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    RNGTT RNA guanylyltransferase and 5'-phosphatase [ Homo sapiens (human) ]

    Gene ID: 8732, updated on 3-Nov-2024

    Summary

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    Official Symbol
    RNGTTprovided by HGNC
    Official Full Name
    RNA guanylyltransferase and 5'-phosphataseprovided by HGNC
    Primary source
    HGNC:HGNC:10073
    See related
    Ensembl:ENSG00000111880 MIM:603512; AllianceGenome:HGNC:10073
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    HCE; HCE1; hCAP; CAP1A
    Summary
    Enables inorganic triphosphate phosphatase activity and mRNA guanylyltransferase activity. Involved in 7-methylguanosine mRNA capping. Predicted to be located in nucleoplasm. [provided by Alliance of Genome Resources, Nov 2024]
    Expression
    Ubiquitous expression in lymph node (RPKM 8.1), testis (RPKM 5.3) and 24 other tissues See more
    Orthologs
    mouse all
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    Genomic context

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    See RNGTT in Genome Data Viewer
    Location:
    6q15
    Exon count:
    18
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 6 NC_000006.12 (88609897..88963618, complement)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 6 NC_060930.1 (89818328..90172178, complement)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 6 NC_000006.11 (89319616..89673337, complement)

    Chromosome 6 - NC_000006.12Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC105377885 Neighboring gene uncharacterized LOC124901358 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr6:89091597-89092538 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 24815 Neighboring gene uncharacterized LOC101928936 Neighboring gene CDK7 strongly-dependent group 2 enhancer GRCh37_chr6:89239515-89240714 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 17381 Neighboring gene uncharacterized LOC124901521 Neighboring gene MPRA-validated peak5946 silencer Neighboring gene ATAC-STARR-seq lymphoblastoid active region 24816 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr6:89438317-89438876 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr6:89439995-89440553 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr6:89440554-89441112 Neighboring gene MPRA-validated peak5947 silencer Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr6:89536615-89537462 Neighboring gene MPRA-validated peak5948 silencer Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr6:89671756-89672682 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 24817 Neighboring gene ReSE screen-validated silencer GRCh37_chr6:89673400-89673634 Neighboring gene OCT4-NANOG hESC enhancer GRCh37_chr6:89682583-89683204 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr6:89731277-89731892 Neighboring gene CRISPRi-validated cis-regulatory element chr6.3824 Neighboring gene MPRA-validated peak5950 silencer Neighboring gene OCT4-NANOG hESC enhancer GRCh37_chr6:89767403-89767931 Neighboring gene adaptor related protein complex 4 subunit sigma 1 pseudogene Neighboring gene CYCS pseudogene 16

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
    • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
    • BioProject: PRJEB4337
    • Publication: PMID 24309898
    • Analysis date: Wed Apr 4 07:08:55 2018

    Bibliography

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    Related articles in PubMed

    1. The immunosuppressive agent mizoribine monophosphate is an inhibitor of the human RNA capping enzyme. Picard-Jean F, et al. PLoS One, 2013. PMID 23349942, Free PMC Article
    2. 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
    3. Structure of the guanylyltransferase domain of human mRNA capping enzyme. Chu C, et al. Proc Natl Acad Sci U S A, 2011 Jun 21. PMID 21636784, Free PMC Article
    4. Tat stimulates cotranscriptional capping of HIV mRNA. Chiu YL, et al. Mol Cell, 2002 Sep. PMID 12408826
    5. c-Myc deregulation induces mRNA capping enzyme dependency. Lombardi O, et al. Oncotarget, 2016 Dec 13. PMID 27756891, Free PMC Article

    See all (75) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. c-Myc deregulation induces mRNA capping enzyme dependency in tumor cells.
      Title: c-Myc deregulation induces mRNA capping enzyme dependency.
    2. These results identify a new domain of CE that is specific to its function in cytoplasmic capping, and a new role for Nck1 in regulating gene expression through its role as the scaffold for assembly of the cytoplasmic capping complex.
      Title: The cytoplasmic capping complex assembles on adapter protein nck1 bound to the proline-rich C-terminus of Mammalian capping enzyme.
    3. Our biochemical studies provide the first insight that MZP can inhibit the formation of the RNA cap structure catalyzed by HCE.
      Title: The immunosuppressive agent mizoribine monophosphate is an inhibitor of the human RNA capping enzyme.
    4. Data show that human capping enzyme residues 229-567 comprise the minimum enzymatically active human GTase (hGTase) domain and determine the structure by X-ray crystallography.
      Title: Structure of the guanylyltransferase domain of human mRNA capping enzyme.
    5. Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)
      Title: Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Submit: New GeneRIF Correction

    Phenotypes

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    Find tests for this gene in the NIH Genetic Testing Registry (GTR)

    Review eQTL and phenotype association data in this region using PheGenI

    EBI GWAS Catalog

    Description
    Genome-wide association for abdominal subcutaneous and visceral adipose reveals a novel locus for visceral fat in women.
    EBI GWAS Catalog
    Genome-wide association of lipid-lowering response to statins in combined study populations.
    EBI GWAS Catalog

    Variation

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    See variants in ClinVar

    See studies and variants in dbVar

    See Variation Viewer (GRCh37.p13)

    See Variation Viewer (GRCh38)

    Genotypes

    HIV-1 interactions

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    Protein interactions

    Protein Gene Interaction Pubs
    Tat tat HIV-1 Tat interacts with mammalian capping enzyme (Mce1), stimulating its guanylyl-transferase and triphosphatase activities, thereby enhancing cap formation on TAR stem-loop RNA PubMed
    tat HIV-1 Tat binding to mammalian capping enzyme (Mce1) is mediated through the C-terminal domain of Tat (amino acids 49-86) and amino acids 211-597 of Mce1 PubMed

    Go to the HIV-1, Human Interaction Database

    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

    Clone Names

    • DKFZp686J2031

    Gene Ontology Provided by GOA

    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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables inorganic triphosphate phosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables phosphoprotein phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables polynucleotide 5'-phosphatase activity TAS
    Traceable Author Statement
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in 7-methylguanosine mRNA capping TAS
    Traceable Author Statement
    more info
    		  
    involved_in RNA processing IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein dephosphorylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in nucleoplasm TAS
    Traceable Author Statement
    more info
    		  
    located_in nucleus TAS
    Traceable Author Statement
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    mRNA-capping enzyme
    Names
    HCAP1
    NP_001273355.1
    NP_001273357.1
    NP_003791.3
    XP_047275398.1
    XP_047275399.1
    XP_054212620.1
    XP_054212621.1

    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_001286426.2 → NP_001273355.1  mRNA-capping enzyme isoform b

      See identical proteins and their annotated locations for NP_001273355.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (2) lacks an alternate in-frame exon in the 3' coding region, compared to variant 1, resulting in an isoform (b) that is shorter than isoform a.
      Source sequence(s)
      AB009023, AI193199, BC019954, BP256840, BP396964, BX537450
      Consensus CDS
      CCDS69153.1
      UniProtKB/TrEMBL
      B2R623
      Related
      ENSP00000358487.4, ENST00000369475.7
      Conserved Domains (3) summary
      cd07895
      Location:248 → 438
      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
      pfam03919
      Location:442 → 535
      mRNA_cap_C; mRNA capping enzyme, C-terminal domain

    2. NM_001286428.2 → NP_001273357.1  mRNA-capping enzyme isoform c

      See identical proteins and their annotated locations for NP_001273357.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (3) differs in its 5' UTR, lacks a portion of the 5' coding region, initiates translation at a downstream in-frame start codon, and lacks an alternate in-frame exon in the 3' coding region, compared to variant 1. The encoded isoform (c) is shorter at the N-terminus, compared to isoform a.
      Source sequence(s)
      AI193199, AK299777, BC019954, BP396964, BX537450
      UniProtKB/TrEMBL
      B4DIQ0, B4DSJ8
      Conserved Domains (3) summary
      cd07895
      Location:188 → 378
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      pfam03919
      Location:382 → 475
      mRNA_cap_C; mRNA capping enzyme, C-terminal domain
      cl21483
      Location:14 → 83
      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 ...

    3. NM_003800.5 → NP_003791.3  mRNA-capping enzyme isoform a

      See identical proteins and their annotated locations for NP_003791.3

      Status: VALIDATED

      Description
      Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (a).
      Source sequence(s)
      AB009022, AI193199, BC019954, BP256840, BP396964, BX537450
      Consensus CDS
      CCDS5017.1
      UniProtKB/Swiss-Prot
      E1P513, E1P514, O43483, O60257, O60351, O60942, Q5TCW8, Q8WUM8
      UniProtKB/TrEMBL
      B2R623
      Related
      ENSP00000358497.4, ENST00000369485.9
      Conserved Domains (3) 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
      pfam03919
      Location:465 → 558
      mRNA_cap_C; mRNA capping enzyme, C-terminal domain

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

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

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000006.12 Reference GRCh38.p14 Primary Assembly

      Range
      88609897..88963618 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_047419443.1 → XP_047275399.1  mRNA-capping enzyme isoform X2

      Related
      ENSP00000442609.2, ENST00000538899.2

    2. XM_047419442.1 → XP_047275398.1  mRNA-capping enzyme isoform X1

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060930.1 Alternate T2T-CHM13v2.0

      Range
      89818328..90172178 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_054356646.1 → XP_054212621.1  mRNA-capping enzyme isoform X2

    2. XM_054356645.1 → XP_054212620.1  mRNA-capping enzyme isoform X1

    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    O60942.1 GenPept UniProtKB/Swiss-Prot:O60942

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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