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Q96KQ7 (EHMT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 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.16 Ref.22 Ref.27 Ref.29

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.9 Ref.29

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. 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.10 Ref.11 Ref.12 Ref.15 Ref.20 Ref.22 Ref.25

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.17

The ANK repeats bind H3K9me1 and H3K9me2. Ref.17

In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster. Ref.17

Post-translational modification

Methylated at Lys-185; automethylated. Ref.16

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. 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 componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainANK repeat
Repeat
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from sequence or structural similarity. Source: UniProtKB

DNA methylation on cytosine within a CG sequence

Inferred from electronic annotation. Source: Ensembl

fertilization

Inferred from electronic annotation. Source: Ensembl

histone methylation

Inferred from mutant phenotype Ref.27. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

organ growth

Inferred from electronic annotation. Source: Ensembl

peptidyl-lysine dimethylation

Inferred from direct assay Ref.22. Source: UniProtKB

regulation of DNA replication

Inferred from mutant phenotype Ref.27. Source: UniProtKB

spermatid development

Inferred from electronic annotation. Source: Ensembl

synaptonemal complex assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionC2H2 zinc finger domain binding

Inferred from physical interaction Ref.12. Source: UniProt

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

histone-lysine N-methyltransferase activity

Inferred from mutant phenotype Ref.27. Source: UniProtKB

p53 binding

Inferred from physical interaction Ref.22. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17636019Ref.15Ref.25. Source: UniProtKB

protein-lysine N-methyltransferase activity

Inferred from direct assay Ref.22. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 12101209Histone-lysine N-methyltransferase EHMT2
PRO_0000186068

Regions

Repeat649 – 67830ANK 1
Repeat684 – 71330ANK 2
Repeat717 – 74630ANK 3
Repeat750 – 78031ANK 4
Repeat784 – 81330ANK 5
Repeat817 – 84630ANK 6
Repeat850 – 87930ANK 7
Domain972 – 103564Pre-SET
Domain1038 – 1155118SET
Domain1164 – 118017Post-SET
Region817 – 8193Histone H3K9me binding By similarity
Region1048 – 10503S-adenosyl-L-methionine binding
Region1074 – 109320Interaction with histone H3 By similarity
Region1112 – 11132S-adenosyl-L-methionine binding
Region1154 – 11574Interaction with histone H3 By similarity
Compositional bias2 – 1312Poly-Ala
Compositional bias160 – 1634Poly-Ala
Compositional bias300 – 32627Poly-Glu

Sites

Metal binding9741Zinc 1
Metal binding9741Zinc 2
Metal binding9761Zinc 1
Metal binding9801Zinc 1
Metal binding9801Zinc 3
Metal binding9851Zinc 1
Metal binding9871Zinc 2
Metal binding10171Zinc 2
Metal binding10171Zinc 3
Metal binding10211Zinc 2
Metal binding10231Zinc 3
Metal binding10271Zinc 3
Metal binding11151Zinc 4
Metal binding11681Zinc 4
Metal binding11701Zinc 4
Metal binding11751Zinc 4
Binding site10671Histone H3K9me By similarity
Binding site10851S-adenosyl-L-methionine
Binding site11691S-adenosyl-L-methionine; via amide nitrogen

Amino acid modifications

Modified residue21N-acetylalanine Ref.19 Ref.28
Modified residue1401Phosphoserine Ref.18 Ref.24 Ref.26
Modified residue1731Phosphoserine Ref.18
Modified residue1851N6,N6,N6-trimethyllysine; by EHMT2; alternate Ref.16
Modified residue1851N6,N6-dimethyllysine; by EHMT2; alternate Ref.16
Modified residue2321Phosphoserine Ref.18 Ref.24 Ref.26
Modified residue2461Phosphoserine Ref.13 Ref.18 Ref.24 Ref.26
Modified residue4131Phosphoserine Ref.26
Modified residue5691Phosphoserine Ref.14
Modified residue12041Phosphoserine Ref.26
Modified residue12101Phosphothreonine Ref.18

Natural variations

Alternative sequence195 – 2028PPVPEKRP → VSGMGEMG in isoform 3.
VSP_002212
Alternative sequence203 – 12101008Missing in isoform 3.
VSP_002213
Alternative sequence373 – 40634Missing in isoform 2.
VSP_002211
Natural variant551T → N. Ref.1 Ref.5 Ref.6 Ref.7
Corresponds to variant rs7887 [ dbSNP | Ensembl ].
VAR_027973
Natural variant11651Y → F.
Corresponds to variant rs13919 [ dbSNP | Ensembl ].
VAR_027974

Experimental info

Mutagenesis7861W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.17
Mutagenesis7911W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.17
Mutagenesis7941E → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.17
Mutagenesis8171E → R: Impairs binding to histone H3K9me. Ref.17
Mutagenesis8241W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.17
Mutagenesis8521D → R: Impairs binding to histone H3K9me. Ref.17
Sequence conflict1781P → S in CAC86666. Ref.2
Sequence conflict9851C → R in CAC86666. Ref.2
Sequence conflict9941C → R in CAA49491. Ref.8

Secondary structure

.................................................... 1210
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 3.
Checksum: A6C5DC6B72801520

FASTA1,210132,370
        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 

« Hide

Isoform 2 (NG36G9a-SPI) [UniParc].

Checksum: 887FC5E322B772B9
Show »

FASTA1,176129,019
Isoform 3 (NG36) [UniParc].

Checksum: 339618C3DA895788
Show »

FASTA20219,864

References

« Hide '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. 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 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"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; EHMT1 AND WIZ.
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"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.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[20]"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.
[21]"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.
[22]"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.
[23]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)
[24]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"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.
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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.
[28]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"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, FUNCTION, CATALYTIC ACTIVITY.
+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.
CCDSCCDS4725.1. [Q96KQ7-1]
CCDS4726.1. [Q96KQ7-2]
RefSeqNP_001276342.1. NM_001289413.1.
NP_006700.3. NM_006709.4. [Q96KQ7-1]
NP_079532.5. NM_025256.6. [Q96KQ7-2]
UniGeneHs.709218.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O8JX-ray1.80A/B/C/D913-1193[»]
3DM1X-ray2.40B/D/F/H179-190[»]
3K5KX-ray1.70A/B913-1193[»]
3RJWX-ray2.56A/B913-1193[»]
4NVQX-ray2.03A/B913-1193[»]
ProteinModelPortalQ96KQ7.
SMRQ96KQ7. Positions 632-908, 922-1192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116123. 79 interactions.
DIPDIP-34461N.
IntActQ96KQ7. 37 interactions.
MINTMINT-1441977.
STRING9606.ENSP00000397323.

Chemistry

BindingDBQ96KQ7.
ChEMBLCHEMBL6032.
GuidetoPHARMACOLOGY2652.

Polymorphism databases

DMDM116241348.

Proteomic databases

MaxQBQ96KQ7.
PaxDbQ96KQ7.
PRIDEQ96KQ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375530; ENSP00000364680; ENSG00000204371. [Q96KQ7-2]
ENST00000375537; ENSP00000364687; ENSG00000204371. [Q96KQ7-1]
ENST00000383372; ENSP00000372863; ENSG00000206376. [Q96KQ7-2]
ENST00000383373; ENSP00000372864; ENSG00000206376. [Q96KQ7-1]
ENST00000420336; ENSP00000396119; ENSG00000238134.
ENST00000420874; ENSP00000411035; ENSG00000236759. [Q96KQ7-2]
ENST00000421926; ENSP00000416957; ENSG00000232045.
ENST00000429506; ENSP00000406110; ENSG00000227333. [Q96KQ7-1]
ENST00000450075; ENSP00000392305; ENSG00000236759. [Q96KQ7-1]
ENST00000450229; ENSP00000400838; ENSG00000227333. [Q96KQ7-2]
GeneID10919.
KEGGhsa:10919.
UCSCuc003nxz.1. human. [Q96KQ7-1]
uc003nya.1. human. [Q96KQ7-2]
uc003nyb.1. human. [Q96KQ7-3]

Organism-specific databases

CTD10919.
GeneCardsGC06M031847.
GC06Mi31858.
GC06Mj31835.
GC06Mk31829.
GC06Mm31924.
GC06Mn31837.
H-InvDBHIX0166078.
HIX0166345.
HIX0167369.
HIX0184162.
HGNCHGNC:14129. EHMT2.
HPAHPA050550.
MIM604599. gene.
neXtProtNX_Q96KQ7.
PharmGKBPA25267.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOVERGENHBG028394.
KOK11420.
PhylomeDBQ96KQ7.
TreeFamTF106443.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ96KQ7.
BgeeQ96KQ7.
CleanExHS_EHMT2.
GenevestigatorQ96KQ7.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. 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]
PfamPF00023. Ank. 6 hits.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 6 hits.
SM00508. PostSET. 1 hit.
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

ChiTaRSEHMT2. human.
EvolutionaryTraceQ96KQ7.
GeneWikiEHMT2.
GenomeRNAi10919.
NextBio41475.
PROQ96KQ7.
SOURCESearch...

Entry information

Entry nameEHMT2_HUMAN
AccessionPrimary (citable) accession number: Q96KQ7
Secondary accession number(s): B0UZY2 expand/collapse secondary AC list , 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: July 9, 2014
This is version 148 of the entry and version 3 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 6

Human chromosome 6: entries, gene names and cross-references to MIM