Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

mRNA cap guanine-N7 methyltransferase

Gene

Rnmt

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

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 sitei169 – 1691S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei194 – 1941S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei197 – 1971mRNA cap bindingPROSITE-ProRule annotation
Sitei203 – 2031mRNA cap bindingPROSITE-ProRule annotation
Binding sitei216 – 2161S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei228 – 2281mRNA cap bindingPROSITE-ProRule annotation
Binding sitei277 – 2771mRNA capPROSITE-ProRule annotation
Binding sitei359 – 3591mRNA capPROSITE-ProRule annotation
Binding sitei456 – 4561mRNA capPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-MMU-72086. mRNA Capping.
R-MMU-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
Gene namesi
Name:Rnmt
Synonyms:Kiaa0398
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1915147. Rnmt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465mRNA cap guanine-N7 methyltransferasePRO_0000248323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei15 – 151PhosphoserineCombined sources
Modified residuei64 – 641PhosphoserineCombined sources
Modified residuei100 – 1001PhosphoserineCombined sources
Modified residuei105 – 1051PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D0L8.
MaxQBiQ9D0L8.
PaxDbiQ9D0L8.
PeptideAtlasiQ9D0L8.
PRIDEiQ9D0L8.

PTM databases

iPTMnetiQ9D0L8.
PhosphoSiteiQ9D0L8.

Expressioni

Gene expression databases

BgeeiENSMUSG00000009535.
CleanExiMM_RNMT.
ExpressionAtlasiQ9D0L8. baseline and differential.
GenevisibleiQ9D0L8. MM.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000009679.

Structurei

3D structure databases

ProteinModelPortaliQ9D0L8.
SMRiQ9D0L8. Positions 158-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 465349mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 1662mRNA cap bindingPROSITE-ProRule annotation
Regioni250 – 2512S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni273 – 2753S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi113 – 1153Nuclear localization signalBy similarity

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.
HOGENOMiHOG000242614.
HOVERGENiHBG081963.
InParanoidiQ9D0L8.
KOiK00565.
OMAiCGQVDTP.
OrthoDBiEOG091G0C9Y.
PhylomeDBiQ9D0L8.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9D0L8-1) [UniParc]FASTAAdd to basket

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
MEGSAKASVA SDPESPPGGN EPAAASGQRL PENTPPCQQV DQPKMQKEFG
60 70 80 90 100
EDLVEQNSSY VQDSPSKKRK LDVEIILEEK HSEDDGGSAK RSKLERGDVS
110 120 130 140 150
EDEPSLGRLN QTKRKLQPQD DEVPQKLQKL EEGHSSAVAA HYNELQEVGL
160 170 180 190 200
AKRSQSRIFY LRNFNNWIKS ILIGEILEKV RQRKTRDITV LDLGCGKGGD
210 220 230 240 250
LLKWRKGRIS RLVCADIADI SMKQCQQRYE DMRCRRDNEH IFSAEFITAD
260 270 280 290 300
CSKELLVEKF RDPEMYFDVC SCQFACHYSF ESQVQADTML RNACGRLNPG
310 320 330 340 350
GYFIGTTPNS FELIRRLEAS ETESFGNEIY TVKFQKKGNY PLFGCKYDFN
360 370 380 390 400
LEGVVDVPEF LVYFPLLTEM AKKYNMKLIY KKTFLEFYEE KIKNNENKML
410 420 430 440 450
LKRMQALEQY PAHENSKLAS EKVGDYTHAA EYLKKSQVRL PLGTLSKSEW
460
EATSIYLVFA FEKQQ
Length:465
Mass (Da):53,291
Last modified:June 1, 2001 - v1
Checksum:iD1422D9621EE2A1A
GO
Isoform 2 (identifier: Q9D0L8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     370-465: Missing.

Note: No experimental confirmation available.
Show »
Length:369
Mass (Da):41,908
Checksum:iCBC66ABB10D0F940
GO
Isoform 3 (identifier: Q9D0L8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     315-369: Missing.

Note: No experimental confirmation available.
Show »
Length:410
Mass (Da):46,867
Checksum:i7654F2915B8EB905
GO

Sequence cautioni

The sequence BAC97940 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321E → K in BAB29834 (PubMed:16141072).Curated
Sequence conflicti53 – 531L → H in BAE43278 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei315 – 36955Missing in isoform 3. 1 PublicationVSP_020242Add
BLAST
Alternative sequencei370 – 46596Missing in isoform 2. 1 PublicationVSP_020243Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129130 mRNA. Translation: BAC97940.1. Different initiation.
AK011300 mRNA. Translation: BAB27527.1.
AK015403 mRNA. Translation: BAB29834.1.
AK031780 mRNA. Translation: BAE43278.1.
BC021794 mRNA. Translation: AAH21794.1.
AK082331 mRNA. Translation: BAC38469.1.
CCDSiCCDS37852.1. [Q9D0L8-1]
CCDS50314.1. [Q9D0L8-3]
RefSeqiNP_001164424.1. NM_001170953.1. [Q9D0L8-3]
NP_080716.1. NM_026440.4. [Q9D0L8-1]
XP_006526256.1. XM_006526193.2. [Q9D0L8-1]
XP_006526257.1. XM_006526194.2. [Q9D0L8-1]
XP_006526259.1. XM_006526196.2. [Q9D0L8-1]
XP_006526260.1. XM_006526197.2. [Q9D0L8-1]
XP_011245293.1. XM_011246991.1. [Q9D0L8-1]
UniGeneiMm.27544.

Genome annotation databases

EnsembliENSMUST00000009679; ENSMUSP00000009679; ENSMUSG00000009535. [Q9D0L8-1]
ENSMUST00000025427; ENSMUSP00000025427; ENSMUSG00000009535. [Q9D0L8-3]
GeneIDi67897.
KEGGimmu:67897.
UCSCiuc008fnj.2. mouse. [Q9D0L8-1]
uc012bem.1. mouse. [Q9D0L8-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129130 mRNA. Translation: BAC97940.1. Different initiation.
AK011300 mRNA. Translation: BAB27527.1.
AK015403 mRNA. Translation: BAB29834.1.
AK031780 mRNA. Translation: BAE43278.1.
BC021794 mRNA. Translation: AAH21794.1.
AK082331 mRNA. Translation: BAC38469.1.
CCDSiCCDS37852.1. [Q9D0L8-1]
CCDS50314.1. [Q9D0L8-3]
RefSeqiNP_001164424.1. NM_001170953.1. [Q9D0L8-3]
NP_080716.1. NM_026440.4. [Q9D0L8-1]
XP_006526256.1. XM_006526193.2. [Q9D0L8-1]
XP_006526257.1. XM_006526194.2. [Q9D0L8-1]
XP_006526259.1. XM_006526196.2. [Q9D0L8-1]
XP_006526260.1. XM_006526197.2. [Q9D0L8-1]
XP_011245293.1. XM_011246991.1. [Q9D0L8-1]
UniGeneiMm.27544.

3D structure databases

ProteinModelPortaliQ9D0L8.
SMRiQ9D0L8. Positions 158-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000009679.

PTM databases

iPTMnetiQ9D0L8.
PhosphoSiteiQ9D0L8.

Proteomic databases

EPDiQ9D0L8.
MaxQBiQ9D0L8.
PaxDbiQ9D0L8.
PeptideAtlasiQ9D0L8.
PRIDEiQ9D0L8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000009679; ENSMUSP00000009679; ENSMUSG00000009535. [Q9D0L8-1]
ENSMUST00000025427; ENSMUSP00000025427; ENSMUSG00000009535. [Q9D0L8-3]
GeneIDi67897.
KEGGimmu:67897.
UCSCiuc008fnj.2. mouse. [Q9D0L8-1]
uc012bem.1. mouse. [Q9D0L8-3]

Organism-specific databases

CTDi8731.
MGIiMGI:1915147. Rnmt.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1975. Eukaryota.
ENOG410Y7HG. LUCA.
GeneTreeiENSGT00390000002368.
HOGENOMiHOG000242614.
HOVERGENiHBG081963.
InParanoidiQ9D0L8.
KOiK00565.
OMAiCGQVDTP.
OrthoDBiEOG091G0C9Y.
PhylomeDBiQ9D0L8.
TreeFamiTF314347.

Enzyme and pathway databases

ReactomeiR-MMU-72086. mRNA Capping.
R-MMU-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

ChiTaRSiRnmt. mouse.
PROiQ9D0L8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000009535.
CleanExiMM_RNMT.
ExpressionAtlasiQ9D0L8. baseline and differential.
GenevisibleiQ9D0L8. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q9D0L8
Secondary accession number(s): Q3V3U9, Q6ZQC6, Q9D5F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.