Q9H9B1 (EHMT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase EHMT1
EC=2.1.1.-
EC=2.1.1.43

Alternative name(s):
Euchromatic histone-lysine N-methyltransferase 1
Short name=Eu-HMTase1
G9a-like protein 1
Short name=GLP
Short name=GLP1
Histone H3-K9 methyltransferase 5
Short name=H3-K9-HMTase 5
Lysine N-methyltransferase 1D

Gene names

Name:	EHMT1
Synonyms:	EUHMTASE1, GLP, KIAA1876, KMT1D

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	1298 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 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. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Ref.4 Ref.14
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.4
Enzyme regulation	Methyltransferase activity is inhibited by BIX-01294. Efficiently inhibited by compound E72, a BIX-01294 derivative in which the diazepane ring and the benzyl are replaced with a 3-dimethylaminopropyl and a 5-aminopentyl group at sites B and C, respectively. Ref.19
Subunit structure	Heterodimer; heterodimerizes with EHMT2/G9a. Interacts with WIZ and EHMT2. 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. Interacts (via ANK repeats) with RELA (when monomethylated at 'Lys-310'). Interacts with MPHOSPH8. Ref.4 Ref.10 Ref.13 Ref.14
Subcellular location	Nucleus. Chromosome. Note: Associates with euchromatic regions.
Tissue specificity	Widely expressed. Ref.6
Domain	The ANK repeats recognize and bind RELA subunit of NF-kappa-B, when RELA is monomethylated at 'Lys-310' By similarity. They also specifically recognize and bind H3K9me1 and H3K9me2. Ref.18 The SET domain mediates interaction with WIZ. Ref.18
Involvement in disease	Kleefstra syndrome (KLESTS) [MIM:610253]: A syndrome characterized by severe mental retardation, hypotonia, brachy(micro)cephaly, and facial dysmorphisms. Additionally, congenital heart defects, urogenital defects, epilepsy and behavioral problems are frequently observed. Note: The disease is caused by mutations affecting the gene represented in this entry (Ref.9). The syndrome can be either caused by intragenic EHMT1 mutations leading to haploinsufficiency of the EHMT1 gene or by a submicroscopic 9q34.3 deletion. Although it is not known if and to what extent other genes in the 9q34.3 region contribute to the syndrome observed in deletion cases, EHMT1 seems to be the major determinant of the core disease phenotype (Ref.22). Ref.9 Ref.22
Sequence similarities	Belongs to the histone-lysine methyltransferase family. Contains 8 ANK repeats. Contains 1 pre-SET domain. Contains 1 SET domain.
Sequence caution	The sequence CAD28534.1 differs from that shown. Reason: Intron retention. The sequence CAH71077.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI17354.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Mental retardation
Domain	ANK repeat Repeat
Ligand	Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Chromatin regulator Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA methylation Inferred from sequence or structural similarity. Source: UniProtKB embryo development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-lysine dimethylation Inferred from direct assay Ref.14. Source: UniProtKB peptidyl-lysine monomethylation Inferred from sequence or structural similarity. Source: UniProtKB
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
RELA	Q04206	3	EBI-766087,EBI-73886
Rela	Q04207	5	EBI-766087,EBI-644400	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9H9B1-1)

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: Q9H9B1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.
     836-856: DAEGSTCLHLAAKKGHYEVVQ → IQKTSKVYTESQETQRSQTIL
     857-1298: Missing.

Isoform 3 (identifier: Q9H9B1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1181-1184: DGEV → ISSA
     1185-1298: Missing.

Isoform 4 (identifier: Q9H9B1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     795-808: AGANIDTCSEDQRT → FCRLGSPRSRGCLW
     809-1298: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1298

1298

Histone-lysine N-methyltransferase EHMT1

PRO_0000186067

Regions

Repeat

737 – 766

30

ANK 1

Repeat

772 – 801

30

ANK 2

Repeat

805 – 834

30

ANK 3

Repeat

838 – 868

31

ANK 4

Repeat

872 – 901

30

ANK 5

Repeat

905 – 934

30

ANK 6

Repeat

938 – 967

30

ANK 7

Repeat

971 – 1004

34

ANK 8

Domain

1060 – 1123

64

Pre-SET

Domain

1125 – 1247

123

SET

Region

905 – 907

3

Histone H3K9me binding

Region

1136 – 1138

3

S-adenosyl-L-methionine binding

Region

1162 – 1181

20

Interaction with histone H3

Region

1200 – 1201

2

S-adenosyl-L-methionine binding

Region

1242 – 1245

4

Interaction with histone H3

Compositional bias

406 – 409

4

Poly-Glu

Compositional bias

442 – 449

8

Poly-Arg

Compositional bias

1292 – 1295

4

Poly-Ala

Sites

Metal binding

1062

1

Zinc 1

Metal binding

1062

1

Zinc 2

Metal binding

1064

1

Zinc 1

Metal binding

1068

1

Zinc 1

Metal binding

1068

1

Zinc 3

Metal binding

1073

1

Zinc 1

Metal binding

1075

1

Zinc 2

Metal binding

1105

1

Zinc 2

Metal binding

1105

1

Zinc 3

Metal binding

1109

1

Zinc 2

Metal binding

1111

1

Zinc 3

Metal binding

1115

1

Zinc 3

Metal binding

1203

1

Zinc 4

Metal binding

1256

1

Zinc 4

Metal binding

1258

1

Zinc 4

Metal binding

1263

1

Zinc 4

Binding site

1155

1

Histone H3K9me

Binding site

1173

1

S-adenosyl-L-methionine

Binding site

1257

1

S-adenosyl-L-methionine; via amide nitrogen

Natural variations

Alternative sequence

1 – 31

31

Missing in isoform 2.

VSP_040716

Alternative sequence

795 – 808

14

AGANI…EDQRT → FCRLGSPRSRGCLW in isoform 4.

VSP_040717

Alternative sequence

809 – 1298

490

Missing in isoform 4.

VSP_040718

Alternative sequence

836 – 856

21

DAEGS…YEVVQ → IQKTSKVYTESQETQRSQTI L in isoform 2.

VSP_002222

Alternative sequence

857 – 1298

442

Missing in isoform 2.

VSP_002223

Alternative sequence

1181 – 1184

4

DGEV → ISSA in isoform 3.

VSP_002224

Alternative sequence

1185 – 1298

114

Missing in isoform 3.

VSP_002225

Natural variant

43

1

A → V in a breast cancer sample; somatic mutation. Ref.21

VAR_036345

Natural variant

388

1

A → T.
Corresponds to variant rs11137198 [ dbSNP | Ensembl ].

VAR_027642

Natural variant

1075

1

C → Y in KLESTS. Ref.22

VAR_069183

Natural variant

1173

1

Y → F in a breast cancer sample; somatic mutation. Ref.21

VAR_036346

Experimental info

Mutagenesis

905

1

E → A: Abolishes binding to histone H3K9me. Ref.18

Sequence conflict

555

1

N → D in AAH47504. Ref.3

Sequence conflict

561

1

E → G in AAM09024. Ref.1

Sequence conflict

561

1

E → G in BAB14321. Ref.2

Secondary structure

1

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1298

Helix Strand Turn

Details...

Helix

776 – 783

8

Helix

786 – 794

9

Helix

809 – 815

7

Helix

819 – 826

8

Turn

827 – 829

3

Helix

842 – 848

7

Helix

852 – 859

8

Turn

860 – 862

3

Helix

876 – 882

7

Helix

886 – 894

9

Helix

909 – 916

8

Helix

919 – 926

8

Turn

927 – 929

3

Helix

942 – 948

7

Helix

952 – 959

8

Turn

960 – 962

3

Helix

975 – 978

4

Helix

983 – 994

12

Beta strand

1008 – 1012

5

Turn

1014 – 1017

4

Beta strand

1019 – 1021

3

Beta strand

1025 – 1031

7

Beta strand

1037 – 1040

4

Beta strand

1045 – 1048

4

Helix

1056 – 1058

3

Beta strand

1065 – 1068

4

Helix

1074 – 1078

5

Beta strand

1096 – 1098

3

Beta strand

1109 – 1111

3

Beta strand

1115 – 1117

3

Helix

1120 – 1122

3

Beta strand

1128 – 1132

5

Beta strand

1134 – 1144

11

Beta strand

1151 – 1155

5

Beta strand

1157 – 1161

5

Helix

1162 – 1166

5

Beta strand

1174 – 1177

4

Beta strand

1180 – 1183

4

Beta strand

1185 – 1193

9

Helix

1195 – 1198

4

Beta strand

1206 – 1215

10

Beta strand

1223 – 1230

8

Helix

1244 – 1250

7

Turn

1251 – 1253

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 8, 2011. Version 4. Checksum: 071574F3FB3D371E	FASTA	1,298	141,466
	10 20 30 40 50 60 MAAADAEAVP ARGEPQQDCC VKTELLGEET PMAADEGSAE KQAGEAHMAA DGETNGSCEN 70 80 90 100 110 120 SDASSHANAA KHTQDSARVN PQDGTNTLTR IAENGVSERD SEAAKQNHVT ADDFVQTSVI 130 140 150 160 170 180 GSNGYILNKP ALQAQPLRTT STLASSLPGH AAKTLPGGAG KGRTPSAFPQ TPAAPPATLG 190 200 210 220 230 240 EGSADTEDRK LPAPGADVKV HRARKTMPKS VVGLHAASKD PREVREARDH KEPKEEINKN 250 260 270 280 290 300 ISDFGRQQLL PPFPSLHQSL PQNQCYMATT KSQTACLPFV LAAAVSRKKK RRMGTYSLVP 310 320 330 340 350 360 KKKTKVLKQR TVIEMFKSIT HSTVGSKGEK DLGASSLHVN GESLEMDSDE DDSEELEEDD 370 380 390 400 410 420 GHGAEQAAAF PTEDSRTSKE SMSEADRAQK MDGESEEEQE SVDTGEEEEG GDESDLSSES 430 440 450 460 470 480 SIKKKFLKRK GKTDSPWIKP ARKRRRRSRK KPSGALGSES YKSSAGSAEQ TAPGDSTGYM 490 500 510 520 530 540 EVSLDSLDLR VKGILSSQAE GLANGPDVLE TDGLQEVPLC SCRMETPKSR EITTLANNQC 550 560 570 580 590 600 MATESVDHEL GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF 610 620 630 640 650 660 MECQPESSIS HRFHKDCASR VNNASYCPHC GEESSKAKEV TIAKADTTST VTPVPGQEKG 670 680 690 700 710 720 SALEGRADTT TGSAAGPPLS EDDKLQGAAS HVPEGFDPTG PAGLGRPTPG LSQGPGKETL 730 740 750 760 770 780 ESALIALDSE KPKKLRFHPK QLYFSARQGE LQKVLLMLVD GIDPNFKMEH QNKRSPLHAA 790 800 810 820 830 840 AEAGHVDICH MLVQAGANID TCSEDQRTPL MEAAENNHLE AVKYLIKAGA LVDPKDAEGS 850 860 870 880 890 900 TCLHLAAKKG HYEVVQYLLS NGQMDVNCQD DGGWTPMIWA TEYKHVDLVK LLLSKGSDIN 910 920 930 940 950 960 IRDNEENICL HWAAFSGCVD IAEILLAAKC DLHAVNIHGD SPLHIAAREN RYDCVVLFLS 970 980 990 1000 1010 1020 RDSDVTLKNK EGETPLQCAS LNSQVWSALQ MSKALQDSAP DRPSPVERIV SRDIARGYER 1030 1040 1050 1060 1070 1080 IPIPCVNAVD SEPCPSNYKY VSQNCVTSPM NIDRNITHLQ YCVCIDDCSS SNCMCGQLSM 1090 1100 1110 1120 1130 1140 RCWYDKDGRL LPEFNMAEPP LIFECNHACS CWRNCRNRVV QNGLRARLQL YRTRDMGWGV 1150 1160 1170 1180 1190 1200 RSLQDIPPGT FVCEYVGELI SDSEADVREE DSYLFDLDNK DGEVYCIDAR FYGNVSRFIN 1210 1220 1230 1240 1250 1260 HHCEPNLVPV RVFMAHQDLR FPRIAFFSTR LIEAGEQLGF DYGERFWDIK GKLFSCRCGS 1270 1280 1290 PKCRHSSAAL AQRQASAAQE AQEDGLPDTS SAAAADPL
	Isoform 2 [UniParc]. Checksum: 2315F62F7806915B	FASTA	825	88,702
	10 20 30 40 50 60 MAADEGSAEK QAGEAHMAAD GETNGSCENS DASSHANAAK HTQDSARVNP QDGTNTLTRI 70 80 90 100 110 120 AENGVSERDS EAAKQNHVTA DDFVQTSVIG SNGYILNKPA LQAQPLRTTS TLASSLPGHA 130 140 150 160 170 180 AKTLPGGAGK GRTPSAFPQT PAAPPATLGE GSADTEDRKL PAPGADVKVH RARKTMPKSV 190 200 210 220 230 240 VGLHAASKDP REVREARDHK EPKEEINKNI SDFGRQQLLP PFPSLHQSLP QNQCYMATTK 250 260 270 280 290 300 SQTACLPFVL AAAVSRKKKR RMGTYSLVPK KKTKVLKQRT VIEMFKSITH STVGSKGEKD 310 320 330 340 350 360 LGASSLHVNG ESLEMDSDED DSEELEEDDG HGAEQAAAFP TEDSRTSKES MSEADRAQKM 370 380 390 400 410 420 DGESEEEQES VDTGEEEEGG DESDLSSESS IKKKFLKRKG KTDSPWIKPA RKRRRRSRKK 430 440 450 460 470 480 PSGALGSESY KSSAGSAEQT APGDSTGYME VSLDSLDLRV KGILSSQAEG LANGPDVLET 490 500 510 520 530 540 DGLQEVPLCS CRMETPKSRE ITTLANNQCM ATESVDHELG RCTNSVVKYE LMRPSNKAPL 550 560 570 580 590 600 LVLCEDHRGR MVKHQCCPGC GYFCTAGNFM ECQPESSISH RFHKDCASRV NNASYCPHCG 610 620 630 640 650 660 EESSKAKEVT IAKADTTSTV TPVPGQEKGS ALEGRADTTT GSAAGPPLSE DDKLQGAASH 670 680 690 700 710 720 VPEGFDPTGP AGLGRPTPGL SQGPGKETLE SALIALDSEK PKKLRFHPKQ LYFSARQGEL 730 740 750 760 770 780 QKVLLMLVDG IDPNFKMEHQ NKRSPLHAAA EAGHVDICHM LVQAGANIDT CSEDQRTPLM 790 800 810 820 EAAENNHLEA VKYLIKAGAL VDPKIQKTSK VYTESQETQR SQTIL
	Isoform 3 [UniParc]. Checksum: 1382C5327D3579D7	FASTA	1,184	128,689
	10 20 30 40 50 60 MAAADAEAVP ARGEPQQDCC VKTELLGEET PMAADEGSAE KQAGEAHMAA DGETNGSCEN 70 80 90 100 110 120 SDASSHANAA KHTQDSARVN PQDGTNTLTR IAENGVSERD SEAAKQNHVT ADDFVQTSVI 130 140 150 160 170 180 GSNGYILNKP ALQAQPLRTT STLASSLPGH AAKTLPGGAG KGRTPSAFPQ TPAAPPATLG 190 200 210 220 230 240 EGSADTEDRK LPAPGADVKV HRARKTMPKS VVGLHAASKD PREVREARDH KEPKEEINKN 250 260 270 280 290 300 ISDFGRQQLL PPFPSLHQSL PQNQCYMATT KSQTACLPFV LAAAVSRKKK RRMGTYSLVP 310 320 330 340 350 360 KKKTKVLKQR TVIEMFKSIT HSTVGSKGEK DLGASSLHVN GESLEMDSDE DDSEELEEDD 370 380 390 400 410 420 GHGAEQAAAF PTEDSRTSKE SMSEADRAQK MDGESEEEQE SVDTGEEEEG GDESDLSSES 430 440 450 460 470 480 SIKKKFLKRK GKTDSPWIKP ARKRRRRSRK KPSGALGSES YKSSAGSAEQ TAPGDSTGYM 490 500 510 520 530 540 EVSLDSLDLR VKGILSSQAE GLANGPDVLE TDGLQEVPLC SCRMETPKSR EITTLANNQC 550 560 570 580 590 600 MATESVDHEL GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF 610 620 630 640 650 660 MECQPESSIS HRFHKDCASR VNNASYCPHC GEESSKAKEV TIAKADTTST VTPVPGQEKG 670 680 690 700 710 720 SALEGRADTT TGSAAGPPLS EDDKLQGAAS HVPEGFDPTG PAGLGRPTPG LSQGPGKETL 730 740 750 760 770 780 ESALIALDSE KPKKLRFHPK QLYFSARQGE LQKVLLMLVD GIDPNFKMEH QNKRSPLHAA 790 800 810 820 830 840 AEAGHVDICH MLVQAGANID TCSEDQRTPL MEAAENNHLE AVKYLIKAGA LVDPKDAEGS 850 860 870 880 890 900 TCLHLAAKKG HYEVVQYLLS NGQMDVNCQD DGGWTPMIWA TEYKHVDLVK LLLSKGSDIN 910 920 930 940 950 960 IRDNEENICL HWAAFSGCVD IAEILLAAKC DLHAVNIHGD SPLHIAAREN RYDCVVLFLS 970 980 990 1000 1010 1020 RDSDVTLKNK EGETPLQCAS LNSQVWSALQ MSKALQDSAP DRPSPVERIV SRDIARGYER 1030 1040 1050 1060 1070 1080 IPIPCVNAVD SEPCPSNYKY VSQNCVTSPM NIDRNITHLQ YCVCIDDCSS SNCMCGQLSM 1090 1100 1110 1120 1130 1140 RCWYDKDGRL LPEFNMAEPP LIFECNHACS CWRNCRNRVV QNGLRARLQL YRTRDMGWGV 1150 1160 1170 1180 RSLQDIPPGT FVCEYVGELI SDSEADVREE DSYLFDLDNK ISSA
	Isoform 4 [UniParc]. Checksum: 2CA1BA8DACAE22A8	FASTA	808	86,704
	10 20 30 40 50 60 MAAADAEAVP ARGEPQQDCC VKTELLGEET PMAADEGSAE KQAGEAHMAA DGETNGSCEN 70 80 90 100 110 120 SDASSHANAA KHTQDSARVN PQDGTNTLTR IAENGVSERD SEAAKQNHVT ADDFVQTSVI 130 140 150 160 170 180 GSNGYILNKP ALQAQPLRTT STLASSLPGH AAKTLPGGAG KGRTPSAFPQ TPAAPPATLG 190 200 210 220 230 240 EGSADTEDRK LPAPGADVKV HRARKTMPKS VVGLHAASKD PREVREARDH KEPKEEINKN 250 260 270 280 290 300 ISDFGRQQLL PPFPSLHQSL PQNQCYMATT KSQTACLPFV LAAAVSRKKK RRMGTYSLVP 310 320 330 340 350 360 KKKTKVLKQR TVIEMFKSIT HSTVGSKGEK DLGASSLHVN GESLEMDSDE DDSEELEEDD 370 380 390 400 410 420 GHGAEQAAAF PTEDSRTSKE SMSEADRAQK MDGESEEEQE SVDTGEEEEG GDESDLSSES 430 440 450 460 470 480 SIKKKFLKRK GKTDSPWIKP ARKRRRRSRK KPSGALGSES YKSSAGSAEQ TAPGDSTGYM 490 500 510 520 530 540 EVSLDSLDLR VKGILSSQAE GLANGPDVLE TDGLQEVPLC SCRMETPKSR EITTLANNQC 550 560 570 580 590 600 MATESVDHEL GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF 610 620 630 640 650 660 MECQPESSIS HRFHKDCASR VNNASYCPHC GEESSKAKEV TIAKADTTST VTPVPGQEKG 670 680 690 700 710 720 SALEGRADTT TGSAAGPPLS EDDKLQGAAS HVPEGFDPTG PAGLGRPTPG LSQGPGKETL 730 740 750 760 770 780 ESALIALDSE KPKKLRFHPK QLYFSARQGE LQKVLLMLVD GIDPNFKMEH QNKRSPLHAA 790 800 AEAGHVDICH MLVQFCRLGS PRSRGCLW

References

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[1]	"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 2). Tissue: Teratocarcinoma.
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 583-1298 (ISOFORM 1). Tissue: Brain and Testis.
[4]	"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: NUCLEOTIDE SEQUENCE [MRNA] OF 32-1298 (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; BAT8; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2. Tissue: Cervix carcinoma.
[5]	Tsuritani K., Ukai Y., Yajima Y., Amemiya C., Yoshimoto M. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 382-1298 (ISOFORM 1). Tissue: Brain.
[6]	"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1298 (ISOFORM 3), TISSUE SPECIFICITY. Tissue: Brain.
[7]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1089-1298 (ISOFORM 1). Tissue: Lymph node.
[9]	"Loss-of-function mutations in euchromatin histone methyl transferase 1 (EHMT1) cause the 9q34 subtelomeric deletion syndrome." Kleefstra T., Brunner H.G., Amiel J., Oudakker A.R., Nillesen W.M., Magee A., Genevieve D., Cormier-Daire V., van Esch H., Fryns J.-P., Hamel B.C.J., Sistermans E.A., de Vries B.B.A., van Bokhoven H. Am. J. Hum. Genet. 79:370-377(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN KLESTS.
[10]	"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 EHMT2.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[12]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and promotes tumour cell motility and invasion." Kokura K., Sun L., Bedford M.T., Fang J. EMBO J. 29:3673-3687(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MPHOSPH8.
[14]	"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.
[15]	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)
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"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: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 765-999 IN COMPLEX WITH HISTONE H3, DOMAIN ANK REPEATS, MUTAGENESIS OF GLU-905.
[19]	"Adding a lysine mimic in the design of potent inhibitors of histone lysine methyltransferases." Chang Y., Ganesh T., Horton J.R., Spannhoff A., Liu J., Sun A., Zhang X., Bedford M.T., Shinkai Y., Snyder J.P., Cheng X. J. Mol. Biol. 400:1-7(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 982-1266 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE; ZINC ION AND E72 INHIBITOR, ENZYME REGULATION.
[20]	"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 (2.0 ANGSTROMS) OF 982-1266 IN COMPLEX WITH HISTONE H3; S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS.
[21]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-43 AND PHE-1173.
[22]	"Further clinical and molecular delineation of the 9q subtelomeric deletion syndrome supports a major contribution of EHMT1 haploinsufficiency to the core phenotype." Kleefstra T., van Zelst-Stams W.A., Nillesen W.M., Cormier-Daire V., Houge G., Foulds N., van Dooren M., Willemsen M.H., Pfundt R., Turner A., Wilson M., McGaughran J., Rauch A., Zenker M., Adam M.P., Innes M., Davies C., Lopez A.G. , Casalone R., Weber A., Brueton L.A., Navarro A.D., Bralo M.P., Venselaar H., Stegmann S.P., Yntema H.G., van Bokhoven H., Brunner H.G. J. Med. Genet. 46:598-606(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT KLESTS TYR-1075.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK022941 mRNA. Translation: BAB14321.1.
AL590627, AL611925 Genomic DNA. Translation: CAI17354.1. Sequence problems.
AL590627, AL611925 Genomic DNA. Translation: CAI17355.1.
AL611925, AL590627 Genomic DNA. Translation: CAH71076.1.
AL611925, AL590627 Genomic DNA. Translation: CAH71077.1. Sequence problems.
BC011608 mRNA. Translation: AAH11608.2.
BC047504 mRNA. Translation: AAH47504.1.
AY083210 mRNA. Translation: AAM09024.1.
AB028932 mRNA. Translation: BAB56104.1.
AB058779 mRNA. Translation: BAB47505.2.
AL713772 mRNA. Translation: CAD28534.1. Sequence problems.

IPI

IPI00645334.
IPI00942420.
IPI00946054.
IPI00946234.

RefSeq

NP_001138999.1. NM_001145527.1.
NP_079033.4. NM_024757.4.

UniGene

Hs.495511.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IGQ	X-ray	2.00	A/B	982-1266	[»]
2RFI	X-ray	1.59	A/B	982-1266	[»]
3B7B	X-ray	2.99	A/B	765-999	[»]
3B95	X-ray	2.99	A/B	765-999	[»]
3FPD	X-ray	2.40	A/B	1006-1266	[»]
3HNA	X-ray	1.50	A/B	982-1266	[»]
3MO0	X-ray	2.78	A/B	982-1266	[»]
3MO2	X-ray	2.49	A/B/C/D	982-1266	[»]
3MO5	X-ray	2.14	A/B/C/D	982-1266	[»]
3SW9	X-ray	3.05	A/B	982-1266	[»]
3SWC	X-ray	2.33	A/B	982-1266	[»]
4I51	X-ray	1.90	A/B	982-1266	[»]

ProteinModelPortal

Q9H9B1.

SMR

Q9H9B1. Positions 695-1266.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34585N.

IntAct

Q9H9B1. 10 interactions.

STRING

9606.ENSP00000417980.

PTM databases

PhosphoSite

Q9H9B1.

Polymorphism databases

DMDM

116241347.

Proteomic databases

PaxDb

Q9H9B1.

PRIDE

Q9H9B1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000334856; ENSP00000334476; ENSG00000181090.
ENST00000460843; ENSP00000417980; ENSG00000181090.
ENST00000462484; ENSP00000417328; ENSG00000181090.
ENST00000462942; ENSP00000436107; ENSG00000181090.

GeneID

79813.

KEGG

hsa:79813.

UCSC

uc004coa.3. human.
uc004cob.1. human.
uc011mfc.2. human.

Organism-specific databases

CTD

79813.

GeneCards

GC09P140513.

HGNC

HGNC:24650. EHMT1.

MIM

607001. gene.
610253. phenotype.

neXtProt

NX_Q9H9B1.

Orphanet

261652. Kleefstra syndrome due to a point mutation.
96147. Kleefstra syndrome due to monosomy 9q34.

PharmGKB

PA134941393.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOVERGEN

HBG028394.

InParanoid

Q9H9B1.

KO

K11420.

OMA

ISHRFHK.

Gene expression databases

ArrayExpress

Q9H9B1.

Bgee

Q9H9B1.

CleanEx

HS_EHMT1.

Genevestigator

Q9H9B1.

GermOnline

ENSG00000181090. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR007728. Pre-SET_dom.
IPR003606. Pre-SET_Zn-bd_sub.
IPR001214. SET_dom.
[Graphical view]

Pfam

PF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 7 hits.
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.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9H9B1.

ChEMBL

CHEMBL6031.

ChiTaRS

EHMT1. human.

EvolutionaryTrace

Q9H9B1.

GenomeRNAi

79813.

NextBio

69410.

SOURCE

Search...

Entry information

Entry name

EHMT1_HUMAN

Accession

Primary (citable) accession number: Q9H9B1
Secondary accession number(s): B1AQ58 , B1AQ59, Q86X08, Q8TCN7, Q96F53, Q96JF1, Q96KH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	March 8, 2011
Last modified:	May 1, 2013
This is version 135 of the entry and version 4 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.