Purine nucleoside phosphorylase
Details
- Name
- Purine nucleoside phosphorylase
- Synonyms
- 2.4.2.1
- Inosine phosphorylase
- Inosine-guanosine phosphorylase
- NP
- PNP
- Gene Name
- PNP
- UniProtKB Entry
- P00491Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0010033|Purine nucleoside phosphorylase MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
- Number of residues
- 289
- Molecular Weight
- 32117.69
- Theoretical pI
- 6.95
- GO Classification
- Functionsguanosine phosphorylase activity / identical protein bindingProcessesallantoin metabolic process / dAMP catabolic process / deoxyadenosine catabolic process / deoxyinosine catabolic process / IMP catabolic process / nucleotide biosynthetic process / positive regulation of interleukin-2 production / purine ribonucleoside salvage / response to xenobiotic stimulusComponentsextracellular region / ficolin-1-rich granule lumen / secretory granule lumen
- General Function
- Catalyzes 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 (PubMed:23438750, PubMed:9305964). Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine (PubMed:9305964)
- Specific Function
- guanosine phosphorylase activity
- Pfam Domain Function
- PNP_UDP_1 (PF01048)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0010034|Purine nucleoside phosphorylase (PNP) ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAC ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT AAATTAACTCAGGCCCAGATCTTTGACTACGGTGAAATCCCCAACTTTCCCCGAAGTACA GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC AGCATTCCACTCCCTGACAAAGCCAGTTGA
- Chromosome Location
- 14
- Locus
- 14q11.2
- External Identifiers
Resource Link UniProtKB ID P00491 UniProtKB Entry Name PNPH_HUMAN GenBank Protein ID 35565 GenBank Gene ID X00737 GeneCard ID PNP GenAtlas ID NP HGNC ID HGNC:7892 PDB ID(s) 1M73, 1PF7, 1PWY, 1RCT, 1RFG, 1RR6, 1RSZ, 1RT9, 1ULA, 1ULB, 1V2H, 1V3Q, 1V41, 1V45, 1YRY, 2A0W, 2A0X, 2A0Y, 2OC4, 2OC9, 2ON6, 2Q7O, 3BGS, 3D1V, 3GB9, 3GGS, 3INY, 3K8O, 3K8Q, 3PHB, 4EAR, 4EB8, 4ECE, 4GKA, 5ETJ, 5UGF, 7ZSL, 7ZSM, 7ZSN, 7ZSO, 7ZSP KEGG ID hsa:4860 IUPHAR/Guide To Pharmacology ID 2841 NCBI Gene ID 4860 - General References
- 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. [Article]
- 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. [Article]
- Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [Article]
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- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
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- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
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- Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [Article]
- Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [Article]
- Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type Purine nucleoside phosphorylase (Humans) protein primary- Drug Relations