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Protein

mRNA cap guanine-N7 methyltransferase

Gene

RNMT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs (PubMed:9790902, PubMed:9705270, PubMed:10347220, PubMed:11114884, PubMed:22099306, PubMed:27422871). Binds RNA containing 5'-terminal GpppC (PubMed:11114884).6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Methyltransferase activity is activated by RAMAC (PubMed:27422871).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei180S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources1 Publication1
Binding sitei205S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotationCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei208mRNA cap bindingPROSITE-ProRule annotation1
Sitei214mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei227S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources1 Publication1
Sitei239mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei261S-adenosyl-L-methionine; via amide nitrogenCombined sources1 Publication1
Binding sitei284S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
Sitei288mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei289S-adenosyl-L-methionineCombined sources1 Publication1
Sitei370mRNA cap bindingPROSITE-ProRule annotation1
Sitei467mRNA cap bindingPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMethyltransferase, RNA-binding, Transferase
Biological processmRNA capping, mRNA processing
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS02296-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-167160 RNA Pol II CTD phosphorylation and interaction with CE during HIV infection
R-HSA-72086 mRNA Capping
R-HSA-77075 RNA Pol II CTD phosphorylation and interaction with CE

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
mRNA cap guanine-N7 methyltransferase (EC:2.1.1.564 Publications)
Alternative name(s):
RG7MT1
mRNA (guanine-N(7)-)-methyltransferase
mRNA cap methyltransferase
Short name:
hCMT1
Short name:
hMet
Short name:
hcm1p
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RNMT
Synonyms:KIAA0398
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 18

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000101654.17

Human Gene Nomenclature Database

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HGNCi
HGNC:10075 RNMT

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
603514 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O43148

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi80 – 83KKRK → AAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 103-AAAAA-107 and I-127. 1 Publication4
Mutagenesisi103 – 107KKRKR → AAAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and I-127. 1 Publication5
Mutagenesisi127R → I: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and 103-AAAAA-107. 1 Publication1
Mutagenesisi178W → C: Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-417. Complete restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-417. Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-417; C-393 and C-398. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-417; C-393 and C-398. 1 Publication1
Mutagenesisi203D → A: Loss of activity. 1 Publication1
Mutagenesisi239R → A: Loss of activity. 1 Publication1
Mutagenesisi289Y → A: Loss of activity. 1 Publication1
Mutagenesisi291F → A: Strongly impairs enzyme activity. 1 Publication1
Mutagenesisi354F → A: Loss of activity. 1 Publication1
Mutagenesisi393K → C: Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178; C-398 and C-417. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-398 and C-417. 1 Publication1
Mutagenesisi398F → C: Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178; C-393 and C-417. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-393 and C-417. 1 Publication1
Mutagenesisi409K → E: Decreased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-413. Decreased interaction with RAMAC; when associated with E-413. 1 Publication1
Mutagenesisi413K → E: Decreased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-409. Decreased interaction with RAMAC; when associated with E-409. 1 Publication1
Mutagenesisi417A → C: Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178. Complete restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178. Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178. Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178; C-393 and C-398. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-393 and C-398. 1 Publication1
Mutagenesisi450R → E: Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-452. No change in interaction with RAMAC; when associated with E-452. 1 Publication1
Mutagenesisi452P → E: Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-450. No change in interaction with RAMAC; when associated with E-450. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
8731

Open Targets

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OpenTargetsi
ENSG00000101654

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34448

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
RNMT

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002483211 – 476mRNA cap guanine-N7 methyltransferaseAdd BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei24PhosphoserineBy similarity1
Modified residuei28PhosphoserineBy similarity1
Modified residuei29PhosphoserineBy similarity1
Modified residuei118PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O43148

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O43148

MaxQB - The MaxQuant DataBase

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MaxQBi
O43148

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O43148

PeptideAtlas

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PeptideAtlasi
O43148

PRoteomics IDEntifications database

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PRIDEi
O43148

ProteomicsDB human proteome resource

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ProteomicsDBi
48765
48766 [O43148-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O43148

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
O43148

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000101654 Expressed in 231 organ(s), highest expression level in amniotic fluid

CleanEx database of gene expression profiles

More...
CleanExi
HS_RNMT

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O43148 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O43148 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA039409

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with importin alpha, leading to stimulate both RNA-binding and methyltransferase activity (PubMed:11114884). Interaction with importin alpha and beta is required for its nuclear localization, importin beta dissociating in response to RanGTP, allowing RNMT-importin alpha to bind RNA substrates (PubMed:11114884). Interacts with elongating form of polymerase II and RNGTT (PubMed:9705270). Interacts with RAMAC, this interaction significantly enhances RNA-binding and cap methyltransferase activity (PubMed:22099306, Ref. 14).4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
RAMACQ9BTL34EBI-877832,EBI-744023

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
114269, 21 interactors

Protein interaction database and analysis system

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IntActi
O43148, 11 interactors

Molecular INTeraction database

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MINTi
O43148

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000262173

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1476
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BGVX-ray2.30A/B/C/D165-476[»]
3EPPX-ray2.41A/B165-476[»]
5E8JX-ray2.35A/B167-476[»]
5E9JX-ray3.47A/B167-416[»]
A/B457-476[»]
5E9WX-ray2.28A/B/C/D167-476[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O43148

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O43148

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O43148

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini128 – 476mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd BLAST349

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni176 – 177mRNA cap bindingPROSITE-ProRule annotation2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi126 – 128Nuclear localization signal3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1975 Eukaryota
ENOG410Y7HG LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000002368

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG081963

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O43148

KEGG Orthology (KO)

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KOi
K00565

Identification of Orthologs from Complete Genome Data

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OMAi
LNLVSCQ

Database of Orthologous Groups

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OrthoDBi
1390749at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O43148

TreeFam database of animal gene trees

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TreeFami
TF314347

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004971 mRNA_G-N7_MeTrfase_dom
IPR016899 mRNA_G-N7_MeTrfase_euk
IPR039753 RG7MT1
IPR029063 SAM-dependent_MTases

The PANTHER Classification System

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PANTHERi
PTHR12189 PTHR12189, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF03291 Pox_MCEL, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF028762 ABD1, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53335 SSF53335, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51562 RNA_CAP0_MT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O43148-1) [UniParc]FASTAAdd to basket
Also known as: hCMT1a

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.

« Hide
        10         20         30         40         50
MANSAKAEEY EKMSLEQAKA SVNSETESSF NINENTTASG TGLSEKTSVC
60 70 80 90 100
RQVDIARKRK EFEDDLVKES SSCGKDTPSK KRKLDPEIVP EEKDCGDAEG
110 120 130 140 150
NSKKRKRETE DVPKDKSSTG DGTQNKRKIA LEDVPEKQKN LEEGHSSTVA
160 170 180 190 200
AHYNELQEVG LEKRSQSRIF YLRNFNNWMK SVLIGEFLEK VRQKKKRDIT
210 220 230 240 250
VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSVKQCQQRY EDMKNRRDSE
260 270 280 290 300
YIFSAEFITA DSSKELLIDK FRDPQMCFDI CSCQFVCHYS FESYEQADMM
310 320 330 340 350
LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD
360 370 380 390 400
YPLFGCKYDF NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE
410 420 430 440 450
EKIKNNENKM LLKRMQALEP YPANESSKLV SEKVDDYEHA AKYMKNSQVR
460 470
LPLGTLSKSE WEATSIYLVF AFEKQQ
Length:476
Mass (Da):54,844
Last modified:June 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEC919BC41BD5E2B3
GO
Isoform 2 (identifier: O43148-2) [UniParc]FASTAAdd to basket
Also known as: hCMT1b

The sequence of this isoform differs from the canonical sequence as follows:
     465-476: SIYLVFAFEKQQ → RLTVTIMREAWLSTVGPGRAPVAASSVKWGTPRPAMQFIL

Show »
Length:504
Mass (Da):57,725
Checksum:i00F822E6867D6D6A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EP06K7EP06_HUMAN
mRNA cap guanine-N7 methyltransfera...
RNMT
298Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ERH6K7ERH6_HUMAN
mRNA cap guanine-N7 methyltransfera...
RNMT
114Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EPP5K7EPP5_HUMAN
mRNA cap guanine-N7 methyltransfera...
RNMT
101Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti179M → I in BAA82447 (PubMed:10589710).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_020241465 – 476SIYLV…FEKQQ → RLTVTIMREAWLSTVGPGRA PVAASSVKWGTPRPAMQFIL in isoform 2. 1 PublicationAdd BLAST12

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB022604 mRNA Translation: BAA74464.1
AB022605 mRNA Translation: BAA74463.1
AF067791 mRNA Translation: AAC63269.1
AB020966 mRNA Translation: BAA82447.1
AB007858 mRNA Translation: BAA23694.1
EF445026 Genomic DNA Translation: ACA06068.1
CH471113 Genomic DNA Translation: EAX01505.1
CH471113 Genomic DNA Translation: EAX01506.1
BC036798 mRNA Translation: AAH36798.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11867.1 [O43148-1]
CCDS77156.1 [O43148-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001295192.1, NM_001308263.1 [O43148-2]
NP_003790.1, NM_003799.2 [O43148-1]
XP_005258219.1, XM_005258162.1 [O43148-1]
XP_016881550.1, XM_017026061.1 [O43148-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.592347

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000262173; ENSP00000262173; ENSG00000101654 [O43148-1]
ENST00000383314; ENSP00000372804; ENSG00000101654 [O43148-1]
ENST00000543302; ENSP00000446426; ENSG00000101654 [O43148-1]
ENST00000589866; ENSP00000466252; ENSG00000101654 [O43148-1]
ENST00000592764; ENSP00000466111; ENSG00000101654 [O43148-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
8731

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:8731

UCSC genome browser

More...
UCSCi
uc002ksk.2 human [O43148-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022604 mRNA Translation: BAA74464.1
AB022605 mRNA Translation: BAA74463.1
AF067791 mRNA Translation: AAC63269.1
AB020966 mRNA Translation: BAA82447.1
AB007858 mRNA Translation: BAA23694.1
EF445026 Genomic DNA Translation: ACA06068.1
CH471113 Genomic DNA Translation: EAX01505.1
CH471113 Genomic DNA Translation: EAX01506.1
BC036798 mRNA Translation: AAH36798.1
CCDSiCCDS11867.1 [O43148-1]
CCDS77156.1 [O43148-2]
RefSeqiNP_001295192.1, NM_001308263.1 [O43148-2]
NP_003790.1, NM_003799.2 [O43148-1]
XP_005258219.1, XM_005258162.1 [O43148-1]
XP_016881550.1, XM_017026061.1 [O43148-2]
UniGeneiHs.592347

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BGVX-ray2.30A/B/C/D165-476[»]
3EPPX-ray2.41A/B165-476[»]
5E8JX-ray2.35A/B167-476[»]
5E9JX-ray3.47A/B167-416[»]
A/B457-476[»]
5E9WX-ray2.28A/B/C/D167-476[»]
ProteinModelPortaliO43148
SMRiO43148
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114269, 21 interactors
IntActiO43148, 11 interactors
MINTiO43148
STRINGi9606.ENSP00000262173

PTM databases

iPTMnetiO43148
PhosphoSitePlusiO43148

Polymorphism and mutation databases

BioMutaiRNMT

Proteomic databases

EPDiO43148
jPOSTiO43148
MaxQBiO43148
PaxDbiO43148
PeptideAtlasiO43148
PRIDEiO43148
ProteomicsDBi48765
48766 [O43148-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262173; ENSP00000262173; ENSG00000101654 [O43148-1]
ENST00000383314; ENSP00000372804; ENSG00000101654 [O43148-1]
ENST00000543302; ENSP00000446426; ENSG00000101654 [O43148-1]
ENST00000589866; ENSP00000466252; ENSG00000101654 [O43148-1]
ENST00000592764; ENSP00000466111; ENSG00000101654 [O43148-2]
GeneIDi8731
KEGGihsa:8731
UCSCiuc002ksk.2 human [O43148-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8731
DisGeNETi8731
EuPathDBiHostDB:ENSG00000101654.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RNMT
HGNCiHGNC:10075 RNMT
HPAiHPA039409
MIMi603514 gene
neXtProtiNX_O43148
OpenTargetsiENSG00000101654
PharmGKBiPA34448

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1975 Eukaryota
ENOG410Y7HG LUCA
GeneTreeiENSGT00390000002368
HOVERGENiHBG081963
InParanoidiO43148
KOiK00565
OMAiLNLVSCQ
OrthoDBi1390749at2759
PhylomeDBiO43148
TreeFamiTF314347

Enzyme and pathway databases

BioCyciMetaCyc:HS02296-MONOMER
ReactomeiR-HSA-167160 RNA Pol II CTD phosphorylation and interaction with CE during HIV infection
R-HSA-72086 mRNA Capping
R-HSA-77075 RNA Pol II CTD phosphorylation and interaction with CE

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
RNMT human
EvolutionaryTraceiO43148

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MRNA_(guanine-N7-)-methyltransferase
RNMT

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
8731

Protein Ontology

More...
PROi
PR:O43148

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000101654 Expressed in 231 organ(s), highest expression level in amniotic fluid
CleanExiHS_RNMT
ExpressionAtlasiO43148 baseline and differential
GenevisibleiO43148 HS

Family and domain databases

InterProiView protein in InterPro
IPR004971 mRNA_G-N7_MeTrfase_dom
IPR016899 mRNA_G-N7_MeTrfase_euk
IPR039753 RG7MT1
IPR029063 SAM-dependent_MTases
PANTHERiPTHR12189 PTHR12189, 1 hit
PfamiView protein in Pfam
PF03291 Pox_MCEL, 1 hit
PIRSFiPIRSF028762 ABD1, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51562 RNA_CAP0_MT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMCES_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O43148
Secondary accession number(s): B0YJ90
, D3DUJ5, O94996, Q9UIJ9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 1998
Last modified: January 16, 2019
This is version 147 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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