Home

NP (human)

Overview NP a metabolic enzyme with purine-nucleoside phosphorylase activity. Defects are the cause of nucleoside phosphorylase deficiency (NP deficiency), with severe T-cell immunodeficiency with neurologic disorder in children. Note: This description may include information from UniProtKB. Protein type: Cofactor and Vitamin Metabolism - nicotinate and nicotinamide; EC 2.4.2.1; Nucleotide Metabolism - pyrimidine; Nucleotide Metabolism - purine; Transferase Cellular Component: cytoskeleton; cytoplasm; intracellular; cytosol Molecular Function: purine binding; nucleoside binding; drug binding; phosphate binding; purine-nucleoside phosphorylase activity Biological Process: response to drug; inosine catabolic process; nucleobase, nucleoside and nucleotide metabolic process; nicotinamide riboside catabolic process; nucleobase, nucleoside, nucleotide and nucleic acid metabolic process; purine nucleotide catabolic process; immune response; positive regulation of T cell proliferation; positive regulation of alpha-beta T cell differentiation; purine base metabolic process; purine salvage Reference #:  P00491 (UniProtKB) Alt. Names/Synonyms: FLJ94043; FLJ97288; FLJ97312; Inosine phosphorylase; MGC117396; MGC125915; MGC125916; NP; nucleoside phosphorylase; PNP; PNPH; PRO1837; PUNP; Purine nucleoside phosphorylase; purine-nucleoside:orthophosphate ribosyltransferase Gene Symbols: PNP Molecular weight: 32,118 Da Basal Isoelectric point: 6.45  Predict pI for various phosphorylation states

Select Structure to View Below NP 1M73 - E=2-289 (human) 1PF7 - E=1-289 (human) 1PWY - E=2-289 (human) 1RCT - E=2-289 (human) 1RFG - E=2-289 (human) 1RR6 - A=1-289 (human) 1RSZ - A=1-289 (human) 1RT9 - A=1-289 (human) 1ULA - A=1-289 (human) 1ULB - A=1-289 (human) 1V2H - E=2-289 (human) 1V3Q - E=2-289 (human) 1V41 - E=2-289 (human) 1V45 - E=2-289 (human) 1YRY - E=1-289 (human) 2A0W - A=1-289 (human) 2A0X - A=1-289 (human) 2A0Y - A=1-289 (human) 2OC4 - A=1-289 (human) 2OC9 - A=1-289 (human) 2ON6 - A=1-289 (human) 2Q7O - E=1-289 (human) 3BGS - A=1-289 (human) 3D1V - A=1-289 (human) 3GB9 - A/C/B=1-289 (human) 3GGS - A/C/B=1-289 (human) 3INY - A=1-289 (human) 3K8O - S/Q/T/Y/E/U=1-289 (human) 3K8Q - A=1-289 (human) 3PHB - S/Q/T/Y/E/U=1-289 (human) 4EAR - A/C/B=1-289 (human) 4EB8 - A/C/B=1-289 (human) 4ECE - F/A/D/C/E/B=1-289 (human) 4GKA - F/A/D/C/E/B=1-289 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 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  |  ENZYME  |  Phospho3D  |  DISEASE  |  InnateDB  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		K22-u	EWLLSHTkHRPQVAI
0	1		K95-a	YEGYPLWkVTFPVRV
0	66		K95-u	YEGYPLWkVTFPVRV
0	3		T169-p	MSDAYDRtMRQRALs
0	2		S176-p	tMRQRALstWkQMGE
0	2		T177-p	MRQRALstWkQMGEQ
0	1		K179-u	QRALstWkQMGEQRE
0	2		K211-u	AECRVLQkLGADAVG
0	1		K244	GFSLITNKVIMDyES
0	17		Y249-p	TNKVIMDyESLEKAN
0	1		K254	MDyESLEKANHEEVL
0	2		K265-u	EEVLAAGkQAAQKLE
0	1		S289	IPLPDKAS_______

	mouse
E22	KWLLQHTEYRPQVAV
K95	YEGYSLSKVTFPVRV
K95-u	YEGYSLSkVTFPVRV
D169	MSDAYDRDMRQKAFT
T176	DMRQKAFTAWKQMGE
A177	MRQKAFTAWKQMGEQ
K179	QKAFTAWKQMGEQRK
K210-u	VAESRLLkMLGADAV
K244-a	GFSLITNkVVMDYEN
Y249	TNkVVMDYENLEkAN
K254-u	MDYENLEkANHMEVL
K265-u	MEVLDAGkAAAQTLE
S289-p	IPLPDRGs_______

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.