NamePurine nucleoside phosphorylase
Synonyms
  • 2.4.2.1
  • Inosine phosphorylase
  • Inosine-guanosine phosphorylase
  • NP
  • PNP
Gene NamePNP
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010033|Purine nucleoside phosphorylase
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Number of residues289
Molecular Weight32117.69
Theoretical pI6.95
GO Classification
Functions
  • drug binding
  • phosphate ion binding
  • purine-nucleoside phosphorylase activity
  • nucleoside binding
  • purine nucleobase binding
Processes
  • nucleobase-containing compound metabolic process
  • inosine catabolic process
  • interleukin-2 secretion
  • NAD biosynthesis via nicotinamide riboside salvage pathway
  • nicotinamide riboside catabolic process
  • response to drug
  • positive regulation of alpha-beta T cell differentiation
  • immune response
  • positive regulation of T cell proliferation
  • purine nucleotide catabolic process
  • urate biosynthetic process
  • small molecule metabolic process
  • nucleobase-containing small molecule metabolic process
  • purine nucleobase metabolic process
  • purine-containing compound salvage
Components
  • intracellular
  • cytoplasm
  • cytoskeleton
  • nucleus
  • cytosol
  • extracellular exosome
General FunctionPurine-nucleoside phosphorylase activity
Specific FunctionThe 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.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID35565
UniProtKB IDP00491
UniProtKB Entry NamePNPH_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0010034|Purine nucleoside phosphorylase (PNP)
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAC
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACGGTGAAATCCCCAACTTTCCCCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
GenBank Gene IDX00737
GeneCard IDNot Available
GenAtlas IDNP
HGNC IDHGNC:7892
Chromosome Location14
Locus14q13.1
References
  1. Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. 6087295
  2. Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. 3029074
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