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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi974 – 9741Zinc 1
Metal bindingi974 – 9741Zinc 2
Metal bindingi976 – 9761Zinc 1
Metal bindingi980 – 9801Zinc 1
Metal bindingi980 – 9801Zinc 3
Metal bindingi985 – 9851Zinc 1
Metal bindingi987 – 9871Zinc 2
Metal bindingi1017 – 10171Zinc 2
Metal bindingi1017 – 10171Zinc 3
Metal bindingi1021 – 10211Zinc 2
Metal bindingi1023 – 10231Zinc 3
Metal bindingi1027 – 10271Zinc 3
Binding sitei1067 – 10671Histone H3K9meBy similarity
Binding sitei1085 – 10851S-adenosyl-L-methionine
Metal bindingi1115 – 11151Zinc 4
Metal bindingi1168 – 11681Zinc 4
Binding sitei1169 – 11691S-adenosyl-L-methionine; via amide nitrogen
Metal bindingi1170 – 11701Zinc 4
Metal bindingi1175 – 11751Zinc 4

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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi786 – 7861W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
Mutagenesisi791 – 7911W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
Mutagenesisi794 – 7941E → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
Mutagenesisi817 – 8171E → R: Impairs binding to histone H3K9me. 1 Publication
Mutagenesisi824 – 8241W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
Mutagenesisi852 – 8521D → R: Impairs binding to histone H3K9me. 1 Publication

Organism-specific databases

PharmGKBiPA25267.

Chemistry

ChEMBLiCHEMBL6032.
GuidetoPHARMACOLOGYi2652.

Polymorphism and mutation databases

BioMutaiEHMT2.
DMDMi116241348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 12101209Histone-lysine N-methyltransferase EHMT2PRO_0000186068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei44 – 441PhosphothreonineCombined sources
Modified residuei47 – 471PhosphoserineCombined sources
Modified residuei140 – 1401PhosphoserineCombined sources
Modified residuei173 – 1731PhosphoserineCombined sources
Modified residuei185 – 1851N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication
Modified residuei185 – 1851N6,N6-dimethyllysine; by EHMT2; alternate1 Publication
Modified residuei232 – 2321PhosphoserineCombined sources
Modified residuei242 – 2421PhosphoserineCombined sources
Modified residuei246 – 2461PhosphoserineCombined sources
Modified residuei350 – 3501PhosphoserineCombined sources
Modified residuei412 – 4121PhosphoserineBy similarity
Modified residuei413 – 4131PhosphoserineCombined sources
Modified residuei555 – 5551PhosphothreonineCombined sources
Modified residuei569 – 5691PhosphoserineCombined sources
Modified residuei1204 – 12041PhosphoserineCombined sources
Modified residuei1210 – 12101PhosphothreonineCombined sources

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.
PhosphoSiteiQ96KQ7.

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
MTA1Q133309EBI-744366,EBI-714236
MTA2O947767EBI-744366,EBI-1783035
MTA3Q9BTC818EBI-744366,EBI-2461787
PRDM5Q9NQX13EBI-744366,EBI-4292031
PRRC2BQ5JSZ52EBI-744366,EBI-744891
REREQ9P2R63EBI-744366,EBI-948076
ZEB2O603156EBI-744366,EBI-717614

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi116123. 117 interactions.
DIPiDIP-34461N.
IntActiQ96KQ7. 58 interactions.
MINTiMINT-1441977.
STRINGi9606.ENSP00000364687.

Chemistry

BindingDBiQ96KQ7.

Structurei

Secondary structure

1
1210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi920 – 9245Combined sources
Turni926 – 9294Combined sources
Beta strandi931 – 9333Combined sources
Beta strandi937 – 9437Combined sources
Beta strandi949 – 9524Combined sources
Beta strandi957 – 9604Combined sources
Helixi968 – 9703Combined sources
Beta strandi977 – 9804Combined sources
Helixi986 – 9905Combined sources
Beta strandi1008 – 10103Combined sources
Beta strandi1021 – 10233Combined sources
Beta strandi1027 – 10293Combined sources
Helixi1032 – 10343Combined sources
Beta strandi1040 – 10445Combined sources
Beta strandi1046 – 105611Combined sources
Beta strandi1063 – 10675Combined sources
Beta strandi1069 – 10735Combined sources
Helixi1074 – 10774Combined sources
Beta strandi1086 – 10894Combined sources
Beta strandi1092 – 10943Combined sources
Beta strandi1097 – 11059Combined sources
Helixi1107 – 11104Combined sources
Beta strandi1118 – 112710Combined sources
Beta strandi1135 – 11428Combined sources
Helixi1156 – 11627Combined sources
Turni1163 – 11653Combined sources
Beta strandi1176 – 11783Combined sources
Helixi1179 – 118810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ96KQ7.
SMRiQ96KQ7. Positions 922-1192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96KQ7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati649 – 67830ANK 1Add
BLAST
Repeati684 – 71330ANK 2Add
BLAST
Repeati717 – 74630ANK 3Add
BLAST
Repeati750 – 78031ANK 4Add
BLAST
Repeati784 – 81330ANK 5Add
BLAST
Repeati817 – 84630ANK 6Add
BLAST
Repeati850 – 87930ANK 7Add
BLAST
Domaini972 – 103564Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini1038 – 1155118SETPROSITE-ProRule annotationAdd
BLAST
Domaini1164 – 118017Post-SETAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni817 – 8193Histone H3K9me bindingBy similarity
Regioni1048 – 10503S-adenosyl-L-methionine binding
Regioni1074 – 109320Interaction with histone H3By similarityAdd
BLAST
Regioni1112 – 11132S-adenosyl-L-methionine binding
Regioni1154 – 11574Interaction with histone H3By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 1312Poly-AlaAdd
BLAST
Compositional biasi160 – 1634Poly-Ala
Compositional biasi300 – 32627Poly-GluAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781P → S in CAC86666 (PubMed:14702039).Curated
Sequence conflicti985 – 9851C → R in CAC86666 (PubMed:14702039).Curated
Sequence conflicti994 – 9941C → R in CAA49491 (PubMed:8457211).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551T → N.4 Publications
Corresponds to variant rs7887 [ dbSNP | Ensembl ].
VAR_027973
Natural varianti1165 – 11651Y → F.
Corresponds to variant rs13919 [ dbSNP | Ensembl ].
VAR_027974

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei195 – 2028PPVPEKRP → VSGMGEMG in isoform 3. 1 PublicationVSP_002212
Alternative sequencei203 – 12101008Missing in isoform 3. 1 PublicationVSP_002213Add
BLAST
Alternative sequencei373 – 40634Missing in isoform 2. CuratedVSP_002211Add
BLAST

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
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[»]
ProteinModelPortaliQ96KQ7.
SMRiQ96KQ7. Positions 922-1192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116123. 117 interactions.
DIPiDIP-34461N.
IntActiQ96KQ7. 58 interactions.
MINTiMINT-1441977.
STRINGi9606.ENSP00000364687.

Chemistry

BindingDBiQ96KQ7.
ChEMBLiCHEMBL6032.
GuidetoPHARMACOLOGYi2652.

PTM databases

iPTMnetiQ96KQ7.
PhosphoSiteiQ96KQ7.

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.
GeneCardsiEHMT2.
H-InvDBHIX0166078.
HIX0166345.
HIX0167369.
HIX0184162.
HGNCiHGNC:14129. EHMT2.
HPAiHPA050550.
HPA060259.
MIMi604599. gene.
neXtProtiNX_Q96KQ7.
PharmGKBiPA25267.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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: September 7, 2016
This is version 171 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.