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Protein

Ribose-phosphate pyrophosphokinase 1

Gene

Prps1

Organism
Mus musculus (Mouse)
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

Mg2+By similarity

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 – 1301ATPBy similarity
Metal bindingi139 – 1391MagnesiumSequence Analysis
Metal bindingi143 – 1431MagnesiumSequence Analysis

Regions

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

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: UniProtKB-UniPathway
  2. hypoxanthine biosynthetic process Source: MGI
  3. nervous system development Source: MGI
  4. purine nucleobase metabolic process Source: MGI
  5. purine nucleotide biosynthetic process Source: MGI
  6. ribonucleoside monophosphate biosynthetic process Source: InterPro
  7. urate biosynthetic process Source: MGI
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

ReactomeiREACT_315948. 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):
Phosphoribosyl pyrophosphate synthase I
Short name:
PRS-I
Gene namesi
Name:Prps1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:97775. Prps1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 318317Ribose-phosphate pyrophosphokinase 1PRO_0000141072Add
BLAST

Proteomic databases

MaxQBiQ9D7G0.
PaxDbiQ9D7G0.
PRIDEiQ9D7G0.

2D gel databases

REPRODUCTION-2DPAGEQ9D7G0.

PTM databases

PhosphoSiteiQ9D7G0.

Expressioni

Developmental stagei

Expressed in both vestibular and cochlea hair cells in early developing and postnatal mice and can also be detected in the spiral ganglion cells in at post natal day 6.1 Publication

Gene expression databases

BgeeiQ9D7G0.
CleanExiMM_PRPS1.
ExpressionAtlasiQ9D7G0. baseline and differential.
GenevestigatoriQ9D7G0.

Interactioni

Subunit structurei

Homodimer. The active form is probably a hexamer composed of 3 homodimers (By similarity).By similarity

Protein-protein interaction databases

BioGridi202401. 1 interaction.
IntActiQ9D7G0. 2 interactions.
MINTiMINT-1858366.

Structurei

3D structure databases

ProteinModelPortaliQ9D7G0.
SMRiQ9D7G0. Positions 3-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0462.
GeneTreeiENSGT00550000074583.
HOVERGENiHBG001520.
InParanoidiQ9D7G0.
KOiK00948.
OMAiAKKIICA.
OrthoDBiEOG7G4QG5.
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]

Sequencei

Sequence statusi: Complete.

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

Q9D7G0-1 [UniParc]FASTAAdd to basket

« 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:July 27, 2011 - v4
Checksum:i46D017E969908BA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831D → E in BAB26181 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025048 mRNA. Translation: BAA84686.1.
AK009265 mRNA. Translation: BAB26181.1.
AK011304 mRNA. Translation: BAB27530.1.
AK089009 mRNA. Translation: BAC40697.1.
AK165524 mRNA. Translation: BAE38237.1.
AK165987 mRNA. Translation: BAE38503.1.
AK166856 mRNA. Translation: BAE39073.1.
AL672297 Genomic DNA. Translation: CAM14818.1.
CH466616 Genomic DNA. Translation: EDL23928.1.
CH466616 Genomic DNA. Translation: EDL23929.1.
BC054772 mRNA. Translation: AAH54772.1.
CCDSiCCDS30439.1.
RefSeqiNP_067438.1. NM_021463.4.
UniGeneiMm.287178.

Genome annotation databases

EnsembliENSMUST00000033809; ENSMUSP00000033809; ENSMUSG00000031432.
GeneIDi19139.
KEGGimmu:19139.
UCSCiuc009uky.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025048 mRNA. Translation: BAA84686.1.
AK009265 mRNA. Translation: BAB26181.1.
AK011304 mRNA. Translation: BAB27530.1.
AK089009 mRNA. Translation: BAC40697.1.
AK165524 mRNA. Translation: BAE38237.1.
AK165987 mRNA. Translation: BAE38503.1.
AK166856 mRNA. Translation: BAE39073.1.
AL672297 Genomic DNA. Translation: CAM14818.1.
CH466616 Genomic DNA. Translation: EDL23928.1.
CH466616 Genomic DNA. Translation: EDL23929.1.
BC054772 mRNA. Translation: AAH54772.1.
CCDSiCCDS30439.1.
RefSeqiNP_067438.1. NM_021463.4.
UniGeneiMm.287178.

3D structure databases

ProteinModelPortaliQ9D7G0.
SMRiQ9D7G0. Positions 3-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202401. 1 interaction.
IntActiQ9D7G0. 2 interactions.
MINTiMINT-1858366.

Chemistry

BindingDBiQ9D7G0.

PTM databases

PhosphoSiteiQ9D7G0.

2D gel databases

REPRODUCTION-2DPAGEQ9D7G0.

Proteomic databases

MaxQBiQ9D7G0.
PaxDbiQ9D7G0.
PRIDEiQ9D7G0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033809; ENSMUSP00000033809; ENSMUSG00000031432.
GeneIDi19139.
KEGGimmu:19139.
UCSCiuc009uky.2. mouse.

Organism-specific databases

CTDi5631.
MGIiMGI:97775. Prps1.

Phylogenomic databases

eggNOGiCOG0462.
GeneTreeiENSGT00550000074583.
HOVERGENiHBG001520.
InParanoidiQ9D7G0.
KOiK00948.
OMAiAKKIICA.
OrthoDBiEOG7G4QG5.
TreeFamiTF106366.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
ReactomeiREACT_315948. 5-Phosphoribose 1-diphosphate biosynthesis.

Miscellaneous databases

ChiTaRSiPrps1. mouse.
NextBioi295766.
PROiQ9D7G0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D7G0.
CleanExiMM_PRPS1.
ExpressionAtlasiQ9D7G0. baseline and differential.
GenevestigatoriQ9D7G0.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse phosphoribosylpyrophosphate synthetase subunit I (PRS I)."
    Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Lung, Thymus and Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  6. Lubec G., Klug S.
    Submitted (FEB-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 35-49; 244-260 AND 303-318, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  7. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiPRPS1_MOUSE
AccessioniPrimary (citable) accession number: Q9D7G0
Secondary accession number(s): Q76MX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 117 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.