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P60891 (PRPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribose-phosphate pyrophosphokinase 1

EC=2.7.6.1
Alternative name(s):
PPRibP
Phosphoribosyl pyrophosphate synthase I
Short name=PRS-I
Gene names
Name:PRPS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. HAMAP-Rule MF_00583_B

Catalytic activity

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00583_B

Cofactor

Magnesium.

Enzyme regulation

Activated by magnesium and inorganic phosphate. HAMAP-Rule MF_00583_B

Pathway

Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. HAMAP-Rule MF_00583_B

Subunit structure

Homodimer. The active form is probably a hexamer composed of 3 homodimers. Ref.11

Involvement in disease

Phosphoribosylpyrophosphate synthetase superactivity (PRPS1 superactivity) [MIM:300661]: Familial disorder characterized by excessive purine production, gout and uric acid urolithiasis.
Note: The disease is caused by mutations affecting the gene represented in this entry.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Coding sequence diversityPolymorphism
   DiseaseCharcot-Marie-Tooth disease
Deafness
Disease mutation
Gout
Mental retardation
Neuropathy
Non-syndromic deafness
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process5-phosphoribose 1-diphosphate biosynthetic process

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

hypoxanthine biosynthetic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

nervous system development

Inferred from mutant phenotype Ref.16PubMed 8253776. Source: UniProtKB

nucleotide biosynthetic process

Inferred from electronic annotation. Source: InterPro

purine nucleotide biosynthetic process

Inferred from mutant phenotype PubMed 12847698. Source: UniProtKB

pyrimidine nucleotide biosynthetic process

Non-traceable author statement Ref.15. Source: UniProtKB

ribonucleoside monophosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

urate biosynthetic process

Inferred from mutant phenotype PubMed 12847698. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from direct assay Ref.11. Source: UniProtKB

kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

ribose phosphate diphosphokinase activity

Inferred from direct assay Ref.11Ref.16. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 318317Ribose-phosphate pyrophosphokinase 1 HAMAP-Rule MF_00583_B
PRO_0000141071

Regions

Nucleotide binding96 – 1016ATP HAMAP-Rule MF_00583_B
Region212 – 22716Binding of phosphoribosylpyrophosphate Potential

Sites

Metal binding1281Magnesium Potential
Metal binding1301Magnesium Potential
Metal binding1391Magnesium Potential
Metal binding1431Magnesium Potential
Binding site1301ATP

Natural variations

Natural variant431E → D in CMTX5. Ref.16
VAR_036941
Natural variant521D → H in PRPS1 superactivity. Ref.13
VAR_016044
Natural variant651D → N in DFNX1. Ref.17
VAR_063522
Natural variant871A → T in DFNX1. Ref.17
VAR_063523
Natural variant1141N → S in PRPS1 superactivity. Ref.12 Ref.13
VAR_004163
Natural variant1151M → T in CMTX5. Ref.16
VAR_036942
Natural variant1291L → I in PRPS1 superactivity. Ref.13
VAR_016045
Natural variant1331Q → P in ARTS. Ref.15
VAR_036943
Natural variant1521L → P in ARTS. Ref.15
VAR_036944
Natural variant1831D → H in PRPS1 superactivity. Ref.12 Ref.13
VAR_004164
Natural variant1901A → V in PRPS1 superactivity. Ref.13
VAR_016046
Natural variant1931H → Q in PRPS1 superactivity. Ref.13
VAR_016047
Natural variant2031D → H in a breast cancer sample; somatic mutation. Ref.14
VAR_036593
Natural variant2191V → G in a breast cancer sample; somatic mutation. Ref.14
VAR_036594
Natural variant2311H → D in a colorectal cancer sample; somatic mutation. Ref.14
VAR_036595
Natural variant2901I → T in DFNX1. Ref.17
VAR_063524
Natural variant3061G → R in DFNX1. Ref.17
VAR_063525

Experimental info

Mutagenesis1321S → A: Reduces catalytic activity. Ref.11
Mutagenesis1321S → F: No effect on catalytic activity. Ref.11
Mutagenesis1441N → H: No effect on catalytic activity. Ref.11
Mutagenesis1461Y → F: No effect on catalytic activity. Ref.11
Mutagenesis1461Y → M: Reduces catalytic activity. Ref.11
Sequence conflict821A → G in BAG35584. Ref.3
Sequence conflict1221D → G in BAG35584. Ref.3
Sequence conflict2781E → G in BAG35584. Ref.3

Secondary structure

........................................................... 318
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60891 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 46D017E969908BA0

FASTA31834,834
        10         20         30         40         50         60 
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIGESVRG EDVYIVQSGC 

        70         80         90        100        110        120 
GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG 

       130        140        150        160        170        180 
ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLKWIRENIS EWRNCTIVSP DAGGAKRVTS 

       190        200        210        220        230        240 
IADRLNVDFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG 

       250        260        270        280        290        300 
ATRVYAILTH GIFSGPAISR INNACFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI 

       310 
RRTHNGESVS YLFSHVPL 

« Hide

References

« Hide 'large scale' references
[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].
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].
[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. expand/collapse author list , 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].
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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].
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.
[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, 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, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-203; GLY-219 AND ASP-231.
[15]"Arts syndrome is caused by loss-of-function mutations in PRPS1."
de Brouwer A.P.M., Williams K.L., Duley J.A., van Kuilenburg A.B.P., Nabuurs S.B., Egmont-Petersen M., Lugtenberg D., Zoetekouw L., Banning M.J.G., Roeffen M., Hamel B.C.J., Weaving L., Ouvrier R.A., Donald J.A., Wevers R.A., Christodoulou J., van Bokhoven H.
Am. J. Hum. Genet. 81:507-518(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15331 mRNA. Translation: CAA33386.1.
D00860 mRNA. Translation: BAA00733.1.
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.
PIRKIHUR1. JX0159.
RefSeqNP_001191331.1. NM_001204402.1.
NP_002755.1. NM_002764.3.
UniGeneHs.56.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP60891.
SMRP60891. Positions 3-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111615. 15 interactions.
IntActP60891. 3 interactions.
STRING9606.ENSP00000361512.

Chemistry

BindingDBP60891.
ChEMBLCHEMBL2638.

PTM databases

PhosphoSiteP60891.

Polymorphism databases

DMDM46397477.

2D gel databases

UCD-2DPAGEP60891.

Proteomic databases

PaxDbP60891.
PRIDEP60891.

Protocols and materials databases

DNASU5631.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372435; ENSP00000361512; ENSG00000147224.
ENST00000543248; ENSP00000443185; ENSG00000147224.
GeneID5631.
KEGGhsa:5631.
UCSCuc004ene.4. human.

Organism-specific databases

CTD5631.
GeneCardsGC0XP106871.
HGNCHGNC:9462. PRPS1.
MIM300661. phenotype.
301835. phenotype.
304500. phenotype.
311070. phenotype.
311850. gene.
neXtProtNX_P60891.
Orphanet1187. 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.
PharmGKBPA33817.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0462.
HOGENOMHOG000210451.
HOVERGENHBG001520.
InParanoidP60891.
KOK00948.
OMAMMFAEAV.
OrthoDBEOG7G4QG5.
PhylomeDBP60891.
TreeFamTF106366.

Enzyme and pathway databases

BioCycMetaCyc:HS07410-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00087; UER00172.

Gene expression databases

ArrayExpressP60891.
BgeeP60891.
CleanExHS_PRPS1.
GenevestigatorP60891.

Family and domain databases

HAMAPMF_00583_B. RibP_PPkinase_B.
InterProIPR000842. PRib_PP_synth_CS.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamPF14572. Pribosyl_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR01251. ribP_PPkin. 1 hit.
PROSITEPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRPS1. human.
EvolutionaryTraceP60891.
GenomeRNAi5631.
NextBio21886.
PROP60891.
SOURCESearch...

Entry information

Entry namePRPS1_HUMAN
AccessionPrimary (citable) accession number: P60891
Secondary accession number(s): B1ALA8 expand/collapse secondary AC list , B2R6T7, D3DUX6, P09329
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM