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Protein

Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Gene

PNPT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • 3'-5'-exoribonuclease activity Source: UniProtKB
  • miRNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • poly(G) binding Source: UniProtKB
  • poly(U) RNA binding Source: UniProtKB
  • polyribonucleotide nucleotidyltransferase activity Source: UniProtKB

GO - Biological processi

  • cellular response to interferon-beta Source: UniProtKB
  • cellular response to oxidative stress Source: UniProtKB
  • mitochondrial mRNA catabolic process Source: UniProtKB
  • mitochondrial mRNA polyadenylation Source: UniProtKB
  • mitochondrial RNA 3'-end processing Source: UniProtKB
  • mitochondrial RNA 5'-end processing Source: UniProtKB
  • mitochondrial RNA catabolic process Source: UniProtKB
  • mitochondrion morphogenesis Source: UniProtKB
  • mitotic cell cycle arrest Source: UniProtKB
  • mRNA catabolic process Source: UniProtKB
  • negative regulation of growth Source: UniProtKB
  • nuclear polyadenylation-dependent mRNA catabolic process Source: UniProtKB
  • positive regulation of miRNA catabolic process Source: UniProtKB
  • positive regulation of mitochondrial RNA catabolic process Source: UniProtKB
  • positive regulation of mRNA catabolic process Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein homotrimerization Source: UniProtKB
  • regulation of cellular respiration Source: UniProtKB
  • regulation of cellular senescence Source: UniProtKB
  • RNA catabolic process Source: UniProtKB
  • RNA import into mitochondrion Source: UniProtKB
  • RNA polyadenylation Source: UniProtKB
  • rRNA import into mitochondrion 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

BioCyciZFISH:HS06440-MONOMER.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:23166. PNPT1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • membrane Source: UniProtKB-KW
  • mitochondrial degradosome Source: UniProtKB
  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 13 (COXPD13)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:614932
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069248387Q → R in COXPD13; the mutation alters multimerization of the protein. 1 PublicationCorresponds to variant rs397514598dbSNPEnsembl.1
Deafness, autosomal recessive, 70 (DFNB70)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic deafness characterized by severe, bilateral hearing impairment with prelingual onset, resulting in inability to acquire normal speech.
See also OMIM:614934
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069249475E → G in DFNB70; results in a hypofunctional protein leading to disturbed enzyme trimerization and impaired mitochondrial RNA import. 1 PublicationCorresponds to variant rs397514599dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi135D → 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 Publication1
Mutagenesisi445 – 446RR → 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. 1 Publication2
Mutagenesisi484S → 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 Publication1
Mutagenesisi544D → 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 Publication1

Keywords - Diseasei

Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

DisGeNETi87178.
MalaCardsiPNPT1.
MIMi614932. phenotype.
614934. phenotype.
OpenTargetsiENSG00000138035.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
319514. Combined oxidative phosphorylation defect type 13.
PharmGKBiPA134915354.

Polymorphism and mutation databases

DMDMi115502437.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 45MitochondrionSequence analysisAdd BLAST45
ChainiPRO_000002475146 – 783Polyribonucleotide nucleotidyltransferase 1, mitochondrialAdd BLAST738

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei250N6-acetyllysineBy similarity1
Modified residuei264N6-acetyllysineCombined sources1
Modified residuei285N6-acetyllysineCombined sources1
Modified residuei289N6-acetyllysineCombined sources1
Modified residuei552N6-succinyllysineBy similarity1
Modified residuei754PhosphoserineCombined sources1
Modified residuei782PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8TCS8.
MaxQBiQ8TCS8.
PaxDbiQ8TCS8.
PeptideAtlasiQ8TCS8.
PRIDEiQ8TCS8.

2D gel databases

REPRODUCTION-2DPAGEIPI00291165.

PTM databases

iPTMnetiQ8TCS8.
PhosphoSitePlusiQ8TCS8.
SwissPalmiQ8TCS8.

Expressioni

Inductioni

Up-regulated in cells upon senescence and terminal differentiation. Up-regulated after treatment with IFNB1/IFN-beta.3 Publications

Gene expression databases

BgeeiENSG00000138035.
CleanExiHS_PNPT1.
ExpressionAtlasiQ8TCS8. baseline and differential.
GenevisibleiQ8TCS8. HS.

Organism-specific databases

HPAiCAB033424.
HPA034602.
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.2 Publications

Protein-protein interaction databases

BioGridi124579. 32 interactors.
IntActiQ8TCS8. 5 interactors.
MINTiMINT-3058521.
STRINGi9606.ENSP00000393953.

Structurei

Secondary structure

1783
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi46 – 50Combined sources5
Beta strandi52 – 63Combined sources12
Beta strandi67 – 75Combined sources9
Beta strandi78 – 86Combined sources9
Beta strandi92 – 95Combined sources4
Beta strandi98 – 103Combined sources6
Beta strandi105 – 107Combined sources3
Turni108 – 111Combined sources4
Helixi125 – 138Combined sources14
Helixi139 – 141Combined sources3
Beta strandi150 – 158Combined sources9
Beta strandi161 – 163Combined sources3
Helixi165 – 179Combined sources15
Beta strandi180 – 182Combined sources3
Beta strandi189 – 196Combined sources8
Beta strandi199 – 203Combined sources5
Helixi206 – 210Combined sources5
Beta strandi212 – 221Combined sources10
Turni222 – 224Combined sources3
Beta strandi225 – 236Combined sources12
Helixi238 – 266Combined sources29
Helixi281 – 299Combined sources19
Helixi306 – 327Combined sources22
Helixi333 – 355Combined sources23
Beta strandi370 – 374Combined sources5
Beta strandi380 – 388Combined sources9
Beta strandi391 – 400Combined sources10
Helixi402 – 405Combined sources4
Helixi410 – 416Combined sources7
Helixi420 – 422Combined sources3
Beta strandi423 – 428Combined sources6
Helixi431 – 434Combined sources4
Helixi445 – 458Combined sources14
Helixi459 – 461Combined sources3
Beta strandi467 – 478Combined sources12
Helixi483 – 497Combined sources15
Beta strandi507 – 517Combined sources11
Beta strandi519 – 522Combined sources4
Beta strandi524 – 532Combined sources9
Helixi535 – 539Combined sources5
Beta strandi541 – 549Combined sources9
Beta strandi554 – 561Combined sources8
Helixi568 – 592Combined sources25
Beta strandi606 – 611Combined sources6
Helixi614 – 621Combined sources8
Helixi623 – 625Combined sources3
Helixi626 – 635Combined sources10
Beta strandi638 – 641Combined sources4
Beta strandi643 – 653Combined sources11
Helixi654 – 663Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3U1KX-ray2.13A/B/C/D46-669[»]
ProteinModelPortaliQ8TCS8.
SMRiQ8TCS8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini605 – 664KHPROSITE-ProRule annotationAdd BLAST60
Domaini679 – 750S1 motifPROSITE-ProRule annotationAdd BLAST72

Sequence similaritiesi

Contains 1 KH domain.PROSITE-ProRule annotation
Contains 1 S1 motif domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1067. Eukaryota.
COG1185. LUCA.
GeneTreeiENSGT00390000014001.
HOVERGENiHBG053625.
InParanoidiQ8TCS8.
KOiK00962.
OMAiRFMFHYN.
OrthoDBiEOG091G03MA.
PhylomeDBiQ8TCS8.
TreeFamiTF315264.

Family and domain databases

Gene3Di1.10.10.400. 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.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR022967. S1_dom.
IPR003029. S1_domain.
[Graphical view]
PANTHERiPTHR11252. PTHR11252. 1 hit.
PfamiPF00013. KH_1. 1 hit.
PF03726. PNPase. 1 hit.
PF01138. RNase_PH. 2 hits.
PF03725. RNase_PH_C. 1 hit.
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

        10         20         30         40         50
MAACRYCCSC LRLRPLSDGP FLLPRRDRAL TQLQVRALWS SAGSRAVAVD
60 70 80 90 100
LGNRKLEISS GKLARFADGS AVVQSGDTAV MVTAVSKTKP SPSQFMPLVV
110 120 130 140 150
DYRQKAAAAG RIPTNYLRRE IGTSDKEILT SRIIDRSIRP LFPAGYFYDT
160 170 180 190 200
QVLCNLLAVD GVNEPDVLAI NGASVALSLS DIPWNGPVGA VRIGIIDGEY
210 220 230 240 250
VVNPTRKEMS SSTLNLVVAG APKSQIVMLE ASAENILQQD FCHAIKVGVK
260 270 280 290 300
YTQQIIQGIQ QLVKETGVTK RTPQKLFTPS PEIVKYTHKL AMERLYAVFT
310 320 330 340 350
DYEHDKVSRD EAVNKIRLDT EEQLKEKFPE ADPYEIIESF NVVAKEVFRS
360 370 380 390 400
IVLNEYKRCD GRDLTSLRNV SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD
410 420 430 440 450
SLESGIKSDQ VITAINGIKD KNFMLHYEFP PYATNEIGKV TGLNRRELGH
460 470 480 490 500
GALAEKALYP VIPRDFPFTI RVTSEVLESN GSSSMASACG GSLALMDSGV
510 520 530 540 550
PISSAVAGVA IGLVTKTDPE KGEIEDYRLL TDILGIEDYN GDMDFKIAGT
560 570 580 590 600
NKGITALQAD IKLPGIPIKI VMEAIQQASV AKKEILQIMN KTISKPRASR
610 620 630 640 650
KENGPVVETV QVPLSKRAKF VGPGGYNLKK LQAETGVTIS QVDEETFSVF
660 670 680 690 700
APTPSAMHEA RDFITEICKD DQEQQLEFGA VYTATITEIR DTGVMVKLYP
710 720 730 740 750
NMTAVLLHNT QLDQRKIKHP TALGLEVGQE IQVKYFGRDP ADGRMRLSRK
760 770 780
VLQSPATTVV RTLNDRSSIV MGEPISQSSS NSQ
Length:783
Mass (Da):85,951
Last modified:October 3, 2006 - v2
Checksum:i52DBC2119F7234E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti656A → V in AAK13047 (PubMed:12473748).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_027787121I → V.3 PublicationsCorresponds to variant rs782572dbSNPEnsembl.1
Natural variantiVAR_050610230E → Q.Corresponds to variant rs34928857dbSNPEnsembl.1
Natural variantiVAR_069248387Q → R in COXPD13; the mutation alters multimerization of the protein. 1 PublicationCorresponds to variant rs397514598dbSNPEnsembl.1
Natural variantiVAR_069249475E → G in DFNB70; results in a hypofunctional protein leading to disturbed enzyme trimerization and impaired mitochondrial RNA import. 1 PublicationCorresponds to variant rs397514599dbSNPEnsembl.1
Natural variantiVAR_027788590N → D.Corresponds to variant rs7594497dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3U1KX-ray2.13A/B/C/D46-669[»]
ProteinModelPortaliQ8TCS8.
SMRiQ8TCS8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124579. 32 interactors.
IntActiQ8TCS8. 5 interactors.
MINTiMINT-3058521.
STRINGi9606.ENSP00000393953.

PTM databases

iPTMnetiQ8TCS8.
PhosphoSitePlusiQ8TCS8.
SwissPalmiQ8TCS8.

Polymorphism and mutation databases

DMDMi115502437.

2D gel databases

REPRODUCTION-2DPAGEIPI00291165.

Proteomic databases

EPDiQ8TCS8.
MaxQBiQ8TCS8.
PaxDbiQ8TCS8.
PeptideAtlasiQ8TCS8.
PRIDEiQ8TCS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000415374; ENSP00000393953; ENSG00000138035.
ENST00000447944; ENSP00000400646; ENSG00000138035.
GeneIDi87178.
KEGGihsa:87178.
UCSCiuc002rzf.4. human.

Organism-specific databases

CTDi87178.
DisGeNETi87178.
GeneCardsiPNPT1.
H-InvDBHIX0023979.
HGNCiHGNC:23166. PNPT1.
HPAiCAB033424.
HPA034602.
HPA034603.
MalaCardsiPNPT1.
MIMi610316. gene.
614932. phenotype.
614934. phenotype.
neXtProtiNX_Q8TCS8.
OpenTargetsiENSG00000138035.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
319514. Combined oxidative phosphorylation defect type 13.
PharmGKBiPA134915354.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1067. Eukaryota.
COG1185. LUCA.
GeneTreeiENSGT00390000014001.
HOVERGENiHBG053625.
InParanoidiQ8TCS8.
KOiK00962.
OMAiRFMFHYN.
OrthoDBiEOG091G03MA.
PhylomeDBiQ8TCS8.
TreeFamiTF315264.

Enzyme and pathway databases

BioCyciZFISH:HS06440-MONOMER.
BRENDAi2.7.7.8. 2681.

Miscellaneous databases

ChiTaRSiPNPT1. human.
GenomeRNAii87178.
PROiQ8TCS8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138035.
CleanExiHS_PNPT1.
ExpressionAtlasiQ8TCS8. baseline and differential.
GenevisibleiQ8TCS8. HS.

Family and domain databases

Gene3Di1.10.10.400. 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.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR022967. S1_dom.
IPR003029. S1_domain.
[Graphical view]
PANTHERiPTHR11252. PTHR11252. 1 hit.
PfamiPF00013. KH_1. 1 hit.
PF03726. PNPase. 1 hit.
PF01138. RNase_PH. 2 hits.
PF03725. RNase_PH_C. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.