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Polyribonucleotide nucleotidyltransferase 1, mitochondrial (EC 2.7.7.8) (3'-5' RNA exonuclease OLD35) (PNPase old-35) (Polynucleotide phosphorylase 1) (PNPase 1) (Polynucleotide phosphorylase-like protein)

 PNPT1_HUMAN             Reviewed;         783 AA.
Q8TCS8; Q53SU0; Q68CN1; Q7Z7D1; Q8IWX1; Q96T05; Q9BRU3; Q9BVX0;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 2.
30-AUG-2017, entry version 145.
RecName: Full=Polyribonucleotide nucleotidyltransferase 1, mitochondrial;
EC=2.7.7.8;
AltName: Full=3'-5' RNA exonuclease OLD35;
AltName: Full=PNPase old-35;
AltName: Full=Polynucleotide phosphorylase 1;
Short=PNPase 1;
AltName: Full=Polynucleotide phosphorylase-like protein;
Flags: Precursor;
Name=PNPT1; Synonyms=PNPASE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-121.
TISSUE=Teratocarcinoma;
PubMed=12419256; DOI=10.1016/S0022-2836(02)00947-6;
Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.;
"Protein-protein interactions between human exosome components support
the assembly of RNase PH-type subunits into a six-membered PNPase-like
ring.";
J. Mol. Biol. 323:653-663(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-121, FUNCTION, AND INDUCTION.
TISSUE=Melanoma;
PubMed=12473748; DOI=10.1073/pnas.252643699;
Leszczyniecka M., Kang D.-C., Sarkar D., Su Z.-Z., Holmes M.,
Valerie K., Fisher P.B.;
"Identification and cloning of human polynucleotide phosphorylase,
hPNPase (old-35), in the context of terminal differentiation and
cellular senescence.";
Proc. Natl. Acad. Sci. U.S.A. 99:16636-16641(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-121.
TISSUE=Cervix, Skin, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 509-783.
Takahashi H., Furukawa T., Yano T., Takizawa J., Abe T., Narita M.,
Fuse I., Koyama S., Takahashi M., Aizawa Y.;
"Immunogenic antigens eliciting humoral immune response identified in
leukemia cells by SEREX method.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-783.
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
FUNCTION.
PubMed=12721301; DOI=10.1074/jbc.M302421200;
Sarkar D., Leszczyniecka M., Kang D.C., Lebedeva I.V., Valerie K.,
Dhar S., Pandita T.K., Fisher P.B.;
"Down-regulation of Myc as a potential target for growth arrest
induced by human polynucleotide phosphorylase (hPNPaseold-35) in human
melanoma cells.";
J. Biol. Chem. 278:24542-24551(2003).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12798676; DOI=10.1016/S0022-2836(03)00528-X;
Piwowarski J., Grzechnik P., Dziembowski A., Dmochowska A.,
Minczuk M., Stepien P.P.;
"Human polynucleotide phosphorylase, hPNPase, is localized in
mitochondria.";
J. Mol. Biol. 329:853-857(2003).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16055741; DOI=10.1128/MCB.25.16.7333-7343.2005;
Sarkar D., Park E.S., Emdad L., Randolph A., Valerie K., Fisher P.B.;
"Defining the domains of human polynucleotide phosphorylase
(hPNPaseOLD-35) mediating cellular senescence.";
Mol. Cell. Biol. 25:7333-7343(2005).
[10]
FUNCTION, AND INDUCTION.
PubMed=16410805; DOI=10.1038/sj.cdd.4401829;
Sarkar D., Park E.S., Fisher P.B.;
"Defining the mechanism by which IFN-beta dowregulates c-myc
expression in human melanoma cells: pivotal role for human
polynucleotide phosphorylase (hPNPaseold-35).";
Cell Death Differ. 13:1541-1553(2006).
[11]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=16966381; DOI=10.1128/MCB.01002-06;
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.;
"Mammalian polynucleotide phosphorylase is an intermembrane space
RNase that maintains mitochondrial homeostasis.";
Mol. Cell. Biol. 26:8475-8487(2006).
[12]
FUNCTION, INTERACTION WITH TCL1A, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16934922; DOI=10.1016/j.canlet.2006.07.006;
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.;
"The TCL1 oncoprotein binds the RNase PH domains of the PNPase
exoribonuclease without affecting its RNA degrading activity.";
Cancer Lett. 248:198-210(2007).
[13]
FUNCTION.
PubMed=18501193; DOI=10.1016/j.bbrc.2008.05.058;
Wu J., Li Z.;
"Human polynucleotide phosphorylase reduces oxidative RNA damage and
protects HeLa cell against oxidative stress.";
Biochem. Biophys. Res. Commun. 372:288-292(2008).
[14]
FUNCTION, AND RNA-BINDING.
PubMed=18083836; DOI=10.1261/rna.698108;
Portnoy V., Palnizky G., Yehudai-Resheff S., Glaser F., Schuster G.;
"Analysis of the human polynucleotide phosphorylase (PNPase) reveals
differences in RNA binding and response to phosphate compared to its
bacterial and chloroplast counterparts.";
RNA 14:297-309(2008).
[15]
FUNCTION.
PubMed=18083837; DOI=10.1261/rna.697308;
Slomovic S., Schuster G.;
"Stable PNPase RNAi silencing: its effect on the processing and
adenylation of human mitochondrial RNA.";
RNA 14:310-323(2008).
[16]
FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL DEGRADOSOME COMPLEX, AND
HOMOTRIMERIZATION.
PubMed=19509288; DOI=10.1074/jbc.M109.009605;
Wang D.D., Shu Z., Lieser S.A., Chen P.L., Lee W.H.;
"Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-
kDa heteropentamer to cooperatively degrade double-stranded RNA with a
3'-to-5' directionality.";
J. Biol. Chem. 284:20812-20821(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264; LYS-285 AND LYS-289,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
FUNCTION, HOMOTRIMERIZATION, HOMOOLIGOMERIZATION, AND MUTAGENESIS OF
ASP-135; 445-ARG-ARG-446; SER-484 AND ASP-544.
PubMed=20691904; DOI=10.1016/j.cell.2010.06.035;
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.;
"PNPASE regulates RNA import into mitochondria.";
Cell 142:456-467(2010).
[19]
FUNCTION.
PubMed=20547861; DOI=10.1073/pnas.0914143107;
Das S.K., Sokhi U.K., Bhutia S.K., Azab B., Su Z.Z., Sarkar D.,
Fisher P.B.;
"Human polynucleotide phosphorylase selectively and preferentially
degrades microRNA-221 in human melanoma cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:11948-11953(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
VARIANT COXPD13 ARG-387, AND CHARACTERIZATION OF VARIANT COXPD13
ARG-387.
PubMed=23084291; DOI=10.1016/j.ajhg.2012.09.001;
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.;
"Mutation in PNPT1, which encodes a polyribonucleotide
nucleotidyltransferase, impairs RNA import into mitochondria and
causes respiratory-chain deficiency.";
Am. J. Hum. Genet. 91:912-918(2012).
[25]
VARIANT DFNB70 GLY-475, AND CHARACTERIZATION OF VARIANT DFNB70
GLY-475.
PubMed=23084290; DOI=10.1016/j.ajhg.2012.09.002;
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., Moser T., Wollnik B., Koehler C.M.,
Teitell M.A., Barakat A., Kubisch C.;
"A mutation in PNPT1, encoding mitochondrial-RNA-import protein
PNPase, causes hereditary hearing loss.";
Am. J. Hum. Genet. 91:919-927(2012).
-!- 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.
{ECO:0000269|PubMed:12473748, ECO:0000269|PubMed:12721301,
ECO:0000269|PubMed:12798676, ECO:0000269|PubMed:16055741,
ECO:0000269|PubMed:16410805, ECO:0000269|PubMed:16934922,
ECO:0000269|PubMed:18083836, ECO:0000269|PubMed:18083837,
ECO:0000269|PubMed:18501193, ECO:0000269|PubMed:19509288,
ECO:0000269|PubMed:20547861, ECO:0000269|PubMed:20691904}.
-!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside
diphosphate.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:16934922,
ECO:0000269|PubMed:19509288}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Mitochondrion
intermembrane space; Peripheral membrane protein.
-!- INDUCTION: Up-regulated in cells upon senescence and terminal
differentiation. Up-regulated after treatment with IFNB1/IFN-beta.
{ECO:0000269|PubMed:12473748, ECO:0000269|PubMed:16410805,
ECO:0000269|PubMed:16966381}.
-!- 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.
{ECO:0000269|PubMed:23084291}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:23084290}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the polyribonucleotide
nucleotidyltransferase family. {ECO:0000305}.
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EMBL; AJ458465; CAD30289.1; -; mRNA.
EMBL; AY027528; AAK13047.1; -; mRNA.
EMBL; AC015982; AAY24271.1; -; Genomic_DNA.
EMBL; BC000862; AAH00862.2; -; mRNA.
EMBL; BC005986; AAH05986.1; -; mRNA.
EMBL; BC053660; AAH53660.1; -; mRNA.
EMBL; AY290863; AAP44472.1; -; mRNA.
EMBL; CR749867; CAH18709.1; -; mRNA.
CCDS; CCDS1856.1; -.
PIR; T50626; T50626.
RefSeq; NP_149100.2; NM_033109.4.
UniGene; Hs.388733; -.
PDB; 3U1K; X-ray; 2.13 A; A/B/C/D=46-669.
PDBsum; 3U1K; -.
ProteinModelPortal; Q8TCS8; -.
SMR; Q8TCS8; -.
BioGrid; 124579; 35.
IntAct; Q8TCS8; 6.
MINT; MINT-3058521; -.
STRING; 9606.ENSP00000393953; -.
iPTMnet; Q8TCS8; -.
PhosphoSitePlus; Q8TCS8; -.
SwissPalm; Q8TCS8; -.
DMDM; 115502437; -.
REPRODUCTION-2DPAGE; IPI00291165; -.
EPD; Q8TCS8; -.
MaxQB; Q8TCS8; -.
PaxDb; Q8TCS8; -.
PeptideAtlas; Q8TCS8; -.
PRIDE; Q8TCS8; -.
Ensembl; ENST00000415374; ENSP00000393953; ENSG00000138035.
Ensembl; ENST00000447944; ENSP00000400646; ENSG00000138035.
GeneID; 87178; -.
KEGG; hsa:87178; -.
UCSC; uc002rzf.4; human.
CTD; 87178; -.
DisGeNET; 87178; -.
GeneCards; PNPT1; -.
H-InvDB; HIX0023979; -.
HGNC; HGNC:23166; PNPT1.
HPA; CAB033424; -.
HPA; HPA034602; -.
HPA; HPA034603; -.
MalaCards; PNPT1; -.
MIM; 610316; gene.
MIM; 614932; phenotype.
MIM; 614934; phenotype.
neXtProt; NX_Q8TCS8; -.
OpenTargets; ENSG00000138035; -.
Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
Orphanet; 319514; Combined oxidative phosphorylation defect type 13.
PharmGKB; PA134915354; -.
eggNOG; KOG1067; Eukaryota.
eggNOG; COG1185; LUCA.
GeneTree; ENSGT00390000014001; -.
HOVERGEN; HBG053625; -.
InParanoid; Q8TCS8; -.
KO; K00962; -.
OMA; RYMHNYN; -.
OrthoDB; EOG091G03MA; -.
PhylomeDB; Q8TCS8; -.
TreeFam; TF315264; -.
BRENDA; 2.7.7.8; 2681.
ChiTaRS; PNPT1; human.
GenomeRNAi; 87178; -.
PRO; PR:Q8TCS8; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138035; -.
CleanEx; HS_PNPT1; -.
ExpressionAtlas; Q8TCS8; baseline and differential.
Genevisible; Q8TCS8; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:0045025; C:mitochondrial degradosome; IDA:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0042788; C:polysomal ribosome; IEA:Ensembl.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0034046; F:poly(G) binding; IDA:UniProtKB.
GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB.
GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; IDA:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0000958; P:mitochondrial mRNA catabolic process; IDA:UniProtKB.
GO; GO:0097222; P:mitochondrial mRNA polyadenylation; IMP:UniProtKB.
GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IMP:UniProtKB.
GO; GO:0000964; P:mitochondrial RNA 5'-end processing; IMP:UniProtKB.
GO; GO:0000957; P:mitochondrial RNA catabolic process; IDA:UniProtKB.
GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
GO; GO:0071850; P:mitotic cell cycle arrest; IDA:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
GO; GO:0045926; P:negative regulation of growth; IDA:UniProtKB.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IDA:UniProtKB.
GO; GO:2000627; P:positive regulation of miRNA catabolic process; IDA:UniProtKB.
GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; IDA:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
GO; GO:0043457; P:regulation of cellular respiration; ISS:UniProtKB.
GO; GO:2000772; P:regulation of cellular senescence; IDA:UniProtKB.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
GO; GO:0035927; P:RNA import into mitochondrion; IDA:UniProtKB.
GO; GO:0043631; P:RNA polyadenylation; IDA:UniProtKB.
GO; GO:0035928; P:rRNA import into mitochondrion; IDA:UniProtKB.
Gene3D; 1.10.10.400; -; 1.
Gene3D; 3.30.1370.10; -; 1.
Gene3D; 3.30.230.70; -; 2.
InterPro; IPR001247; ExoRNase_PH_dom1.
InterPro; IPR015847; ExoRNase_PH_dom2.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR012162; PNPase.
InterPro; IPR027408; PNPase/RNase_PH_dom.
InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR022967; S1_dom.
InterPro; IPR003029; S1_domain.
PANTHER; PTHR11252; PTHR11252; 1.
Pfam; PF00013; KH_1; 1.
Pfam; PF03726; PNPase; 1.
Pfam; PF01138; RNase_PH; 2.
Pfam; PF03725; RNase_PH_C; 1.
Pfam; PF00575; S1; 1.
PIRSF; PIRSF005499; PNPase; 1.
SMART; SM00322; KH; 1.
SMART; SM00316; S1; 1.
SUPFAM; SSF46915; SSF46915; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF54211; SSF54211; 2.
SUPFAM; SSF54791; SSF54791; 1.
SUPFAM; SSF55666; SSF55666; 2.
TIGRFAMs; TIGR03591; polynuc_phos; 1.
PROSITE; PS50084; KH_TYPE_1; 1.
PROSITE; PS50126; S1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm; Deafness;
Disease mutation; Exonuclease; Hydrolase; Membrane; Mitochondrion;
mRNA processing; Non-syndromic deafness; Nuclease;
Nucleotidyltransferase; Phosphoprotein; Polymorphism;
Primary mitochondrial disease; Reference proteome; RNA-binding;
Transferase; Transit peptide; Transport.
TRANSIT 1 45 Mitochondrion. {ECO:0000255}.
CHAIN 46 783 Polyribonucleotide nucleotidyltransferase
1, mitochondrial.
/FTId=PRO_0000024751.
DOMAIN 605 664 KH. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 679 750 S1 motif. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
MOD_RES 250 250 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K1R3}.
MOD_RES 264 264 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 285 285 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 289 289 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 552 552 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8K1R3}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 782 782 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VARIANT 121 121 I -> V (in dbSNP:rs782572).
{ECO:0000269|PubMed:12419256,
ECO:0000269|PubMed:12473748,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_027787.
VARIANT 230 230 E -> Q (in dbSNP:rs34928857).
/FTId=VAR_050610.
VARIANT 387 387 Q -> R (in COXPD13; the mutation alters
multimerization of the protein;
dbSNP:rs397514598).
{ECO:0000269|PubMed:23084291}.
/FTId=VAR_069248.
VARIANT 475 475 E -> G (in DFNB70; results in a
hypofunctional protein leading to
disturbed enzyme trimerization and
impaired mitochondrial RNA import;
dbSNP:rs397514599).
{ECO:0000269|PubMed:23084290}.
/FTId=VAR_069249.
VARIANT 590 590 N -> D (in dbSNP:rs7594497).
/FTId=VAR_027788.
MUTAGEN 135 135 D->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.
{ECO:0000269|PubMed:20691904}.
MUTAGEN 445 446 RR->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.
{ECO:0000269|PubMed:20691904}.
MUTAGEN 484 484 S->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.
{ECO:0000269|PubMed:20691904}.
MUTAGEN 544 544 D->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.
{ECO:0000269|PubMed:20691904}.
CONFLICT 656 656 A -> V (in Ref. 2; AAK13047).
{ECO:0000305}.
STRAND 46 50 {ECO:0000244|PDB:3U1K}.
STRAND 52 63 {ECO:0000244|PDB:3U1K}.
STRAND 67 75 {ECO:0000244|PDB:3U1K}.
STRAND 78 86 {ECO:0000244|PDB:3U1K}.
STRAND 92 95 {ECO:0000244|PDB:3U1K}.
STRAND 98 103 {ECO:0000244|PDB:3U1K}.
STRAND 105 107 {ECO:0000244|PDB:3U1K}.
TURN 108 111 {ECO:0000244|PDB:3U1K}.
HELIX 125 138 {ECO:0000244|PDB:3U1K}.
HELIX 139 141 {ECO:0000244|PDB:3U1K}.
STRAND 150 158 {ECO:0000244|PDB:3U1K}.
STRAND 161 163 {ECO:0000244|PDB:3U1K}.
HELIX 165 179 {ECO:0000244|PDB:3U1K}.
STRAND 180 182 {ECO:0000244|PDB:3U1K}.
STRAND 189 196 {ECO:0000244|PDB:3U1K}.
STRAND 199 203 {ECO:0000244|PDB:3U1K}.
HELIX 206 210 {ECO:0000244|PDB:3U1K}.
STRAND 212 221 {ECO:0000244|PDB:3U1K}.
TURN 222 224 {ECO:0000244|PDB:3U1K}.
STRAND 225 236 {ECO:0000244|PDB:3U1K}.
HELIX 238 266 {ECO:0000244|PDB:3U1K}.
HELIX 281 299 {ECO:0000244|PDB:3U1K}.
HELIX 306 327 {ECO:0000244|PDB:3U1K}.
HELIX 333 355 {ECO:0000244|PDB:3U1K}.
STRAND 370 374 {ECO:0000244|PDB:3U1K}.
STRAND 380 388 {ECO:0000244|PDB:3U1K}.
STRAND 391 400 {ECO:0000244|PDB:3U1K}.
HELIX 402 405 {ECO:0000244|PDB:3U1K}.
HELIX 410 416 {ECO:0000244|PDB:3U1K}.
HELIX 420 422 {ECO:0000244|PDB:3U1K}.
STRAND 423 428 {ECO:0000244|PDB:3U1K}.
HELIX 431 434 {ECO:0000244|PDB:3U1K}.
HELIX 445 458 {ECO:0000244|PDB:3U1K}.
HELIX 459 461 {ECO:0000244|PDB:3U1K}.
STRAND 467 478 {ECO:0000244|PDB:3U1K}.
HELIX 483 497 {ECO:0000244|PDB:3U1K}.
STRAND 507 517 {ECO:0000244|PDB:3U1K}.
STRAND 519 522 {ECO:0000244|PDB:3U1K}.
STRAND 524 532 {ECO:0000244|PDB:3U1K}.
HELIX 535 539 {ECO:0000244|PDB:3U1K}.
STRAND 541 549 {ECO:0000244|PDB:3U1K}.
STRAND 554 561 {ECO:0000244|PDB:3U1K}.
HELIX 568 592 {ECO:0000244|PDB:3U1K}.
STRAND 606 611 {ECO:0000244|PDB:3U1K}.
HELIX 614 621 {ECO:0000244|PDB:3U1K}.
HELIX 623 625 {ECO:0000244|PDB:3U1K}.
HELIX 626 635 {ECO:0000244|PDB:3U1K}.
STRAND 638 641 {ECO:0000244|PDB:3U1K}.
STRAND 643 653 {ECO:0000244|PDB:3U1K}.
HELIX 654 663 {ECO:0000244|PDB:3U1K}.
SEQUENCE 783 AA; 85951 MW; 52DBC2119F7234E9 CRC64;
MAACRYCCSC LRLRPLSDGP FLLPRRDRAL TQLQVRALWS SAGSRAVAVD LGNRKLEISS
GKLARFADGS AVVQSGDTAV MVTAVSKTKP SPSQFMPLVV DYRQKAAAAG RIPTNYLRRE
IGTSDKEILT SRIIDRSIRP LFPAGYFYDT QVLCNLLAVD GVNEPDVLAI NGASVALSLS
DIPWNGPVGA VRIGIIDGEY VVNPTRKEMS SSTLNLVVAG APKSQIVMLE ASAENILQQD
FCHAIKVGVK YTQQIIQGIQ QLVKETGVTK RTPQKLFTPS PEIVKYTHKL AMERLYAVFT
DYEHDKVSRD EAVNKIRLDT EEQLKEKFPE ADPYEIIESF NVVAKEVFRS IVLNEYKRCD
GRDLTSLRNV SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD SLESGIKSDQ VITAINGIKD
KNFMLHYEFP PYATNEIGKV TGLNRRELGH GALAEKALYP VIPRDFPFTI RVTSEVLESN
GSSSMASACG GSLALMDSGV PISSAVAGVA IGLVTKTDPE KGEIEDYRLL TDILGIEDYN
GDMDFKIAGT NKGITALQAD IKLPGIPIKI VMEAIQQASV AKKEILQIMN KTISKPRASR
KENGPVVETV QVPLSKRAKF VGPGGYNLKK LQAETGVTIS QVDEETFSVF APTPSAMHEA
RDFITEICKD DQEQQLEFGA VYTATITEIR DTGVMVKLYP NMTAVLLHNT QLDQRKIKHP
TALGLEVGQE IQVKYFGRDP ADGRMRLSRK VLQSPATTVV RTLNDRSSIV MGEPISQSSS
NSQ


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