STRINGSTRING
SMYD2 SMYD2 KMT2A KMT2A CSKMT CSKMT EHMT1 EHMT1 SETD2 SETD2 KMT5A KMT5A SETD4 SETD4 EEF1AKMT2 EEF1AKMT2 SETD3 SETD3 METTL18 METTL18 SETD7 SETD7 SETD6 SETD6
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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SMYD2N-lysine methyltransferase SMYD2; Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. Belongs to the class V-like SAM-binding methyltransferase superfamily. (433 aa)
KMT2AHistone-lysine N-methyltransferase 2A; Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys- 4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no [...] (3972 aa)
CSKMTCitrate synthase-lysine N-methyltransferase CSKMT, mitochondrial; Protein-lysine methyltransferase that selectively trimethylates citrate synthase (CS) in mitochondria. Seems to conduct trimethylation in a highly distributive manner rather than in a processive manner, and thus introduces a single methly group per binding event. (240 aa)
EHMT1Histone-lysine N-methyltransferase EHMT1; 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 [...] (1298 aa)
SETD2Histone-lysine N-methyltransferase SETD2; Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate. It is capable of trimethylating unmethylated H3K36 (H3K36me0) in vitro. Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation (By similarity). Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A. Acts as a key regulator of DNA mismatch repair [...] (2564 aa)
KMT5AN-lysine methyltransferase KMT5A; Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper [...] (352 aa)
SETD4SET domain containing 4; Belongs to the class V-like SAM-binding methyltransferase superfamily. SETD4 family. (440 aa)
EEF1AKMT2EEF1A lysine methyltransferase 2; Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-318'; Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM4 family. (291 aa)
SETD3Actin-histidine N-methyltransferase; Protein-histidine N-methyltransferase that specifically mediates methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N- methyltransferase activity and probably only catalyzes histidine methylation of actin. (594 aa)
METTL18Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase; Belongs to the methyltransferase superfamily. METTL18 family. (372 aa)
SETD7Histone-lysine N-methyltransferase SETD7; Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys- 1 [...] (366 aa)
SETD6N-lysine methyltransferase SETD6; Protein-lysine N-methyltransferase. Monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulate NF- kappa-B transcription factor activity. Monomethylates 'Lys-8' of H2AZ (H2AZK8me1). Required for the maintenance of embryonic stem cell self-renewal (By similarity). Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SETD6 subfamily. (473 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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