Reviewed, UniProtKB/Swiss-Prot Q9H9B1 (EHMT1_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone-lysine N-methyltransferase, H3 lysine-9 specific 5
    EC=2.1.1.43
Alternative name(s):
    Histone H3-K9 methyltransferase 5
    H3-K9-HMTase 5
    Euchromatic histone-lysine N-methyltransferase 1
      Short name=Eu-HMTase1
    G9a-like protein 1
      Short name=GLP1
    Lysine N-methyltransferase 1D

Gene names

Name:	EHMT1
Synonyms:	EUHMTASE1, KIAA1876, KMT1D

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1267 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Histone methyltransferase. Methylates 'Lys-9' of histone H3 (in vitro). H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. 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.
Catalytic activity	S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. Ref.1
Subunit structure	Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts with WIZ and EHMT2. Ref.10
Subcellular location	Nucleus. Note: Associates with euchromatic regions.
Tissue specificity	Widely expressed. Ref.5
Domain	The SET domain mediates interaction with WIZ.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11
Involvement in disease	Defects in EHMT1 are the cause of chromosome 9q subtelomeric deletion syndrome (9q- syndrome) [MIM:610253]. Common features seen in these patients are severe mental retardation, hypotonia, brachy(micro)cephaly, epileptic seizures, flat face with hypertelorism, synophrys, anteverted nares, cupid bow or tented upper lip, everted lower lip, prognathism, macroglossia, conotruncal heart defects, and behavioral problems.
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: Miscellaneous discrepancy. Intron retention.

Ontologies

Keywords
Cellular component	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	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	histone methylation Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	nucleus Ref.1 Inferred by curator. Source: UniProtKB
Molecular function	histone-lysine N-methyltransferase activity Ref.1 Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 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:
     805-825: DAEGSTCLHLAAKKGHYEVVQ → IQKTSKVYTESQETQRSQTIL
     826-1267: Missing.

Isoform 3 (identifier: Q9H9B1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1150-1153: DGEV → ISSA
     1154-1267: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1267

1267

Histone-lysine N-methyltransferase, H3 lysine-9 specific 5

PRO_0000186067

Regions

Repeat

706 – 735

30

ANK 1

Repeat

741 – 770

30

ANK 2

Repeat

774 – 803

30

ANK 3

Repeat

807 – 837

31

ANK 4

Repeat

841 – 870

30

ANK 5

Repeat

874 – 903

30

ANK 6

Repeat

907 – 936

30

ANK 7

Repeat

940 – 973

34

ANK 8

Domain

1029 – 1092

64

Pre-SET

Domain

1094 – 1216

123

SET

Region

1105 – 1107

3

S-adenosyl-L-methionine binding

Region

1169 – 1170

2

S-adenosyl-L-methionine binding

Compositional bias

375 – 378

4

Poly-Glu

Compositional bias

411 – 418

8

Poly-Arg

Compositional bias

1261 – 1264

4

Poly-Ala

Sites

Metal binding

1031

1

Zinc 1

Metal binding

1031

1

Zinc 2

Metal binding

1033

1

Zinc 1

Metal binding

1037

1

Zinc 1

Metal binding

1037

1

Zinc 3

Metal binding

1042

1

Zinc 1

Metal binding

1044

1

Zinc 2

Metal binding

1074

1

Zinc 2

Metal binding

1074

1

Zinc 3

Metal binding

1078

1

Zinc 2

Metal binding

1080

1

Zinc 3

Metal binding

1084

1

Zinc 3

Metal binding

1172

1

Zinc 4

Metal binding

1225

1

Zinc 4

Metal binding

1227

1

Zinc 4

Metal binding

1232

1

Zinc 4

Binding site

1142

1

S-adenosyl-L-methionine

Binding site

1226

1

S-adenosyl-L-methionine; via amide nitrogen

Amino acid modifications

Modified residue

466

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

805 – 825

21

DAEGS…YEVVQ → IQKTSKVYTESQETQRSQTI L in isoform 2.

VSP_002222

Alternative sequence

826 – 1267

442

Missing in isoform 2.

VSP_002223

Alternative sequence

1150 – 1153

4

DGEV → ISSA in isoform 3.

VSP_002224

Alternative sequence

1154 – 1267

114

Missing in isoform 3.

VSP_002225

Natural variant

12

1

A → V in a breast cancer sample; somatic mutation. Ref.13

VAR_036345

Natural variant

357

1

A → T: dbSNP rs11137198.

VAR_027642

Natural variant

1142

1

Y → F in a breast cancer sample; somatic mutation. Ref.13

VAR_036346

Experimental info

Sequence conflict

530

1

E → G in AAM09024. Ref.1

Sequence conflict

530

1

E → G in BAB14321. Ref.2

Secondary structure

1

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1267

Helix Strand Turn

Details...

Helix

745 – 752

8

Helix

755 – 763

9

Helix

778 – 784

7

Helix

788 – 795

8

Turn

796 – 798

3

Helix

811 – 817

7

Helix

821 – 828

8

Turn

829 – 831

3

Helix

845 – 851

7

Helix

855 – 863

9

Helix

878 – 885

8

Helix

888 – 895

8

Turn

896 – 898

3

Helix

911 – 917

7

Helix

921 – 928

8

Turn

929 – 931

3

Helix

944 – 947

4

Helix

953 – 966

14

Beta strand

977 – 981

5

Turn

983 – 986

4

Beta strand

988 – 990

3

Beta strand

994 – 1000

7

Beta strand

1006 – 1009

4

Beta strand

1014 – 1017

4

Helix

1025 – 1027

3

Beta strand

1034 – 1037

4

Helix

1043 – 1047

5

Beta strand

1065 – 1067

3

Beta strand

1078 – 1080

3

Helix

1089 – 1091

3

Beta strand

1097 – 1101

5

Beta strand

1103 – 1113

11

Beta strand

1120 – 1123

4

Beta strand

1126 – 1130

5

Helix

1131 – 1135

5

Beta strand

1143 – 1145

3

Beta strand

1154 – 1162

9

Helix

1164 – 1167

4

Beta strand

1175 – 1184

10

Beta strand

1192 – 1199

8

Helix

1213 – 1219

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: FF221BEAE9022010	FASTA	1,267	138,254
	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 790 800 810 820 830 840 EAAENNHLEA VKYLIKAGAL VDPKDAEGST CLHLAAKKGH YEVVQYLLSN GQMDVNCQDD 850 860 870 880 890 900 GGWTPMIWAT EYKHVDLVKL LLSKGSDINI RDNEENICLH WAAFSGCVDI AEILLAAKCD 910 920 930 940 950 960 LHAVNIHGDS PLHIAARENR YDCVVLFLSR DSDVTLKNKE GETPLQCASL NSQVWSALQM 970 980 990 1000 1010 1020 SKALQDSAPD RPSPVERIVS RDIARGYERI PIPCVNAVDS EPCPSNYKYV SQNCVTSPMN 1030 1040 1050 1060 1070 1080 IDRNITHLQY CVCIDDCSSS NCMCGQLSMR CWYDKDGRLL PEFNMAEPPL IFECNHACSC 1090 1100 1110 1120 1130 1140 WRNCRNRVVQ NGLRARLQLY RTRDMGWGVR SLQDIPPGTF VCEYVGELIS DSEADVREED 1150 1160 1170 1180 1190 1200 SYLFDLDNKD GEVYCIDARF YGNVSRFINH HCEPNLVPVR VFMAHQDLRF PRIAFFSTRL 1210 1220 1230 1240 1250 1260 IEAGEQLGFD YGERFWDIKG KLFSCRCGSP KCRHSSAALA QRQASAAQEA QEDGLPDTSS AAAADPL
	Isoform 2. 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. Checksum: 6AE88F600131E386	FASTA	1,153	125,476
	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 790 800 810 820 830 840 EAAENNHLEA VKYLIKAGAL VDPKDAEGST CLHLAAKKGH YEVVQYLLSN GQMDVNCQDD 850 860 870 880 890 900 GGWTPMIWAT EYKHVDLVKL LLSKGSDINI RDNEENICLH WAAFSGCVDI AEILLAAKCD 910 920 930 940 950 960 LHAVNIHGDS PLHIAARENR YDCVVLFLSR DSDVTLKNKE GETPLQCASL NSQVWSALQM 970 980 990 1000 1010 1020 SKALQDSAPD RPSPVERIVS RDIARGYERI PIPCVNAVDS EPCPSNYKYV SQNCVTSPMN 1030 1040 1050 1060 1070 1080 IDRNITHLQY CVCIDDCSSS NCMCGQLSMR CWYDKDGRLL PEFNMAEPPL IFECNHACSC 1090 1100 1110 1120 1130 1140 WRNCRNRVVQ NGLRARLQLY RTRDMGWGVR SLQDIPPGTF VCEYVGELIS DSEADVREED 1150 SYLFDLDNKI SSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 12004135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; BAT8; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2. Tissue: Cervix carcinoma.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Teratocarcinoma.
[3]	"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: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 351-1267 (ISOFORM 1). Tissue: Brain.
[5]	"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: 11347906] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 351-1267 (ISOFORM 3), TISSUE SPECIFICITY. Tissue: Brain.
[6]	"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: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 552-1267 (ISOFORM 1). Tissue: Brain.
[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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1056-1267 (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: 16826528] [Abstract] Cited for: INVOLVEMENT IN 9Q- SYNDROME.
[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: 16702210] [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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, MASS SPECTROMETRY.
[12]	"The crystal structure of human euchromatic histone methyltransferase 1." Structural genomics consortium (SGC) Submitted (OCT-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 951-1235 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS.
[13]	"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: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-12 AND PHE-1142.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

IPI

IPI00015526.
IPI00216443.
IPI00645334.

UniGene

Hs.495511

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IGQ	X-ray	2.00	A/B	951-1235	[»]
2RFI	X-ray	1.59	A/B	951-1235	[»]
3B7B	X-ray	2.99	A/B	734-968	[»]
3B95	X-ray	2.99	A/B	734-968	[»]
3FPD	X-ray	2.40	A/B	975-1235	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q9H9B1.

Proteomic databases

PRIDE

Q9H9B1.

Genome annotation databases

Ensembl

ENSG00000181090. Homo sapiens. [Contig view]

KEGG

hsa:79813.

Organism-specific databases

GeneCards

GC09P139633.

H-InvDB

HIX0008578.

HGNC

HGNC:24650. EHMT1.

MIM

607001. gene.
610253. phenotype.

PharmGKB

PA134941393.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9H9B1.

HOVERGEN

Q9H9B1.

OMA

Q9H9B1. PESSISH.

Enzyme and pathway databases

BRENDA

2.1.1.43. 247.

Gene expression databases

ArrayExpress

Q9H9B1.

Bgee

Q9H9B1.

CleanEx

HS_EHMT1.

GermOnline

ENSG00000181090. Homo sapiens.

Family and domain databases

InterPro

IPR002110. ANK.
IPR007728. Pre-SET_Zn_bd.
IPR003606. Pre-SET_Zn_bd_sub.
IPR001214. SET.
[Graphical view]

Gene3D

G3DSA:1.25.40.20. ANK. 1 hit.

Pfam

PF00023. Ank. 7 hits.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]

SMART

SM00248. ANK. 7 hits.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]

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 Resources

NextBio

69410.

SOURCE

Search...

Entry information

Entry name

EHMT1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	October 17, 2006
Last modified:	June 16, 2009
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)