI
  • germ cell development Source: MGI
  • histone H3-K27 methylation Source: MGI
  • histone H3-K9 methylation Source: MGI
  • histone lysine methylation Source: MGI
  • histone methylation Source: UniProtKB
  • long-term memory Source: Ensembl
  • negative regulation of autophagosome assembly Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • neuron fate specification Source: MGI
  • organ growth Source: MGI
  • peptidyl-lysine dimethylation Source: UniProtKB
  • phenotypic switching Source: MGI
  • regulation of DNA methylation Source: Ensembl
  • regulation of DNA replication Source: UniProtKB
  • regulation of histone H3-K4 methylation Source: Ensembl
  • regulation of histone H3-K9 methylation Source: Ensembl
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • response to ethanol Source: Ensembl
  • response to fungicide Source: Ensembl
  • spermatid development Source: MGI
  • 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

BRENDAi1.97.1.10. 3474.
ReactomeiR-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-6804760. Regulation of TP53 Activity through Methylation.

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
Proteomesi
  • UP000000589 Componenti: 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

  • nuclear chromatin Source: MGI
  • nucleoplasm Source: MGI
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi1120Y → V in GM7; defective in methyltransferase activity without affecting DNA methylation; when associated with F-1207. 1 Publication1
Mutagenesisi1162R → H: Strongly reduces histone methyltransferase activity. 1 Publication1
Mutagenesisi1165 – 1168Missing : Abolishes histone methyltransferase activity and subsequent repression. 2 Publications4
Mutagenesisi1165 – 1168Missing in GM3; does not form heterodimer with EHMT1 and is defective in mediating both H3K9me and DNA methylation. 2 Publications4
Mutagenesisi1165 – 1166NH → LE in GM6; does not form heterodimer with EHMT1 and is defective in mediating H3K9me. 1 Publication2
Mutagenesisi1168C → A in GM4; defective in methyltransferase activity without affecting DNA methylation. 1 Publication1
Mutagenesisi1207Y → F in GM7; defective in methyltransferase activity without affecting DNA methylation; when associated with V-1120. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2169718.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001860691 – 1263Histone-lysine N-methyltransferase EHMT2Add BLAST1263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40Asymmetric dimethylarginineCombined sources1
Modified residuei97PhosphoserineBy similarity1
Modified residuei101PhosphothreonineBy similarity1
Modified residuei104PhosphoserineBy similarity1
Modified residuei193PhosphoserineCombined sources1
Modified residuei239N6,N6,N6-trimethyllysine; by EHMT2; alternateBy similarity1
Modified residuei239N6,N6-dimethyllysine; by EHMT2; alternateBy similarity1
Modified residuei285PhosphoserineBy similarity1
Modified residuei294PhosphoserineBy similarity1
Modified residuei298PhosphoserineBy similarity1
Modified residuei403PhosphoserineBy similarity1
Modified residuei465PhosphoserineCombined sources1
Modified residuei466PhosphoserineCombined sources1
Modified residuei608PhosphothreonineBy similarity1
Modified residuei1257PhosphoserineBy similarity1
Modified residuei1263PhosphothreonineBy similarity1

Post-translational modificationi

Methylated at Lys-239; automethylated.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ9Z148.
PeptideAtlasiQ9Z148.
PRIDEiQ9Z148.

PTM databases

iPTMnetiQ9Z148.
PhosphoSitePlusiQ9Z148.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSMUSG00000013787.
CleanExiMM_EHMT2.
ExpressionAtlasiQ9Z148. baseline and differential.
GenevisibleiQ9Z148. MM.

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

GO - Molecular functioni

  • C2H2 zinc finger domain binding Source: UniProtKB
  • p53 binding Source: MGI

Protein-protein interaction databases

BioGridi225335. 8 interactors.
DIPiDIP-31916N.
IntActiQ9Z148. 6 interactors.
MINTiMINT-2736375.
STRINGi10090.ENSMUSP00000013931.

Chemistry databases

BindingDBiQ9Z148.

Structurei

3D structure databases

ProteinModelPortaliQ9Z148.
SMRiQ9Z148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati702 – 731ANK 1Add BLAST30
Repeati737 – 766ANK 2Add BLAST30
Repeati770 – 799ANK 3Add BLAST30
Repeati803 – 833ANK 4Add BLAST31
Repeati837 – 866ANK 5Add BLAST30
Repeati870 – 899ANK 6Add BLAST30
Repeati903 – 932ANK 7Add BLAST30
Domaini1025 – 1088Pre-SETPROSITE-ProRule annotationAdd BLAST64
Domaini1091 – 1208SETPROSITE-ProRule annotationAdd BLAST118
Domaini1217 – 1233Post-SETAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni870 – 872Histone H3K9me bindingBy similarity3
Regioni1101 – 1103S-adenosyl-L-methionine bindingBy similarity3
Regioni1127 – 1146Interaction with histone H3By similarityAdd BLAST20
Regioni1165 – 1166S-adenosyl-L-methionine bindingBy similarity2
Regioni1207 – 1210Interaction with histone H3By similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi352 – 379Poly-GluAdd BLAST28

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

eggNOGiKOG1082. Eukaryota.
COG0666. LUCA.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000231216.
HOVERGENiHBG028394.
InParanoidiQ9Z148.
KOiK11420.
OMAiQASWAPQ.
OrthoDBiEOG091G00U6.
PhylomeDBiQ9Z148.
TreeFamiTF106443.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR007728. Pre-SET_dom.
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.
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. AlignAdd to basket

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

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0022141 – 57Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST57
Alternative sequenceiVSP_00221558 – 71AGLTG…CLPSQ → MAAAAGAAAAAAAE in isoform 2 and isoform 3. 2 PublicationsAdd BLAST14
Alternative sequenceiVSP_002216426 – 459Missing in isoform 2. 1 PublicationAdd BLAST34

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.
UCSCiuc008ceb.3. mouse. [Q9Z148-2]
uc008cec.3. mouse. [Q9Z148-3]
uc008ced.3. 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.
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.

3D structure databases

ProteinModelPortaliQ9Z148.
SMRiQ9Z148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi225335. 8 interactors.
DIPiDIP-31916N.
IntActiQ9Z148. 6 interactors.
MINTiMINT-2736375.
STRINGi10090.ENSMUSP00000013931.

Chemistry databases

BindingDBiQ9Z148.
ChEMBLiCHEMBL2169718.

PTM databases

iPTMnetiQ9Z148.
PhosphoSitePlusiQ9Z148.

Proteomic databases

PaxDbiQ9Z148.
PeptideAtlasiQ9Z148.
PRIDEiQ9Z148.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000013931; ENSMUSP00000013931; ENSMUSG00000013787. [Q9Z148-1]
ENSMUST00000078061; ENSMUSP00000077208; ENSMUSG00000013787. [Q9Z148-2]
ENSMUST00000114033; ENSMUSP00000109667; ENSMUSG00000013787. [Q9Z148-3]
GeneIDi110147.
KEGGimmu:110147.
UCSCiuc008ceb.3. mouse. [Q9Z148-2]
uc008cec.3. mouse. [Q9Z148-3]
uc008ced.3. mouse. [Q9Z148-1]

Organism-specific databases

CTDi10919.
MGIiMGI:2148922. Ehmt2.

Phylogenomic databases

eggNOGiKOG1082. Eukaryota.
COG0666. LUCA.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000231216.
HOVERGENiHBG028394.
InParanoidiQ9Z148.
KOiK11420.
OMAiQASWAPQ.
OrthoDBiEOG091G00U6.
PhylomeDBiQ9Z148.
TreeFamiTF106443.

Enzyme and pathway databases

BRENDAi1.97.1.10. 3474.
ReactomeiR-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-6804760. Regulation of TP53 Activity through Methylation.

Miscellaneous databases

PROiQ9Z148.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000013787.
CleanExiMM_EHMT2.
ExpressionAtlasiQ9Z148. baseline and differential.
GenevisibleiQ9Z148. MM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR007728. Pre-SET_dom.
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.
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]
ProtoNetiSearch...

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 30, 2016
This is version 161 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.