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Protein

mRNA cap guanine-N7 methyltransferase

Gene

Rnmt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei165 – 1651S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei190 – 1901S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei193 – 1931mRNA cap bindingPROSITE-ProRule annotation
Sitei199 – 1991mRNA cap bindingPROSITE-ProRule annotation
Binding sitei212 – 2121S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei224 – 2241mRNA cap bindingPROSITE-ProRule annotation
Binding sitei273 – 2731mRNA capPROSITE-ProRule annotation
Binding sitei355 – 3551mRNA capPROSITE-ProRule annotation
Binding sitei452 – 4521mRNA 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-RNO-72086. mRNA Capping.
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi1309242. Rnmt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461mRNA cap guanine-N7 methyltransferasePRO_0000248324Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei15 – 151PhosphoserineCombined sources
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei58 – 581PhosphoserineBy similarity
Modified residuei94 – 941PhosphoserineCombined sources
Modified residuei99 – 991PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5U2U7.
PRIDEiQ5U2U7.

PTM databases

iPTMnetiQ5U2U7.
PhosphoSiteiQ5U2U7.

Expressioni

Gene expression databases

GenevisibleiQ5U2U7. RN.

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

BioGridi253542. 1 interaction.
STRINGi10116.ENSRNOP00000022410.

Structurei

3D structure databases

ProteinModelPortaliQ5U2U7.
SMRiQ5U2U7. Positions 154-461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini113 – 461349mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni161 – 1622mRNA cap bindingPROSITE-ProRule annotation
Regioni246 – 2472S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni269 – 2713S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi107 – 1093Nuclear 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.
InParanoidiQ5U2U7.
KOiK00565.
OMAiCGQVDTP.
OrthoDBiEOG7ZSHT4.
PhylomeDBiQ5U2U7.
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]

Sequencei

Sequence statusi: Complete.

Q5U2U7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESSVKASVD SETESSPGVN ETAAASGQRL SEKTRQQADQ PKTQDDLVEQ
60 70 80 90 100
NSSYVQDSPS KKRKLDVEII LDEKHSEDDG GASKRSKLER GGGSEDEPSP
110 120 130 140 150
GGLTERKRKL QPQDALETQT RKFQKLEEGH SSAVAAHYNE LQEVGLVKRS
160 170 180 190 200
QSRIFYLRNF NNWIKSILIG EILEKVRQRK NRDITVLDLG CGKGGDLLKW
210 220 230 240 250
RKGRISRLVC ADIADISMKQ CQQRYEDMKC RRDNEYIFSA EFITADCSKE
260 270 280 290 300
LLVEKFHDPE MYFDICSCQF ACHYSFESLE QADMMLRNAC GRLNPGGYFI
310 320 330 340 350
GTTPNSFELI RRLEASETES FGNEIYTVKF QKKGNYPLFG CKYDFNLEGV
360 370 380 390 400
VDVPEFLVYF PLLTEMAKKY NMKLIYKKTF LEFYEEKIKN NENKMLLKRM
410 420 430 440 450
QALESYPANE NSKLASEKAG DYAHAAEYMK NSQVRLPLGT LSKSEWEATS
460
IYLVFAFEKQ Q
Length:461
Mass (Da):52,817
Last modified:December 7, 2004 - v1
Checksum:i6AF6C1B59C829C1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC085858 mRNA. Translation: AAH85858.1.
RefSeqiNP_001008300.1. NM_001008299.2.
XP_006254956.1. XM_006254894.1.
XP_006254957.1. XM_006254895.2.
UniGeneiRn.20871.

Genome annotation databases

EnsembliENSRNOT00000022410; ENSRNOP00000022410; ENSRNOG00000016698.
GeneIDi291534.
KEGGirno:291534.
UCSCiRGD:1309242. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC085858 mRNA. Translation: AAH85858.1.
RefSeqiNP_001008300.1. NM_001008299.2.
XP_006254956.1. XM_006254894.1.
XP_006254957.1. XM_006254895.2.
UniGeneiRn.20871.

3D structure databases

ProteinModelPortaliQ5U2U7.
SMRiQ5U2U7. Positions 154-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi253542. 1 interaction.
STRINGi10116.ENSRNOP00000022410.

PTM databases

iPTMnetiQ5U2U7.
PhosphoSiteiQ5U2U7.

Proteomic databases

PaxDbiQ5U2U7.
PRIDEiQ5U2U7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022410; ENSRNOP00000022410; ENSRNOG00000016698.
GeneIDi291534.
KEGGirno:291534.
UCSCiRGD:1309242. rat.

Organism-specific databases

CTDi8731.
RGDi1309242. Rnmt.

Phylogenomic databases

eggNOGiKOG1975. Eukaryota.
ENOG410Y7HG. LUCA.
GeneTreeiENSGT00390000002368.
HOGENOMiHOG000242614.
HOVERGENiHBG081963.
InParanoidiQ5U2U7.
KOiK00565.
OMAiCGQVDTP.
OrthoDBiEOG7ZSHT4.
PhylomeDBiQ5U2U7.
TreeFamiTF314347.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ5U2U7.

Gene expression databases

GenevisibleiQ5U2U7. RN.

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...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-16; SER-94 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCES_RAT
AccessioniPrimary (citable) accession number: Q5U2U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: December 7, 2004
Last modified: June 8, 2016
This is version 86 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. 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.