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Protein

Purine nucleoside phosphorylase

Gene

PNP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.1 Publication

Catalytic activityi

Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.

Pathwayi: purine nucleoside salvage

This protein is involved in the pathway purine nucleoside salvage, which is part of Purine metabolism.
View all proteins of this organism that are known to be involved in the pathway purine nucleoside salvage and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33PhosphateBy similarity1
Binding sitei64PhosphateBy similarity1
Binding sitei116Phosphate; via amide nitrogenBy similarity1
Binding sitei201Purine nucleosideBy similarity1
Binding sitei220PhosphateBy similarity1
Binding sitei243Purine nucleosideBy similarity1

GO - Molecular functioni

  • drug binding Source: UniProtKB
  • nucleoside binding Source: UniProtKB
  • phosphate ion binding Source: UniProtKB
  • purine nucleobase binding Source: UniProtKB
  • purine-nucleoside phosphorylase activity Source: UniProtKB

GO - Biological processi

  • immune response Source: UniProtKB
  • inosine catabolic process Source: MGI
  • interleukin-2 secretion Source: UniProtKB
  • NAD biosynthesis via nicotinamide riboside salvage pathway Source: UniProtKB
  • nicotinamide riboside catabolic process Source: UniProtKB
  • nucleobase-containing compound metabolic process Source: UniProtKB
  • positive regulation of alpha-beta T cell differentiation Source: MGI
  • positive regulation of T cell proliferation Source: MGI
  • purine-containing compound salvage Source: GO_Central
  • purine nucleotide catabolic process Source: Reactome
  • response to drug Source: UniProtKB
  • urate biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS02151-MONOMER.
ZFISH:HS02151-MONOMER.
BRENDAi2.4.2.1. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-74217. Purine salvage.
R-HSA-74259. Purine catabolism.
SABIO-RKP00491.
SignaLinkiP00491.
UniPathwayiUPA00606.

Names & Taxonomyi

Protein namesi
Recommended name:
Purine nucleoside phosphorylase (EC:2.4.2.1)
Short name:
PNP
Alternative name(s):
Inosine phosphorylase
Inosine-guanosine phosphorylase
Gene namesi
Name:PNP
Synonyms:NP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:7892. PNP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • intracellular Source: UniProtKB
  • nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Purine nucleoside phosphorylase deficiency (PNPD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder that interrupts both the catabolism of inosine into hypoxanthine and guanosine into guanine, and leads to the accumulation of guanosine, inosine, and their deoxified by-products. The main clinical presentation is recurrent infections due to severe T-cell immunodeficiency. Some patients also have neurologic impairment.
See also OMIM:613179
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00224489E → K in PNPD. 1 PublicationCorresponds to variant rs104894453dbSNPEnsembl.1
Natural variantiVAR_002245128D → G in PNPD. 1 PublicationCorresponds to variant rs104894450dbSNPEnsembl.1
Natural variantiVAR_002246174A → P in PNPD. Corresponds to variant rs104894454dbSNPEnsembl.1
Natural variantiVAR_010653192Y → C in PNPD. 1 PublicationCorresponds to variant rs104894452dbSNPEnsembl.1
Natural variantiVAR_002247234R → P in PNPD. 1 PublicationCorresponds to variant rs104894451dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4860.
MalaCardsiPNP.
MIMi613179. phenotype.
OpenTargetsiENSG00000198805.
Orphaneti760. Purine nucleoside phosphorylase deficiency.
PharmGKBiPA31694.

Chemistry databases

ChEMBLiCHEMBL4338.
DrugBankiDB00242. Cladribine.
DB00900. Didanosine.
GuidetoPHARMACOLOGYi2841.

Polymorphism and mutation databases

BioMutaiPNP.
DMDMi108935929.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001845361 – 289Purine nucleoside phosphorylaseAdd BLAST289

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei251PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP00491.
PaxDbiP00491.
PeptideAtlasiP00491.
PRIDEiP00491.
TopDownProteomicsiP00491.

2D gel databases

OGPiP00491.

PTM databases

iPTMnetiP00491.
PhosphoSitePlusiP00491.
SwissPalmiP00491.

Expressioni

Tissue specificityi

Expressed in red blood cells; overexpressed in red blood cells (cytoplasm) of patients with hereditary non-spherocytic hemolytic anemia of unknown etiology.1 Publication

Gene expression databases

BgeeiENSG00000198805.
CleanExiHS_NP.
ExpressionAtlasiP00491. baseline and differential.
GenevisibleiP00491. HS.

Organism-specific databases

HPAiHPA001625.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

BioGridi110921. 38 interactors.
DIPiDIP-50406N.
IntActiP00491. 13 interactors.
MINTiMINT-1375849.
STRINGi9606.ENSP00000354532.

Chemistry databases

BindingDBiP00491.

Structurei

Secondary structure

1289
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 20Combined sources14
Beta strandi26 – 31Combined sources6
Helixi36 – 41Combined sources6
Beta strandi43 – 49Combined sources7
Helixi50 – 52Combined sources3
Beta strandi53 – 55Combined sources3
Helixi62 – 65Combined sources4
Beta strandi67 – 73Combined sources7
Beta strandi76 – 83Combined sources8
Helixi87 – 89Combined sources3
Helixi93 – 96Combined sources4
Helixi98 – 106Combined sources9
Beta strandi110 – 119Combined sources10
Beta strandi121 – 123Combined sources3
Beta strandi129 – 137Combined sources9
Helixi138 – 141Combined sources4
Turni153 – 155Combined sources3
Turni163 – 166Combined sources4
Helixi168 – 179Combined sources12
Turni180 – 182Combined sources3
Beta strandi188 – 194Combined sources7
Beta strandi197 – 199Combined sources3
Helixi203 – 211Combined sources9
Beta strandi215 – 221Combined sources7
Helixi222 – 230Combined sources9
Beta strandi234 – 244Combined sources11
Beta strandi248 – 250Combined sources3
Helixi257 – 266Combined sources10
Helixi268 – 280Combined sources13
Turni285 – 287Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M73X-ray2.30E2-289[»]
1PF7X-ray2.60E1-289[»]
1PWYX-ray2.80E2-289[»]
1RCTX-ray2.80E2-289[»]
1RFGX-ray2.90E2-289[»]
1RR6X-ray2.50A1-289[»]
1RSZX-ray2.20A1-289[»]
1RT9X-ray2.30A1-289[»]
1ULAX-ray2.75A1-289[»]
1ULBX-ray2.75A1-289[»]
1V2HX-ray2.70E2-289[»]
1V3QX-ray2.80E2-289[»]
1V41X-ray2.85E2-289[»]
1V45X-ray2.86E2-289[»]
1YRYX-ray2.80E1-289[»]
2A0WX-ray2.28A1-289[»]
2A0XX-ray2.28A1-289[»]
2A0YX-ray2.28A1-289[»]
2OC4X-ray2.59A1-289[»]
2OC9X-ray2.59A1-289[»]
2ON6X-ray2.50A1-289[»]
2Q7OX-ray2.90E1-289[»]
3BGSX-ray2.10A1-289[»]
3D1VX-ray2.70A1-289[»]
3GB9X-ray2.30A/B/C1-289[»]
3GGSX-ray2.52A/B/C1-289[»]
3INYX-ray2.75A1-289[»]
3K8OX-ray2.40E/Q/S/T/U/Y1-289[»]
3K8QX-ray2.50A1-289[»]
3PHBX-ray2.30E/Q/S/T/U/Y1-289[»]
4EARX-ray1.70A/B/C1-289[»]
4EB8X-ray2.30A/B/C1-289[»]
4ECEX-ray2.60A/B/C/D/E/F1-289[»]
4GKAX-ray2.20A/B/C/D/E/F1-289[»]
5ETJX-ray2.30A/B/C/D/E/F1-289[»]
ProteinModelPortaliP00491.
SMRiP00491.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00491.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni84 – 86Phosphate bindingBy similarity3

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family.Curated

Phylogenomic databases

eggNOGiKOG3984. Eukaryota.
COG0005. LUCA.
GeneTreeiENSGT00550000074740.
HOVERGENiHBG002460.
InParanoidiP00491.
KOiK03783.
OMAiMENGYTY.
OrthoDBiEOG091G0GEE.
PhylomeDBiP00491.
TreeFamiTF300049.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000477. PurNPase. 1 hit.
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01700. PNPH. 1 hit.
TIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00491-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENGYTYEDY KNTAEWLLSH TKHRPQVAII CGSGLGGLTD KLTQAQIFDY
60 70 80 90 100
GEIPNFPRST VPGHAGRLVF GFLNGRACVM MQGRFHMYEG YPLWKVTFPV
110 120 130 140 150
RVFHLLGVDT LVVTNAAGGL NPKFEVGDIM LIRDHINLPG FSGQNPLRGP
160 170 180 190 200
NDERFGDRFP AMSDAYDRTM RQRALSTWKQ MGEQRELQEG TYVMVAGPSF
210 220 230 240 250
ETVAECRVLQ KLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVIMDYE
260 270 280
SLEKANHEEV LAAGKQAAQK LEQFVSILMA SIPLPDKAS
Length:289
Mass (Da):32,118
Last modified:May 30, 2006 - v2
Checksum:i91622FB1D26479D3
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00224351G → S.5 PublicationsCorresponds to variant rs1049564dbSNPEnsembl.1
Natural variantiVAR_00224489E → K in PNPD. 1 PublicationCorresponds to variant rs104894453dbSNPEnsembl.1
Natural variantiVAR_002245128D → G in PNPD. 1 PublicationCorresponds to variant rs104894450dbSNPEnsembl.1
Natural variantiVAR_002246174A → P in PNPD. Corresponds to variant rs104894454dbSNPEnsembl.1
Natural variantiVAR_010653192Y → C in PNPD. 1 PublicationCorresponds to variant rs104894452dbSNPEnsembl.1
Natural variantiVAR_002247234R → P in PNPD. 1 PublicationCorresponds to variant rs104894451dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00737 mRNA. Translation: CAA25320.1.
M13953
, J02672, M13951, M13952 Genomic DNA. Translation: AAA36460.1.
AY817667 Genomic DNA. Translation: AAV68044.1.
AK313490 mRNA. Translation: BAG36272.1.
CR407607 mRNA. Translation: CAG28535.1.
CH471078 Genomic DNA. Translation: EAW66458.1.
CH471078 Genomic DNA. Translation: EAW66459.1.
BC104206 mRNA. Translation: AAI04207.1.
BC104207 mRNA. Translation: AAI04208.1.
BC106074 mRNA. Translation: AAI06075.1.
CCDSiCCDS9552.1.
PIRiA00578. PHHUPN.
RefSeqiNP_000261.2. NM_000270.3.
UniGeneiHs.75514.

Genome annotation databases

EnsembliENST00000361505; ENSP00000354532; ENSG00000198805.
GeneIDi4860.
KEGGihsa:4860.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NPbase

NP mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00737 mRNA. Translation: CAA25320.1.
M13953
, J02672, M13951, M13952 Genomic DNA. Translation: AAA36460.1.
AY817667 Genomic DNA. Translation: AAV68044.1.
AK313490 mRNA. Translation: BAG36272.1.
CR407607 mRNA. Translation: CAG28535.1.
CH471078 Genomic DNA. Translation: EAW66458.1.
CH471078 Genomic DNA. Translation: EAW66459.1.
BC104206 mRNA. Translation: AAI04207.1.
BC104207 mRNA. Translation: AAI04208.1.
BC106074 mRNA. Translation: AAI06075.1.
CCDSiCCDS9552.1.
PIRiA00578. PHHUPN.
RefSeqiNP_000261.2. NM_000270.3.
UniGeneiHs.75514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M73X-ray2.30E2-289[»]
1PF7X-ray2.60E1-289[»]
1PWYX-ray2.80E2-289[»]
1RCTX-ray2.80E2-289[»]
1RFGX-ray2.90E2-289[»]
1RR6X-ray2.50A1-289[»]
1RSZX-ray2.20A1-289[»]
1RT9X-ray2.30A1-289[»]
1ULAX-ray2.75A1-289[»]
1ULBX-ray2.75A1-289[»]
1V2HX-ray2.70E2-289[»]
1V3QX-ray2.80E2-289[»]
1V41X-ray2.85E2-289[»]
1V45X-ray2.86E2-289[»]
1YRYX-ray2.80E1-289[»]
2A0WX-ray2.28A1-289[»]
2A0XX-ray2.28A1-289[»]
2A0YX-ray2.28A1-289[»]
2OC4X-ray2.59A1-289[»]
2OC9X-ray2.59A1-289[»]
2ON6X-ray2.50A1-289[»]
2Q7OX-ray2.90E1-289[»]
3BGSX-ray2.10A1-289[»]
3D1VX-ray2.70A1-289[»]
3GB9X-ray2.30A/B/C1-289[»]
3GGSX-ray2.52A/B/C1-289[»]
3INYX-ray2.75A1-289[»]
3K8OX-ray2.40E/Q/S/T/U/Y1-289[»]
3K8QX-ray2.50A1-289[»]
3PHBX-ray2.30E/Q/S/T/U/Y1-289[»]
4EARX-ray1.70A/B/C1-289[»]
4EB8X-ray2.30A/B/C1-289[»]
4ECEX-ray2.60A/B/C/D/E/F1-289[»]
4GKAX-ray2.20A/B/C/D/E/F1-289[»]
5ETJX-ray2.30A/B/C/D/E/F1-289[»]
ProteinModelPortaliP00491.
SMRiP00491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110921. 38 interactors.
DIPiDIP-50406N.
IntActiP00491. 13 interactors.
MINTiMINT-1375849.
STRINGi9606.ENSP00000354532.

Chemistry databases

BindingDBiP00491.
ChEMBLiCHEMBL4338.
DrugBankiDB00242. Cladribine.
DB00900. Didanosine.
GuidetoPHARMACOLOGYi2841.

PTM databases

iPTMnetiP00491.
PhosphoSitePlusiP00491.
SwissPalmiP00491.

Polymorphism and mutation databases

BioMutaiPNP.
DMDMi108935929.

2D gel databases

OGPiP00491.

Proteomic databases

EPDiP00491.
PaxDbiP00491.
PeptideAtlasiP00491.
PRIDEiP00491.
TopDownProteomicsiP00491.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361505; ENSP00000354532; ENSG00000198805.
GeneIDi4860.
KEGGihsa:4860.

Organism-specific databases

CTDi4860.
DisGeNETi4860.
GeneCardsiPNP.
HGNCiHGNC:7892. PNP.
HPAiHPA001625.
MalaCardsiPNP.
MIMi164050. gene.
613179. phenotype.
neXtProtiNX_P00491.
OpenTargetsiENSG00000198805.
Orphaneti760. Purine nucleoside phosphorylase deficiency.
PharmGKBiPA31694.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3984. Eukaryota.
COG0005. LUCA.
GeneTreeiENSGT00550000074740.
HOVERGENiHBG002460.
InParanoidiP00491.
KOiK03783.
OMAiMENGYTY.
OrthoDBiEOG091G0GEE.
PhylomeDBiP00491.
TreeFamiTF300049.

Enzyme and pathway databases

UniPathwayiUPA00606.
BioCyciMetaCyc:HS02151-MONOMER.
ZFISH:HS02151-MONOMER.
BRENDAi2.4.2.1. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-74217. Purine salvage.
R-HSA-74259. Purine catabolism.
SABIO-RKP00491.
SignaLinkiP00491.

Miscellaneous databases

ChiTaRSiPNP. human.
EvolutionaryTraceiP00491.
GeneWikiiPurine_nucleoside_phosphorylase.
GenomeRNAii4860.
PROiP00491.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198805.
CleanExiHS_NP.
ExpressionAtlasiP00491. baseline and differential.
GenevisibleiP00491. HS.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000477. PurNPase. 1 hit.
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01700. PNPH. 1 hit.
TIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPNPH_HUMAN
AccessioniPrimary (citable) accession number: P00491
Secondary accession number(s): B2R8S5
, D3DS00, Q15160, Q5PZ03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 30, 2006
Last modified: November 30, 2016
This is version 187 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.