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P60891

- PRPS1_HUMAN

UniProt

P60891 - PRPS1_HUMAN

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Protein

Ribose-phosphate pyrophosphokinase 1

Gene

PRPS1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Magnesium.

Enzyme regulationi

Activated by magnesium and inorganic phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi128 – 1281MagnesiumSequence Analysis
Metal bindingi130 – 1301MagnesiumSequence Analysis
Binding sitei130 – 1301ATP
Metal bindingi139 – 1391MagnesiumSequence Analysis
Metal bindingi143 – 1431MagnesiumSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 1016ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. kinase activity Source: UniProtKB-KW
  3. magnesium ion binding Source: InterPro
  4. protein homodimerization activity Source: UniProtKB
  5. ribose phosphate diphosphokinase activity Source: UniProtKB

GO - Biological processi

  1. 5-phosphoribose 1-diphosphate biosynthetic process Source: Reactome
  2. carbohydrate metabolic process Source: Reactome
  3. cell death Source: UniProtKB-KW
  4. hypoxanthine biosynthetic process Source: UniProtKB
  5. nervous system development Source: UniProtKB
  6. purine nucleobase metabolic process Source: UniProtKB
  7. purine nucleotide biosynthetic process Source: UniProtKB
  8. pyrimidine nucleotide biosynthetic process Source: UniProtKB
  9. ribonucleoside monophosphate biosynthetic process Source: InterPro
  10. small molecule metabolic process Source: Reactome
  11. 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.
ReactomeiREACT_850. 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
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:9462. PRPS1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Phosphoribosylpyrophosphate synthetase superactivity (PRPS1 superactivity) [MIM:300661]: Familial disorder characterized by excessive purine production, gout and uric acid urolithiasis.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521D → H in PRPS1 superactivity. 1 Publication
VAR_016044
Natural varianti114 – 1141N → S in PRPS1 superactivity. 2 Publications
VAR_004163
Natural varianti129 – 1291L → I in PRPS1 superactivity. 1 Publication
VAR_016045
Natural varianti183 – 1831D → H in PRPS1 superactivity. 2 Publications
VAR_004164
Natural varianti190 – 1901A → V in PRPS1 superactivity. 1 Publication
VAR_016046
Natural varianti193 – 1931H → Q in PRPS1 superactivity. 1 Publication
VAR_016047
Charcot-Marie-Tooth disease, X-linked recessive, 5 (CMTX5) [MIM:311070]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431E → D in CMTX5. 1 Publication
VAR_036941
Natural varianti115 – 1151M → T in CMTX5. 1 Publication
VAR_036942
ARTS syndrome (ARTS) [MIM:301835]: 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331Q → P in ARTS. 1 Publication
VAR_036943
Natural varianti152 – 1521L → P in ARTS. 1 Publication
VAR_036944
Deafness, X-linked, 1 (DFNX1) [MIM:304500]: A form of deafness characterized by progressive, severe-to-profound sensorineural hearing loss in males. Females manifest mild to moderate hearing loss.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651D → N in DFNX1. 1 Publication
VAR_063522
Natural varianti87 – 871A → T in DFNX1. 1 Publication
VAR_063523
Natural varianti290 – 2901I → T in DFNX1. 1 Publication
VAR_063524
Natural varianti306 – 3061G → R in DFNX1. 1 Publication
VAR_063525

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321S → A: Reduces catalytic activity. 1 Publication
Mutagenesisi132 – 1321S → F: No effect on catalytic activity. 1 Publication
Mutagenesisi144 – 1441N → H: No effect on catalytic activity. 1 Publication
Mutagenesisi146 – 1461Y → F: No effect on catalytic activity. 1 Publication
Mutagenesisi146 – 1461Y → M: Reduces catalytic activity. 1 Publication

Keywords - Diseasei

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

Organism-specific databases

MIMi300661. phenotype.
301835. phenotype.
304500. phenotype.
311070. phenotype.
Orphaneti1187. Lethal ataxia with deafness and optic atrophy.
3222. Phosphoribosylpyrophosphate synthetase superactivity.
99014. X-linked Charcot-Marie-Tooth disease type 5.
90625. X-linked non-syndromic sensorineural deafness type DFN.
PharmGKBiPA33817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 318317Ribose-phosphate pyrophosphokinase 1PRO_0000141071Add
BLAST

Proteomic databases

MaxQBiP60891.
PaxDbiP60891.
PRIDEiP60891.

2D gel databases

UCD-2DPAGEP60891.

PTM databases

PhosphoSiteiP60891.

Expressioni

Gene expression databases

BgeeiP60891.
CleanExiHS_PRPS1.
ExpressionAtlasiP60891. baseline and differential.
GenevestigatoriP60891.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi111615. 38 interactions.
IntActiP60891. 5 interactions.
STRINGi9606.ENSP00000361512.

Structurei

Secondary structure

1
318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi14 – 229Combined sources
Beta strandi30 – 345Combined sources
Beta strandi36 – 383Combined sources
Beta strandi40 – 445Combined sources
Beta strandi52 – 565Combined sources
Helixi63 – 7917Combined sources
Beta strandi83 – 919Combined sources
Turni93 – 964Combined sources
Beta strandi101 – 1044Combined sources
Helixi108 – 11912Combined sources
Beta strandi122 – 1287Combined sources
Helixi132 – 1376Combined sources
Beta strandi142 – 1454Combined sources
Helixi148 – 15811Combined sources
Helixi162 – 1643Combined sources
Beta strandi166 – 1716Combined sources
Helixi172 – 1743Combined sources
Helixi175 – 18511Combined sources
Beta strandi188 – 1947Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi214 – 22512Combined sources
Helixi227 – 23812Combined sources
Beta strandi242 – 25110Combined sources
Helixi257 – 2637Combined sources
Beta strandi267 – 2726Combined sources
Helixi278 – 2825Combined sources
Beta strandi287 – 2904Combined sources
Helixi293 – 30513Combined sources
Helixi310 – 3134Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP60891.
SMRiP60891. Positions 3-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60891.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni212 – 22716Binding of phosphoribosylpyrophosphateSequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0462.
GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP60891.
KOiK00948.
OMAiINERTLP.
OrthoDBiEOG7G4QG5.
PhylomeDBiP60891.
TreeFamiTF106366.

Family and domain databases

Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821A → G in BAG35584. (PubMed:14702039)Curated
Sequence conflicti122 – 1221D → G in BAG35584. (PubMed:14702039)Curated
Sequence conflicti278 – 2781E → G in BAG35584. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431E → D in CMTX5. 1 Publication
VAR_036941
Natural varianti52 – 521D → H in PRPS1 superactivity. 1 Publication
VAR_016044
Natural varianti65 – 651D → N in DFNX1. 1 Publication
VAR_063522
Natural varianti87 – 871A → T in DFNX1. 1 Publication
VAR_063523
Natural varianti114 – 1141N → S in PRPS1 superactivity. 2 Publications
VAR_004163
Natural varianti115 – 1151M → T in CMTX5. 1 Publication
VAR_036942
Natural varianti129 – 1291L → I in PRPS1 superactivity. 1 Publication
VAR_016045
Natural varianti133 – 1331Q → P in ARTS. 1 Publication
VAR_036943
Natural varianti152 – 1521L → P in ARTS. 1 Publication
VAR_036944
Natural varianti183 – 1831D → H in PRPS1 superactivity. 2 Publications
VAR_004164
Natural varianti190 – 1901A → V in PRPS1 superactivity. 1 Publication
VAR_016046
Natural varianti193 – 1931H → Q in PRPS1 superactivity. 1 Publication
VAR_016047
Natural varianti203 – 2031D → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_036593
Natural varianti219 – 2191V → G in a breast cancer sample; somatic mutation. 1 Publication
VAR_036594
Natural varianti231 – 2311H → D in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036595
Natural varianti290 – 2901I → T in DFNX1. 1 Publication
VAR_063524
Natural varianti306 – 3061G → R in DFNX1. 1 Publication
VAR_063525

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6767Missing in isoform 2. 1 PublicationVSP_056028Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UniGeneiHs.56.

Genome annotation databases

EnsembliENST00000372435; ENSP00000361512; ENSG00000147224. [P60891-1]
GeneIDi5631.
KEGGihsa:5631.
UCSCiuc004ene.4. human. [P60891-1]

Polymorphism databases

DMDMi46397477.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14529.1. [P60891-1 ]
PIRi JX0159. KIHUR1.
RefSeqi NP_001191331.1. NM_001204402.1.
NP_002755.1. NM_002764.3.
UniGenei Hs.56.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H06 X-ray 2.20 A/B 1-318 [» ]
2H07 X-ray 2.20 A/B 1-318 [» ]
2H08 X-ray 2.50 A/B 1-318 [» ]
2HCR X-ray 2.20 A/B 1-318 [» ]
3EFH X-ray 2.60 A/B 1-318 [» ]
3S5J X-ray 2.02 A/B 1-318 [» ]
4F8E X-ray 2.27 A/B 1-318 [» ]
ProteinModelPortali P60891.
SMRi P60891. Positions 3-317.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111615. 38 interactions.
IntActi P60891. 5 interactions.
STRINGi 9606.ENSP00000361512.

Chemistry

BindingDBi P60891.
ChEMBLi CHEMBL2638.

PTM databases

PhosphoSitei P60891.

Polymorphism databases

DMDMi 46397477.

2D gel databases

UCD-2DPAGE P60891.

Proteomic databases

MaxQBi P60891.
PaxDbi P60891.
PRIDEi P60891.

Protocols and materials databases

DNASUi 5631.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372435 ; ENSP00000361512 ; ENSG00000147224 . [P60891-1 ]
GeneIDi 5631.
KEGGi hsa:5631.
UCSCi uc004ene.4. human. [P60891-1 ]

Organism-specific databases

CTDi 5631.
GeneCardsi GC0XP106871.
GeneReviewsi PRPS1.
HGNCi HGNC:9462. PRPS1.
MIMi 300661. phenotype.
301835. phenotype.
304500. phenotype.
311070. phenotype.
311850. gene.
neXtProti NX_P60891.
Orphaneti 1187. Lethal ataxia with deafness and optic atrophy.
3222. Phosphoribosylpyrophosphate synthetase superactivity.
99014. X-linked Charcot-Marie-Tooth disease type 5.
90625. X-linked non-syndromic sensorineural deafness type DFN.
PharmGKBi PA33817.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0462.
GeneTreei ENSGT00550000074583.
HOGENOMi HOG000210451.
HOVERGENi HBG001520.
InParanoidi P60891.
KOi K00948.
OMAi INERTLP.
OrthoDBi EOG7G4QG5.
PhylomeDBi P60891.
TreeFami TF106366.

Enzyme and pathway databases

UniPathwayi UPA00087 ; UER00172 .
BioCyci MetaCyc:HS07410-MONOMER.
Reactomei REACT_850. 5-Phosphoribose 1-diphosphate biosynthesis.

Miscellaneous databases

ChiTaRSi PRPS1. human.
EvolutionaryTracei P60891.
GenomeRNAii 5631.
NextBioi 21886.
PROi P60891.
SOURCEi Search...

Gene expression databases

Bgeei P60891.
CleanExi HS_PRPS1.
ExpressionAtlasi P60891. baseline and differential.
Genevestigatori P60891.

Family and domain databases

Gene3Di 3.40.50.2020. 2 hits.
HAMAPi MF_00583_B. RibP_PPkinase_B.
InterProi IPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view ]
Pfami PF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53271. SSF53271. 1 hit.
TIGRFAMsi TIGR01251. ribP_PPkin. 1 hit.
PROSITEi PS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of two distinct copies of human phosphoribosylpyrophosphate synthetase cDNA."
    Roessler B.J., Bell G., Heidler S., Seino S., Becker M., Palella T.D.
    Nucleic Acids Res. 18:193-193(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lymphoblast.
  2. "Complete nucleotide sequence of human phosphoribosyl pyrophosphate synthetase subunit I (PRS I) cDNA and a comparison with human and rat PRPS gene families."
    Sonoda T., Taira M., Ishijima S., Ishizuka T., Iizaka T., Tatibana M.
    J. Biochem. 109:361-364(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph.
  7. "Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms."
    Ishizuka T., Iizasa T., Taira M., Ishijima S., Sonoda T., Shimada H., Nagatake N., Tatibana M.
    Biochim. Biophys. Acta 1130:139-148(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-41 (ISOFORM 1).
  8. Bienvenut W.V., Zebisch A., Kolch W.
    Submitted (JUL-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-33; 85-96; 164-176; 205-214; 236-260 AND 303-318, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  9. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 244-260 AND 303-318, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site."
    Li S., Lu Y., Peng B., Ding J.
    Biochem. J. 401:39-47(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH AMP, SUBUNIT, MUTAGENESIS OF SER-132; ASN-144 AND TYR-146.
  12. "Identification of distinct PRPS1 mutations in two patients with X-linked phosphoribosylpyrophosphate synthetase superactivity."
    Roessler B.J., Palella T.D., Heidler S., Becker M.A.
    Clin. Res. 39:267A-267A(1991)
    Cited for: VARIANTS PRPS1 SUPERACTIVITY SER-114 AND HIS-183.
  13. "The genetic and functional basis of purine nucleotide feedback-resistant phosphoribosylpyrophosphate synthetase superactivity."
    Becker M.A., Smith P.R., Taylor W., Mustafi R., Switzer R.L.
    J. Clin. Invest. 96:2133-2141(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRPS1 SUPERACTIVITY HIS-52; SER-114; ILE-129; HIS-183; VAL-190 AND GLN-193.
  14. Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-203; GLY-219 AND ASP-231.
  15. Cited for: VARIANTS ARTS PRO-133 AND PRO-152.
  16. "Mutations in PRPS1, which encodes the phosphoribosyl pyrophosphate synthetase enzyme critical for nucleotide biosynthesis, cause hereditary peripheral neuropathy with hearing loss and optic neuropathy (cmtx5)."
    Kim H.-J., Sohn K.-M., Shy M.E., Krajewski K.M., Hwang M., Park J.-H., Jang S.-Y., Won H.-H., Choi B.-O., Hong S.H., Kim B.-J., Suh Y.-L., Ki C.-S., Lee S.-Y., Kim S.-H., Kim J.-W.
    Am. J. Hum. Genet. 81:552-558(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CMTX5 ASP-43 AND THR-115.
  17. "Loss-of-function mutations in the PRPS1 gene cause a type of nonsyndromic X-linked sensorineural deafness, DFN2."
    Liu X., Han D., Li J., Han B., Ouyang X., Cheng J., Li X., Jin Z., Wang Y., Bitner-Glindzicz M., Kong X., Xu H., Kantardzhieva A., Eavey R.D., Seidman C.E., Seidman J.G., Du L.L., Chen Z.Y.
    , Dai P., Teng M., Yan D., Yuan H.
    Am. J. Hum. Genet. 86:65-71(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DFNX1 ASN-65; THR-87; THR-290 AND ARG-306.

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: October 29, 2014
This is version 122 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

External Data

Dasty 3