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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-Experimental evidence at protein leveli

Functioni

mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.4 Publications

Catalytic activityi

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei180 – 1801S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei205 – 2051S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei208 – 2081mRNA cap bindingPROSITE-ProRule annotation
Sitei214 – 2141mRNA cap bindingPROSITE-ProRule annotation
Binding sitei227 – 2271S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei239 – 2391mRNA cap bindingPROSITE-ProRule annotation
Binding sitei288 – 2881mRNA capPROSITE-ProRule annotation
Binding sitei370 – 3701mRNA capPROSITE-ProRule annotation
Binding sitei467 – 4671mRNA capPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA cap guanine-N7 methyltransferase (EC:2.1.1.56)
Alternative name(s):
RG7MT1
mRNA (guanine-N(7)-)-methyltransferase
mRNA cap methyltransferase
Short name:
hCMT1
Short name:
hMet
Short name:
hcm1p
Gene namesi
Name:RNMT
Synonyms:KIAA0398
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:10075. RNMT.

Subcellular locationi

GO - Cellular componenti

  • mRNA cap binding complex Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 834KKRK → AAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 103-AAAAA-107 and I-127. 1 Publication
Mutagenesisi103 – 1075KKRKR → AAAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and I-127. 1 Publication
Mutagenesisi127 – 1271R → I: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and 103-AAAAA-107. 1 Publication
Mutagenesisi203 – 2031D → A: Loss of activity. 1 Publication
Mutagenesisi239 – 2391R → A: Loss of activity. 1 Publication
Mutagenesisi289 – 2891Y → A: Loss of activity. 1 Publication
Mutagenesisi291 – 2911F → A: Strongly impairs enzyme activity. 1 Publication
Mutagenesisi354 – 3541F → A: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA34448.

Polymorphism and mutation databases

BioMutaiRNMT.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476mRNA cap guanine-N7 methyltransferasePRO_0000248321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO43148.
MaxQBiO43148.
PaxDbiO43148.
PeptideAtlasiO43148.
PRIDEiO43148.

PTM databases

iPTMnetiO43148.
PhosphoSiteiO43148.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiENSG00000101654.
CleanExiHS_RNMT.
ExpressionAtlasiO43148. baseline and differential.
GenevisibleiO43148. HS.

Organism-specific databases

HPAiHPA039409.

Interactioni

Subunit structurei

Interacts with importin alpha, leading to stimulate both RNA-binding and methyltransferase activity. 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. Interacts with elongating form of polymerase II and RNGTT. Interacts with RAM/FAM103A1, the interaction significantly enhances RNA-binding and cap methyltransferase activity.3 Publications

Protein-protein interaction databases

BioGridi114269. 19 interactions.
IntActiO43148. 3 interactions.
STRINGi9606.ENSP00000262173.

Structurei

Secondary structure

1
476
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi170 – 19324Combined sources
Beta strandi200 – 2045Combined sources
Turni207 – 2115Combined sources
Helixi212 – 2176Combined sources
Beta strandi221 – 2288Combined sources
Helixi230 – 24415Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi254 – 2596Combined sources
Turni262 – 2643Combined sources
Turni268 – 2703Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi278 – 2858Combined sources
Helixi287 – 2926Combined sources
Helixi294 – 30512Combined sources
Beta strandi308 – 31912Combined sources
Helixi321 – 3288Combined sources
Beta strandi331 – 3377Combined sources
Beta strandi339 – 3468Combined sources
Beta strandi357 – 3626Combined sources
Beta strandi369 – 3713Combined sources
Helixi375 – 3817Combined sources
Helixi382 – 3854Combined sources
Beta strandi387 – 3948Combined sources
Helixi395 – 4028Combined sources
Helixi406 – 41510Combined sources
Beta strandi453 – 4564Combined sources
Helixi458 – 4647Combined sources
Beta strandi467 – 4748Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BGVX-ray2.30A/B/C/D165-476[»]
3EPPX-ray2.41A/B165-476[»]
ProteinModelPortaliO43148.
SMRiO43148. Positions 169-476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43148.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini128 – 476349mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni176 – 1772mRNA cap bindingPROSITE-ProRule annotation
Regioni261 – 2622S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni284 – 2863S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi126 – 1283Nuclear localization signal

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.PROSITE-ProRule annotation
Contains 1 mRNA cap 0 methyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1975. Eukaryota.
ENOG410Y7HG. LUCA.
GeneTreeiENSGT00390000002368.
HOVERGENiHBG081963.
InParanoidiO43148.
KOiK00565.
OMAiPAMQFIL.
OrthoDBiEOG091G0C9Y.
PhylomeDBiO43148.
TreeFamiTF314347.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR016899. mRNA_G-N7_MeTrfase.
IPR004971. mRNA_G-N7_MeTrfase_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF03291. Pox_MCEL. 1 hit.
[Graphical view]
PIRSFiPIRSF028762. ABD1. 1 hit.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51562. RNA_CAP0_MT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791M → I in BAA82447 (PubMed:10589710).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei465 – 47612SIYLV…FEKQQ → RLTVTIMREAWLSTVGPGRA PVAASSVKWGTPRPAMQFIL in isoform 2. 1 PublicationVSP_020241Add
BLAST

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]
UniGeneiHs.592347.

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]

Keywords - Coding sequence diversityi

Alternative splicing

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]
UniGeneiHs.592347.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BGVX-ray2.30A/B/C/D165-476[»]
3EPPX-ray2.41A/B165-476[»]
ProteinModelPortaliO43148.
SMRiO43148. Positions 169-476.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114269. 19 interactions.
IntActiO43148. 3 interactions.
STRINGi9606.ENSP00000262173.

PTM databases

iPTMnetiO43148.
PhosphoSiteiO43148.

Polymorphism and mutation databases

BioMutaiRNMT.

Proteomic databases

EPDiO43148.
MaxQBiO43148.
PaxDbiO43148.
PeptideAtlasiO43148.
PRIDEiO43148.

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

CTDi8731.
GeneCardsiRNMT.
HGNCiHGNC:10075. RNMT.
HPAiHPA039409.
MIMi603514. gene.
neXtProtiNX_O43148.
PharmGKBiPA34448.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1975. Eukaryota.
ENOG410Y7HG. LUCA.
GeneTreeiENSGT00390000002368.
HOVERGENiHBG081963.
InParanoidiO43148.
KOiK00565.
OMAiPAMQFIL.
OrthoDBiEOG091G0C9Y.
PhylomeDBiO43148.
TreeFamiTF314347.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiRNMT. human.
EvolutionaryTraceiO43148.
GeneWikiiMRNA_(guanine-N7-)-methyltransferase.
RNMT.
GenomeRNAii8731.
PROiO43148.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101654.
CleanExiHS_RNMT.
ExpressionAtlasiO43148. baseline and differential.
GenevisibleiO43148. HS.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR016899. mRNA_G-N7_MeTrfase.
IPR004971. mRNA_G-N7_MeTrfase_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF03291. Pox_MCEL. 1 hit.
[Graphical view]
PIRSFiPIRSF028762. ABD1. 1 hit.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51562. RNA_CAP0_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCES_HUMAN
AccessioniPrimary (citable) accession number: O43148
Secondary accession number(s): B0YJ90
, D3DUJ5, O94996, Q9UIJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 1998
Last modified: September 7, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.