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Information on EC 2.1.1.296 - methyltransferase cap2 and Organism(s) Homo sapiens and UniProt Accession Q8IYT2

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.296 methyltransferase cap2
IUBMB Comments
The enzyme, found in higher eukaryotes including insects and vertebrates, and their viruses, methylates the ribose of the ribonucleotide at the second transcribed position of mRNAs and snRNAs. This methylation event is known as cap2. The human enzyme can also methylate mRNA molecules where the upstream ribonucleotide is not methylated (see EC 2.1.1.57, methyltransferase cap1), but with lower efficiency .
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This record set is specific for:
Homo sapiens
UNIPROT: Q8IYT2
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Word Map
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  • 2.1.1.296
  • c-mannosylation
  • mannose
  • neuroblast
  • thrombospondin
  • 2'-o-ribose
  • r-spondin1
  • methyltransferases
  • netrin
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
S-adenosyl-L-methionine
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(ribonucleotide)-[mRNA]
=
S-adenosyl-L-homocysteine
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(ribonucleotide)-[mRNA]
=
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
Synonyms
hmtr2, cmtr2, ftsjd1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CMTr2
-
-
-
-
MTR2
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-ribonucleotide-[mRNA] 2'-O-methyltransferase
The enzyme, found in higher eukaryotes including insects and vertebrates, and their viruses, methylates the ribose of the ribonucleotide at the second transcribed position of mRNAs and snRNAs. This methylation event is known as cap2. The human enzyme can also methylate mRNA molecules where the upstream ribonucleotide is not methylated (see EC 2.1.1.57, methyltransferase cap1), but with lower efficiency [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CapG
the hMTr2 MTase activity is dependent on the presence of capG
-
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the Rossmann-fold MTase (RFM) family, hMTr1 and hMTr2 are paralogues forming a subfamily with higher eukaryotic and viral members, minimum evolution tree of homologues of known 2'-O-ribose mRNA cap MTases, overview
malfunction
the substitutions of residues S78, H86 and Q113 only mildly affect RNA binding and catalysis, so they are not essential for CMTr2 MTase activity
metabolism
the 5' cap of human messenger RNA contains 2'-O-methylation of the first and often second transcribed nucleotide that is important for its processing, translation and stability. Enzyme responsible for the methylations are CMTr1 and CMTr2, respectively
physiological function
the 5' cap of human messenger RNA consists of an inverted 7-methylguanosine linked to the first transcribed nucleotide by a unique 5'-5' triphosphate bond followed by 2'-O-ribose methylation of the first and often the second transcribed nucleotides, likely serving to modify efficiency of transcript processing, translation and stability. Cap2 methylates the ribose of the second transcribed nucleotide. Relationship to other cap-modifying enzymes, overview
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CMTR2_HUMAN
770
0
88120
Swiss-Prot
other Location (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E145A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
H142A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
K307A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
K74A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
L77A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
T89A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
W85A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CMTR2, recombinant overexpression of wild-type and mutant enzymes in HEK-293 cells
gene HMTR2 or FTSJD1, phylogenetic tree, functional overexpression of the cap2 MTase hMTr2 and of c-myc-tagged enzyme in MCF7 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Werner, M.; Purta, E.; Kaminska, K.; Cymerman, I.; Campbell, D.; Mittra, B.; Zamudio, J.; Sturm, N.; Jaworski, J.; Bujnicki, J.
2'-O-ribose methylation of cap2 in human: function and evolution in a horizontally mobile family
Nucleic Acids Res.
39
4756-4768
2011
Homo sapiens (Q8IYT2), Homo sapiens
Manually annotated by BRENDA team
Smietanski, M.; Werner, M.; Purta, E.; Kaminska, K.; Stepinski, J.; Darzynkiewicz, E.; Nowotny, M.; Bujnicki, J.
Structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation
Nat. Commun.
5
3004
2014
Homo sapiens (Q8IYT2), Homo sapiens
Manually annotated by BRENDA team