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Q8K1R3

- PNPT1_MOUSE

UniProt

Q8K1R3 - PNPT1_MOUSE

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Protein
Polyribonucleotide nucleotidyltransferase 1, mitochondrial
Gene
Pnpt1, Pnpase
Organism
Mus musculus (Mouse)
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.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
Complete GO annotation...

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: Ensembl
  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

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; 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
Complete GO annotation...

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 – 4545Mitochondrion Reviewed prediction
Add
BLAST
Chaini46 – 783738Polyribonucleotide nucleotidyltransferase 1, mitochondrial
PRO_0000024752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei250 – 2501N6-acetyllysine1 Publication
Modified residuei264 – 2641N6-acetyllysine By similarity
Modified residuei285 – 2851N6-acetyllysine By 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.

Protein-protein interaction databases

MINTiMINT-1853678.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ8K1R3.

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.
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei535 – 5406GIEDYN → ASIFPV in isoform 2.
VSP_013639
Alternative sequencei541 – 783243Missing in isoform 2.
VSP_013640Add
BLAST

Sequence conflict

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

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...

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

« 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] (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: July 9, 2014
This is version 113 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

Similar proteinsi