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Q8TCS8 (PNPT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PNPT1
Synonyms:PNPASE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length783 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19

Catalytic activity

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

Subunit structure

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. Ref.12 Ref.16 Ref.18

Subcellular location

Cytoplasm. Mitochondrion. Mitochondrion intermembrane space; Peripheral membrane protein Ref.8 Ref.9 Ref.11.

Induction

Up-regulated in cells upon senescence and terminal differentiation. Up-regulated after treatment with IFNB1/IFN-beta. Ref.2 Ref.10 Ref.11

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Sequence similarities

Belongs to the polyribonucleotide nucleotidyltransferase family.

Contains 1 KH domain.

Contains 1 S1 motif domain.

Ontologies

Keywords
   Biological processmRNA processing
Transport
   Cellular componentCytoplasm
Membrane
Mitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDeafness
Disease mutation
Non-syndromic deafness
   DomainTransit peptide
   LigandRNA-binding
   Molecular functionExonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA catabolic process

Inferred from direct assay Ref.14. Source: UniProtKB

RNA import into mitochondrion

Inferred from direct assay Ref.18. Source: UniProtKB

RNA phosphodiester bond hydrolysis, exonucleolytic

Inferred from direct assay Ref.16. Source: GOC

RNA polyadenylation

Inferred from direct assay Ref.14. Source: UniProtKB

cellular response to interferon-beta

Inferred from direct assay Ref.10. Source: UniProtKB

cellular response to oxidative stress

Inferred from direct assay Ref.13. Source: UniProtKB

mRNA catabolic process

Inferred from direct assay Ref.7Ref.9. Source: UniProtKB

mitochondrial RNA 3'-end processing

Inferred from mutant phenotype Ref.15. Source: UniProtKB

mitochondrial RNA 5'-end processing

Inferred from mutant phenotype Ref.15. Source: UniProtKB

mitochondrial RNA catabolic process

Inferred from direct assay Ref.13. Source: UniProtKB

mitochondrial mRNA catabolic process

Inferred from direct assay Ref.18. Source: UniProtKB

mitochondrial mRNA polyadenylation

Inferred from mutant phenotype Ref.15. Source: UniProtKB

mitochondrion morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle arrest

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of growth

Inferred from direct assay Ref.7. Source: UniProtKB

nuclear polyadenylation-dependent mRNA catabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of mRNA catabolic process

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of miRNA catabolic process

Inferred from direct assay Ref.19. Source: UniProtKB

positive regulation of mitochondrial RNA catabolic process

Inferred from direct assay Ref.16. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.18. Source: UniProtKB

protein homotrimerization

Inferred from direct assay Ref.16Ref.18. Source: UniProtKB

rRNA import into mitochondrion

Inferred from direct assay Ref.18. Source: UniProtKB

regulation of cellular respiration

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cellular senescence

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial degradosome

Inferred from direct assay Ref.16. Source: UniProtKB

mitochondrial intermembrane space

Inferred from direct assay Ref.11. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.9PubMed 19864255Ref.18. Source: UniProtKB

   Molecular_function3'-5'-exoribonuclease activity

Inferred from direct assay Ref.16. Source: UniProtKB

miRNA binding

Inferred from direct assay Ref.19. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

poly(G) binding

Inferred from direct assay Ref.14. Source: UniProtKB

poly(U) RNA binding

Inferred from direct assay Ref.14. Source: UniProtKB

polyribonucleotide nucleotidyltransferase activity

Inferred from direct assay Ref.14. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4545Mitochondrion Potential
Chain46 – 783738Polyribonucleotide nucleotidyltransferase 1, mitochondrial
PRO_0000024751

Regions

Domain605 – 66460KH
Domain679 – 75072S1 motif

Amino acid modifications

Modified residue2501N6-acetyllysine By similarity
Modified residue2641N6-acetyllysine Ref.17
Modified residue2851N6-acetyllysine Ref.17
Modified residue2891N6-acetyllysine Ref.17
Modified residue5521N6-succinyllysine By similarity
Modified residue7821Phosphoserine Ref.21

Natural variations

Natural variant1211I → V. Ref.1 Ref.2 Ref.4
Corresponds to variant rs782572 [ dbSNP | Ensembl ].
VAR_027787
Natural variant2301E → Q.
Corresponds to variant rs34928857 [ dbSNP | Ensembl ].
VAR_050610
Natural variant3871Q → R in COXPD13; the mutation alters multimerization of the protein. Ref.22
VAR_069248
Natural variant4751E → G in DFNB70; results in a hypofunctional protein leading to disturbed enzyme trimerization and impaired mitochondrial RNA import. Ref.23
VAR_069249
Natural variant5901N → D.
Corresponds to variant rs7594497 [ dbSNP | Ensembl ].
VAR_027788

Experimental info

Mutagenesis1351D → 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. Ref.18
Mutagenesis445 – 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.
Mutagenesis4841S → 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. Ref.18
Mutagenesis5441D → 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. Ref.18
Sequence conflict6561A → V in AAK13047. Ref.2

Secondary structure

............................................................................................ 783
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8TCS8 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: 52DBC2119F7234E9

FASTA78385,951
        10         20         30         40         50         60 
MAACRYCCSC LRLRPLSDGP FLLPRRDRAL TQLQVRALWS SAGSRAVAVD LGNRKLEISS 

        70         80         90        100        110        120 
GKLARFADGS AVVQSGDTAV MVTAVSKTKP SPSQFMPLVV DYRQKAAAAG RIPTNYLRRE 

       130        140        150        160        170        180 
IGTSDKEILT SRIIDRSIRP LFPAGYFYDT QVLCNLLAVD GVNEPDVLAI NGASVALSLS 

       190        200        210        220        230        240 
DIPWNGPVGA VRIGIIDGEY VVNPTRKEMS SSTLNLVVAG APKSQIVMLE ASAENILQQD 

       250        260        270        280        290        300 
FCHAIKVGVK YTQQIIQGIQ QLVKETGVTK RTPQKLFTPS PEIVKYTHKL AMERLYAVFT 

       310        320        330        340        350        360 
DYEHDKVSRD EAVNKIRLDT EEQLKEKFPE ADPYEIIESF NVVAKEVFRS IVLNEYKRCD 

       370        380        390        400        410        420 
GRDLTSLRNV SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD SLESGIKSDQ VITAINGIKD 

       430        440        450        460        470        480 
KNFMLHYEFP PYATNEIGKV TGLNRRELGH GALAEKALYP VIPRDFPFTI RVTSEVLESN 

       490        500        510        520        530        540 
GSSSMASACG GSLALMDSGV PISSAVAGVA IGLVTKTDPE KGEIEDYRLL TDILGIEDYN 

       550        560        570        580        590        600 
GDMDFKIAGT NKGITALQAD IKLPGIPIKI VMEAIQQASV AKKEILQIMN KTISKPRASR 

       610        620        630        640        650        660 
KENGPVVETV QVPLSKRAKF VGPGGYNLKK LQAETGVTIS QVDEETFSVF APTPSAMHEA 

       670        680        690        700        710        720 
RDFITEICKD DQEQQLEFGA VYTATITEIR DTGVMVKLYP NMTAVLLHNT QLDQRKIKHP 

       730        740        750        760        770        780 
TALGLEVGQE IQVKYFGRDP ADGRMRLSRK VLQSPATTVV RTLNDRSSIV MGEPISQSSS 


NSQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"PNPASE regulates RNA import into mitochondria."
Wang G., Chen H.W., Oktay Y., Zhang J., Allen E.L., Smith G.M., Fan K.C., Hong J.S., French S.W., McCaffery J.M., Lightowlers R.N., Morse H.C. III, Koehler C.M., Teitell M.A.
Cell 142:456-467(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"A mutation in PNPT1, encoding mitochondrial-RNA-import protein PNPase, causes hereditary hearing loss."
von Ameln S., Wang G., Boulouiz R., Rutherford M.A., Smith G.M., Li Y., Pogoda H.M., Nurnberg G., Stiller B., Volk A.E., Borck G., Hong J.S., Goodyear R.J., Abidi O., Nurnberg P., Hofmann K., Richardson G.P., Hammerschmidt M. expand/collapse author list , Moser T., Wollnik B., Koehler C.M., Teitell M.A., Barakat A., Kubisch C.
Am. J. Hum. Genet. 91:919-927(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNB70 GLY-475, CHARACTERIZATION OF VARIANT DFNB70 GLY-475.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1856.1.
PIRT50626.
RefSeqNP_149100.2. NM_033109.4.
UniGeneHs.388733.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3U1KX-ray2.13A/B/C/D46-669[»]
ProteinModelPortalQ8TCS8.
SMRQ8TCS8. Positions 44-752.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124579. 15 interactions.
IntActQ8TCS8. 1 interaction.
MINTMINT-3058521.
STRING9606.ENSP00000393953.

PTM databases

PhosphoSiteQ8TCS8.

Polymorphism databases

DMDM115502437.

2D gel databases

REPRODUCTION-2DPAGEIPI00291165.

Proteomic databases

MaxQBQ8TCS8.
PaxDbQ8TCS8.
PeptideAtlasQ8TCS8.
PRIDEQ8TCS8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000415374; ENSP00000393953; ENSG00000138035.
ENST00000447944; ENSP00000400646; ENSG00000138035.
GeneID87178.
KEGGhsa:87178.
UCSCuc002rzf.3. human.

Organism-specific databases

CTD87178.
GeneCardsGC02M055861.
H-InvDBHIX0023979.
HGNCHGNC:23166. PNPT1.
HPAHPA034602.
HPA034603.
MIM610316. gene.
614932. phenotype.
614934. phenotype.
neXtProtNX_Q8TCS8.
Orphanet90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
319514. Combined oxidative phosphorylation defect type 13.
PharmGKBPA134915354.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1185.
HOVERGENHBG053625.
InParanoidQ8TCS8.
KOK00962.
OMARRIITHD.
OrthoDBEOG7NCV30.
PhylomeDBQ8TCS8.
TreeFamTF315264.

Enzyme and pathway databases

BRENDA2.7.7.8. 2681.

Gene expression databases

ArrayExpressQ8TCS8.
BgeeQ8TCS8.
CleanExHS_PNPT1.
GenevestigatorQ8TCS8.

Family and domain databases

Gene3D1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
3.30.1370.10. 1 hit.
3.30.230.70. 2 hits.
InterProIPR001247. 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]
PANTHERPTHR11252. PTHR11252. 1 hit.
PfamPF00013. 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]
PIRSFPIRSF005499. PNPase. 1 hit.
SMARTSM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF46915. SSF46915. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
TIGRFAMsTIGR03591. polynuc_phos. 1 hit.
PROSITEPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi87178.
NextBio76209.
PROQ8TCS8.
SOURCESearch...

Entry information

Entry namePNPT1_HUMAN
AccessionPrimary (citable) accession number: Q8TCS8
Secondary accession number(s): Q53SU0 expand/collapse secondary AC list , Q68CN1, Q7Z7D1, Q8IWX1, Q96T05, Q9BRU3, Q9BVX0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM