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Q9H9B1 (EHMT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1298 AA.
Sequence statusComplete.
Protein existenceEvidence 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.15

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.20

Subunit structure

Heterodimer; heterodimerizes with EHMT2. 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. 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. Ref.4 Ref.10 Ref.12 Ref.14 Ref.15

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.19

The SET domain mediates interaction with WIZ. Ref.19

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.23). Ref.9 Ref.23

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily.

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 componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainANK repeat
Repeat
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin modification

Inferred from direct assay Ref.4. Source: UniProtKB

embryo development

Inferred from sequence or structural similarity. Source: UniProtKB

histone methylation

Inferred from direct assay Ref.4. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-lysine dimethylation

Inferred from direct assay Ref.15. Source: UniProtKB

peptidyl-lysine monomethylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionhistone 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

histone-lysine N-methyltransferase activity

Inferred from direct assay Ref.4. Source: UniProtKB

methyltransferase activity

Inferred from direct assay Ref.4. Source: UniProtKB

p53 binding

Inferred from physical interaction Ref.15. Source: UniProtKB

protein-lysine N-methyltransferase activity

Inferred from direct assay Ref.15. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MPHOSPH8Q995492EBI-766087,EBI-2653928
RELAQ042063EBI-766087,EBI-73886
RelaQ042075EBI-766087,EBI-644400From 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12981298Histone-lysine N-methyltransferase EHMT1
PRO_0000186067

Regions

Repeat737 – 76630ANK 1
Repeat772 – 80130ANK 2
Repeat805 – 83430ANK 3
Repeat838 – 86831ANK 4
Repeat872 – 90130ANK 5
Repeat905 – 93430ANK 6
Repeat938 – 96730ANK 7
Repeat971 – 100434ANK 8
Domain1060 – 112364Pre-SET
Domain1126 – 1243118SET
Region905 – 9073Histone H3K9me binding
Region1136 – 11383S-adenosyl-L-methionine binding
Region1162 – 118120Interaction with histone H3
Region1200 – 12012S-adenosyl-L-methionine binding
Region1242 – 12454Interaction with histone H3
Compositional bias406 – 4094Poly-Glu
Compositional bias442 – 4498Poly-Arg
Compositional bias1292 – 12954Poly-Ala

Sites

Metal binding10621Zinc 1
Metal binding10621Zinc 2
Metal binding10641Zinc 1
Metal binding10681Zinc 1
Metal binding10681Zinc 3
Metal binding10731Zinc 1
Metal binding10751Zinc 2
Metal binding11051Zinc 2
Metal binding11051Zinc 3
Metal binding11091Zinc 2
Metal binding11111Zinc 3
Metal binding11151Zinc 3
Metal binding12031Zinc 4
Metal binding12561Zinc 4
Metal binding12581Zinc 4
Metal binding12631Zinc 4
Binding site11551Histone H3K9me
Binding site11731S-adenosyl-L-methionine
Binding site12571S-adenosyl-L-methionine; via amide nitrogen

Natural variations

Alternative sequence1 – 3131Missing in isoform 2.
VSP_040716
Alternative sequence795 – 80814AGANI…EDQRT → FCRLGSPRSRGCLW in isoform 4.
VSP_040717
Alternative sequence809 – 1298490Missing in isoform 4.
VSP_040718
Alternative sequence836 – 85621DAEGS…YEVVQ → IQKTSKVYTESQETQRSQTI L in isoform 2.
VSP_002222
Alternative sequence857 – 1298442Missing in isoform 2.
VSP_002223
Alternative sequence1181 – 11844DGEV → ISSA in isoform 3.
VSP_002224
Alternative sequence1185 – 1298114Missing in isoform 3.
VSP_002225
Natural variant431A → V in a breast cancer sample; somatic mutation. Ref.22
VAR_036345
Natural variant3881A → T.
Corresponds to variant rs11137198 [ dbSNP | Ensembl ].
VAR_027642
Natural variant10751C → Y in KLESTS. Ref.23
VAR_069183
Natural variant11731Y → F in a breast cancer sample; somatic mutation. Ref.22
VAR_036346

Experimental info

Mutagenesis9051E → A: Abolishes binding to histone H3K9me. Ref.19
Sequence conflict5551N → D in AAH47504. Ref.3
Sequence conflict5611E → G in AAM09024. Ref.1
Sequence conflict5611E → G in BAB14321. Ref.2

Secondary structure

................................................................................... 1298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 8, 2011. Version 4.
Checksum: 071574F3FB3D371E

FASTA1,298141,466
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 2315F62F7806915B
Show »

FASTA82588,702
Isoform 3 [UniParc].

Checksum: 1382C5327D3579D7
Show »

FASTA1,184128,689
Isoform 4 [UniParc].

Checksum: 2CA1BA8DACAE22A8
Show »

FASTA80886,704

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDYL AND REST, IDENTIFICATION IN A COMPLEX WITH REST; CDYL; SETB1; EHMT2 AND WIZ.
[13]"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.
[14]"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.
[15]"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.
[16]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)
[17]"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].
[18]"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].
[19]"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.
[20]"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.
[21]"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.
[22]"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. expand/collapse author list , 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.
[23]"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. expand/collapse author list , 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.
RefSeqNP_001138999.1. NM_001145527.1.
NP_079033.4. NM_024757.4.
UniGeneHs.495511.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IGQX-ray2.00A/B982-1266[»]
2RFIX-ray1.59A/B982-1266[»]
3B7BX-ray2.99A/B765-999[»]
3B95X-ray2.99A/B765-999[»]
3FPDX-ray2.40A/B1006-1266[»]
3HNAX-ray1.50A/B982-1266[»]
3MO0X-ray2.78A/B982-1266[»]
3MO2X-ray2.49A/B/C/D982-1266[»]
3MO5X-ray2.14A/B/C/D982-1266[»]
3SW9X-ray3.05A/B982-1266[»]
3SWCX-ray2.33A/B982-1266[»]
4I51X-ray1.90A/B982-1266[»]
ProteinModelPortalQ9H9B1.
SMRQ9H9B1. Positions 695-1266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122908. 28 interactions.
DIPDIP-34585N.
IntActQ9H9B1. 13 interactions.
MINTMINT-7945009.
STRING9606.ENSP00000417980.

Chemistry

BindingDBQ9H9B1.
ChEMBLCHEMBL6031.

PTM databases

PhosphoSiteQ9H9B1.

Polymorphism databases

DMDM325511404.

Proteomic databases

PaxDbQ9H9B1.
PRIDEQ9H9B1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334856; ENSP00000334476; ENSG00000181090. [Q9H9B1-2]
ENST00000460843; ENSP00000417980; ENSG00000181090. [Q9H9B1-1]
ENST00000462484; ENSP00000417328; ENSG00000181090. [Q9H9B1-4]
ENST00000462942; ENSP00000436107; ENSG00000181090.
GeneID79813.
KEGGhsa:79813.
UCSCuc004coa.3. human. [Q9H9B1-4]
uc004cob.1. human. [Q9H9B1-2]
uc011mfc.2. human. [Q9H9B1-1]

Organism-specific databases

CTD79813.
GeneCardsGC09P140513.
HGNCHGNC:24650. EHMT1.
HPAHPA053043.
MIM607001. gene.
610253. phenotype.
neXtProtNX_Q9H9B1.
Orphanet96147. Kleefstra syndrome due to 9q34 microdeletion.
261652. Kleefstra syndrome due to a point mutation.
PharmGKBPA134941393.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOVERGENHBG028394.
InParanoidQ9H9B1.
KOK11420.
OMASDFGRQQ.
OrthoDBEOG744T8D.
PhylomeDBQ9H9B1.
TreeFamTF106443.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ9H9B1.
BgeeQ9H9B1.
CleanExHS_EHMT1.
GenevestigatorQ9H9B1.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR007728. Pre-SET_dom.
IPR003606. Pre-SET_Zn-bd_sub.
IPR001214. SET_dom.
[Graphical view]
PfamPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 7 hits.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEHMT1. human.
EvolutionaryTraceQ9H9B1.
GeneWikiEHMT1.
GenomeRNAi79813.
NextBio69410.
PROQ9H9B1.
SOURCESearch...

Entry information

Entry nameEHMT1_HUMAN
AccessionPrimary (citable) accession number: Q9H9B1
Secondary accession number(s): B1AQ58 expand/collapse secondary AC list , B1AQ59, Q86X08, Q8TCN7, Q96F53, Q96JF1, Q96KH4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: March 8, 2011
Last modified: April 16, 2014
This is version 144 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM