UniProt Accession

 PNPH_HUMAN; P00491; B2R8S5; D3DS00; Q15160; Q5PZ03 

Genbank Protein ID

 X00737; M13953; J02672; M13951; M13952; AY817667; AK313490; CR407607; CH471078; CH471078; BC104206; BC104207; BC106074 

Genbank Nucleotide ID

 CAA25320.1; AAA36460.1; AAA36460.1; AAA36460.1; AAA36460.1; AAV68044.1; BAG36272.1; CAG28535.1; EAW66458.1; EAW66459.1; AAI04207.1; AAI04208.1; AAI06075.1 

Protein Name

 Purine nucleoside phosphorylase 

Protein Synonyms/Alias

 PNP; Inosine phosphorylase; Inosine-guanosine phosphorylase 

Gene Name

 PNP 

Gene Synonyms/Alias

 NP 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
22	EWLLSHTKHRPQVAI	ubiquitination	[1, 2]
95	YEGYPLWKVTFPVRV	acetylation	[3]
95	YEGYPLWKVTFPVRV	ubiquitination	[2, 4, 5]
179	QRALSTWKQMGEQRE	ubiquitination	[1, 4, 6, 7, 8, 9]
211	AECRVLQKLGADAVG	acetylation	[9]
211	AECRVLQKLGADAVG	ubiquitination	[4, 5, 8, 10]
254	MDYESLEKANHEEVL	acetylation	[9, 11]
254	MDYESLEKANHEEVL	ubiquitination	[4]
265	EEVLAAGKQAAQKLE	ubiquitination	[4, 5, 6, 9, 10]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [10] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [11] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 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. 

Sequence Annotation

 MOD_RES 1 1 N-acetylmethionine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Glycosyltransferase; Polymorphism; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 289 AA 

Protein Sequence

Gene Ontology

 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0008144; F:drug binding; IDA:UniProtKB.
 GO:0001882; F:nucleoside binding; IDA:UniProtKB.
 GO:0042301; F:phosphate ion binding; IDA:UniProtKB.
 GO:0002060; F:purine nucleobase binding; IDA:UniProtKB.
 GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:UniProtKB.
 GO:0006955; P:immune response; IMP:UniProtKB.
 GO:0006148; P:inosine catabolic process; IDA:MGI.
 GO:0070970; P:interleukin-2 secretion; IMP:UniProtKB.
 GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; IGI:UniProtKB.
 GO:0006738; P:nicotinamide riboside catabolic process; IDA:UniProtKB.
 GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IDA:MGI.
 GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
 GO:0043101; P:purine-containing compound salvage; TAS:Reactome.
 GO:0042493; P:response to drug; IDA:UniProtKB.
 GO:0034418; P:urate biosynthetic process; IDA:MGI. 

Interpro

 IPR000845; Nucleoside_phosphorylase_d.
 IPR001369; PNP/MTAP.
 IPR011270; Pur_Nuc_Pase_Ino/Guo-sp.
 IPR011268; Purine_phosphorylase.
 IPR018099; Purine_phosphorylase-2_CS. 

Pfam

 PF01048; PNP_UDP_1 

SMART

  

PROSITE

 PS01240; PNP_MTAP_2 

PRINTS