Q8TCS8 (PNPT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PNPT1
Synonyms:	PNPASE

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	783 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	RNA-binding protein implicated in numerous RNA metabolic processes. Hydrolyzes 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.15 Ref.16 Ref.17 Ref.18 Ref.21 Ref.22
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.18 Ref.21
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
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.13 Ref.14 Ref.19
Sequence similarities	Belongs to the polyribonucleotide nucleotidyltransferase family. Contains 1 KH domain. Contains 1 S1 motif domain.

Ontologies

Keywords
Biological process	Transport mRNA processing
Cellular component	Cytoplasm Membrane Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	RNA-binding
Molecular function	Exonuclease Hydrolase Nuclease Nucleotidyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to interferon-beta Inferred from direct assay Ref.10. Source: UniProtKB cellular response to oxidative stress Inferred from direct assay Ref.15. Source: UniProtKB mRNA polyadenylation Inferred from mutant phenotype Ref.17. Source: UniProtKB mitochondrial RNA 3'-end processing Inferred from mutant phenotype Ref.17. Source: UniProtKB mitochondrial RNA 5'-end processing Inferred from mutant phenotype Ref.17. Source: UniProtKB mitochondrial mRNA catabolic process Inferred from direct assay Ref.21. 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.22. Source: UniProtKB positive regulation of mitochondrial RNA catabolic process Inferred from direct assay Ref.18. Source: UniProtKB protein homotrimerization Inferred from direct assay Ref.18Ref.21. Source: UniProtKB rRNA import into mitochondrion Inferred from direct assay Ref.21. 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 component	mitochondrial degradosome Inferred from direct assay Ref.18. Source: UniProtKB mitochondrial intermembrane space Inferred from direct assay Ref.11. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA
Molecular function	3'-5'-exoribonuclease activity Inferred from direct assay Ref.18. Source: UniProtKB miRNA binding Inferred from direct assay Ref.22. Source: UniProtKB poly(G) RNA binding Inferred from direct assay Ref.16. Source: UniProtKB poly(U) RNA binding Inferred from direct assay Ref.16. Source: UniProtKB polyribonucleotide nucleotidyltransferase activity Inferred from direct assay Ref.16. Source: UniProtKB protein binding Inferred from physical interaction Ref.12. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 45	45	Mitochondrion Potential
	Chain	46 – 783	738	Polyribonucleotide nucleotidyltransferase 1, mitochondrial		PRO_0000024751
Regions
	Domain	605 – 664	60	KH
	Domain	679 – 750	72	S1 motif
Amino acid modifications
	Modified residue	123	1	Phosphothreonine Ref.13
	Modified residue	124	1	Phosphoserine Ref.13
	Modified residue	264	1	N6-acetyllysine Ref.20
	Modified residue	285	1	N6-acetyllysine Ref.20
	Modified residue	289	1	N6-acetyllysine Ref.20
	Modified residue	356	1	Phosphotyrosine Ref.19
	Modified residue	591	1	N6-acetyllysine Ref.20
	Modified residue	758	1	Phosphothreonine Ref.14
	Modified residue	776	1	Phosphoserine Ref.14
	Modified residue	782	1	Phosphoserine Ref.14
Natural variations
	Natural variant	121	1	I → V. Ref.1 Ref.2 Ref.4 Corresponds to variant rs782572 [ dbSNP | Ensembl ].		VAR_027787
	Natural variant	230	1	E → Q. Corresponds to variant rs34928857 [ dbSNP | Ensembl ].		VAR_050610
	Natural variant	590	1	N → D. Corresponds to variant rs7594497 [ dbSNP | Ensembl ].		VAR_027788
Experimental info
	Mutagenesis	135	1	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. Ref.21
	Mutagenesis	445 – 446	2	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.
	Mutagenesis	484	1	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. Ref.21
	Mutagenesis	544	1	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. Ref.21
	Sequence conflict	656	1	A → V in AAK13047. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8TCS8 [UniParc]. Last modified October 3, 2006. Version 2. Checksum: 52DBC2119F7234E9	FASTA	783	85,951
	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

References

	« Hide 'large scale' referencesShow '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: 12419256] [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: 12473748] [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: 15815621] [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: 15489334] [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: 17974005] [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: 12721301] [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: 12798676] [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: 16055741] [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: 16410805] [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: 16966381] [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: 16934922] [Abstract] Cited for: FUNCTION, INTERACTION WITH TCL1A, IDENTIFICATION BY MASS SPECTROMETRY.
[13]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-123 AND SER-124, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-758; SER-776 AND SER-782, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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: 18501193] [Abstract] Cited for: FUNCTION.
[16]	"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: 18083836] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[17]	"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: 18083837] [Abstract] Cited for: FUNCTION.
[18]	"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: 19509288] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL DEGRADOSOME COMPLEX, HOMOTRIMERIZATION.
[19]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-356, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264; LYS-285; LYS-289 AND LYS-591, MASS SPECTROMETRY.
[21]	"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: 20691904] [Abstract] Cited for: FUNCTION, HOMOTRIMERIZATION, HOMOOLIGOMERIZATION, MUTAGENESIS OF ASP-135; 445-ARG-ARG-446; SER-484 AND ASP-544.
[22]	"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: 20547861] [Abstract] Cited for: FUNCTION.
[23]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	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.
IPI	IPI00744711.
PIR	T50626.
RefSeq	NP_149100.2. NM_033109.3.
UniGene	Hs.388733.
3D structure databases
ProteinModelPortal	Q8TCS8.
SMR	Q8TCS8. Positions 43-751.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8TCS8.
PTM databases
PhosphoSite	Q8TCS8.
Polymorphism databases
DMDM	115502437.
2D gel databases
REPRODUCTION-2DPAGE	IPI00291165.
Proteomic databases
PeptideAtlas	Q8TCS8.
PRIDE	Q8TCS8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000415374; ENSP00000393953; ENSG00000138035. ENST00000447944; ENSP00000400646; ENSG00000138035. ENST00000450096; ENSP00000402488; ENSG00000138035.
GeneID	87178.
KEGG	hsa:87178.
NMPDR	fig|9606.3.peg.17886.
UCSC	uc002rzf.2. human.
Organism-specific databases
CTD	87178.
GeneCards	GC02M055861.
H-InvDB	HIX0023979.
HGNC	HGNC:23166. PNPT1.
HPA	HPA034603.
MIM	610316. gene.
neXtProt	NX_Q8TCS8.
PharmGKB	PA134915354.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08894.
GeneTree	ENSGT00390000014001.
HOVERGEN	HBG053625.
InParanoid	Q8TCS8.
OMA	IYAVFTD.
OrthoDB	EOG4T4CTT.
PhylomeDB	Q8TCS8.
Enzyme and pathway databases
BRENDA	2.7.7.8. 2681.
Gene expression databases
ArrayExpress	Q8TCS8.
Bgee	Q8TCS8.
CleanEx	HS_PNPT1.
Genevestigator	Q8TCS8.
GermOnline	ENSG00000138035. Homo sapiens.
Family and domain databases
InterPro	IPR001247. ExoRNase_PH_dom1. IPR015847. ExoRNase_PH_dom2. IPR004087. KH. IPR004088. KH_type_1. IPR018111. KH_type_1_subgr. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR012162. PNPase. 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]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. G3DSA:1.10.10.400. PNPase_PH_RNA-bd_bac/org-type. 1 hit.
KO	K00962.
PANTHER	PTHR11252. PNPase. 1 hit.
Pfam	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]
PIRSF	PIRSF005499. PNPase. 1 hit.
SMART	SM00322. KH. 1 hit. SM00316. S1. 1 hit. [Graphical view]
SUPFAM	SSF46915. 3_ExoRNase. 1 hit. SSF55666. 3_ExoRNase. 2 hits. SSF50249. Nucleic_acid_OB. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 2 hits.
TIGRFAMs	TIGR03591. Polynuc_phos. 1 hit.
PROSITE	PS50084. KH_TYPE_1. 1 hit. PS50126. S1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	76209.
SOURCE	Search...

Entry information

Entry name

PNPT1_HUMAN

Accession

Primary (citable) accession number: Q8TCS8
Secondary accession number(s): Q53SU0 , Q68CN1, Q7Z7D1, Q8IWX1, Q96T05, Q9BRU3, Q9BVX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	October 3, 2006
Last modified:	January 25, 2012
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.