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Protein

mRNA-capping enzyme

Gene

Rngtt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.2 Publications

Catalytic activityi

A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.1 Publication
GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.1 Publication

Activity regulationi

RNA triphosphatase activity is inhibited by vanadate, iodoacetate and magnesium.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei126For RNA 5'-triphosphatase activityBy similarity1
Active sitei294N6-GMP-lysine intermediate1
Binding sitei299GTP1
Binding sitei315GTPSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi343 – 345GTPSequence analysis3
Nucleotide bindingi458 – 460GTPSequence analysis3
Nucleotide bindingi528 – 533GTPSequence analysis6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme, Nucleotidyltransferase, Transferase
Biological processmRNA capping, mRNA processing
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.7.50 3474
ReactomeiR-MMU-72086 mRNA Capping
R-MMU-77075 RNA Pol II CTD phosphorylation and interaction with CE

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-capping enzyme
Alternative name(s):
HCE
MCE1
Including the following 2 domains:
Polynucleotide 5'-triphosphatase (EC:3.1.3.33)
Short name:
TPase
Short name:
mRNA 5'-triphosphatase
mRNA guanylyltransferase (EC:2.7.7.50)
Alternative name(s):
GTP--RNA guanylyltransferase
Short name:
GTase
Gene namesi
Name:Rngtt
Synonyms:Cap1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1329041 Rngtt

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
Mutagenesisi36D → A: No effect. 1 Publication1
Mutagenesisi66D → A: Decrease of >90% of TPase activity. 1 Publication1
Mutagenesisi110C → S: No effect. 1 Publication1
Mutagenesisi125H → A: Decrease of 55-60% of TPase activity. 1 Publication1
Mutagenesisi126C → S: Loss of TPase activity. 1 Publication1
Mutagenesisi132R → A: Loss of TPase activity. 1 Publication1
Mutagenesisi133T → A: Decrease of 55-60% of TPase activity. 1 Publication1
Mutagenesisi138C → S: No effect. 1 Publication1
Mutagenesisi168D → A: No effect. 1 Publication1
Mutagenesisi290K → A: No effect. 1 Publication1
Mutagenesisi294K → A: Loss of GTase activity. 1 Publication1
Mutagenesisi315R → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication1
Mutagenesisi315R → K: At least 60% of RNA-binding activity and loss of GTase activity. 1 Publication1
Mutagenesisi375C → R: Increases stimulation of GTase activity by POLR2A binding. 1 Publication1
Mutagenesisi530R → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication1
Mutagenesisi530R → K: Loss of GTase activity. 1 Publication1
Mutagenesisi533K → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication1
Mutagenesisi533K → R: At least 60% of RNA-binding activity and loss of GTase activity. 1 Publication1
Mutagenesisi537N → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication1
Mutagenesisi537N → Q: At least 60% of RNA binding activity and loss of GTase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002101091 – 597mRNA-capping enzymeAdd BLAST597

Proteomic databases

EPDiO55236
PaxDbiO55236
PeptideAtlasiO55236
PRIDEiO55236

PTM databases

iPTMnetiO55236
PhosphoSitePlusiO55236

Expressioni

Gene expression databases

BgeeiENSMUSG00000028274 Expressed in 262 organ(s), highest expression level in blood
CleanExiMM_RNGTT
ExpressionAtlasiO55236 baseline and differential
GenevisibleiO55236 MM

Interactioni

Subunit structurei

Interacts with SUPT5H and RNMT (By similarity). Interacts with POLR2A (via C-terminus); this enhances guanylyltransferase activity. Binds (via GTase domain) to the elongating phosphorylated form of RNA polymerase II; can form direct interactions with the phosphorylated POLR2A C-terminal domain and indirect interactions via bound RNA.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P16333-13EBI-16118241,EBI-15578122From a different organism.

Protein-protein interaction databases

BioGridi204857, 1 interactor
DIPiDIP-61013N
IntActiO55236, 1 interactor
STRINGi10090.ENSMUSP00000103788

Structurei

Secondary structure

1597
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO55236
SMRiO55236
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO55236

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 212TPaseAdd BLAST212
Regioni229 – 597GTaseAdd BLAST369
Regioni330 – 386Interaction with POLR2A1 PublicationAdd BLAST57

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi195 – 205Asp/Glu-richAdd BLAST11

Sequence similaritiesi

In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family.Curated
In the C-terminal section; belongs to the eukaryotic GTase family.Curated

Phylogenomic databases

eggNOGiKOG2386 Eukaryota
COG5226 LUCA
GeneTreeiENSGT00530000063473
HOGENOMiHOG000264524
HOVERGENiHBG006332
InParanoidiO55236
KOiK13917
OMAiPELPEWC
OrthoDBiEOG091G063D
PhylomeDBiO55236
TreeFamiTF314914

Family and domain databases

Gene3Di3.90.190.10, 1 hit
InterProiView protein in InterPro
IPR000340 Dual-sp_phosphatase_cat-dom
IPR017074 mRNA_cap_enz_bifunc
IPR001339 mRNA_cap_enzyme
IPR013846 mRNA_cap_enzyme_C
IPR012340 NA-bd_OB-fold
IPR029021 Prot-tyrosine_phosphatase-like
IPR016130 Tyr_Pase_AS
IPR000387 TYR_PHOSPHATASE_dom
PfamiView protein in Pfam
PF00782 DSPc, 1 hit
PF03919 mRNA_cap_C, 1 hit
PF01331 mRNA_cap_enzyme, 1 hit
PIRSFiPIRSF036958 mRNA_capping_HCE, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
SSF52799 SSF52799, 1 hit
PROSITEiView protein in PROSITE
PS00383 TYR_PHOSPHATASE_1, 1 hit
PS50056 TYR_PHOSPHATASE_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O55236-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAYNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML
60 70 80 90 100
SNYLKSLKVK MSLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT
110 120 130 140 150
ENTETFIRLC ERFNERSPPE LIGVHCTHGF NRTGFLICAF LVEKMDWSIE
160 170 180 190 200
AAVATFAQAR PPGIYKGDYL KELFRRYGDI EEAPPPPVLP DWCFEDEDEE
210 220 230 240 250
DEDEDGKKDS EPGSSASFSK RRKERLKLGA IFLEGITVKG VTQVTTQPKL
260 270 280 290 300
GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IRLLEQKPYK VSWKADGTRY
310 320 330 340 350
MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDK
360 370 380 390 400
VNGQAVPRYL IYDIIKFNAQ PVGDCDFNIR LQCIEREIIS PRHEKMKTGL
410 420 430 440 450
IDKTQEPFSV RPKQFFDINI SRKLLEGNFA KEVSHEMDGL IFQPIGKYKP
460 470 480 490 500
GRCDDILKWK PPSLNSVDFR LKITRMGGEG LLPQNVGLLY VGGYERPFAQ
510 520 530 540 550
IKVTKELKQY DNKIIECKFE NNSWVFMRQR IDKSFPNAYN TAMAVCNSIS
560 570 580 590
NPVTKEMLFE FIDRCAAAAQ GQKRKYPLDP DTELMPPPPP KRLHRPT
Length:597
Mass (Da):68,684
Last modified:June 1, 1998 - v1
Checksum:iB2A9E711889D8EA7
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q9DCC1Q9DCC1_MOUSE
mRNA-capping enzyme
Rngtt mCG_123462
581Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025653 mRNA Translation: AAB91558.1
AF034568 mRNA Translation: AAB88903.1
BC043657 mRNA Translation: AAH43657.1
CCDSiCCDS38705.1
RefSeqiNP_036014.1, NM_011884.3
UniGeneiMm.240024
Mm.464346

Genome annotation databases

EnsembliENSMUST00000108153; ENSMUSP00000103788; ENSMUSG00000028274
GeneIDi24018
KEGGimmu:24018
UCSCiuc008sfv.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025653 mRNA Translation: AAB91558.1
AF034568 mRNA Translation: AAB88903.1
BC043657 mRNA Translation: AAH43657.1
CCDSiCCDS38705.1
RefSeqiNP_036014.1, NM_011884.3
UniGeneiMm.240024
Mm.464346

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I9SX-ray1.65A1-210[»]
1I9TX-ray1.70A1-210[»]
3RTXX-ray2.81A/B226-567[»]
ProteinModelPortaliO55236
SMRiO55236
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204857, 1 interactor
DIPiDIP-61013N
IntActiO55236, 1 interactor
STRINGi10090.ENSMUSP00000103788

PTM databases

iPTMnetiO55236
PhosphoSitePlusiO55236

Proteomic databases

EPDiO55236
PaxDbiO55236
PeptideAtlasiO55236
PRIDEiO55236

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108153; ENSMUSP00000103788; ENSMUSG00000028274
GeneIDi24018
KEGGimmu:24018
UCSCiuc008sfv.2 mouse

Organism-specific databases

CTDi8732
MGIiMGI:1329041 Rngtt

Phylogenomic databases

eggNOGiKOG2386 Eukaryota
COG5226 LUCA
GeneTreeiENSGT00530000063473
HOGENOMiHOG000264524
HOVERGENiHBG006332
InParanoidiO55236
KOiK13917
OMAiPELPEWC
OrthoDBiEOG091G063D
PhylomeDBiO55236
TreeFamiTF314914

Enzyme and pathway databases

BRENDAi2.7.7.50 3474
ReactomeiR-MMU-72086 mRNA Capping
R-MMU-77075 RNA Pol II CTD phosphorylation and interaction with CE

Miscellaneous databases

EvolutionaryTraceiO55236
PROiPR:O55236
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028274 Expressed in 262 organ(s), highest expression level in blood
CleanExiMM_RNGTT
ExpressionAtlasiO55236 baseline and differential
GenevisibleiO55236 MM

Family and domain databases

Gene3Di3.90.190.10, 1 hit
InterProiView protein in InterPro
IPR000340 Dual-sp_phosphatase_cat-dom
IPR017074 mRNA_cap_enz_bifunc
IPR001339 mRNA_cap_enzyme
IPR013846 mRNA_cap_enzyme_C
IPR012340 NA-bd_OB-fold
IPR029021 Prot-tyrosine_phosphatase-like
IPR016130 Tyr_Pase_AS
IPR000387 TYR_PHOSPHATASE_dom
PfamiView protein in Pfam
PF00782 DSPc, 1 hit
PF03919 mRNA_cap_C, 1 hit
PF01331 mRNA_cap_enzyme, 1 hit
PIRSFiPIRSF036958 mRNA_capping_HCE, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
SSF52799 SSF52799, 1 hit
PROSITEiView protein in PROSITE
PS00383 TYR_PHOSPHATASE_1, 1 hit
PS50056 TYR_PHOSPHATASE_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMCE1_MOUSE
AccessioniPrimary (citable) accession number: O55236
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: November 7, 2018
This is version 158 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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