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Protein

mRNA-capping enzyme

Gene

Rngtt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei126For RNA 5'-triphosphatase activityBy similarity1
Active sitei294N6-GMP-lysine intermediate1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei299GTP1
Binding sitei315GTPSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi343 – 345GTPSequence analysis3
Nucleotide bindingi458 – 460GTPSequence analysis3
Nucleotide bindingi528 – 533GTPSequence analysis6

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.50 3474

Reactome - a knowledgebase of biological pathways and processes

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Rngtt
Synonyms:Cap1a
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1329041 Rngtt

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002101091 – 597mRNA-capping enzymeAdd BLAST597

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O55236

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O55236

PeptideAtlas

More...
PeptideAtlasi
O55236

PRoteomics IDEntifications database

More...
PRIDEi
O55236

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O55236

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O55236

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000028274 Expressed in 262 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

More...
CleanExi
MM_RNGTT

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O55236 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O55236 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
204857, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-61013N

Protein interaction database and analysis system

More...
IntActi
O55236, 2 interactors

Molecular INTeraction database

More...
MINTi
O55236

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000103788

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I9SX-ray1.65A1-210[»]
1I9TX-ray1.70A1-210[»]
3RTXX-ray2.81A/B226-567[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
O55236

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O55236

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O55236

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 212TPaseAdd BLAST212
Regioni229 – 597GTaseAdd BLAST369
Regioni330 – 386Interaction with POLR2A1 PublicationAdd BLAST57

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi195 – 205Asp/Glu-richAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2386 Eukaryota
COG5226 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156953

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000264524

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG006332

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O55236

KEGG Orthology (KO)

More...
KOi
K13917

Identification of Orthologs from Complete Genome Data

More...
OMAi
PELPEWC

Database of Orthologous Groups

More...
OrthoDBi
1544021at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O55236

TreeFam database of animal gene trees

More...
TreeFami
TF314914

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.190.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00782 DSPc, 1 hit
PF03919 mRNA_cap_C, 1 hit
PF01331 mRNA_cap_enzyme, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036958 mRNA_capping_HCE, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50249 SSF50249, 1 hit
SSF52799 SSF52799, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00383 TYR_PHOSPHATASE_1, 1 hit
PS50056 TYR_PHOSPHATASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB2A9E711889D8EA7
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF025653 mRNA Translation: AAB91558.1
AF034568 mRNA Translation: AAB88903.1
BC043657 mRNA Translation: AAH43657.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS38705.1

NCBI Reference Sequences

More...
RefSeqi
NP_036014.1, NM_011884.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.240024
Mm.464346

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000108153; ENSMUSP00000103788; ENSMUSG00000028274

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24018

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:24018

UCSC genome browser

More...
UCSCi
uc008sfv.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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, 2 interactors
MINTiO55236
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

Comparative Toxicogenomics Database

More...
CTDi
8732
MGIiMGI:1329041 Rngtt

Phylogenomic databases

eggNOGiKOG2386 Eukaryota
COG5226 LUCA
GeneTreeiENSGT00940000156953
HOGENOMiHOG000264524
HOVERGENiHBG006332
InParanoidiO55236
KOiK13917
OMAiPELPEWC
OrthoDBi1544021at2759
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

Protein Ontology

More...
PROi
PR:O55236

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

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

ProtoNet; Automatic hierarchical classification of proteins

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMCE1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O55236
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: January 16, 2019
This is version 160 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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