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Protein Page:
PRPS1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PRPS1 Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. Defects in PRPS1 are the cause of phosphoribosylpyrophosphate synthetase superactivity (PRPS1 superactivity); also known as PRPS-related gout. It is a familial disorder characterized by excessive purine production, gout and uric acid urolithiasis. Defects in PRPS1 are the cause of Charcot-Marie-Tooth disease X-linked recessive type 5 (CMTX5); also known as optic atrophy-polyneuropathy-deafness or Rosenberg-Chutorian syndrome. CMTX5 is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies characterized by severely reduced motor nerve conduction velocities (NCVs) (less than 38m/s) and segmental demyelination and remyelination, and primary peripheral axonal neuropathies characterized by normal or mildly reduced NCVs and chronic axonal degeneration and regeneration on nerve biopsy. Defects in PRPS1 are the cause of ARTS syndrome (ARTS); also known as fatal ataxia X-linked with deafness and loss of vision. ARTS is a disorder characterized by mental retardation, early-onset hypotonia, ataxia, delayed motor development, hearing impairment, and optic atrophy. Susceptibility to infections, especially of the upper respiratory tract, can result in early death. Defects in PRPS1 are the cause of deafness X-linked type 1 (DFNX1); also known as congenital sensorineural deafness X-linked 2 (DFN2). It is a form of deafness characterized by progressive, severe-to-profound sensorineural hearing loss in males. Females manifest mild to moderate hearing loss. Belongs to the ribose-phosphate pyrophosphokinase family. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.6.1; Nucleotide Metabolism - purine; Carbohydrate Metabolism - pentose phosphate pathway; Kinase, other
Chromosomal Location of Human Ortholog: Xq22.3
Cellular Component: cytosol
Molecular Function: ribose phosphate diphosphokinase activity; protein homodimerization activity; GDP binding; magnesium ion binding; kinase activity; ADP binding; carbohydrate binding; ATP binding; AMP binding
Biological Process: cell death; AMP biosynthetic process; nervous system development; organ regeneration; hypoxanthine biosynthetic process; carbohydrate metabolic process; 5-phosphoribose 1-diphosphate biosynthetic process; purine nucleotide biosynthetic process; phosphorylation; purine base metabolic process; pyrimidine nucleotide biosynthetic process
Reference #:  P60891 (UniProtKB)
Alt. Names/Synonyms: ARTS; CMTX5; DFN2; DFNX1; dJ1070B1.2 (phosphoribosyl pyrophosphate synthetase 1); KIAA0967; Phosphoribosyl pyrophosphate synthase I; phosphoribosyl pyrophosphate synthetase 1; PPRibP; PRPS1; PRS-I; PRSI; Ribose-phosphate pyrophosphokinase 1
Gene Symbols: PRPS1
Molecular weight: 34,834 Da
Basal Isoelectric point: 6.51  Predict pI for various phosphorylation states
Select Structure to View Below

PRPS1

Protein Structure Not Found.


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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
 

Show Multiple Sequence Alignment


 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 3 K18-ub SHQDLSQkIADRLGL
0 4 K29-ub RLGLELGkVVTKKFs
0 2 S36-p kVVTKKFsNQETCVE
0 1 S47 TCVEIGESVRGEDVY
0 1 K99 FPYARQDKKDKSRAP
0 9 Y146-p DIPVDNLyAEPAVLK
0 6 K176-ac SPDAGGAkRVTSIAD
0 2 K176-ub SPDAGGAkRVTSIAD
0 2 K194-ac VDFALIHkERKKANE
0 3 K194-ub VDFALIHkERKKANE
0 1 K212-ac MVLVGDVkDRVAILV
0 29 K212-ub MVLVGDVkDRVAILV
0 1 T228-p DMADTCGtICHAADK
0 18 Y245-p SAGATRVyAILTHGI
0 1 K280-ub NTIPQEDkMKHCSKI
0 7 S310-p THNGESVsyLFSHVP
0 13 Y311-p HNGESVsyLFSHVPL
  mouse

 
K18-ub SHQDLSQkIADRLGL
K29-ub RLGLELGkVVTKKFS
S36 kVVTKKFSNQETCVE
S47 TCVEIGESVRGEDVY
K99-ac FPYARQDkKDKSRAP
Y146 DIPVDNLYAEPAVLK
K176-ac SPDAGGAkRVTSIAD
K176-ub SPDAGGAkRVTSIAD
K194 VDFALIHKERKKANE
K194 VDFALIHKERKKANE
K212 MVLVGDVKDRVAILV
K212-ub MVLVGDVkDRVAILV
T228 DMADTCGTICHAADK
Y245 SAGATRVYAILTHGI
K280 NTIPQEDKMKHCSKI
S310-p THNGESVsyLFSHVP
Y311-p HNGESVsyLFSHVPL
  rat

 
K18 SHQDLSQKIADRLGL
K29 RLGLELGKVVTKKFs
S36-p KVVTKKFsNQETCVE
S47-p TCVEIGEsVRGEDVY
K99 FPYARQDKKDKSRAP
Y146 DIPVDNLYAEPAVLK
K176 SPDAGGAKRVTSIAD
K176 SPDAGGAKRVTSIAD
K194-ac VDFALIHkERKKANE
K194 VDFALIHKERKKANE
K212 MVLVGDVKDRVAILV
K212 MVLVGDVKDRVAILV
T228 DMADTCGTICHAADK
Y245 SAGATRVYAILTHGI
K280 NTIPQEDKMKHCSKI
S310 THNGESVSYLFSHVP
Y311 HNGESVSYLFSHVPL
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