VCPKMT protein (human) - STRING database

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VCPKMT

Protein-lysine methyltransferase METTL21D; Protein-lysine N-methyltransferase that specifically trimethylates ’Lys-315’ of VCP/p97; this modification may decrease VCP ATPase activity; Belongs to the methyltransferase superfamily. METTL21 family (229 aa)

Predicted Functional Partners:

VCP

0.996

UBXN6

0.954

METTL18

0.886

METTL20

0.849

METTL10

0.811

N6AMT2

0.806

FAM86A

0.804

CAMKMT

0.783

METTL22

0.771

KIN

0.735

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CAMKMT	FAM86A	ENSP00000367755	ENSP00000398502	Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	0.478
CAMKMT	KIN	ENSP00000367755	ENSP00000368881	Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing	DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family	0.462
CAMKMT	METTL10	ENSP00000367755	ENSP00000357829	Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing	EEF1A lysine methyltransferase 2; Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at ’Lys-318’	0.515
CAMKMT	METTL18	ENSP00000367755	ENSP00000307975	Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing	Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase	0.771
CAMKMT	METTL20	ENSP00000367755	ENSP00000350353	Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing	Electron transfer flavoprotein beta subunit lysine methyltransferase; Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases to the main respiratory chain	0.700
CAMKMT	METTL22	ENSP00000367755	ENSP00000371345	Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing	Methyltransferase-like protein 22; Protein N-lysine methyltransferase. In vitro methylates KIN; Belongs to the methyltransferase superfamily. METTL22 family	0.556
CAMKMT	VCPKMT	ENSP00000367755	ENSP00000379201	Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing	Protein-lysine methyltransferase METTL21D; Protein-lysine N-methyltransferase that specifically trimethylates ’Lys-315’ of VCP/p97; this modification may decrease VCP ATPase activity; Belongs to the methyltransferase superfamily. METTL21 family	0.783
FAM86A	CAMKMT	ENSP00000398502	ENSP00000367755	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing	0.478
FAM86A	KIN	ENSP00000398502	ENSP00000368881	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family	0.631
FAM86A	METTL10	ENSP00000398502	ENSP00000357829	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	EEF1A lysine methyltransferase 2; Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at ’Lys-318’	0.875
FAM86A	METTL18	ENSP00000398502	ENSP00000307975	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase	0.791
FAM86A	METTL20	ENSP00000398502	ENSP00000350353	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	Electron transfer flavoprotein beta subunit lysine methyltransferase; Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases to the main respiratory chain	0.792
FAM86A	METTL22	ENSP00000398502	ENSP00000371345	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	Methyltransferase-like protein 22; Protein N-lysine methyltransferase. In vitro methylates KIN; Belongs to the methyltransferase superfamily. METTL22 family	0.766
FAM86A	N6AMT2	ENSP00000398502	ENSP00000372206	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	EEF1A lysine methyltransferase 1; Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at ’Lys-79’	0.681
FAM86A	VCPKMT	ENSP00000398502	ENSP00000379201	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	Protein-lysine methyltransferase METTL21D; Protein-lysine N-methyltransferase that specifically trimethylates ’Lys-315’ of VCP/p97; this modification may decrease VCP ATPase activity; Belongs to the methyltransferase superfamily. METTL21 family	0.804
KIN	CAMKMT	ENSP00000368881	ENSP00000367755	DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family	Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing	0.462
KIN	FAM86A	ENSP00000368881	ENSP00000398502	DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’	0.631
KIN	METTL10	ENSP00000368881	ENSP00000357829	DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family	EEF1A lysine methyltransferase 2; Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at ’Lys-318’	0.413
KIN	METTL18	ENSP00000368881	ENSP00000307975	DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family	Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase	0.792
KIN	METTL20	ENSP00000368881	ENSP00000350353	DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family	Electron transfer flavoprotein beta subunit lysine methyltransferase; Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases to the main respiratory chain	0.672

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