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Q8K1R3

- PNPT1_MOUSE

UniProt

Q8K1R3 - PNPT1_MOUSE

Protein

Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Gene

Pnpt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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.1 Publication

    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(G) binding Source: UniProtKB
    4. poly(U) RNA binding Source: UniProtKB
    5. polyribonucleotide nucleotidyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to interferon-beta Source: Ensembl
    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

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1918951. Pnpt1.

    Subcellular locationi

    Cytoplasm By similarity. Mitochondrion By similarity. Mitochondrion intermembrane space 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. mitochondrial degradosome Source: UniProtKB
    2. mitochondrial intermembrane space Source: MGI
    3. mitochondrion Source: UniProtKB
    4. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion

    Pathology & Biotechi

    Disruption phenotypei

    Mice show alteration in the mechanisms of polycistronic mtRNAs processing in mitochondria, resulting in fewer mature mtRNAs and a reduction in electron transport chain (ETC) components formation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4545MitochondrionSequence AnalysisAdd
    BLAST
    Chaini46 – 783738Polyribonucleotide nucleotidyltransferase 1, mitochondrialPRO_0000024752Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei250 – 2501N6-acetyllysine1 Publication
    Modified residuei264 – 2641N6-acetyllysineBy similarity
    Modified residuei285 – 2851N6-acetyllysineBy similarity
    Modified residuei552 – 5521N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8K1R3.
    PaxDbiQ8K1R3.
    PRIDEiQ8K1R3.

    PTM databases

    PhosphoSiteiQ8K1R3.

    Expressioni

    Gene expression databases

    BgeeiQ8K1R3.
    GenevestigatoriQ8K1R3.

    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 By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-1853678.

    Structurei

    Secondary structure

    1
    783
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi281 – 29919
    Helixi307 – 32418
    Turni325 – 3273
    Beta strandi329 – 3313
    Helixi333 – 35220

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WHUNMR-A273-363[»]
    ProteinModelPortaliQ8K1R3.
    SMRiQ8K1R3. Positions 44-666.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8K1R3.

    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.
    GeneTreeiENSGT00390000014001.
    HOGENOMiHOG000218327.
    HOVERGENiHBG053625.
    InParanoidiQ8K1R3.
    KOiK00962.
    OMAiPRWDWVA.
    OrthoDBiEOG7NCV30.
    PhylomeDBiQ8K1R3.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8K1R3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAACRLCCLC PCLRPLGCGP LGRPGRNRAL SYLQMRALWS STGSRAVTVD    50
    LGHRKLEISS GKLARFADGC AVIQSGDTAV MVTAVSKTKA SPSQFMPLVV 100
    DYRQKAAAAG RIPTNYLRRE IGSSDREVLT SRVIDRSIRP LFPAGYFYDT 150
    QVLCNLLAVD GINEPDILAV NGASVALSLS DIPWNGPVGA VRIGMIDGEC 200
    VVNPTRREMS SSTLNLVVAG APKSQIVMLE ASAENILQQD FCHAIKVGVK 250
    YTQQIIQGIQ QLVKEIGVAK RTPQKIFTPS AEIVKYTKII AMEKLYAVFT 300
    DYEHDKVSRD EAVNKIRLDT EEHLKEKFPE VDQFEIIESF NIVAKEVFRS 350
    IILNEYKRCD GRDLTSLRNI SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD 400
    SLESSIKSDQ IITAINGVKD KNFMLHYEFP PYATNETGKV TGVNRRELGH 450
    GALAEKALCP VIPKDFPFTI RVTSEVLESN GSSSMASACG GSLALMDAGV 500
    PISSAVAGVA VGLVTKTNPE KGEIEDYRLL TDILGIEDYN GDMDFKIAGT 550
    NKGITALQAD IKLPGVPIKI IMEAIQQASV AKKEILQIMN KTISKPRASR 600
    KENGPVVETV KVPLSKRAKF VGPGGYHLKK LQAETGVTIS QVDEETFSIF 650
    APTPTAMHEA RDFITEICRD DQEQQLEFGA VYTATITEIR DTGVMVKLYP 700
    NMTAVLLHNS QLDQRKIKHP TALGLEVGQE IQVKYFGRDP ADGRMRLSRK 750
    VLQSPATTAL KTLNDRSSIV MGEPVSQSSN SNP 783
    Length:783
    Mass (Da):85,683
    Last modified:October 1, 2002 - v1
    Checksum:iF35F6BE91AAB5626
    GO
    Isoform 2 (identifier: Q8K1R3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         535-540: GIEDYN → ASIFPV
         541-783: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:540
    Mass (Da):58,923
    Checksum:iE57BFA2B602361C4
    GO

    Sequence cautioni

    The sequence AAO33354.1 differs from that shown. Reason: Frameshift at positions 3, 6, 20, 23, 273, 286, 300, 312, 314, 320 and 325.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901A → P in AAO33354. 1 PublicationCurated
    Sequence conflicti298 – 2981V → G in AAO33354. 1 PublicationCurated
    Sequence conflicti315 – 3151K → Q in AAO33354. 1 PublicationCurated
    Sequence conflicti415 – 4151I → V in AAO33354. 1 PublicationCurated
    Sequence conflicti431 – 4311P → L in BAB23374. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei535 – 5406GIEDYN → ASIFPV in isoform 2. 1 PublicationVSP_013639
    Alternative sequencei541 – 783243Missing in isoform 2. 1 PublicationVSP_013640Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ507387 mRNA. Translation: CAD45436.1.
    AF465249 mRNA. Translation: AAO33354.1. Frameshift.
    AK004563 mRNA. Translation: BAB23374.1.
    AK149419 mRNA. Translation: BAE28862.1.
    BX000351 Genomic DNA. Translation: CAI25081.1.
    BC027228 mRNA. Translation: AAH27228.2.
    BC049283 mRNA. Translation: AAH49283.1.
    BC055826 mRNA. Translation: AAH55826.1.
    CCDSiCCDS24490.1. [Q8K1R3-1]
    RefSeqiNP_082145.1. NM_027869.1. [Q8K1R3-1]
    UniGeneiMm.211131.

    Genome annotation databases

    EnsembliENSMUST00000020756; ENSMUSP00000020756; ENSMUSG00000020464. [Q8K1R3-1]
    GeneIDi71701.
    KEGGimmu:71701.
    UCSCiuc007igp.1. mouse. [Q8K1R3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ507387 mRNA. Translation: CAD45436.1 .
    AF465249 mRNA. Translation: AAO33354.1 . Frameshift.
    AK004563 mRNA. Translation: BAB23374.1 .
    AK149419 mRNA. Translation: BAE28862.1 .
    BX000351 Genomic DNA. Translation: CAI25081.1 .
    BC027228 mRNA. Translation: AAH27228.2 .
    BC049283 mRNA. Translation: AAH49283.1 .
    BC055826 mRNA. Translation: AAH55826.1 .
    CCDSi CCDS24490.1. [Q8K1R3-1 ]
    RefSeqi NP_082145.1. NM_027869.1. [Q8K1R3-1 ]
    UniGenei Mm.211131.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WHU NMR - A 273-363 [» ]
    ProteinModelPortali Q8K1R3.
    SMRi Q8K1R3. Positions 44-666.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1853678.

    PTM databases

    PhosphoSitei Q8K1R3.

    Proteomic databases

    MaxQBi Q8K1R3.
    PaxDbi Q8K1R3.
    PRIDEi Q8K1R3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020756 ; ENSMUSP00000020756 ; ENSMUSG00000020464 . [Q8K1R3-1 ]
    GeneIDi 71701.
    KEGGi mmu:71701.
    UCSCi uc007igp.1. mouse. [Q8K1R3-1 ]

    Organism-specific databases

    CTDi 87178.
    MGIi MGI:1918951. Pnpt1.

    Phylogenomic databases

    eggNOGi COG1185.
    GeneTreei ENSGT00390000014001.
    HOGENOMi HOG000218327.
    HOVERGENi HBG053625.
    InParanoidi Q8K1R3.
    KOi K00962.
    OMAi PRWDWVA.
    OrthoDBi EOG7NCV30.
    PhylomeDBi Q8K1R3.
    TreeFami TF315264.

    Miscellaneous databases

    EvolutionaryTracei Q8K1R3.
    NextBioi 334263.
    PROi Q8K1R3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8K1R3.
    Genevestigatori Q8K1R3.

    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] (ISOFORM 1).
    2. "Cloning of mouse homolog of old-35."
      Leszczyniecka M., Fisher P.B.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Liver and Lung.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Mammary gland and Mammary tumor.
    6. "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.
    7. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Solution structure of the alpha-helical domain from mouse hypothetical PNPase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 273-363.

    Entry informationi

    Entry nameiPNPT1_MOUSE
    AccessioniPrimary (citable) accession number: Q8K1R3
    Secondary accession number(s): Q3UEP9
    , Q810U7, Q812B3, Q8R2U3, Q9DC52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3