Q8N1G2 · CMTR1_HUMAN
- ProteinCap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1
- GeneCMTR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids835 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m7GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m7GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway.
Catalytic activity
- a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H+ + S-adenosyl-L-homocysteine
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 203-207 | substrate | ||||
Sequence: KSVFD | ||||||
Binding site | 218 | substrate | ||||
Sequence: R | ||||||
Binding site | 234 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 239 | |||||
Sequence: K | ||||||
Binding site | 277-283 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: CAGPGGF | ||||||
Binding site | 335-336 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DI | ||||||
Active site | 364 | |||||
Sequence: D | ||||||
Binding site | 374-376 | substrate | ||||
Sequence: NLQ | ||||||
Active site | 404 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 439 | substrate | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | mRNA (nucleoside-2'-O-)-methyltransferase activity | |
Molecular Function | nucleic acid binding | |
Biological Process | 7-methylguanosine mRNA capping | |
Biological Process | methylation | |
Biological Process | mRNA processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8N1G2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 203 | Reduces both mRNA cap binding and catalytic activity of the enzyme. | ||||
Sequence: K → A | ||||||
Mutagenesis | 228 | No effect. | ||||
Sequence: R → A | ||||||
Mutagenesis | 239 | Abolishes catalytic activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 364 | Abolishes catalytic activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 404 | Abolishes catalytic activity. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 607 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000251239 | 1-835 | UniProt | Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 | |||
Sequence: MKRRTDPECTAPIKKQKKRVAELALSLSSTSDDEPPSSVSHGAKASTTSLSGSDSETEGKQHSSDSFDDAFKADSLVEGTSSRYSMYNSVSQKLMAKMGFREGEGLGKYSQGRKDIVEASSQKGRRGLGLTLRGFDQELNVDWRDEPEPSACEQVSWFPECTTEIPDTQEMSDWMVVGKRKMIIEDETEFCGEELLHSVLQCKSVFDVLDGEEMRRARTRANPYEMIRGVFFLNRAAMKMANMDFVFDRMFTNPRDSYGKPLVKDREAELLYFADVCAGPGGFSEYVLWRKKWHAKGFGMTLKGPNDFKLEDFYSASSELFEPYYGEGGIDGDGDITRPENISAFRNFVLDNTDRKGVHFLMADGGFSVEGQENLQEILSKQLLLCQFLMALSIVRTGGHFICKTFDLFTPFSVGLVYLLYCCFERVCLFKPITSRPANSERYVVCKGLKVGIDDVRDYLFAVNIKLNQLRNTDSDVNLVVPLEVIKGDHEFTDYMIRSNESHCSLQIKALAKIHAFVQDTTLSEPRQAEIRKECLRLWGIPDQARVAPSSSDPKSKFFELIQGTEIDIFSYKPTLLTSKTLEKIRPVFDYRCMVSGSEQKFLIGLGKSQIYTWDGRQSDRWIKLDLKTELPRDTLLSVEIVHELKGEGKAQRKISAIHILDVLVLNGTDVREQHFNQRIQLAEKFVKAVSKPSRPDMNPIRVKEVYRLEEMEKIFVRLEMKIIKGSSGTPKLSYTGRDDRHFVPMGLYIVRTVNEPWTMGFSKSFKKKFFYNKKTKDSTFDLPADSIAPFHICYYGRLFWEWGDGIRVHDSQKPQDQDKLSKEDVLSFIQMHRA | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 28 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 31 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 53 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 53 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 66 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 66 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 91 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 108 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By interferons alpha and beta, and by Vaccinia virus infection.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MKRRTDPECTAPIKKQKKRVA | ||||||
Region | 1-67 | Disordered | ||||
Sequence: MKRRTDPECTAPIKKQKKRVAELALSLSSTSDDEPPSSVSHGAKASTTSLSGSDSETEGKQHSSDSF | ||||||
Motif | 2-19 | Bipartite nuclear localization signal | ||||
Sequence: KRRTDPECTAPIKKQKKR | ||||||
Compositional bias | 23-57 | Polar residues | ||||
Sequence: LALSLSSTSDDEPPSSVSHGAKASTTSLSGSDSET | ||||||
Domain | 87-133 | G-patch | ||||
Sequence: YNSVSQKLMAKMGFREGEGLGKYSQGRKDIVEASSQKGRRGLGLTLR | ||||||
Domain | 231-450 | RrmJ-type SAM-dependent 2'-O-MTase | ||||
Sequence: FFLNRAAMKMANMDFVFDRMFTNPRDSYGKPLVKDREAELLYFADVCAGPGGFSEYVLWRKKWHAKGFGMTLKGPNDFKLEDFYSASSELFEPYYGEGGIDGDGDITRPENISAFRNFVLDNTDRKGVHFLMADGGFSVEGQENLQEILSKQLLLCQFLMALSIVRTGGHFICKTFDLFTPFSVGLVYLLYCCFERVCLFKPITSRPANSERYVVCKGLK | ||||||
Region | 727-835 | Interaction with POLR2A | ||||
Sequence: SSGTPKLSYTGRDDRHFVPMGLYIVRTVNEPWTMGFSKSFKKKFFYNKKTKDSTFDLPADSIAPFHICYYGRLFWEWGDGIRVHDSQKPQDQDKLSKEDVLSFIQMHRA | ||||||
Domain | 752-786 | WW | ||||
Sequence: RTVNEPWTMGFSKSFKKKFFYNKKTKDSTFDLPAD |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length835
- Mass (Da)95,321
- Last updated2002-10-01 v1
- Checksum03919512A73C30FB
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MKRRTDPECTAPIKKQKKRVA | ||||||
Compositional bias | 23-57 | Polar residues | ||||
Sequence: LALSLSSTSDDEPPSSVSHGAKASTTSLSGSDSET | ||||||
Sequence conflict | 795 | in Ref. 3; BAF85253 | ||||
Sequence: Y → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D43949 EMBL· GenBank· DDBJ | BAA07893.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK292564 EMBL· GenBank· DDBJ | BAF85253.1 EMBL· GenBank· DDBJ | mRNA | ||
AL353597 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC010731 EMBL· GenBank· DDBJ | AAH10731.2 EMBL· GenBank· DDBJ | mRNA | ||
BC031890 EMBL· GenBank· DDBJ | AAH31890.1 EMBL· GenBank· DDBJ | mRNA |