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Protein

Histone-lysine N-methyltransferase EHMT2

Gene

EHMT2

Organism
Homo sapiens (Human)
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.6 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 bindingi974Zinc 11
Metal bindingi974Zinc 21
Metal bindingi976Zinc 11
Metal bindingi980Zinc 11
Metal bindingi980Zinc 31
Metal bindingi985Zinc 11
Metal bindingi987Zinc 21
Metal bindingi1017Zinc 21
Metal bindingi1017Zinc 31
Metal bindingi1021Zinc 21
Metal bindingi1023Zinc 31
Metal bindingi1027Zinc 31
Binding sitei1067Histone H3K9meBy similarity1
Binding sitei1085S-adenosyl-L-methionine1
Metal bindingi1115Zinc 41
Metal bindingi1168Zinc 41
Binding sitei1169S-adenosyl-L-methionine; via amide nitrogen1
Metal bindingi1170Zinc 41
Metal bindingi1175Zinc 41

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: UniProtKB
  • promoter-specific chromatin binding Source: MGI
  • protein-lysine N-methyltransferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to starvation Source: MGI
  • DNA methylation Source: UniProtKB
  • histone lysine methylation Source: MGI
  • histone methylation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • peptidyl-lysine dimethylation Source: UniProtKB
  • regulation of DNA replication Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:HS06313-MONOMER.
ReactomeiR-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
R-HSA-73762. 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
Lysine N-methyltransferase 1C
Protein G9a
Gene namesi
Name:EHMT2
Synonyms:BAT8, C6orf30, G9A, KMT1C, NG36
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:14129. EHMT2.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication

  • Note: Associates with euchromatic regions. Does not associate with heterochromatin.

GO - Cellular componenti

  • nuclear chromatin Source: MGI
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi786W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication1
Mutagenesisi791W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication1
Mutagenesisi794E → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication1
Mutagenesisi817E → R: Impairs binding to histone H3K9me. 1 Publication1
Mutagenesisi824W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication1
Mutagenesisi852D → R: Impairs binding to histone H3K9me. 1 Publication1

Organism-specific databases

DisGeNETi10919.
OpenTargetsiENSG00000204371.
ENSG00000206376.
ENSG00000227333.
ENSG00000236759.
PharmGKBiPA25267.

Chemistry databases

ChEMBLiCHEMBL6032.
GuidetoPHARMACOLOGYi2652.

Polymorphism and mutation databases

BioMutaiEHMT2.
DMDMi116241348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001860682 – 1210Histone-lysine N-methyltransferase EHMT2Add BLAST1209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei40PhosphoserineCombined sources1
Modified residuei44PhosphothreonineCombined sources1
Modified residuei47PhosphoserineCombined sources1
Modified residuei140PhosphoserineCombined sources1
Modified residuei173PhosphoserineCombined sources1
Modified residuei185N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication1
Modified residuei185N6,N6-dimethyllysine; by EHMT2; alternate1 Publication1
Modified residuei232PhosphoserineCombined sources1
Modified residuei242PhosphoserineCombined sources1
Modified residuei246PhosphoserineCombined sources1
Modified residuei350PhosphoserineCombined sources1
Modified residuei412PhosphoserineBy similarity1
Modified residuei413PhosphoserineCombined sources1
Modified residuei555PhosphothreonineCombined sources1
Modified residuei569PhosphoserineCombined sources1
Modified residuei1204PhosphoserineCombined sources1
Modified residuei1210PhosphothreonineCombined sources1

Post-translational modificationi

Methylated at Lys-185; automethylated.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ96KQ7.
MaxQBiQ96KQ7.
PaxDbiQ96KQ7.
PeptideAtlasiQ96KQ7.
PRIDEiQ96KQ7.

PTM databases

iPTMnetiQ96KQ7.
PhosphoSitePlusiQ96KQ7.

Expressioni

Tissue specificityi

Expressed in all tissues examined, with high levels in fetal liver, thymus, lymph node, spleen and peripheral blood leukocytes and lower level in bone marrow.1 Publication

Gene expression databases

BgeeiENSG00000204371.
CleanExiHS_EHMT2.
ExpressionAtlasiQ96KQ7. baseline and differential.
GenevisibleiQ96KQ7. HS.

Organism-specific databases

HPAiHPA050550.
HPA060259.

Interactioni

Subunit structurei

Heterodimer; heterodimerizes with EHMT1/GLP. Interacts with GFI1B and 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. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with UHRF1. 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 EHMT2.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GATA3P2377120EBI-744366,EBI-6664760
GFI1Q996842EBI-744366,EBI-949368
Gfi1Q071203EBI-744366,EBI-4289236From a different organism.
HDAC1Q135477EBI-744366,EBI-301834
KAT2BQ928313EBI-744366,EBI-477430
KLF12Q9Y4X43EBI-744366,EBI-750750
MTA1Q133309EBI-744366,EBI-714236
MTA2O947767EBI-744366,EBI-1783035
MTA3Q9BTC818EBI-744366,EBI-2461787
PLOD3O605684EBI-744366,EBI-741582
PRDM5Q9NQX13EBI-744366,EBI-4292031
PRRC2BQ5JSZ52EBI-744366,EBI-744891
REREQ9P2R63EBI-744366,EBI-948076
ZEB2O603156EBI-744366,EBI-717614
ZNF462Q96JM23EBI-744366,EBI-1210359

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi116123. 117 interactors.
DIPiDIP-34461N.
IntActiQ96KQ7. 86 interactors.
MINTiMINT-1441977.
STRINGi9606.ENSP00000364687.

Chemistry databases

BindingDBiQ96KQ7.

Structurei

Secondary structure

11210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi920 – 924Combined sources5
Turni926 – 929Combined sources4
Beta strandi931 – 933Combined sources3
Beta strandi937 – 943Combined sources7
Beta strandi949 – 952Combined sources4
Beta strandi957 – 960Combined sources4
Helixi968 – 970Combined sources3
Beta strandi977 – 980Combined sources4
Helixi986 – 989Combined sources4
Beta strandi1008 – 1010Combined sources3
Beta strandi1021 – 1023Combined sources3
Beta strandi1027 – 1029Combined sources3
Helixi1032 – 1034Combined sources3
Beta strandi1040 – 1044Combined sources5
Beta strandi1046 – 1056Combined sources11
Beta strandi1063 – 1067Combined sources5
Beta strandi1069 – 1073Combined sources5
Helixi1074 – 1077Combined sources4
Beta strandi1084 – 1089Combined sources6
Beta strandi1092 – 1095Combined sources4
Beta strandi1097 – 1105Combined sources9
Helixi1107 – 1110Combined sources4
Beta strandi1118 – 1127Combined sources10
Beta strandi1135 – 1142Combined sources8
Helixi1156 – 1162Combined sources7
Turni1163 – 1165Combined sources3
Beta strandi1176 – 1178Combined sources3
Helixi1179 – 1187Combined sources9
Helixi1188 – 1192Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O8JX-ray1.80A/B/C/D913-1193[»]
3DM1X-ray2.40B/D/F/H179-190[»]
3K5KX-ray1.70A/B913-1193[»]
3RJWX-ray2.56A/B913-1193[»]
4NVQX-ray2.03A/B913-1193[»]
5JHNX-ray1.67A/B916-1189[»]
5JINX-ray1.85A/B916-1189[»]
5JIYX-ray1.48A/B916-1189[»]
5JJ0X-ray1.72A/B916-1189[»]
5T0KX-ray1.70A/B913-1193[»]
5T0MX-ray1.90A/B913-1193[»]
ProteinModelPortaliQ96KQ7.
SMRiQ96KQ7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96KQ7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati649 – 678ANK 1Add BLAST30
Repeati684 – 713ANK 2Add BLAST30
Repeati717 – 746ANK 3Add BLAST30
Repeati750 – 780ANK 4Add BLAST31
Repeati784 – 813ANK 5Add BLAST30
Repeati817 – 846ANK 6Add BLAST30
Repeati850 – 879ANK 7Add BLAST30
Domaini972 – 1035Pre-SETPROSITE-ProRule annotationAdd BLAST64
Domaini1038 – 1155SETPROSITE-ProRule annotationAdd BLAST118
Domaini1164 – 1180Post-SETAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni817 – 819Histone H3K9me bindingBy similarity3
Regioni1048 – 1050S-adenosyl-L-methionine binding3
Regioni1074 – 1093Interaction with histone H3By similarityAdd BLAST20
Regioni1112 – 1113S-adenosyl-L-methionine binding2
Regioni1154 – 1157Interaction with histone H3By similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 13Poly-AlaAdd BLAST12
Compositional biasi160 – 163Poly-Ala4
Compositional biasi300 – 326Poly-GluAdd BLAST27

Domaini

The SET domain mediates interaction with WIZ.1 Publication
The ANK repeats bind H3K9me1 and H3K9me2.1 Publication
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.1 Publication

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.
HOVERGENiHBG028394.
InParanoidiQ96KQ7.
KOiK11420.
PhylomeDBiQ96KQ7.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q96KQ7-1) [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

        10         20         30         40         50
MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET
60 70 80 90 100
LPKATPDSLE PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG
110 120 130 140 150
DLRGGRILLG HATKSFPSSP SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR
160 170 180 190 200
LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV HRARKTMSKP GNGQPPVPEK
210 220 230 240 250
RPPEIQHFRM SDDVHSLGKV TSDLAKRRKL NSGGGLSEEL GSARRSGEVT
260 270 280 290 300
LTKGDPGSLE EWETVVGDDF SLYYDSYSVD ERVDSDSKSE VEALTEQLSE
310 320 330 340 350
EEEEEEEEEE EEEEEEEEEE EEEDEESGNQ SDRSGSSGRR KAKKKWRKDS
360 370 380 390 400
PWVKPSRKRR KREPPRAKEP RGVNGVGSSG PSEYMEVPLG SLELPSEGTL
410 420 430 440 450
SPNHAGVSND TSSLETERGF EELPLCSCRM EAPKIDRISE RAGHKCMATE
460 470 480 490 500
SVDGELSGCN AAILKRETMR PSSRVALMVL CETHRARMVK HHCCPGCGYF
510 520 530 540 550
CTAGTFLECH PDFRVAHRFH KACVSQLNGM VFCPHCGEDA SEAQEVTIPR
560 570 580 590 600
GDGVTPPAGT AAPAPPPLSQ DVPGRADTSQ PSARMRGHGE PRRPPCDPLA
610 620 630 640 650
DTIDSSGPSL TLPNGGCLSA VGLPLGPGRE ALEKALVIQE SERRKKLRFH
660 670 680 690 700
PRQLYLSVKQ GELQKVILML LDNLDPNFQS DQQSKRTPLH AAAQKGSVEI
710 720 730 740 750
CHVLLQAGAN INAVDKQQRT PLMEAVVNNH LEVARYMVQR GGCVYSKEED
760 770 780 790 800
GSTCLHHAAK IGNLEMVSLL LSTGQVDVNA QDSGGWTPII WAAEHKHIEV
810 820 830 840 850
IRMLLTRGAD VTLTDNEENI CLHWASFTGS AAIAEVLLNA RCDLHAVNYH
860 870 880 890 900
GDTPLHIAAR ESYHDCVLLF LSRGANPELR NKEGDTAWDL TPERSDVWFA
910 920 930 940 950
LQLNRKLRLG VGNRAIRTEK IICRDVARGY ENVPIPCVNG VDGEPCPEDY
960 970 980 990 1000
KYISENCETS TMNIDRNITH LQHCTCVDDC SSSNCLCGQL SIRCWYDKDG
1010 1020 1030 1040 1050
RLLQEFNKIE PPLIFECNQA CSCWRNCKNR VVQSGIKVRL QLYRTAKMGW
1060 1070 1080 1090 1100
GVRALQTIPQ GTFICEYVGE LISDAEADVR EDDSYLFDLD NKDGEVYCID
1110 1120 1130 1140 1150
ARYYGNISRF INHLCDPNII PVRVFMLHQD LRFPRIAFFS SRDIRTGEEL
1160 1170 1180 1190 1200
GFDYGDRFWD IKSKYFTCQC GSEKCKHSAE AIALEQSRLA RLDPHPELLP
1210
ELGSLPPVNT
Length:1,210
Mass (Da):132,370
Last modified:October 17, 2006 - v3
Checksum:iA6C5DC6B72801520
GO
Isoform 2 (identifier: Q96KQ7-2) [UniParc]FASTAAdd to basket
Also known as: NG36G9a-SPI

The sequence of this isoform differs from the canonical sequence as follows:
     373-406: Missing.

Show »
Length:1,176
Mass (Da):129,019
Checksum:i887FC5E322B772B9
GO
Isoform 3 (identifier: Q96KQ7-3) [UniParc]FASTAAdd to basket
Also known as: NG36

The sequence of this isoform differs from the canonical sequence as follows:
     195-202: PPVPEKRP → VSGMGEMG
     203-1210: Missing.

Show »
Length:202
Mass (Da):19,864
Checksum:i339618C3DA895788
GO

Sequence cautioni

The sequence AAD21811 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAD21812 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAH02686 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH09351 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH18718 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH20970 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB63294 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAB63295 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAA49491 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti178P → S in CAC86666 (PubMed:14702039).Curated1
Sequence conflicti985C → R in CAC86666 (PubMed:14702039).Curated1
Sequence conflicti994C → R in CAA49491 (PubMed:8457211).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02797355T → N.4 PublicationsCorresponds to variant rs7887dbSNPEnsembl.1
Natural variantiVAR_0279741165Y → F.Corresponds to variant rs13919dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002212195 – 202PPVPEKRP → VSGMGEMG in isoform 3. 1 Publication8
Alternative sequenceiVSP_002213203 – 1210Missing in isoform 3. 1 PublicationAdd BLAST1008
Alternative sequenceiVSP_002211373 – 406Missing in isoform 2. CuratedAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ315532 mRNA. Translation: CAC86666.1.
AK056936 mRNA. Translation: BAB71314.1.
AF134726 Genomic DNA. Translation: AAD21811.1. Sequence problems.
AF134726 Genomic DNA. Translation: AAD21812.1. Sequence problems.
BA000025 Genomic DNA. Translation: BAB63294.1. Sequence problems.
BA000025 Genomic DNA. Translation: BAB63295.1. Sequence problems.
AL662834 Genomic DNA. Translation: CAI17747.2.
AL662834 Genomic DNA. Translation: CAI17748.1.
AL671762 Genomic DNA. Translation: CAI18224.2.
AL671762 Genomic DNA. Translation: CAI18226.2.
AL844853 Genomic DNA. Translation: CAI41852.1.
AL844853 Genomic DNA. Translation: CAI41853.1.
CR388219, CR388202 Genomic DNA. Translation: CAQ07473.1.
CR388219, CR388202 Genomic DNA. Translation: CAQ07474.1.
CR936237 Genomic DNA. Translation: CAQ09159.1.
CR759784 Genomic DNA. Translation: CAQ09311.1.
CR388202, CR388219 Genomic DNA. Translation: CAQ09508.1.
CR388202, CR388219 Genomic DNA. Translation: CAQ09509.1.
CH471081 Genomic DNA. Translation: EAX03542.1.
BC002686 mRNA. Translation: AAH02686.2. Different initiation.
BC009351 mRNA. Translation: AAH09351.1. Different initiation.
BC018718 mRNA. Translation: AAH18718.1. Different initiation.
BC020970 mRNA. Translation: AAH20970.2. Different initiation.
X69838 mRNA. Translation: CAA49491.1. Different initiation.
CCDSiCCDS4725.1. [Q96KQ7-1]
CCDS4726.1. [Q96KQ7-2]
RefSeqiNP_001276342.1. NM_001289413.1.
NP_001305762.1. NM_001318833.1.
NP_006700.3. NM_006709.4. [Q96KQ7-1]
NP_079532.5. NM_025256.6. [Q96KQ7-2]
UniGeneiHs.709218.

Genome annotation databases

EnsembliENST00000375530; ENSP00000364680; ENSG00000204371. [Q96KQ7-2]
ENST00000375537; ENSP00000364687; ENSG00000204371. [Q96KQ7-1]
ENST00000383372; ENSP00000372863; ENSG00000206376. [Q96KQ7-2]
ENST00000383373; ENSP00000372864; ENSG00000206376. [Q96KQ7-1]
ENST00000420336; ENSP00000396119; ENSG00000238134.
ENST00000420874; ENSP00000411035; ENSG00000236759. [Q96KQ7-2]
ENST00000421926; ENSP00000416957; ENSG00000232045.
ENST00000429506; ENSP00000406110; ENSG00000227333. [Q96KQ7-1]
ENST00000450075; ENSP00000392305; ENSG00000236759. [Q96KQ7-1]
ENST00000450229; ENSP00000400838; ENSG00000227333. [Q96KQ7-2]
GeneIDi10919.
KEGGihsa:10919.
UCSCiuc003nxz.3. human. [Q96KQ7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ315532 mRNA. Translation: CAC86666.1.
AK056936 mRNA. Translation: BAB71314.1.
AF134726 Genomic DNA. Translation: AAD21811.1. Sequence problems.
AF134726 Genomic DNA. Translation: AAD21812.1. Sequence problems.
BA000025 Genomic DNA. Translation: BAB63294.1. Sequence problems.
BA000025 Genomic DNA. Translation: BAB63295.1. Sequence problems.
AL662834 Genomic DNA. Translation: CAI17747.2.
AL662834 Genomic DNA. Translation: CAI17748.1.
AL671762 Genomic DNA. Translation: CAI18224.2.
AL671762 Genomic DNA. Translation: CAI18226.2.
AL844853 Genomic DNA. Translation: CAI41852.1.
AL844853 Genomic DNA. Translation: CAI41853.1.
CR388219, CR388202 Genomic DNA. Translation: CAQ07473.1.
CR388219, CR388202 Genomic DNA. Translation: CAQ07474.1.
CR936237 Genomic DNA. Translation: CAQ09159.1.
CR759784 Genomic DNA. Translation: CAQ09311.1.
CR388202, CR388219 Genomic DNA. Translation: CAQ09508.1.
CR388202, CR388219 Genomic DNA. Translation: CAQ09509.1.
CH471081 Genomic DNA. Translation: EAX03542.1.
BC002686 mRNA. Translation: AAH02686.2. Different initiation.
BC009351 mRNA. Translation: AAH09351.1. Different initiation.
BC018718 mRNA. Translation: AAH18718.1. Different initiation.
BC020970 mRNA. Translation: AAH20970.2. Different initiation.
X69838 mRNA. Translation: CAA49491.1. Different initiation.
CCDSiCCDS4725.1. [Q96KQ7-1]
CCDS4726.1. [Q96KQ7-2]
RefSeqiNP_001276342.1. NM_001289413.1.
NP_001305762.1. NM_001318833.1.
NP_006700.3. NM_006709.4. [Q96KQ7-1]
NP_079532.5. NM_025256.6. [Q96KQ7-2]
UniGeneiHs.709218.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O8JX-ray1.80A/B/C/D913-1193[»]
3DM1X-ray2.40B/D/F/H179-190[»]
3K5KX-ray1.70A/B913-1193[»]
3RJWX-ray2.56A/B913-1193[»]
4NVQX-ray2.03A/B913-1193[»]
5JHNX-ray1.67A/B916-1189[»]
5JINX-ray1.85A/B916-1189[»]
5JIYX-ray1.48A/B916-1189[»]
5JJ0X-ray1.72A/B916-1189[»]
5T0KX-ray1.70A/B913-1193[»]
5T0MX-ray1.90A/B913-1193[»]
ProteinModelPortaliQ96KQ7.
SMRiQ96KQ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116123. 117 interactors.
DIPiDIP-34461N.
IntActiQ96KQ7. 86 interactors.
MINTiMINT-1441977.
STRINGi9606.ENSP00000364687.

Chemistry databases

BindingDBiQ96KQ7.
ChEMBLiCHEMBL6032.
GuidetoPHARMACOLOGYi2652.

PTM databases

iPTMnetiQ96KQ7.
PhosphoSitePlusiQ96KQ7.

Polymorphism and mutation databases

BioMutaiEHMT2.
DMDMi116241348.

Proteomic databases

EPDiQ96KQ7.
MaxQBiQ96KQ7.
PaxDbiQ96KQ7.
PeptideAtlasiQ96KQ7.
PRIDEiQ96KQ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375530; ENSP00000364680; ENSG00000204371. [Q96KQ7-2]
ENST00000375537; ENSP00000364687; ENSG00000204371. [Q96KQ7-1]
ENST00000383372; ENSP00000372863; ENSG00000206376. [Q96KQ7-2]
ENST00000383373; ENSP00000372864; ENSG00000206376. [Q96KQ7-1]
ENST00000420336; ENSP00000396119; ENSG00000238134.
ENST00000420874; ENSP00000411035; ENSG00000236759. [Q96KQ7-2]
ENST00000421926; ENSP00000416957; ENSG00000232045.
ENST00000429506; ENSP00000406110; ENSG00000227333. [Q96KQ7-1]
ENST00000450075; ENSP00000392305; ENSG00000236759. [Q96KQ7-1]
ENST00000450229; ENSP00000400838; ENSG00000227333. [Q96KQ7-2]
GeneIDi10919.
KEGGihsa:10919.
UCSCiuc003nxz.3. human. [Q96KQ7-1]

Organism-specific databases

CTDi10919.
DisGeNETi10919.
GeneCardsiEHMT2.
H-InvDBHIX0166078.
HIX0166345.
HIX0167369.
HIX0184162.
HGNCiHGNC:14129. EHMT2.
HPAiHPA050550.
HPA060259.
MIMi604599. gene.
neXtProtiNX_Q96KQ7.
OpenTargetsiENSG00000204371.
ENSG00000206376.
ENSG00000227333.
ENSG00000236759.
PharmGKBiPA25267.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1082. Eukaryota.
COG0666. LUCA.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOVERGENiHBG028394.
InParanoidiQ96KQ7.
KOiK11420.
PhylomeDBiQ96KQ7.
TreeFamiTF106443.

Enzyme and pathway databases

BioCyciZFISH:HS06313-MONOMER.
ReactomeiR-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiEHMT2. human.
EvolutionaryTraceiQ96KQ7.
GeneWikiiEHMT2.
GenomeRNAii10919.
PROiQ96KQ7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204371.
CleanExiHS_EHMT2.
ExpressionAtlasiQ96KQ7. baseline and differential.
GenevisibleiQ96KQ7. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q96KQ7
Secondary accession number(s): B0UZY2
, Q14349, Q5JP83, Q5JQ92, Q5JQA1, Q5JQG3, Q6PK06, Q96MH5, Q96QD0, Q9UQL8, Q9Y331
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 174 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

While NG36 and G9a were originally thought to derive from 2 separate genes, all G9A transcripts also contain the in frame coding sequence of NG36.1 Publication
It is uncertain whether Met-1 or Met-21 is the initiator methionine.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.