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Q8TCS8

- PNPT1_HUMAN

UniProt

Q8TCS8 - PNPT1_HUMAN

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Protein
Polyribonucleotide nucleotidyltransferase 1, mitochondrial
Gene
PNPT1, PNPASE
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

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

Cytoplasm. Mitochondrion. Mitochondrion intermembrane space; Peripheral membrane protein 3 Publications

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 4545Mitochondrion Reviewed prediction
Add
BLAST
Chaini46 – 783738Polyribonucleotide nucleotidyltransferase 1, mitochondrial
PRO_0000024751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei250 – 2501N6-acetyllysine By similarity
Modified residuei264 – 2641N6-acetyllysine1 Publication
Modified residuei285 – 2851N6-acetyllysine1 Publication
Modified residuei289 – 2891N6-acetyllysine1 Publication
Modified residuei552 – 5521N6-succinyllysine By 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.3 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini605 – 66460KH
Add
BLAST
Domaini679 – 75072S1 motif
Add
BLAST

Sequence similaritiesi

Contains 1 KH domain.
Contains 1 S1 motif domain.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti656 – 6561A → V in AAK13047. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 118 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

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