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    DUSP11 dual specificity phosphatase 11 [ Homo sapiens (human) ]

    Gene ID: 8446, updated on 27-Nov-2024

    Summary

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    Official Symbol
    DUSP11provided by HGNC
    Official Full Name
    dual specificity phosphatase 11provided by HGNC
    Primary source
    HGNC:HGNC:3066
    See related
    Ensembl:ENSG00000144048 MIM:603092; AllianceGenome:HGNC:3066
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    PIR1
    Summary
    The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product is localized to the nucleus and binds directly to RNA and splicing factors, and thus it is suggested to participate in nuclear mRNA metabolism. [provided by RefSeq, Sep 2008]
    Expression
    Ubiquitous expression in esophagus (RPKM 14.8), urinary bladder (RPKM 12.3) and 25 other tissues See more
    Orthologs
    mouse all
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    Genomic context

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    See DUSP11 in Genome Data Viewer
    Location:
    2p13.1
    Exon count:
    9
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 2 NC_000002.12 (73762213..73780149, complement)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 2 NC_060926.1 (73775309..73793243, complement)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 2 NC_000002.11 (73989340..74007276, complement)

    Chromosome 2 - NC_000002.12Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC124905592 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16030 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16031 Neighboring gene TP53RK binding protein Neighboring gene ReSE screen-validated silencer GRCh37_chr2:73981125-73981308 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16032 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16033 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16034 Neighboring gene chromosome 2 open reading frame 78 Neighboring gene uncharacterized LOC105374807 Neighboring gene ReSE screen-validated silencer GRCh37_chr2:74055859-74056077 Neighboring gene STAM binding protein

    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
    • 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. Isolation and characterization of DUSP11, a novel p53 target gene. Caprara G, et al. J Cell Mol Med, 2009 Aug. PMID 19120688, Free PMC Article
    2. DUSP11 activity on triphosphorylated transcripts promotes Argonaute association with noncanonical viral microRNAs and regulates steady-state levels of cellular noncoding RNAs. Burke JM, et al. Genes Dev, 2016 Sep 15. PMID 27798849, Free PMC Article
    3. DUSP11 - An RNA phosphatase that regulates host and viral non-coding RNAs in mammalian cells. Burke JM, et al. RNA Biol, 2017 Nov 2. PMID 28296624, Free PMC Article
    4. Upregulation of PIR gene expression induced by human papillomavirus E6 and E7 in epithelial oral and cervical cells. Carrillo D, et al. Open Biol, 2017 Nov. PMID 29118270, Free PMC Article
    5. RNA triphosphatase DUSP11 enables exonuclease XRN-mediated restriction of hepatitis C virus. Kincaid RP, et al. Proc Natl Acad Sci U S A, 2018 Aug 7. PMID 30038017, Free PMC Article

    See all (42) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Atypical phosphatase DUSP11 inhibition promotes nc886 expression and potentiates gemcitabine-mediated cell death through NF-kB modulation.
      Title: Atypical phosphatase DUSP11 inhibition promotes nc886 expression and potentiates gemcitabine-mediated cell death through NF-kB modulation.
    2. DUSP11 limits both miR-122-dependent and miR-122-independent Hepatitis C RNA accumulation.
      Title: miR-122 does not impact recognition of the HCV genome by innate sensors of RNA but rather protects the 5' end from the cellular pyrophosphatases, DOM3Z and DUSP11.
    3. Results implicate DUSP11 as an important component of XRN-mediated restriction of hepatitis C virus replication.
      Title: RNA triphosphatase DUSP11 enables exonuclease XRN-mediated restriction of hepatitis C virus.
    4. DUSP11 regulates host and viral non-coding RNAs in mammalian cells.
      Title: DUSP11 - An RNA phosphatase that regulates host and viral non-coding RNAs in mammalian cells.
    5. PIR gene expression is highly dependent on the expression of HR-HPV E6 and E7 oncoproteins HPV-positive cell lines.
      Title: Upregulation of PIR gene expression induced by human papillomavirus E6 and E7 in epithelial oral and cervical cells.
    6. DUSP11 converts the 5' triphosphate of miRNA precursors to a 5' monophosphate, promoting loading of derivative 5p miRNAs into Argonaute proteins via a Dicer-coupled 5' monophosphate-dependent strand selection mechanism.
      Title: DUSP11 activity on triphosphorylated transcripts promotes Argonaute association with noncanonical viral microRNAs and regulates steady-state levels of cellular noncoding RNAs.
    7. the atomic structure of a catalytically inactive mutant (C152S) of the human PIR1 phosphatase core (PIR1-core, residues 29-205), refined at 1.20 A resolution.
      Title: Structure of human PIR1, an atypical dual-specificity phosphatase.
    8. results suggest that DUSP11 contributes to p53-dependent inhibition of cell proliferation and that it might be involved in regulating RNA splicing through SAM68
      Title: Isolation and characterization of DUSP11, a novel p53 target gene.
    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
    A genome-wide metabolic QTL analysis in Europeans implicates two loci shaped by recent positive selection.
    EBI GWAS Catalog
    Genetic loci influencing kidney function and chronic kidney disease.
    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)

    HIV-1 interactions

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    Replication interactions

    Interaction Pubs
    Knockdown of dual specificity phosphatase 11 (RNA/RNP complex 1-interacting, DUSP11) by shRNA library screening inhibits HIV-1 replication in cultured Jurkat T-cells PubMed

    Go to the HIV-1, Human Interaction Database

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Potential readthrough

    Included gene: TPRKB

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    enables RNA binding HDA PubMed 
    enables RNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables phosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables polynucleotide 5'-phosphatase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables polynucleotide 5'-phosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein tyrosine phosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in RNA processing TAS
    Traceable Author Statement
    more info
    		 PubMed 
    involved_in protein dephosphorylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in fibrillar center IDA
    Inferred from Direct Assay
    more info
    		  
    located_in intercellular bridge IDA
    Inferred from Direct Assay
    more info
    		  
    located_in mitochondrion HTP PubMed 
    located_in nuclear speck IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleoplasm IDA
    Inferred from Direct Assay
    more info
    		  
    located_in nucleus TAS
    Traceable Author Statement
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    RNA/RNP complex-1-interacting phosphatase
    Names
    RNA/RNP complex 1-interacting
    RNA/RNP complex-interacting phosphatase
    dual specificity protein phosphatase 11
    phosphatase that interacts with RNA/RNP complex 1
    serine/threonine specific protein phosphatase
    NP_001411578.1
    NP_003575.3

    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_001424649.1 → NP_001411578.1  RNA/RNP complex-1-interacting phosphatase isoform 2

      Status: REVIEWED

      Description
      Transcript Variant: This transcript variant (2) uses upstream transcription and translation start sites compared to transcript variant 1. The encoded isoform (2) has a longer N-terminus than isoform 1.
      Source sequence(s)
      AC092653
      Related
      ENSP00000520634.1, ENST00000717658.1

    2. NM_003584.3 → NP_003575.3  RNA/RNP complex-1-interacting phosphatase isoform 1

      Status: REVIEWED

      Description
      Transcript Variant: This transcript variant (1) encodes isoform 1.
      Source sequence(s)
      AC092653
      Consensus CDS
      CCDS1928.3
      UniProtKB/Swiss-Prot
      B2RCT8, C9JYA6, O75319, Q6AI47, Q9BWE3
      UniProtKB/TrEMBL
      A0A8Q3SIB0
      Related
      ENSP00000272444.4, ENST00000272444.8
      Conserved Domains (1) summary
      cd17665
      Location:34 → 201
      DSP_DUSP11; dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins

    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_000002.12 Reference GRCh38.p14 Primary Assembly

      Range
      73762213..73780149 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Reference GRCh38.p14 PATCHES

    Genomic

    1. NW_025791766.1 Reference GRCh38.p14 PATCHES

      Range
      431711..449647 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060926.1 Alternate T2T-CHM13v2.0

      Range
      73775309..73793243 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    O75319.3 GenPept UniProtKB/Swiss-Prot:O75319

    Gene LinkOut

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

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