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P60891

- PRPS1_HUMAN

UniProt

P60891 - PRPS1_HUMAN

Protein

Ribose-phosphate pyrophosphokinase 1

Gene

PRPS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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. ADP binding Source: Ensembl
    2. AMP binding Source: Ensembl
    3. ATP binding Source: UniProtKB
    4. carbohydrate binding Source: Ensembl
    5. GDP binding Source: Ensembl
    6. kinase activity Source: UniProtKB-KW
    7. magnesium ion binding Source: Ensembl
    8. protein homodimerization activity Source: UniProtKB
    9. ribose phosphate diphosphokinase activity Source: UniProtKB

    GO - Biological processi

    1. 5-phosphoribose 1-diphosphate biosynthetic process Source: Reactome
    2. AMP biosynthetic process Source: Ensembl
    3. carbohydrate metabolic process Source: Reactome
    4. cell death Source: UniProtKB-KW
    5. hypoxanthine biosynthetic process Source: UniProtKB
    6. nervous system development Source: UniProtKB
    7. organ regeneration Source: Ensembl
    8. purine nucleobase metabolic process Source: UniProtKB
    9. purine nucleotide biosynthetic process Source: UniProtKB
    10. pyrimidine nucleotide biosynthetic process Source: UniProtKB
    11. small molecule metabolic process Source: Reactome
    12. urate biosynthetic process Source: UniProtKB

    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
    2. ribose phosphate diphosphokinase complex Source: Ensembl

    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 nonsyndromic 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

    ArrayExpressiP60891.
    BgeeiP60891.
    CleanExiHS_PRPS1.
    GenevestigatoriP60891.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi111615. 17 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 – 85
    Helixi14 – 229
    Beta strandi30 – 345
    Beta strandi36 – 383
    Beta strandi40 – 445
    Beta strandi52 – 565
    Helixi63 – 7917
    Beta strandi83 – 919
    Turni93 – 964
    Beta strandi101 – 1044
    Helixi108 – 11912
    Beta strandi122 – 1287
    Helixi132 – 1376
    Beta strandi142 – 1454
    Helixi148 – 15811
    Helixi162 – 1643
    Beta strandi166 – 1716
    Helixi172 – 1743
    Helixi175 – 18511
    Beta strandi188 – 1947
    Beta strandi205 – 2095
    Beta strandi214 – 22512
    Helixi227 – 23812
    Beta strandi242 – 25110
    Helixi257 – 2637
    Beta strandi267 – 2726
    Helixi278 – 2825
    Beta strandi287 – 2904
    Helixi293 – 30513
    Helixi310 – 3134

    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.
    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

    MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIGESVRG    50
    EDVYIVQSGC GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK 100
    DKSRAPISAK LVANMLSVAG ADHIITMDLH ASQIQGFFDI PVDNLYAEPA 150
    VLKWIRENIS EWRNCTIVSP DAGGAKRVTS IADRLNVDFA LIHKERKKAN 200
    EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG ATRVYAILTH 250
    GIFSGPAISR INNACFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI 300
    RRTHNGESVS YLFSHVPL 318
    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.
    PIRiJX0159. KIHUR1.
    RefSeqiNP_001191331.1. NM_001204402.1.
    NP_002755.1. NM_002764.3.
    UniGeneiHs.56.

    Genome annotation databases

    EnsembliENST00000372428; ENSP00000361505; ENSG00000147224.
    ENST00000372435; ENSP00000361512; ENSG00000147224.
    GeneIDi5631.
    KEGGihsa:5631.
    UCSCiuc004ene.4. human.

    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.
    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. 17 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 ENST00000372428 ; ENSP00000361505 ; ENSG00000147224 .
    ENST00000372435 ; ENSP00000361512 ; ENSG00000147224 .
    GeneIDi 5631.
    KEGGi hsa:5631.
    UCSCi uc004ene.4. human.

    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 nonsyndromic sensorineural deafness type DFN.
    PharmGKBi PA33817.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0462.
    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

    ArrayExpressi P60891.
    Bgeei P60891.
    CleanExi HS_PRPS1.
    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

    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 1, 2014
    This is version 121 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