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Q8TCS8

- PNPT1_HUMAN

UniProt

Q8TCS8 - PNPT1_HUMAN

Protein

Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Gene

PNPT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (03 Oct 2006)
      Previous versions | rss
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    Functioni

    RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.12 Publications

    Catalytic activityi

    RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: UniProtKB
    2. miRNA binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. poly(G) binding Source: UniProtKB
    5. poly(U) RNA binding Source: UniProtKB
    6. polyribonucleotide nucleotidyltransferase activity Source: UniProtKB
    7. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to interferon-beta Source: UniProtKB
    2. cellular response to oxidative stress Source: UniProtKB
    3. mitochondrial mRNA catabolic process Source: UniProtKB
    4. mitochondrial mRNA polyadenylation Source: UniProtKB
    5. mitochondrial RNA 3'-end processing Source: UniProtKB
    6. mitochondrial RNA 5'-end processing Source: UniProtKB
    7. mitochondrial RNA catabolic process Source: UniProtKB
    8. mitochondrion morphogenesis Source: UniProtKB
    9. mitotic cell cycle arrest Source: UniProtKB
    10. mRNA catabolic process Source: UniProtKB
    11. negative regulation of growth Source: UniProtKB
    12. nuclear polyadenylation-dependent mRNA catabolic process Source: UniProtKB
    13. positive regulation of miRNA catabolic process Source: UniProtKB
    14. positive regulation of mitochondrial RNA catabolic process Source: UniProtKB
    15. positive regulation of mRNA catabolic process Source: UniProtKB
    16. protein homooligomerization Source: UniProtKB
    17. protein homotrimerization Source: UniProtKB
    18. regulation of cellular respiration Source: UniProtKB
    19. regulation of cellular senescence Source: UniProtKB
    20. RNA catabolic process Source: UniProtKB
    21. RNA import into mitochondrion Source: UniProtKB
    22. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    23. RNA polyadenylation Source: UniProtKB
    24. rRNA import into mitochondrion Source: UniProtKB

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    mRNA processing, Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BRENDAi2.7.7.8. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyribonucleotide nucleotidyltransferase 1, mitochondrial (EC:2.7.7.8)
    Alternative name(s):
    3'-5' RNA exonuclease OLD35
    PNPase old-35
    Polynucleotide phosphorylase 1
    Short name:
    PNPase 1
    Polynucleotide phosphorylase-like protein
    Gene namesi
    Name:PNPT1
    Synonyms:PNPASE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:23166. PNPT1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. membrane Source: UniProtKB-KW
    3. mitochondrial degradosome Source: UniProtKB
    4. mitochondrial intermembrane space Source: UniProtKB
    5. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Combined oxidative phosphorylation deficiency 13 (COXPD13) [MIM:614932]: A mitochondrial disorder characterized by early onset severe encephalomyopathy, dystonia, choreoathetosis, bucofacial dyskinesias and combined mitochondrial respiratory chain deficiency. Nerve conductions velocities are decreased. Levels of plasma and cerebrospinal fluid lactate are increased.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti387 – 3871Q → R in COXPD13; the mutation alters multimerization of the protein. 1 Publication
    VAR_069248
    Deafness, autosomal recessive, 70 (DFNB70) [MIM:614934]: A form of non-syndromic deafness characterized by severe, bilateral hearing impairment with prelingual onset, resulting in inability to acquire normal speech.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti475 – 4751E → G in DFNB70; results in a hypofunctional protein leading to disturbed enzyme trimerization and impaired mitochondrial RNA import. 1 Publication
    VAR_069249

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi135 – 1351D → G: Inhibits poly(A) polymerase and RNA degradation activities. Inhibits the import or stabilization of RNase P RNA into the mitochondrial matrix. Does not inhibit homotrimerization activity. 1 Publication
    Mutagenesisi445 – 4462RR → EE: Stimulates in vitro poly(A) polymerase activity. Inhibits RNA degradation activity. Does not inhibit the import or stabilization of RNase P RNA into the mitochondrial matrix. Does not inhibit homotrimerization activity.
    Mutagenesisi484 – 4841S → A: Inhibits poly(A) polymerase and RNA degradation activities. Does not inhibit the import or stabilization of RNase P RNA into the mitochondrial matrix. Does not inhibit homotrimerization activity. 1 Publication
    Mutagenesisi544 – 5441D → A: Stimulates in vitro poly(A) polymerase activity. Inhibits RNA degradation activity. Inhibits the import or stabilization of RNase P RNA into the mitochondrial matrix. Does not inhibit homotrimerization activity. 1 Publication

    Keywords - Diseasei

    Deafness, Disease mutation, Non-syndromic deafness

    Organism-specific databases

    MIMi614932. phenotype.
    614934. phenotype.
    Orphaneti90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
    319514. Combined oxidative phosphorylation defect type 13.
    PharmGKBiPA134915354.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4545MitochondrionSequence AnalysisAdd
    BLAST
    Chaini46 – 783738Polyribonucleotide nucleotidyltransferase 1, mitochondrialPRO_0000024751Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei250 – 2501N6-acetyllysineBy similarity
    Modified residuei264 – 2641N6-acetyllysine1 Publication
    Modified residuei285 – 2851N6-acetyllysine1 Publication
    Modified residuei289 – 2891N6-acetyllysine1 Publication
    Modified residuei552 – 5521N6-succinyllysineBy similarity
    Modified residuei782 – 7821Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8TCS8.
    PaxDbiQ8TCS8.
    PeptideAtlasiQ8TCS8.
    PRIDEiQ8TCS8.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00291165.

    PTM databases

    PhosphoSiteiQ8TCS8.

    Expressioni

    Inductioni

    Up-regulated in cells upon senescence and terminal differentiation. Up-regulated after treatment with IFNB1/IFN-beta.3 Publications

    Gene expression databases

    ArrayExpressiQ8TCS8.
    BgeeiQ8TCS8.
    CleanExiHS_PNPT1.
    GenevestigatoriQ8TCS8.

    Organism-specific databases

    HPAiHPA034602.
    HPA034603.

    Interactioni

    Subunit structurei

    Homotrimer; in free form. Homooligomer. Component of the mitochondrial degradosome (mtEXO) complex which is a heteropentamer containing 2 copies of SUPV3L1 and 3 copies of PNPT1. Interacts with TCL1A; the interaction has no effect on PNPT1 exonuclease activity.2 Publications

    Protein-protein interaction databases

    BioGridi124579. 15 interactions.
    IntActiQ8TCS8. 1 interaction.
    MINTiMINT-3058521.
    STRINGi9606.ENSP00000393953.

    Structurei

    Secondary structure

    1
    783
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi46 – 505
    Beta strandi52 – 6312
    Beta strandi67 – 759
    Beta strandi78 – 869
    Beta strandi92 – 954
    Beta strandi98 – 1036
    Beta strandi105 – 1073
    Turni108 – 1114
    Helixi125 – 13814
    Helixi139 – 1413
    Beta strandi150 – 1589
    Beta strandi161 – 1633
    Helixi165 – 17915
    Beta strandi180 – 1823
    Beta strandi189 – 1968
    Beta strandi199 – 2035
    Helixi206 – 2105
    Beta strandi212 – 22110
    Turni222 – 2243
    Beta strandi225 – 23612
    Helixi238 – 26629
    Helixi281 – 29919
    Helixi306 – 32722
    Helixi333 – 35523
    Beta strandi370 – 3745
    Beta strandi380 – 3889
    Beta strandi391 – 40010
    Helixi402 – 4054
    Helixi410 – 4167
    Helixi420 – 4223
    Beta strandi423 – 4286
    Helixi431 – 4344
    Helixi445 – 45814
    Helixi459 – 4613
    Beta strandi467 – 47812
    Helixi483 – 49715
    Beta strandi507 – 51711
    Beta strandi519 – 5224
    Beta strandi524 – 5329
    Helixi535 – 5395
    Beta strandi541 – 5499
    Beta strandi554 – 5618
    Helixi568 – 59225
    Beta strandi606 – 6116
    Helixi614 – 6218
    Helixi623 – 6253
    Helixi626 – 63510
    Beta strandi638 – 6414
    Beta strandi643 – 65311
    Helixi654 – 66310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3U1KX-ray2.13A/B/C/D46-669[»]
    ProteinModelPortaliQ8TCS8.
    SMRiQ8TCS8. Positions 44-752.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini605 – 66460KHPROSITE-ProRule annotationAdd
    BLAST
    Domaini679 – 75072S1 motifPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 KH domain.PROSITE-ProRule annotation
    Contains 1 S1 motif domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1185.
    HOVERGENiHBG053625.
    InParanoidiQ8TCS8.
    KOiK00962.
    OMAiRRIITHD.
    OrthoDBiEOG7NCV30.
    PhylomeDBiQ8TCS8.
    TreeFamiTF315264.

    Family and domain databases

    Gene3Di1.10.10.400. 1 hit.
    2.40.50.140. 1 hit.
    3.30.1370.10. 1 hit.
    3.30.230.70. 2 hits.
    InterProiIPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012340. NA-bd_OB-fold.
    IPR012162. PNPase.
    IPR027408. PNPase/RNase_PH_dom.
    IPR015848. PNPase_PH_RNA-bd_bac/org-type.
    IPR003029. Rbsml_prot_S1_RNA-bd_dom.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view]
    PANTHERiPTHR11252. PTHR11252. 1 hit.
    PfamiPF00013. KH_1. 1 hit.
    PF03726. PNPase. 1 hit.
    PF01138. RNase_PH. 2 hits.
    PF03725. RNase_PH_C. 2 hits.
    PF00575. S1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005499. PNPase. 1 hit.
    SMARTiSM00322. KH. 1 hit.
    SM00316. S1. 1 hit.
    [Graphical view]
    SUPFAMiSSF46915. SSF46915. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF54211. SSF54211. 2 hits.
    SSF54791. SSF54791. 1 hit.
    SSF55666. SSF55666. 2 hits.
    TIGRFAMsiTIGR03591. polynuc_phos. 1 hit.
    PROSITEiPS50084. KH_TYPE_1. 1 hit.
    PS50126. S1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8TCS8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAACRYCCSC LRLRPLSDGP FLLPRRDRAL TQLQVRALWS SAGSRAVAVD    50
    LGNRKLEISS GKLARFADGS AVVQSGDTAV MVTAVSKTKP SPSQFMPLVV 100
    DYRQKAAAAG RIPTNYLRRE IGTSDKEILT SRIIDRSIRP LFPAGYFYDT 150
    QVLCNLLAVD GVNEPDVLAI NGASVALSLS DIPWNGPVGA VRIGIIDGEY 200
    VVNPTRKEMS SSTLNLVVAG APKSQIVMLE ASAENILQQD FCHAIKVGVK 250
    YTQQIIQGIQ QLVKETGVTK RTPQKLFTPS PEIVKYTHKL AMERLYAVFT 300
    DYEHDKVSRD EAVNKIRLDT EEQLKEKFPE ADPYEIIESF NVVAKEVFRS 350
    IVLNEYKRCD GRDLTSLRNV SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD 400
    SLESGIKSDQ VITAINGIKD KNFMLHYEFP PYATNEIGKV TGLNRRELGH 450
    GALAEKALYP VIPRDFPFTI RVTSEVLESN GSSSMASACG GSLALMDSGV 500
    PISSAVAGVA IGLVTKTDPE KGEIEDYRLL TDILGIEDYN GDMDFKIAGT 550
    NKGITALQAD IKLPGIPIKI VMEAIQQASV AKKEILQIMN KTISKPRASR 600
    KENGPVVETV QVPLSKRAKF VGPGGYNLKK LQAETGVTIS QVDEETFSVF 650
    APTPSAMHEA RDFITEICKD DQEQQLEFGA VYTATITEIR DTGVMVKLYP 700
    NMTAVLLHNT QLDQRKIKHP TALGLEVGQE IQVKYFGRDP ADGRMRLSRK 750
    VLQSPATTVV RTLNDRSSIV MGEPISQSSS NSQ 783
    Length:783
    Mass (Da):85,951
    Last modified:October 3, 2006 - v2
    Checksum:i52DBC2119F7234E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti656 – 6561A → V in AAK13047. (PubMed:12473748)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti121 – 1211I → V.3 Publications
    Corresponds to variant rs782572 [ dbSNP | Ensembl ].
    VAR_027787
    Natural varianti230 – 2301E → Q.
    Corresponds to variant rs34928857 [ dbSNP | Ensembl ].
    VAR_050610
    Natural varianti387 – 3871Q → R in COXPD13; the mutation alters multimerization of the protein. 1 Publication
    VAR_069248
    Natural varianti475 – 4751E → G in DFNB70; results in a hypofunctional protein leading to disturbed enzyme trimerization and impaired mitochondrial RNA import. 1 Publication
    VAR_069249
    Natural varianti590 – 5901N → D.
    Corresponds to variant rs7594497 [ dbSNP | Ensembl ].
    VAR_027788

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ458465 mRNA. Translation: CAD30289.1.
    AY027528 mRNA. Translation: AAK13047.1.
    AC015982 Genomic DNA. Translation: AAY24271.1.
    BC000862 mRNA. Translation: AAH00862.2.
    BC005986 mRNA. Translation: AAH05986.1.
    BC053660 mRNA. Translation: AAH53660.1.
    AY290863 mRNA. Translation: AAP44472.1.
    CR749867 mRNA. Translation: CAH18709.1.
    CCDSiCCDS1856.1.
    PIRiT50626.
    RefSeqiNP_149100.2. NM_033109.4.
    UniGeneiHs.388733.

    Genome annotation databases

    EnsembliENST00000415374; ENSP00000393953; ENSG00000138035.
    ENST00000447944; ENSP00000400646; ENSG00000138035.
    GeneIDi87178.
    KEGGihsa:87178.
    UCSCiuc002rzf.3. human.

    Polymorphism databases

    DMDMi115502437.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ458465 mRNA. Translation: CAD30289.1 .
    AY027528 mRNA. Translation: AAK13047.1 .
    AC015982 Genomic DNA. Translation: AAY24271.1 .
    BC000862 mRNA. Translation: AAH00862.2 .
    BC005986 mRNA. Translation: AAH05986.1 .
    BC053660 mRNA. Translation: AAH53660.1 .
    AY290863 mRNA. Translation: AAP44472.1 .
    CR749867 mRNA. Translation: CAH18709.1 .
    CCDSi CCDS1856.1.
    PIRi T50626.
    RefSeqi NP_149100.2. NM_033109.4.
    UniGenei Hs.388733.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3U1K X-ray 2.13 A/B/C/D 46-669 [» ]
    ProteinModelPortali Q8TCS8.
    SMRi Q8TCS8. Positions 44-752.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124579. 15 interactions.
    IntActi Q8TCS8. 1 interaction.
    MINTi MINT-3058521.
    STRINGi 9606.ENSP00000393953.

    PTM databases

    PhosphoSitei Q8TCS8.

    Polymorphism databases

    DMDMi 115502437.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00291165.

    Proteomic databases

    MaxQBi Q8TCS8.
    PaxDbi Q8TCS8.
    PeptideAtlasi Q8TCS8.
    PRIDEi Q8TCS8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000415374 ; ENSP00000393953 ; ENSG00000138035 .
    ENST00000447944 ; ENSP00000400646 ; ENSG00000138035 .
    GeneIDi 87178.
    KEGGi hsa:87178.
    UCSCi uc002rzf.3. human.

    Organism-specific databases

    CTDi 87178.
    GeneCardsi GC02M055861.
    H-InvDB HIX0023979.
    HGNCi HGNC:23166. PNPT1.
    HPAi HPA034602.
    HPA034603.
    MIMi 610316. gene.
    614932. phenotype.
    614934. phenotype.
    neXtProti NX_Q8TCS8.
    Orphaneti 90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
    319514. Combined oxidative phosphorylation defect type 13.
    PharmGKBi PA134915354.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1185.
    HOVERGENi HBG053625.
    InParanoidi Q8TCS8.
    KOi K00962.
    OMAi RRIITHD.
    OrthoDBi EOG7NCV30.
    PhylomeDBi Q8TCS8.
    TreeFami TF315264.

    Enzyme and pathway databases

    BRENDAi 2.7.7.8. 2681.

    Miscellaneous databases

    GenomeRNAii 87178.
    NextBioi 76209.
    PROi Q8TCS8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TCS8.
    Bgeei Q8TCS8.
    CleanExi HS_PNPT1.
    Genevestigatori Q8TCS8.

    Family and domain databases

    Gene3Di 1.10.10.400. 1 hit.
    2.40.50.140. 1 hit.
    3.30.1370.10. 1 hit.
    3.30.230.70. 2 hits.
    InterProi IPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012340. NA-bd_OB-fold.
    IPR012162. PNPase.
    IPR027408. PNPase/RNase_PH_dom.
    IPR015848. PNPase_PH_RNA-bd_bac/org-type.
    IPR003029. Rbsml_prot_S1_RNA-bd_dom.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view ]
    PANTHERi PTHR11252. PTHR11252. 1 hit.
    Pfami PF00013. KH_1. 1 hit.
    PF03726. PNPase. 1 hit.
    PF01138. RNase_PH. 2 hits.
    PF03725. RNase_PH_C. 2 hits.
    PF00575. S1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005499. PNPase. 1 hit.
    SMARTi SM00322. KH. 1 hit.
    SM00316. S1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46915. SSF46915. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF54211. SSF54211. 2 hits.
    SSF54791. SSF54791. 1 hit.
    SSF55666. SSF55666. 2 hits.
    TIGRFAMsi TIGR03591. polynuc_phos. 1 hit.
    PROSITEi PS50084. KH_TYPE_1. 1 hit.
    PS50126. S1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring."
      Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.
      J. Mol. Biol. 323:653-663(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-121.
      Tissue: Teratocarcinoma.
    2. "Identification and cloning of human polynucleotide phosphorylase, hPNPase (old-35), in the context of terminal differentiation and cellular senescence."
      Leszczyniecka M., Kang D.-C., Sarkar D., Su Z.-Z., Holmes M., Valerie K., Fisher P.B.
      Proc. Natl. Acad. Sci. U.S.A. 99:16636-16641(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-121, FUNCTION, INDUCTION.
      Tissue: Melanoma.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-121.
      Tissue: Cervix, Skin and Urinary bladder.
    5. "Immunogenic antigens eliciting humoral immune response identified in leukemia cells by SEREX method."
      Takahashi H., Furukawa T., Yano T., Takizawa J., Abe T., Narita M., Fuse I., Koyama S., Takahashi M., Aizawa Y.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 509-783.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-783.
      Tissue: Melanoma.
    7. "Down-regulation of Myc as a potential target for growth arrest induced by human polynucleotide phosphorylase (hPNPaseold-35) in human melanoma cells."
      Sarkar D., Leszczyniecka M., Kang D.C., Lebedeva I.V., Valerie K., Dhar S., Pandita T.K., Fisher P.B.
      J. Biol. Chem. 278:24542-24551(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Human polynucleotide phosphorylase, hPNPase, is localized in mitochondria."
      Piwowarski J., Grzechnik P., Dziembowski A., Dmochowska A., Minczuk M., Stepien P.P.
      J. Mol. Biol. 329:853-857(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Defining the domains of human polynucleotide phosphorylase (hPNPaseOLD-35) mediating cellular senescence."
      Sarkar D., Park E.S., Emdad L., Randolph A., Valerie K., Fisher P.B.
      Mol. Cell. Biol. 25:7333-7343(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Defining the mechanism by which IFN-beta dowregulates c-myc expression in human melanoma cells: pivotal role for human polynucleotide phosphorylase (hPNPaseold-35)."
      Sarkar D., Park E.S., Fisher P.B.
      Cell Death Differ. 13:1541-1553(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    11. "Mammalian polynucleotide phosphorylase is an intermembrane space RNase that maintains mitochondrial homeostasis."
      Chen H.W., Rainey R.N., Balatoni C.E., Dawson D.W., Troke J.J., Wasiak S., Hong J.S., McBride H.M., Koehler C.M., Teitell M.A., French S.W.
      Mol. Cell. Biol. 26:8475-8487(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION.
    12. "The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity."
      French S.W., Dawson D.W., Chen H.-W., Rainey R.N., Sievers S.A., Balatoni C.E., Wong L., Troke J.J., Nguyen M.T.N., Koehler C.M., Teitell M.A.
      Cancer Lett. 248:198-210(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TCL1A, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Human polynucleotide phosphorylase reduces oxidative RNA damage and protects HeLa cell against oxidative stress."
      Wu J., Li Z.
      Biochem. Biophys. Res. Commun. 372:288-292(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts."
      Portnoy V., Palnizky G., Yehudai-Resheff S., Glaser F., Schuster G.
      RNA 14:297-309(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    15. "Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA."
      Slomovic S., Schuster G.
      RNA 14:310-323(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5' directionality."
      Wang D.D., Shu Z., Lieser S.A., Chen P.L., Lee W.H.
      J. Biol. Chem. 284:20812-20821(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL DEGRADOSOME COMPLEX, HOMOTRIMERIZATION.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264; LYS-285 AND LYS-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: FUNCTION, HOMOTRIMERIZATION, HOMOOLIGOMERIZATION, MUTAGENESIS OF ASP-135; 445-ARG-ARG-446; SER-484 AND ASP-544.
    19. "Human polynucleotide phosphorylase selectively and preferentially degrades microRNA-221 in human melanoma cells."
      Das S.K., Sokhi U.K., Bhutia S.K., Azab B., Su Z.Z., Sarkar D., Fisher P.B.
      Proc. Natl. Acad. Sci. U.S.A. 107:11948-11953(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Mutation in PNPT1, which encodes a polyribonucleotide nucleotidyltransferase, impairs RNA import into mitochondria and causes respiratory-chain deficiency."
      Vedrenne V., Gowher A., De Lonlay P., Nitschke P., Serre V., Boddaert N., Altuzarra C., Mager-Heckel A.M., Chretien F., Entelis N., Munnich A., Tarassov I., Rotig A.
      Am. J. Hum. Genet. 91:912-918(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT COXPD13 ARG-387, CHARACTERIZATION OF VARIANT COXPD13 ARG-387.
    23. Cited for: VARIANT DFNB70 GLY-475, CHARACTERIZATION OF VARIANT DFNB70 GLY-475.

    Entry informationi

    Entry nameiPNPT1_HUMAN
    AccessioniPrimary (citable) accession number: Q8TCS8
    Secondary accession number(s): Q53SU0
    , Q68CN1, Q7Z7D1, Q8IWX1, Q96T05, Q9BRU3, Q9BVX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3