Q96KQ7 (EHMT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	EHMT2
Synonyms:	BAT8, C6orf30, G9A, KMT1C, NG36

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1210 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.9 Ref.15 Ref.20 Ref.25
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.9
Subunit structure	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. Ref.10 Ref.11 Ref.12 Ref.18 Ref.20 Ref.23
Subcellular location	Nucleus. Chromosome. Note: Associates with euchromatic regions. Does not associate with heterochromatin. Ref.9
Tissue specificity	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. Ref.1
Domain	The SET domain mediates interaction with WIZ. Ref.16 The ANK repeats bind H3K9me1 and H3K9me2. Ref.16
Post-translational modification	Methylated at Lys-185; automethylated. Ref.15
Sequence similarities	Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily. Contains 7 ANK repeats. Contains 1 post-SET domain. Contains 1 pre-SET domain. Contains 1 SET domain.
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 (Ref.1). It is uncertain whether Met-1 or Met-21 is the initiator methionine.
Sequence caution	The sequence AAD21811.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAD21812.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAH02686.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAH09351.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAH18718.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH20970.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB63294.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAB63295.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA49491.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	ANK repeat Repeat
Ligand	Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA methylation Inferred from sequence or structural similarity. Source: UniProtKB DNA methylation on cytosine within a CG sequence Inferred from electronic annotation. Source: Compara fertilization Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara organ growth Inferred from electronic annotation. Source: Compara pachytene Inferred from electronic annotation. Source: Compara peptidyl-lysine dimethylation Inferred from direct assay Ref.20. Source: UniProtKB regulation of DNA replication Inferred from mutant phenotype Ref.25. Source: UniProtKB spermatid development Inferred from electronic annotation. Source: Compara synaptonemal complex assembly Inferred from electronic annotation. Source: Compara
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	histone methyltransferase activity (H3-K27 specific) Inferred from sequence or structural similarity. Source: UniProtKB histone methyltransferase activity (H3-K9 specific) Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GFI1	Q99684	2	EBI-744366,EBI-949368
Gfi1	Q07120	3	EBI-744366,EBI-4289236	From a different organism.
HDAC1	Q13547	2	EBI-744366,EBI-301834
PRDM5	Q9NQX1	3	EBI-744366,EBI-4292031
PRRC2B	Q5JSZ5	2	EBI-744366,EBI-744891

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q96KQ7-1)

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.

Isoform 2 (identifier: Q96KQ7-2)

Also known as: NG36G9a-SPI;

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

Isoform 3 (identifier: Q96KQ7-3)

Also known as: NG36;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1210

1210

Histone-lysine N-methyltransferase EHMT2

PRO_0000186068

Regions

Repeat

649 – 678

30

ANK 1

Repeat

684 – 713

30

ANK 2

Repeat

717 – 746

30

ANK 3

Repeat

750 – 780

31

ANK 4

Repeat

784 – 813

30

ANK 5

Repeat

817 – 846

30

ANK 6

Repeat

850 – 879

30

ANK 7

Domain

972 – 1035

64

Pre-SET

Domain

1037 – 1159

123

SET

Domain

1164 – 1180

17

Post-SET

Region

817 – 819

3

Histone H3K9me binding By similarity

Region

1048 – 1050

3

S-adenosyl-L-methionine binding

Region

1074 – 1093

20

Interaction with histone H3 By similarity

Region

1112 – 1113

2

S-adenosyl-L-methionine binding

Region

1154 – 1157

4

Interaction with histone H3 By similarity

Compositional bias

2 – 13

12

Poly-Ala

Compositional bias

160 – 163

4

Poly-Ala

Compositional bias

300 – 326

27

Poly-Glu

Sites

Metal binding

974

1

Zinc 1

Metal binding

974

1

Zinc 2

Metal binding

976

1

Zinc 1

Metal binding

980

1

Zinc 1

Metal binding

980

1

Zinc 3

Metal binding

985

1

Zinc 1

Metal binding

987

1

Zinc 2

Metal binding

1017

1

Zinc 2

Metal binding

1017

1

Zinc 3

Metal binding

1021

1

Zinc 2

Metal binding

1023

1

Zinc 3

Metal binding

1027

1

Zinc 3

Metal binding

1115

1

Zinc 4

Metal binding

1168

1

Zinc 4

Metal binding

1170

1

Zinc 4

Metal binding

1175

1

Zinc 4

Binding site

1067

1

Histone H3K9me By similarity

Binding site

1085

1

S-adenosyl-L-methionine

Amino acid modifications

Modified residue

140

1

Phosphoserine Ref.17 Ref.22 Ref.24

Modified residue

173

1

Phosphoserine Ref.17

Modified residue

185

1

N6,N6,N6-trimethyllysine; by EHMT2; alternate Ref.15

Modified residue

185

1

N6,N6-dimethyllysine; by EHMT2; alternate Ref.15

Modified residue

232

1

Phosphoserine Ref.17 Ref.22 Ref.24

Modified residue

246

1

Phosphoserine Ref.13 Ref.17 Ref.22 Ref.24

Modified residue

413

1

Phosphoserine Ref.24

Modified residue

555

1

Phosphothreonine By similarity

Modified residue

569

1

Phosphoserine Ref.14

Modified residue

1204

1

Phosphoserine Ref.24

Modified residue

1210

1

Phosphothreonine Ref.17

Natural variations

Alternative sequence

195 – 202

8

PPVPEKRP → VSGMGEMG in isoform 3.

VSP_002212

Alternative sequence

203 – 1210

1008

Missing in isoform 3.

VSP_002213

Alternative sequence

373 – 406

34

Missing in isoform 2.

VSP_002211

Natural variant

55

1

T → N. Ref.1 Ref.5 Ref.6 Ref.7
Corresponds to variant rs7887 [ dbSNP | Ensembl ].

VAR_027973

Natural variant

1165

1

Y → F.
Corresponds to variant rs13919 [ dbSNP | Ensembl ].

VAR_027974

Experimental info

Mutagenesis

786

1

W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.16

Mutagenesis

791

1

W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.16

Mutagenesis

794

1

E → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.16

Mutagenesis

817

1

E → R: Impairs binding to histone H3K9me. Ref.16

Mutagenesis

824

1

W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.16

Mutagenesis

852

1

D → R: Impairs binding to histone H3K9me. Ref.16

Sequence conflict

178

1

P → S in CAC86666. Ref.2

Sequence conflict

985

1

C → R in CAC86666. Ref.2

Sequence conflict

994

1

C → R in CAA49491. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1210

Helix Strand Turn

Details...

Beta strand

920 – 924

5

Turn

926 – 929

4

Beta strand

931 – 933

3

Beta strand

937 – 943

7

Beta strand

949 – 952

4

Beta strand

957 – 960

4

Helix

968 – 970

3

Beta strand

977 – 980

4

Helix

986 – 990

5

Beta strand

1008 – 1010

3

Beta strand

1021 – 1023

3

Beta strand

1027 – 1029

3

Helix

1032 – 1034

3

Beta strand

1040 – 1044

5

Beta strand

1046 – 1056

11

Beta strand

1063 – 1067

5

Beta strand

1069 – 1073

5

Helix

1074 – 1077

4

Beta strand

1086 – 1089

4

Beta strand

1097 – 1105

9

Helix

1107 – 1110

4

Beta strand

1118 – 1127

10

Beta strand

1135 – 1142

8

Helix

1156 – 1162

7

Turn

1163 – 1165

3

Beta strand

1176 – 1178

3

Helix

1179 – 1188

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: A6C5DC6B72801520	FASTA	1,210	132,370
	10 20 30 40 50 60 MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET LPKATPDSLE 70 80 90 100 110 120 PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG DLRGGRILLG HATKSFPSSP 130 140 150 160 170 180 SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV 190 200 210 220 230 240 HRARKTMSKP GNGQPPVPEK RPPEIQHFRM SDDVHSLGKV TSDLAKRRKL NSGGGLSEEL 250 260 270 280 290 300 GSARRSGEVT LTKGDPGSLE EWETVVGDDF SLYYDSYSVD ERVDSDSKSE VEALTEQLSE 310 320 330 340 350 360 EEEEEEEEEE EEEEEEEEEE EEEDEESGNQ SDRSGSSGRR KAKKKWRKDS PWVKPSRKRR 370 380 390 400 410 420 KREPPRAKEP RGVNGVGSSG PSEYMEVPLG SLELPSEGTL SPNHAGVSND TSSLETERGF 430 440 450 460 470 480 EELPLCSCRM EAPKIDRISE RAGHKCMATE SVDGELSGCN AAILKRETMR PSSRVALMVL 490 500 510 520 530 540 CETHRARMVK HHCCPGCGYF CTAGTFLECH PDFRVAHRFH KACVSQLNGM VFCPHCGEDA 550 560 570 580 590 600 SEAQEVTIPR GDGVTPPAGT AAPAPPPLSQ DVPGRADTSQ PSARMRGHGE PRRPPCDPLA 610 620 630 640 650 660 DTIDSSGPSL TLPNGGCLSA VGLPLGPGRE ALEKALVIQE SERRKKLRFH PRQLYLSVKQ 670 680 690 700 710 720 GELQKVILML LDNLDPNFQS DQQSKRTPLH AAAQKGSVEI CHVLLQAGAN INAVDKQQRT 730 740 750 760 770 780 PLMEAVVNNH LEVARYMVQR GGCVYSKEED GSTCLHHAAK IGNLEMVSLL LSTGQVDVNA 790 800 810 820 830 840 QDSGGWTPII WAAEHKHIEV IRMLLTRGAD VTLTDNEENI CLHWASFTGS AAIAEVLLNA 850 860 870 880 890 900 RCDLHAVNYH GDTPLHIAAR ESYHDCVLLF LSRGANPELR NKEGDTAWDL TPERSDVWFA 910 920 930 940 950 960 LQLNRKLRLG VGNRAIRTEK IICRDVARGY ENVPIPCVNG VDGEPCPEDY KYISENCETS 970 980 990 1000 1010 1020 TMNIDRNITH LQHCTCVDDC SSSNCLCGQL SIRCWYDKDG RLLQEFNKIE PPLIFECNQA 1030 1040 1050 1060 1070 1080 CSCWRNCKNR VVQSGIKVRL QLYRTAKMGW GVRALQTIPQ GTFICEYVGE LISDAEADVR 1090 1100 1110 1120 1130 1140 EDDSYLFDLD NKDGEVYCID ARYYGNISRF INHLCDPNII PVRVFMLHQD LRFPRIAFFS 1150 1160 1170 1180 1190 1200 SRDIRTGEEL GFDYGDRFWD IKSKYFTCQC GSEKCKHSAE AIALEQSRLA RLDPHPELLP 1210 ELGSLPPVNT
	Isoform 2 (NG36G9a-SPI) [UniParc]. Checksum: 887FC5E322B772B9	FASTA	1,176	129,019
	10 20 30 40 50 60 MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET LPKATPDSLE 70 80 90 100 110 120 PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG DLRGGRILLG HATKSFPSSP 130 140 150 160 170 180 SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV 190 200 210 220 230 240 HRARKTMSKP GNGQPPVPEK RPPEIQHFRM SDDVHSLGKV TSDLAKRRKL NSGGGLSEEL 250 260 270 280 290 300 GSARRSGEVT LTKGDPGSLE EWETVVGDDF SLYYDSYSVD ERVDSDSKSE VEALTEQLSE 310 320 330 340 350 360 EEEEEEEEEE EEEEEEEEEE EEEDEESGNQ SDRSGSSGRR KAKKKWRKDS PWVKPSRKRR 370 380 390 400 410 420 KREPPRAKEP RGVSNDTSSL ETERGFEELP LCSCRMEAPK IDRISERAGH KCMATESVDG 430 440 450 460 470 480 ELSGCNAAIL KRETMRPSSR VALMVLCETH RARMVKHHCC PGCGYFCTAG TFLECHPDFR 490 500 510 520 530 540 VAHRFHKACV SQLNGMVFCP HCGEDASEAQ EVTIPRGDGV TPPAGTAAPA PPPLSQDVPG 550 560 570 580 590 600 RADTSQPSAR MRGHGEPRRP PCDPLADTID SSGPSLTLPN GGCLSAVGLP LGPGREALEK 610 620 630 640 650 660 ALVIQESERR KKLRFHPRQL YLSVKQGELQ KVILMLLDNL DPNFQSDQQS KRTPLHAAAQ 670 680 690 700 710 720 KGSVEICHVL LQAGANINAV DKQQRTPLME AVVNNHLEVA RYMVQRGGCV YSKEEDGSTC 730 740 750 760 770 780 LHHAAKIGNL EMVSLLLSTG QVDVNAQDSG GWTPIIWAAE HKHIEVIRML LTRGADVTLT 790 800 810 820 830 840 DNEENICLHW ASFTGSAAIA EVLLNARCDL HAVNYHGDTP LHIAARESYH DCVLLFLSRG 850 860 870 880 890 900 ANPELRNKEG DTAWDLTPER SDVWFALQLN RKLRLGVGNR AIRTEKIICR DVARGYENVP 910 920 930 940 950 960 IPCVNGVDGE PCPEDYKYIS ENCETSTMNI DRNITHLQHC TCVDDCSSSN CLCGQLSIRC 970 980 990 1000 1010 1020 WYDKDGRLLQ EFNKIEPPLI FECNQACSCW RNCKNRVVQS GIKVRLQLYR TAKMGWGVRA 1030 1040 1050 1060 1070 1080 LQTIPQGTFI CEYVGELISD AEADVREDDS YLFDLDNKDG EVYCIDARYY GNISRFINHL 1090 1100 1110 1120 1130 1140 CDPNIIPVRV FMLHQDLRFP RIAFFSSRDI RTGEELGFDY GDRFWDIKSK YFTCQCGSEK 1150 1160 1170 CKHSAEAIAL EQSRLARLDP HPELLPELGS LPPVNT
	Isoform 3 (NG36) [UniParc]. Checksum: 339618C3DA895788	FASTA	202	19,864
	10 20 30 40 50 60 MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET LPKATPDSLE 70 80 90 100 110 120 PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG DLRGGRILLG HATKSFPSSP 130 140 150 160 170 180 SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV 190 200 HRARKTMSKP GNGQVSGMGE MG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, VARIANT ASN-55.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Salivary gland.
[3]	"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].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-55.
[6]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-55.
[7]	"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] OF 6-1210 (ISOFORM 1), VARIANT ASN-55. Tissue: Muscle and Uterus.
[8]	"The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats." Milner C.M., Campbell R.D. Biochem. J. 290:811-818(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-1210, FUNCTION. Tissue: Histiocytic lymphoma.
[9]	"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, FUNCTION, SUBCELLULAR LOCATION.
[10]	"A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells." Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y. Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EHMT1; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
[11]	"Gfi1b alters histone methylation at target gene promoters and sites of gamma-satellite containing heterochromatin." Vassen L., Fiolka K., Moeroey T. EMBO J. 25:2409-2419(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GFI1B.
[12]	"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.
[13]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Protein lysine methyltransferase G9a acts on non-histone targets." Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A. Nat. Chem. Biol. 4:344-346(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, METHYLATION AT LYS-185, MASS SPECTROMETRY.
[16]	"The ankyrin repeats of G9a and GLP histone methyltransferases are mono-and dimethyllysine binding modules." Collins R.E., Northrop J.P., Horton J.R., Lee D.Y., Zhang X., Stallcup M.R., Cheng X. Nat. Struct. Mol. Biol. 15:245-250(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN ANK REPEATS, MUTAGENESIS OF TRP-786; TRP-791; GLU-794; GLU-817; TRP-824 AND ASP-852.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-173; SER-232; SER-246 AND THR-1210, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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.
[19]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[20]	"G9a and Glp methylate lysine 373 in the tumor suppressor p53." Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X., Jenuwein T., Reinberg D., Berger S.L. J. Biol. Chem. 285:9636-9641(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53.
[21]	Erratum Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X., Jenuwein T., Reinberg D., Berger S.L. J. Biol. Chem. 285:18122-18122(2010)
[22]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232 AND SER-246, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1." Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E. Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SMARCAD1.
[24]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232; SER-246; SER-413 AND SER-1204, MASS SPECTROMETRY.
[25]	"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.
[26]	"Structural biology of human H3K9 methyltransferases." Wu H., Min J., Lunin V.V., Antoshenko T., Dombrovski L., Zeng H., Allali-Hassani A., Campagna-Slater V., Vedadi M., Arrowsmith C.H., Plotnikov A.N., Schapira M. PLoS ONE 5:E8570-E8570(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 913-1193 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00096972.
IPI00220795.
IPI00220796.

RefSeq

NP_006700.3. NM_006709.3.
NP_079532.5. NM_025256.5.

UniGene

Hs.709218.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2O8J	X-ray	1.80	A/B/C/D	913-1193	[»]
3DM1	X-ray	2.40	B/D/F/H	179-190	[»]
3K5K	X-ray	1.70	A/B	913-1193	[»]
3RJW	X-ray	2.56	A/B	913-1193	[»]

ProteinModelPortal

Q96KQ7.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34461N.

IntAct

Q96KQ7. 31 interactions.

MINT

MINT-1441977.

STRING

9606.ENSP00000397323.

Polymorphism databases

DMDM

116241348.

Proteomic databases

PaxDb

Q96KQ7.

PRIDE

Q96KQ7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375530; ENSP00000364680; ENSG00000204371.
ENST00000375537; ENSP00000364687; ENSG00000204371.
ENST00000383372; ENSP00000372863; ENSG00000206376.
ENST00000383373; ENSP00000372864; ENSG00000206376.
ENST00000420336; ENSP00000396119; ENSG00000238134.
ENST00000420874; ENSP00000411035; ENSG00000236759.
ENST00000421926; ENSP00000416957; ENSG00000232045.
ENST00000429506; ENSP00000406110; ENSG00000227333.
ENST00000450075; ENSP00000392305; ENSG00000236759.
ENST00000450229; ENSP00000400838; ENSG00000227333.

GeneID

10919.

KEGG

hsa:10919.

UCSC

uc003nxz.1. human.
uc003nya.1. human.
uc003nyb.1. human.

Organism-specific databases

CTD

10919.

GeneCards

GC06M031847.

H-InvDB

HIX0166078.
HIX0166345.
HIX0167369.
HIX0184162.

HGNC

HGNC:14129. EHMT2.

HPA

HPA050550.

MIM

604599. gene.

neXtProt

NX_Q96KQ7.

PharmGKB

PA25267.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOVERGEN

HBG028394.

KO

K11420.

OrthoDB

EOG4KSPJ5.

PhylomeDB

Q96KQ7.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_tf_pathway. Regulation of Androgen receptor activity.

Gene expression databases

ArrayExpress

Q96KQ7.

Bgee

Q96KQ7.

CleanEx

HS_EHMT2.

Genevestigator

Q96KQ7.

GermOnline

ENSG00000204371. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

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]

Pfam

PF00023. Ank. 6 hits.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 6 hits.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50868. POST_SET. False negative.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q96KQ7.

ChEMBL

CHEMBL6032.

ChiTaRS

EHMT2. human.

EvolutionaryTrace

Q96KQ7.

GenomeRNAi

10919.

NextBio

41475.

SOURCE

Search...

Entry information

Entry name

EHMT2_HUMAN

Accession

Primary (citable) accession number: Q96KQ7
Secondary accession number(s): B0UZY2 , Q14349, Q5JP83, Q5JQ92, Q5JQA1, Q5JQG3, Q6PK06, Q96MH5, Q96QD0, Q9UQL8, Q9Y331

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.