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Protein

mRNA cap guanine-N7 methyltransferase

Gene

RNMT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

Catalytic activityi

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation4 Publications

Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei180S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources1 Publication1
Binding sitei205S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotationCombined sources1 Publication1
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
Binding sitei288mRNA capPROSITE-ProRule annotation1
Binding sitei289S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei370mRNA capPROSITE-ProRule annotation1
Binding sitei467mRNA capPROSITE-ProRule annotation1

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

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

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

Names & Taxonomyi

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
Gene namesi
Name:RNMT
Synonyms:KIAA0398
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

EuPathDBiHostDB:ENSG00000101654.17
HGNCiHGNC:10075 RNMT
MIMi603514 gene
neXtProtiNX_O43148

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi8731
OpenTargetsiENSG00000101654
PharmGKBiPA34448

Polymorphism and mutation databases

BioMutaiRNMT

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002483211 – 476mRNA cap guanine-N7 methyltransferaseAdd BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24PhosphoserineBy similarity1
Modified residuei28PhosphoserineBy similarity1
Modified residuei29PhosphoserineBy similarity1
Modified residuei118PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

PTM databases

iPTMnetiO43148
PhosphoSitePlusiO43148

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiENSG00000101654 Expressed in 231 organ(s), highest expression level in amniotic fluid
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 (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

Binary interactionsi

WithEntry#Exp.IntActNotes
RAMMETQ9BTL34EBI-877832,EBI-744023

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliO43148
SMRiO43148
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43148

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini128 – 476mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd BLAST349

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni176 – 177mRNA cap bindingPROSITE-ProRule annotation2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi126 – 128Nuclear localization signal3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1975 Eukaryota
ENOG410Y7HG LUCA
GeneTreeiENSGT00390000002368
HOVERGENiHBG081963
InParanoidiO43148
KOiK00565
OMAiLNLVSCQ
OrthoDBiEOG091G0C9Y
PhylomeDBiO43148
TreeFamiTF314347

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

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 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
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

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:
K7ERH6K7ERH6_HUMAN
mRNA cap guanine-N7 methyltransfera...
RNMT
114Annotation score:
K7EPP5K7EPP5_HUMAN
mRNA cap guanine-N7 methyltransfera...
RNMT
101Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti179M → I in BAA82447 (PubMed:10589710).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_020241465 – 476SIYLV…FEKQQ → RLTVTIMREAWLSTVGPGRA PVAASSVKWGTPRPAMQFIL in isoform 2. 1 PublicationAdd BLAST12

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

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

Similar proteinsi

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
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

CTDi8731
DisGeNETi8731
EuPathDBiHostDB:ENSG00000101654.17
GeneCardsiRNMT
HGNCiHGNC:10075 RNMT
HPAiHPA039409
MIMi603514 gene
neXtProtiNX_O43148
OpenTargetsiENSG00000101654
PharmGKBiPA34448
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1975 Eukaryota
ENOG410Y7HG LUCA
GeneTreeiENSGT00390000002368
HOVERGENiHBG081963
InParanoidiO43148
KOiK00565
OMAiLNLVSCQ
OrthoDBiEOG091G0C9Y
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

ChiTaRSiRNMT human
EvolutionaryTraceiO43148
GeneWikiiMRNA_(guanine-N7-)-methyltransferase
RNMT
GenomeRNAii8731
PROiPR:O43148
SOURCEiSearch...

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
ProtoNetiSearch...

Entry informationi

Entry nameiMCES_HUMAN
AccessioniPrimary (citable) accession number: O43148
Secondary accession number(s): B0YJ90
, D3DUJ5, O94996, Q9UIJ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 1998
Last modified: November 7, 2018
This is version 145 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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