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Rngtt RNA guanylyltransferase and 5'-phosphatase [ Mus musculus (house mouse) ]

Gene ID: 24018, updated on 11-Apr-2024

Summary

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Official Symbol
Rngttprovided by MGI
Official Full Name
RNA guanylyltransferase and 5'-phosphataseprovided by MGI
Primary source
MGI:MGI:1329041
See related
Ensembl:ENSMUSG00000028274 AllianceGenome:MGI:1329041
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Mus musculus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as
HCE; MCE1
Summary
Predicted to enable mRNA guanylyltransferase activity and triphosphatase activity. Predicted to be involved in 7-methylguanosine mRNA capping. Predicted to act upstream of or within mRNA processing. Predicted to be located in nucleus. Is expressed in several structures, including heart; liver; lung; metanephros; and spleen. Orthologous to human RNGTT (RNA guanylyltransferase and 5'-phosphatase). [provided by Alliance of Genome Resources, Apr 2022]
Expression
Ubiquitous expression in CNS E11.5 (RPKM 2.4), CNS E14 (RPKM 2.1) and 28 other tissues See more
Orthologs
human all
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Genomic context

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See Rngtt in Genome Data Viewer
Location:
4 A5; 4 14.78 cM
Exon count:
22
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCm39 (GCF_000001635.27) 4 NC_000070.7 (33310300..33502610)
108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 4 NC_000070.6 (33310300..33502614)

Chromosome 4 - NC_000070.7Genomic Context describing neighboring genes Neighboring gene serine and arginine-rich splicing factor 12 Neighboring gene STARR-positive B cell enhancer ABC_E9235 Neighboring gene STARR-positive B cell enhancer ABC_E6159 Neighboring gene STARR-seq mESC enhancer starr_09889 Neighboring gene STARR-seq mESC enhancer starr_09890 Neighboring gene proline-rich nuclear receptor coactivator 1 Neighboring gene STARR-seq mESC enhancer starr_09892 Neighboring gene STARR-positive B cell enhancer ABC_E833 Neighboring gene STARR-seq mESC enhancer starr_09894 Neighboring gene STARR-seq mESC enhancer starr_09895 Neighboring gene STARR-seq mESC enhancer starr_09897 Neighboring gene microRNA 8118 Neighboring gene predicted gene, 52726 Neighboring gene STARR-seq mESC enhancer starr_09900 Neighboring gene predicted gene, 32893

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: Mouse ENCODE transcriptome data
  • Description: RNA profiling data sets generated by the Mouse ENCODE project.
  • BioProject: PRJNA66167
  • Publication: PMID 25409824
  • Analysis date: n/a

Bibliography

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Related articles in PubMed

  1. Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme. Changela A, et al. EMBO J, 2001 May 15. PMID 11350947, Free PMC Article
  2. Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism. Wen Y, et al. Proc Natl Acad Sci U S A, 1998 Oct 13. PMID 9770468, Free PMC Article
  3. Functional characterization of the C-terminal domain of mouse capping enzyme. Liu L. Cell Biochem Funct, 2006 Mar-Apr. PMID 16342145
  4. Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II. Yue Z, et al. Proc Natl Acad Sci U S A, 1997 Nov 25. PMID 9371772, Free PMC Article
  5. The cytoplasmic capping complex assembles on adapter protein nck1 bound to the proline-rich C-terminus of Mammalian capping enzyme. Mukherjee C, et al. PLoS Biol, 2014 Aug. PMID 25137142, Free PMC Article

See all (28) citations in PubMed

GeneRIFs: Gene References Into Functions

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics  (MGI)
  • Gene trapped (1) 
  • Endonuclease-mediated (1) 

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by MGI

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables GTP binding IEA
Inferred from Electronic Annotation
more info
  
enables RNA guanylyltransferase activity ISO
Inferred from Sequence Orthology
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables inorganic triphosphate phosphatase activity ISO
Inferred from Sequence Orthology
more info
  
enables mRNA 5'-triphosphate monophosphatase activity IEA
Inferred from Electronic Annotation
more info
  
enables mRNA guanylyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables mRNA guanylyltransferase activity ISO
Inferred from Sequence Orthology
more info
  
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables nucleotidyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables phosphoprotein phosphatase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein tyrosine/serine/threonine phosphatase activity IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in 7-methylguanosine mRNA capping IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in 7-methylguanosine mRNA capping ISO
Inferred from Sequence Orthology
more info
  
involved_in RNA processing ISO
Inferred from Sequence Orthology
more info
  
involved_in dephosphorylation IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within mRNA processing IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in protein dephosphorylation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in nucleus IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
mRNA-capping enzyme
NP_001292202.1
NP_001413065.1
NP_001413066.1
NP_036014.1
XP_006537952.1
XP_006537953.1
XP_011248317.1
XP_017175678.2
XP_030109377.1
XP_036019988.1
XP_036019989.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001305273.2 → NP_001292202.1  mRNA-capping enzyme isoform 2

    See identical proteins and their annotated locations for NP_001292202.1

    Status: VALIDATED

    Source sequence(s)
    AC093925, AL772272, BX842672
    Consensus CDS
    CCDS84712.1
    UniProtKB/TrEMBL
    Q3UCK1, Q9DCC1
    Related
    ENSMUSP00000029942.8, ENSMUST00000029942.8
    Conserved Domains (3) summary
    cd07895
    Location:248 → 461
    Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
    pfam03919
    Location:465 → 545
    mRNA_cap_C; mRNA capping enzyme, C-terminal domain
    cl21483
    Location:47 → 143
    PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

  2. NM_001426136.1 → NP_001413065.1  mRNA-capping enzyme isoform 3

    Status: VALIDATED

    Source sequence(s)
    AC093925, AL772272, BX842672

  3. NM_001426137.1 → NP_001413066.1  mRNA-capping enzyme isoform 4

    Status: VALIDATED

    Source sequence(s)
    AC093925, AL772272, BX842672

  4. NM_011884.4 → NP_036014.1  mRNA-capping enzyme isoform 1

    See identical proteins and their annotated locations for NP_036014.1

    Status: VALIDATED

    Source sequence(s)
    AC093925, AL772272, BX842672
    Consensus CDS
    CCDS38705.1
    UniProtKB/Swiss-Prot
    O55236
    UniProtKB/TrEMBL
    Q3UA94, Q3UCK1
    Related
    ENSMUSP00000103788.3, ENSMUST00000108153.9
    Conserved Domains (3) summary
    cd07895
    Location:248 → 461
    Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
    pfam03919
    Location:465 → 558
    mRNA_cap_C; mRNA capping enzyme, C-terminal domain
    cl21483
    Location:47 → 143
    PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

  1. NC_000070.7 Reference GRCm39 C57BL/6J

    Range
    33310300..33502610
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_017320189.3 → XP_017175678.2  mRNA-capping enzyme isoform X3

    UniProtKB/TrEMBL
    Q3TUK6
    Conserved Domains (2) summary
    cd07895
    Location:238 → 451
    Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
    cl28904
    Location:45 → 165
    PTP_DSP_cys; cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily

  2. XM_030253517.1 → XP_030109377.1  mRNA-capping enzyme isoform X7

    Conserved Domains (2) summary
    cd07895
    Location:238 → 414
    Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
    cl28904
    Location:45 → 165
    PTP_DSP_cys; cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily

  3. XM_036164096.1 → XP_036019989.1  mRNA-capping enzyme isoform X2

    UniProtKB/TrEMBL
    Q3TUK6
    Conserved Domains (2) summary
    cd07895
    Location:248 → 461
    Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
    cd17664
    Location:9 → 175
    Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme

  4. XM_036164095.1 → XP_036019988.1  mRNA-capping enzyme isoform X1

    UniProtKB/TrEMBL
    Q3TUK6
    Conserved Domains (2) summary
    cd07895
    Location:248 → 461
    Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
    cd17664
    Location:9 → 175
    Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme

  5. XM_006537889.5 → XP_006537952.1  mRNA-capping enzyme isoform X4

    UniProtKB/TrEMBL
    Q3TUK6
    Conserved Domains (2) summary
    cd07895
    Location:248 → 447
    Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
    cd17664
    Location:9 → 175
    Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme

  6. XM_006537890.4 → XP_006537953.1  mRNA-capping enzyme isoform X5

    UniProtKB/TrEMBL
    Q3TUK6
    Conserved Domains (2) summary
    cd07895
    Location:248 → 456
    Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
    cd17664
    Location:9 → 175
    Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme

  7. XM_011250015.3 → XP_011248317.1  mRNA-capping enzyme isoform X6

    UniProtKB/TrEMBL
    Q3TUK6
    Conserved Domains (2) summary
    cd07895
    Location:248 → 424
    Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
    cd17664
    Location:9 → 175
    Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
O55236.1 GenPept UniProtKB/Swiss-Prot:O55236

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