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Protein

Ribose-phosphate pyrophosphokinase 1

Gene

PRPS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.

Catalytic activityi

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.

Cofactori

Enzyme regulationi

Activated by magnesium and inorganic phosphate.

Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase 3 (PRPS1L1), Ribose-phosphate pyrophosphokinase 1 (PRPS1), Ribose-phosphate pyrophosphokinase 2 (PRPS2)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi128MagnesiumSequence analysis1
Metal bindingi130MagnesiumSequence analysis1
Binding sitei130ATP1
Metal bindingi139MagnesiumSequence analysis1
Metal bindingi143MagnesiumSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi96 – 101ATP6

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • kinase activity Source: UniProtKB-KW
  • magnesium ion binding Source: InterPro
  • protein homodimerization activity Source: UniProtKB
  • ribose phosphate diphosphokinase activity Source: UniProtKB

GO - Biological processi

  • 5-phosphoribose 1-diphosphate biosynthetic process Source: Reactome
  • hypoxanthine biosynthetic process Source: UniProtKB
  • nervous system development Source: UniProtKB
  • nucleoside metabolic process Source: InterPro
  • purine nucleobase metabolic process Source: UniProtKB
  • purine nucleotide biosynthetic process Source: UniProtKB
  • pyrimidine nucleotide biosynthetic process Source: UniProtKB
  • ribonucleoside monophosphate biosynthetic process Source: InterPro
  • urate biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07410-MONOMER.
ZFISH:HS07410-MONOMER.
BRENDAi2.7.6.1. 2681.
ReactomeiR-HSA-73843. 5-Phosphoribose 1-diphosphate biosynthesis.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase 1 (EC:2.7.6.1)
Alternative name(s):
PPRibP
Phosphoribosyl pyrophosphate synthase I
Short name:
PRS-I
Gene namesi
Name:PRPS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:9462. PRPS1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Phosphoribosyl pyrophosphate synthetase I deficiency is a rare condition caused by mutations in PRPS1 that lead to variable disease phenotypes including optic atrophy, retinitis pigmentosa, ataxia, peripheral neuropathy and hearing loss.

Phosphoribosylpyrophosphate synthetase superactivity (PRPS1 superactivity)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionFamilial disorder characterized by excessive purine production, gout and uric acid urolithiasis.
See also OMIM:300661
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01604452D → H in PRPS1 superactivity. 1 PublicationCorresponds to variant rs137852542dbSNPEnsembl.1
Natural variantiVAR_004163114N → S in PRPS1 superactivity. 2 PublicationsCorresponds to variant rs137852540dbSNPEnsembl.1
Natural variantiVAR_016045129L → I in PRPS1 superactivity. 1 PublicationCorresponds to variant rs137852543dbSNPEnsembl.1
Natural variantiVAR_004164183D → H in PRPS1 superactivity. 2 PublicationsCorresponds to variant rs137852541dbSNPEnsembl.1
Natural variantiVAR_016046190A → V in PRPS1 superactivity. 1 PublicationCorresponds to variant rs137852544dbSNPEnsembl.1
Natural variantiVAR_016047193H → Q in PRPS1 superactivity. 1 PublicationCorresponds to variant rs137852545dbSNPEnsembl.1
Charcot-Marie-Tooth disease, X-linked recessive, 5 (CMTX5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. 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.
See also OMIM:311070
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03694143E → D in CMTX5. 1 PublicationCorresponds to variant rs80338731dbSNPEnsembl.1
Natural variantiVAR_036942115M → T in CMTX5. 1 PublicationCorresponds to variant rs80338732dbSNPEnsembl.1
ARTS syndrome (ARTS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:301835
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036943133Q → P in ARTS. 1 PublicationCorresponds to variant rs80338675dbSNPEnsembl.1
Natural variantiVAR_036944152L → P in ARTS. 1 PublicationCorresponds to variant rs80338676dbSNPEnsembl.1
Deafness, X-linked, 1 (DFNX1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of deafness characterized by progressive, severe-to-profound sensorineural hearing loss in males. Females manifest mild to moderate hearing loss.
See also OMIM:304500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06352265D → N in DFNX1. 1 PublicationCorresponds to variant rs180177151dbSNPEnsembl.1
Natural variantiVAR_06352387A → T in DFNX1. 1 PublicationCorresponds to variant rs180177152dbSNPEnsembl.1
Natural variantiVAR_063524290I → T in DFNX1. 1 PublicationCorresponds to variant rs180177153dbSNPEnsembl.1
Natural variantiVAR_063525306G → R in DFNX1. 1 PublicationCorresponds to variant rs180177154dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi132S → A: Reduces catalytic activity. 1 Publication1
Mutagenesisi132S → F: No effect on catalytic activity. 1 Publication1
Mutagenesisi144N → H: No effect on catalytic activity. 1 Publication1
Mutagenesisi146Y → F: No effect on catalytic activity. 1 Publication1
Mutagenesisi146Y → M: Reduces catalytic activity. 1 Publication1

Keywords - Diseasei

Charcot-Marie-Tooth disease, Deafness, Disease mutation, Gout, Mental retardation, Neurodegeneration, Neuropathy, Non-syndromic deafness, Retinitis pigmentosa

Organism-specific databases

DisGeNETi5631.
MalaCardsiPRPS1.
MIMi300661. phenotype.
301835. phenotype.
304500. phenotype.
311070. phenotype.
OpenTargetsiENSG00000147224.
Orphaneti1187. Lethal ataxia with deafness and optic atrophy.
411536. Mild phosphoribosylpyrophosphate synthetase superactivity.
411543. Severe phosphoribosylpyrophosphate synthetase superactivity.
99014. X-linked Charcot-Marie-Tooth disease type 5.
90625. X-linked non-syndromic sensorineural deafness type DFN.
PharmGKBiPA33817.

Chemistry databases

ChEMBLiCHEMBL2638.

Polymorphism and mutation databases

BioMutaiPRPS1.
DMDMi46397477.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001410712 – 318Ribose-phosphate pyrophosphokinase 1Add BLAST317

Proteomic databases

EPDiP60891.
MaxQBiP60891.
PaxDbiP60891.
PeptideAtlasiP60891.
PRIDEiP60891.

2D gel databases

UCD-2DPAGEP60891.

PTM databases

iPTMnetiP60891.
PhosphoSitePlusiP60891.
SwissPalmiP60891.

Expressioni

Gene expression databases

BgeeiENSG00000147224.
CleanExiHS_PRPS1.
ExpressionAtlasiP60891. baseline and differential.
GenevisibleiP60891. HS.

Interactioni

Subunit structurei

Homodimer. The active form is probably a hexamer composed of 3 homodimers.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-749195,EBI-749195
GORASP2Q9H8Y83EBI-749195,EBI-739467
PRPS2P119086EBI-749195,EBI-4290895
PRPSAP1Q145588EBI-749195,EBI-724449
PRPSAP2O602565EBI-749195,EBI-724960
SPG21Q9NZD86EBI-749195,EBI-742688

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi111615. 49 interactors.
DIPiDIP-61999N.
IntActiP60891. 17 interactors.
STRINGi9606.ENSP00000361512.

Chemistry databases

BindingDBiP60891.

Structurei

Secondary structure

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Helixi14 – 22Combined sources9
Beta strandi30 – 34Combined sources5
Beta strandi36 – 38Combined sources3
Beta strandi40 – 44Combined sources5
Beta strandi52 – 56Combined sources5
Helixi63 – 79Combined sources17
Beta strandi83 – 91Combined sources9
Turni93 – 96Combined sources4
Beta strandi101 – 104Combined sources4
Helixi108 – 119Combined sources12
Beta strandi122 – 128Combined sources7
Helixi132 – 137Combined sources6
Beta strandi142 – 145Combined sources4
Helixi148 – 158Combined sources11
Helixi162 – 164Combined sources3
Beta strandi166 – 171Combined sources6
Helixi172 – 174Combined sources3
Helixi175 – 185Combined sources11
Beta strandi188 – 194Combined sources7
Beta strandi205 – 209Combined sources5
Beta strandi214 – 225Combined sources12
Helixi227 – 238Combined sources12
Beta strandi242 – 251Combined sources10
Turni254 – 256Combined sources3
Helixi257 – 263Combined sources7
Beta strandi267 – 272Combined sources6
Helixi278 – 282Combined sources5
Beta strandi287 – 290Combined sources4
Helixi293 – 305Combined sources13
Helixi310 – 313Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H06X-ray2.20A/B1-318[»]
2H07X-ray2.20A/B1-318[»]
2H08X-ray2.50A/B1-318[»]
2HCRX-ray2.20A/B1-318[»]
3EFHX-ray2.60A/B1-318[»]
3S5JX-ray2.02A/B1-318[»]
4F8EX-ray2.27A/B1-318[»]
4LYGX-ray3.00A/B1-318[»]
4LZNX-ray2.14A/B1-318[»]
4LZOX-ray3.31A/B1-318[»]
4M0PX-ray2.11A/B1-318[»]
4M0UX-ray2.74A/B1-318[»]
ProteinModelPortaliP60891.
SMRiP60891.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60891.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni212 – 227Binding of phosphoribosylpyrophosphateSequence analysisAdd BLAST16

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1448. Eukaryota.
COG0462. LUCA.
GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP60891.
KOiK00948.
OMAiDGEIMVE.
OrthoDBiEOG091G0ZG8.
PhylomeDBiP60891.
TreeFamiTF106366.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B. 1 hit.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P60891-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIGESVRG
60 70 80 90 100
EDVYIVQSGC GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK
110 120 130 140 150
DKSRAPISAK LVANMLSVAG ADHIITMDLH ASQIQGFFDI PVDNLYAEPA
160 170 180 190 200
VLKWIRENIS EWRNCTIVSP DAGGAKRVTS IADRLNVDFA LIHKERKKAN
210 220 230 240 250
EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG ATRVYAILTH
260 270 280 290 300
GIFSGPAISR INNACFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI
310
RRTHNGESVS YLFSHVPL
Length:318
Mass (Da):34,834
Last modified:January 23, 2007 - v2
Checksum:i46D017E969908BA0
GO
Isoform 2 (identifier: P60891-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: Missing.

Note: No experimental confirmation available.
Show »
Length:251
Mass (Da):27,526
Checksum:iA43F363C2E2ECF33
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82A → G in BAG35584 (PubMed:14702039).Curated1
Sequence conflicti122D → G in BAG35584 (PubMed:14702039).Curated1
Sequence conflicti278E → G in BAG35584 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07271916S → P Probable disease-associated mutation found in patients with phosphoribosyl pyrophosphate synthetase I deficiency. 1 Publication1
Natural variantiVAR_03694143E → D in CMTX5. 1 PublicationCorresponds to variant rs80338731dbSNPEnsembl.1
Natural variantiVAR_01604452D → H in PRPS1 superactivity. 1 PublicationCorresponds to variant rs137852542dbSNPEnsembl.1
Natural variantiVAR_06352265D → N in DFNX1. 1 PublicationCorresponds to variant rs180177151dbSNPEnsembl.1
Natural variantiVAR_06352387A → T in DFNX1. 1 PublicationCorresponds to variant rs180177152dbSNPEnsembl.1
Natural variantiVAR_004163114N → S in PRPS1 superactivity. 2 PublicationsCorresponds to variant rs137852540dbSNPEnsembl.1
Natural variantiVAR_036942115M → T in CMTX5. 1 PublicationCorresponds to variant rs80338732dbSNPEnsembl.1
Natural variantiVAR_016045129L → I in PRPS1 superactivity. 1 PublicationCorresponds to variant rs137852543dbSNPEnsembl.1
Natural variantiVAR_036943133Q → P in ARTS. 1 PublicationCorresponds to variant rs80338675dbSNPEnsembl.1
Natural variantiVAR_036944152L → P in ARTS. 1 PublicationCorresponds to variant rs80338676dbSNPEnsembl.1
Natural variantiVAR_004164183D → H in PRPS1 superactivity. 2 PublicationsCorresponds to variant rs137852541dbSNPEnsembl.1
Natural variantiVAR_016046190A → V in PRPS1 superactivity. 1 PublicationCorresponds to variant rs137852544dbSNPEnsembl.1
Natural variantiVAR_016047193H → Q in PRPS1 superactivity. 1 PublicationCorresponds to variant rs137852545dbSNPEnsembl.1
Natural variantiVAR_036593203D → H in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_036594219V → G in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_036595231H → D in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_063524290I → T in DFNX1. 1 PublicationCorresponds to variant rs180177153dbSNPEnsembl.1
Natural variantiVAR_063525306G → R in DFNX1. 1 PublicationCorresponds to variant rs180177154dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0560281 – 67Missing in isoform 2. 1 PublicationAdd BLAST67

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15331 mRNA. Translation: CAA33386.1.
D00860 mRNA. Translation: BAA00733.1.
AK297968 mRNA. Translation: BAG60278.1.
AK312706 mRNA. Translation: BAG35584.1.
AL137787, AL772400 Genomic DNA. Translation: CAI42173.1.
AL772400, AL137787 Genomic DNA. Translation: CAI41098.1.
CH471120 Genomic DNA. Translation: EAX02709.1.
CH471120 Genomic DNA. Translation: EAX02710.1.
CH471120 Genomic DNA. Translation: EAX02711.1.
BC001605 mRNA. Translation: AAH01605.1.
CCDSiCCDS14529.1. [P60891-1]
PIRiJX0159. KIHUR1.
RefSeqiNP_001191331.1. NM_001204402.1.
NP_002755.1. NM_002764.3. [P60891-1]
UniGeneiHs.56.

Genome annotation databases

EnsembliENST00000372435; ENSP00000361512; ENSG00000147224. [P60891-1]
GeneIDi5631.
KEGGihsa:5631.
UCSCiuc004ene.5. human. [P60891-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15331 mRNA. Translation: CAA33386.1.
D00860 mRNA. Translation: BAA00733.1.
AK297968 mRNA. Translation: BAG60278.1.
AK312706 mRNA. Translation: BAG35584.1.
AL137787, AL772400 Genomic DNA. Translation: CAI42173.1.
AL772400, AL137787 Genomic DNA. Translation: CAI41098.1.
CH471120 Genomic DNA. Translation: EAX02709.1.
CH471120 Genomic DNA. Translation: EAX02710.1.
CH471120 Genomic DNA. Translation: EAX02711.1.
BC001605 mRNA. Translation: AAH01605.1.
CCDSiCCDS14529.1. [P60891-1]
PIRiJX0159. KIHUR1.
RefSeqiNP_001191331.1. NM_001204402.1.
NP_002755.1. NM_002764.3. [P60891-1]
UniGeneiHs.56.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H06X-ray2.20A/B1-318[»]
2H07X-ray2.20A/B1-318[»]
2H08X-ray2.50A/B1-318[»]
2HCRX-ray2.20A/B1-318[»]
3EFHX-ray2.60A/B1-318[»]
3S5JX-ray2.02A/B1-318[»]
4F8EX-ray2.27A/B1-318[»]
4LYGX-ray3.00A/B1-318[»]
4LZNX-ray2.14A/B1-318[»]
4LZOX-ray3.31A/B1-318[»]
4M0PX-ray2.11A/B1-318[»]
4M0UX-ray2.74A/B1-318[»]
ProteinModelPortaliP60891.
SMRiP60891.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111615. 49 interactors.
DIPiDIP-61999N.
IntActiP60891. 17 interactors.
STRINGi9606.ENSP00000361512.

Chemistry databases

BindingDBiP60891.
ChEMBLiCHEMBL2638.

PTM databases

iPTMnetiP60891.
PhosphoSitePlusiP60891.
SwissPalmiP60891.

Polymorphism and mutation databases

BioMutaiPRPS1.
DMDMi46397477.

2D gel databases

UCD-2DPAGEP60891.

Proteomic databases

EPDiP60891.
MaxQBiP60891.
PaxDbiP60891.
PeptideAtlasiP60891.
PRIDEiP60891.

Protocols and materials databases

DNASUi5631.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372435; ENSP00000361512; ENSG00000147224. [P60891-1]
GeneIDi5631.
KEGGihsa:5631.
UCSCiuc004ene.5. human. [P60891-1]

Organism-specific databases

CTDi5631.
DisGeNETi5631.
GeneCardsiPRPS1.
GeneReviewsiPRPS1.
HGNCiHGNC:9462. PRPS1.
MalaCardsiPRPS1.
MIMi300661. phenotype.
301835. phenotype.
304500. phenotype.
311070. phenotype.
311850. gene.
neXtProtiNX_P60891.
OpenTargetsiENSG00000147224.
Orphaneti1187. Lethal ataxia with deafness and optic atrophy.
411536. Mild phosphoribosylpyrophosphate synthetase superactivity.
411543. Severe phosphoribosylpyrophosphate synthetase superactivity.
99014. X-linked Charcot-Marie-Tooth disease type 5.
90625. X-linked non-syndromic sensorineural deafness type DFN.
PharmGKBiPA33817.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1448. Eukaryota.
COG0462. LUCA.
GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP60891.
KOiK00948.
OMAiDGEIMVE.
OrthoDBiEOG091G0ZG8.
PhylomeDBiP60891.
TreeFamiTF106366.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
BioCyciMetaCyc:HS07410-MONOMER.
ZFISH:HS07410-MONOMER.
BRENDAi2.7.6.1. 2681.
ReactomeiR-HSA-73843. 5-Phosphoribose 1-diphosphate biosynthesis.

Miscellaneous databases

ChiTaRSiPRPS1. human.
EvolutionaryTraceiP60891.
GenomeRNAii5631.
PROiP60891.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147224.
CleanExiHS_PRPS1.
ExpressionAtlasiP60891. baseline and differential.
GenevisibleiP60891. HS.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B. 1 hit.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRPS1_HUMAN
AccessioniPrimary (citable) accession number: P60891
Secondary accession number(s): B1ALA8
, B2R6T7, B4DNL6, D3DUX6, P09329
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.