Q96KQ7 (EHMT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 121.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Histone-lysine N-methyltransferase EHMT2 EC=2.1.1.- EC=2.1.1.43 Alternative name(s): Euchromatic histone-lysine N-methyltransferase 2 HLA-B-associated transcript 8 Histone H3-K9 methyltransferase 3 Short name=H3-K9-HMTase 3 Lysine N-methyltransferase 1C Protein G9a | ||||
| Gene names |
| ||||
| 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 | 1210 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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. 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.17 Ref.22 |
| Catalytic activity | S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.9 |
| Subunit structure | Heterodimer; heterodimerizes with EHMT1/GLP. Interacts with GFI1B and WIZ. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Ref.11 Ref.12 Ref.22 |
| 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.18 The ANK repeats bind H3K9me1 and H3K9me2. Ref.18 |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.20 Ref.21 Methylated at Lys-185; automethylated. Ref.17 |
| Sequence similarities | Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily. Contains 7 ANK repeats. Contains 1 post-SET domain. Contains 1 pre-SET domain. Contains 1 SET domain. |
| Caution | While NG36 and G9a were originally thought to derive from 2 separate genes, all G9A transcripts also contain the in frame coding sequence of NG36 (Ref.1). It is uncertain whether Met-1 or Met-21 is the initiator methionine. |
| Sequence caution | The sequence AAD21811.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAD21812.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAH02686.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAH09351.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAH18718.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH20970.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB63294.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAB63295.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA49491.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| GFI1 | Q99684 | 2 | EBI-744366,EBI-949368 | |
| Gfi1 | Q07120 | 3 | EBI-744366,EBI-4289236 | From a different organism. |
| HDAC1 | Q13547 | 2 | EBI-744366,EBI-301834 | |
| PRDM5 | Q9NQX1 | 3 | EBI-744366,EBI-4292031 | |
| PRRC2B | Q5JSZ5 | 2 | EBI-744366,EBI-744891 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: Q96KQ7-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q96KQ7-2) Also known as: NG36G9a-SPI; The sequence of this isoform differs from the canonical sequence as follows: 373-406: Missing. | ||||||
| Isoform 3 (identifier: Q96KQ7-3) Also known as: NG36; The sequence of this isoform differs from the canonical sequence as follows: 195-202: PPVPEKRP → VSGMGEMG 203-1210: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 1210 | 1209 | Histone-lysine N-methyltransferase EHMT2 | PRO_0000186068 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 649 – 678 | 30 | ANK 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 684 – 713 | 30 | ANK 2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 717 – 746 | 30 | ANK 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 750 – 780 | 31 | ANK 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 784 – 813 | 30 | ANK 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 817 – 846 | 30 | ANK 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 850 – 879 | 30 | ANK 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 972 – 1035 | 64 | Pre-SET | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 1037 – 1159 | 123 | SET | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 1164 – 1180 | 17 | Post-SET | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 817 – 819 | 3 | Histone H3K9me binding By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 1048 – 1050 | 3 | S-adenosyl-L-methionine binding | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 1074 – 1093 | 20 | Interaction with histone H3 By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 1112 – 1113 | 2 | S-adenosyl-L-methionine binding | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 1154 – 1157 | 4 | Interaction with histone H3 By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 2 – 13 | 12 | Poly-Ala | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 160 – 163 | 4 | Poly-Ala | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 300 – 326 | 27 | Poly-Glu | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 974 | 1 | Zinc 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 974 | 1 | Zinc 2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 976 | 1 | Zinc 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 980 | 1 | Zinc 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 980 | 1 | Zinc 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 985 | 1 | Zinc 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 987 | 1 | Zinc 2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 1017 | 1 | Zinc 2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 1017 | 1 | Zinc 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 1021 | 1 | Zinc 2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 1023 | 1 | Zinc 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 1027 | 1 | Zinc 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 1115 | 1 | Zinc 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 1168 | 1 | Zinc 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 1170 | 1 | Zinc 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 1175 | 1 | Zinc 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 1067 | 1 | Histone H3K9me By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 1085 | 1 | S-adenosyl-L-methionine | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.20 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 140 | 1 | Phosphoserine Ref.16 Ref.19 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 173 | 1 | Phosphoserine Ref.19 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 185 | 1 | N6,N6,N6-trimethyllysine; by EHMT2; alternate Ref.17 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 185 | 1 | N6,N6-dimethyllysine; by EHMT2; alternate Ref.17 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 232 | 1 | Phosphoserine Ref.16 Ref.19 Ref.20 Ref.21 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 246 | 1 | Phosphoserine Ref.13 Ref.15 Ref.19 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 555 | 1 | Phosphothreonine By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 569 | 1 | Phosphoserine Ref.14 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 1210 | 1 | Phosphothreonine Ref.19 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 195 – 202 | 8 | PPVPEKRP → VSGMGEMG in isoform 3. | VSP_002212 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 203 – 1210 | 1008 | Missing in isoform 3. | VSP_002213 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 373 – 406 | 34 | Missing in isoform 2. | VSP_002211 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 55 | 1 | T → N. Ref.1 Ref.5 Ref.6 Ref.7 Corresponds to variant rs7887 [ dbSNP | Ensembl ]. | VAR_027973 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 1165 | 1 | Y → F. Corresponds to variant rs13919 [ dbSNP | Ensembl ]. | VAR_027974 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 786 | 1 | W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 791 | 1 | W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 794 | 1 | E → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 817 | 1 | E → R: Impairs binding to histone H3K9me. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 824 | 1 | W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 852 | 1 | D → R: Impairs binding to histone H3K9me. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 178 | 1 | P → S in CAC86666. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 985 | 1 | C → R in CAC86666. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 994 | 1 | C → R in CAA49491. Ref.8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 922 – 924 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 926 – 929 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 931 – 933 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 940 – 943 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 949 – 952 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 968 – 970 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 986 – 990 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1008 – 1010 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1021 – 1023 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1027 – 1029 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 1032 – 1034 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1040 – 1044 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1046 – 1056 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1063 – 1066 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1069 – 1073 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 1074 – 1079 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1086 – 1089 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1097 – 1105 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 1107 – 1110 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1118 – 1127 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1135 – 1142 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 1156 – 1159 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1176 – 1179 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 1182 – 1191 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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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: 11707778] [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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: 14656967] [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. 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. Beck S.Nature 425:805-811(2003) [PubMed: 14574404] [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: 15489334] [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: 8457211] [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: 11316813] [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: 12004135] [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: 16688220] [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: 16702210] [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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [15] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [16] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "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: 18438403] [Abstract] Cited for: FUNCTION, METHYLATION AT LYS-185, MASS SPECTROMETRY. |
| [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: 18264113] [Abstract] Cited for: DOMAIN ANK REPEATS, MUTAGENESIS OF TRP-786; TRP-791; GLU-794; GLU-817; TRP-824 AND ASP-852. |
| [19] | "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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-173; SER-232; SER-246 AND THR-1210, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [20] | "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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY. 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: 20118233] [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] | "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: 20084102] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 913-1193 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AJ315532 mRNA. Translation: CAC86666.1. AK056936 mRNA. Translation: BAB71314.1. AF134726 Genomic DNA. Translation: AAD21811.1. Sequence problems. AF134726 Genomic DNA. Translation: AAD21812.1. Sequence problems. BA000025 Genomic DNA. Translation: BAB63294.1. Sequence problems. BA000025 Genomic DNA. Translation: BAB63295.1. Sequence problems. AL662834 Genomic DNA. Translation: CAI17747.2. AL662834 Genomic DNA. Translation: CAI17748.1. AL671762 Genomic DNA. Translation: CAI18224.2. AL671762 Genomic DNA. Translation: CAI18226.2. AL844853 Genomic DNA. Translation: CAI41852.1. AL844853 Genomic DNA. Translation: CAI41853.1. CR388219, CR388202 Genomic DNA. Translation: CAQ07473.1. CR388219, CR388202 Genomic DNA. Translation: CAQ07474.1. CR936237 Genomic DNA. Translation: CAQ09159.1. CR759784 Genomic DNA. Translation: CAQ09311.1. CR388202, CR388219 Genomic DNA. Translation: CAQ09508.1. CR388202, CR388219 Genomic DNA. Translation: CAQ09509.1. CH471081 Genomic DNA. Translation: EAX03542.1. BC002686 mRNA. Translation: AAH02686.2. Different initiation. BC009351 mRNA. Translation: AAH09351.1. Different initiation. BC018718 mRNA. Translation: AAH18718.1. Different initiation. BC020970 mRNA. Translation: AAH20970.2. Different initiation. X69838 mRNA. Translation: CAA49491.1. Different initiation. | ||||||||||||||||||||||||||||||
| IPI | IPI00096972. IPI00220795. IPI00220796. | ||||||||||||||||||||||||||||||
| RefSeq | NP_006700.3. NM_006709.3. NP_079532.5. NM_025256.5. | ||||||||||||||||||||||||||||||
| UniGene | Hs.709218. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||||||||
| ProteinModelPortal | Q96KQ7. | ||||||||||||||||||||||||||||||
| SMR | Q96KQ7. Positions 618-1192. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| DIP | DIP-34461N. | ||||||||||||||||||||||||||||||
| IntAct | Q96KQ7. 29 interactions. | ||||||||||||||||||||||||||||||
| MINT | MINT-1441977. | ||||||||||||||||||||||||||||||
| STRING | Q96KQ7. | ||||||||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||||||||
| DMDM | 116241348. | ||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||
| PRIDE | Q96KQ7. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| Ensembl | ENST00000375537; ENSP00000364687; ENSG00000204371. ENST00000383373; ENSP00000372864; ENSG00000206376. ENST00000429506; ENSP00000406110; ENSG00000227333. ENST00000450075; ENSP00000392305; ENSG00000236759. | ||||||||||||||||||||||||||||||
| GeneID | 10919. | ||||||||||||||||||||||||||||||
| KEGG | hsa:10919. | ||||||||||||||||||||||||||||||
| UCSC | uc003nxz.1. human. uc003nyb.1. human. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| CTD | 10919. | ||||||||||||||||||||||||||||||
| GeneCards | GC06M031847. | ||||||||||||||||||||||||||||||
| HGNC | HGNC:14129. EHMT2. | ||||||||||||||||||||||||||||||
| MIM | 604599. gene. | ||||||||||||||||||||||||||||||
| neXtProt | NX_Q96KQ7. | ||||||||||||||||||||||||||||||
| PharmGKB | PA25267. | ||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| GeneTree | ENSGT00600000084355. | ||||||||||||||||||||||||||||||
| HOVERGEN | HBG028394. | ||||||||||||||||||||||||||||||
| OrthoDB | EOG4KSPJ5. | ||||||||||||||||||||||||||||||
| PhylomeDB | Q96KQ7. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| Pathway_Interaction_DB | ar_tf_pathway. Regulation of Androgen receptor activity. | ||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||
| Bgee | Q96KQ7. | ||||||||||||||||||||||||||||||
| CleanEx | HS_EHMT2. | ||||||||||||||||||||||||||||||
| Genevestigator | Q96KQ7. | ||||||||||||||||||||||||||||||
| GermOnline | ENSG00000204371. Homo sapiens. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR003616. Post-SET_dom. IPR007728. Pre-SET_dom. IPR003606. Pre-SET_Zn-bd_sub. IPR001214. SET_dom. [Graphical view] | ||||||||||||||||||||||||||||||
| Gene3D | G3DSA:1.25.40.20. ANK. 2 hits. | ||||||||||||||||||||||||||||||
| KO | K11420. | ||||||||||||||||||||||||||||||
| Pfam | PF00023. Ank. 4 hits. PF05033. Pre-SET. 1 hit. PF00856. SET. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| PRINTS | PR01415. ANKYRIN. | ||||||||||||||||||||||||||||||
| SMART | SM00248. ANK. 6 hits. SM00508. PostSET. 1 hit. SM00468. PreSET. 1 hit. SM00317. SET. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| SUPFAM | SSF48403. ANK. 1 hit. | ||||||||||||||||||||||||||||||
| PROSITE | PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 5 hits. PS50868. POST_SET. False negative. PS50867. PRE_SET. 1 hit. PS50280. SET. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||
| NextBio | 41475. | ||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | EHMT2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q96KQ7 Secondary accession number(s): B0UZY2 Q9Y331 | ||||||||
| Entry 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. | ||||||||
Relevant documents
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with