Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ribose-phosphate pyrophosphokinase 1 (EC 2.7.6.1) (PPRibP) (Phosphoribosyl pyrophosphate synthase I) (PRS-I)

 PRPS1_HUMAN             Reviewed;         318 AA.
P60891; B1ALA8; B2R6T7; B4DNL6; D3DUX6; P09329;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 153.
RecName: Full=Ribose-phosphate pyrophosphokinase 1;
EC=2.7.6.1;
AltName: Full=PPRibP;
AltName: Full=Phosphoribosyl pyrophosphate synthase I;
Short=PRS-I;
Name=PRPS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lymphoblast;
PubMed=2155397; DOI=10.1093/nar/18.1.193;
Roessler B.J., Bell G., Heidler S., Seino S., Becker M., Palella T.D.;
"Cloning of two distinct copies of human phosphoribosylpyrophosphate
synthetase cDNA.";
Nucleic Acids Res. 18:193-193(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1650777;
Sonoda T., Taira M., Ishijima S., Ishizuka T., Iizaka T., Tatibana M.;
"Complete nucleotide sequence of human phosphoribosyl pyrophosphate
synthetase subunit I (PRS I) cDNA and a comparison with human and rat
PRPS gene families.";
J. Biochem. 109:361-364(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
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.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-41 (ISOFORM 1).
PubMed=1314091; DOI=10.1016/0167-4781(92)90521-Z;
Ishizuka T., Iizasa T., Taira M., Ishijima S., Sonoda T., Shimada H.,
Nagatake N., Tatibana M.;
"Promoter regions of the human X-linked housekeeping genes PRPS1 and
PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II
isoforms.";
Biochim. Biophys. Acta 1130:139-148(1992).
[8]
PROTEIN SEQUENCE OF 2-33; 85-96; 164-176; 205-214; 236-260 AND
303-318, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (JUL-2009) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 244-260 AND 303-318, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH AMP, SUBUNIT,
AND MUTAGENESIS OF SER-132; ASN-144 AND TYR-146.
PubMed=16939420; DOI=10.1042/BJ20061066;
Li S., Lu Y., Peng B., Ding J.;
"Crystal structure of human phosphoribosylpyrophosphate synthetase 1
reveals a novel allosteric site.";
Biochem. J. 401:39-47(2007).
[12]
VARIANTS PRPS1 SUPERACTIVITY SER-114 AND HIS-183.
Roessler B.J., Palella T.D., Heidler S., Becker M.A.;
"Identification of distinct PRPS1 mutations in two patients with X-
linked phosphoribosylpyrophosphate synthetase superactivity.";
Clin. Res. 39:267A-267A(1991).
[13]
VARIANTS PRPS1 SUPERACTIVITY HIS-52; SER-114; ILE-129; HIS-183;
VAL-190 AND GLN-193.
PubMed=7593598; DOI=10.1172/JCI118267;
Becker M.A., Smith P.R., Taylor W., Mustafi R., Switzer R.L.;
"The genetic and functional basis of purine nucleotide feedback-
resistant phosphoribosylpyrophosphate synthetase superactivity.";
J. Clin. Invest. 96:2133-2141(1995).
[14]
VARIANTS [LARGE SCALE ANALYSIS] HIS-203; GLY-219 AND ASP-231.
PubMed=16959974; DOI=10.1126/science.1133427;
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., 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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[15]
VARIANTS ARTS PRO-133 AND PRO-152.
PubMed=17701896; DOI=10.1086/520706;
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.;
"Arts syndrome is caused by loss-of-function mutations in PRPS1.";
Am. J. Hum. Genet. 81:507-518(2007).
[16]
VARIANTS CMTX5 ASP-43 AND THR-115.
PubMed=17701900; DOI=10.1086/519529;
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.;
"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).";
Am. J. Hum. Genet. 81:552-558(2007).
[17]
VARIANTS DFNX1 ASN-65; THR-87; THR-290 AND ARG-306.
PubMed=20021999; DOI=10.1016/j.ajhg.2009.11.015;
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.;
"Loss-of-function mutations in the PRPS1 gene cause a type of
nonsyndromic X-linked sensorineural deafness, DFN2.";
Am. J. Hum. Genet. 86:65-71(2010).
[18]
INVOLVEMENT IN DISEASE, VARIANT LEU-142, AND CHARACTERIZATION OF
VARIANT LEU-142.
PubMed=22246954; DOI=10.1002/ajmg.a.34428;
Moran R., Kuilenburg A.B., Duley J., Nabuurs S.B., Retno-Fitri A.,
Christodoulou J., Roelofsen J., Yntema H.G., Friedman N.R.,
van Bokhoven H., de Brouwer A.P.;
"Phosphoribosylpyrophosphate synthetase superactivity and recurrent
infections is caused by a p.Val142Leu mutation in PRS-I.";
Am. J. Med. Genet. A 158A:455-460(2012).
[19]
VARIANT PRO-16.
PubMed=25491489; DOI=10.1186/s13023-014-0190-9;
Almoguera B., He S., Corton M., Fernandez-San Jose P.,
Blanco-Kelly F., Lopez-Molina M., Garcia-Sandoval B., Del Val J.,
Guo Y., Tian L., Liu X., Guan L., Torres R.J., Puig J.G.,
Hakonarson H., Xu X., Keating B., Ayuso C.;
"Expanding the phenotype of PRPS1 syndromes in females: neuropathy,
hearing loss and retinopathy.";
Orphanet J. Rare Dis. 9:190-190(2014).
-!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate
(PRPP) that is essential for nucleotide synthesis.
-!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
alpha-D-ribose 1-diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Activated by magnesium and inorganic phosphate.
-!- 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.
-!- SUBUNIT: Homodimer. The active form is probably a hexamer composed
of 3 homodimers. {ECO:0000269|PubMed:16939420}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-749195, EBI-749195;
Q9H8Y8:GORASP2; NbExp=3; IntAct=EBI-749195, EBI-739467;
P50053-2:KHK; NbExp=4; IntAct=EBI-16205225, EBI-12204387;
P11908:PRPS2; NbExp=6; IntAct=EBI-749195, EBI-4290895;
P11908-2:PRPS2; NbExp=3; IntAct=EBI-749195, EBI-12063547;
Q14558:PRPSAP1; NbExp=11; IntAct=EBI-749195, EBI-724449;
O60256:PRPSAP2; NbExp=7; IntAct=EBI-749195, EBI-724960;
Q9NZD8:SPG21; NbExp=6; IntAct=EBI-749195, EBI-742688;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P60891-1; Sequence=Displayed;
Name=2;
IsoId=P60891-2; Sequence=VSP_056028;
Note=No experimental confirmation available.;
-!- DISEASE: Note=Phosphoribosyl pyrophosphate synthetase I deficiency
is a rare condition caused by mutations in PRPS1 that lead to
variable disease phenotypes including optic atrophy, retinitis
pigmentosa, ataxia, peripheral neuropathy and hearing loss.
{ECO:0000269|PubMed:25491489}.
-!- DISEASE: Phosphoribosylpyrophosphate synthetase superactivity
(PRPS1 superactivity) [MIM:300661]: Familial disorder
characterized by excessive purine production, gout and uric acid
urolithiasis. {ECO:0000269|PubMed:7593598, ECO:0000269|Ref.12}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:17701900}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:17701896}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:20021999}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=A mutation in PRPS1 has been found in a patient with
a phenotype that bridges that of PRSPS1 superactivity and ARTS
syndrome with uric acid overproduction without gout but with
recurrent infections, sensorineural hearing loss and motor
neuropathy. The intermediate phenotype may be because Leu-142
variant affects both allosteric sites that are involved in
inhibition of PRPS1 and the ATP-binding site, which suggests that
this substitution can result both in a gain-of-function and loss-
of-function of PRPP synthetase. {ECO:0000269|PubMed:22246954}.
-!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X15331; CAA33386.1; -; mRNA.
EMBL; D00860; BAA00733.1; -; mRNA.
EMBL; AK297968; BAG60278.1; -; mRNA.
EMBL; AK312706; BAG35584.1; -; mRNA.
EMBL; AL137787; CAI42173.1; -; Genomic_DNA.
EMBL; AL772400; CAI42173.1; JOINED; Genomic_DNA.
EMBL; AL772400; CAI41098.1; -; Genomic_DNA.
EMBL; AL137787; CAI41098.1; JOINED; Genomic_DNA.
EMBL; CH471120; EAX02709.1; -; Genomic_DNA.
EMBL; CH471120; EAX02710.1; -; Genomic_DNA.
EMBL; CH471120; EAX02711.1; -; Genomic_DNA.
EMBL; BC001605; AAH01605.1; -; mRNA.
CCDS; CCDS14529.1; -. [P60891-1]
PIR; JX0159; KIHUR1.
RefSeq; NP_001191331.1; NM_001204402.1.
RefSeq; NP_002755.1; NM_002764.3. [P60891-1]
UniGene; Hs.56; -.
PDB; 2H06; X-ray; 2.20 A; A/B=1-318.
PDB; 2H07; X-ray; 2.20 A; A/B=1-318.
PDB; 2H08; X-ray; 2.50 A; A/B=1-318.
PDB; 2HCR; X-ray; 2.20 A; A/B=1-318.
PDB; 3EFH; X-ray; 2.60 A; A/B=1-318.
PDB; 3S5J; X-ray; 2.02 A; A/B=1-318.
PDB; 4F8E; X-ray; 2.27 A; A/B=1-318.
PDB; 4LYG; X-ray; 3.00 A; A/B=1-318.
PDB; 4LZN; X-ray; 2.14 A; A/B=1-318.
PDB; 4LZO; X-ray; 3.31 A; A/B=1-318.
PDB; 4M0P; X-ray; 2.11 A; A/B=1-318.
PDB; 4M0U; X-ray; 2.74 A; A/B=1-318.
PDBsum; 2H06; -.
PDBsum; 2H07; -.
PDBsum; 2H08; -.
PDBsum; 2HCR; -.
PDBsum; 3EFH; -.
PDBsum; 3S5J; -.
PDBsum; 4F8E; -.
PDBsum; 4LYG; -.
PDBsum; 4LZN; -.
PDBsum; 4LZO; -.
PDBsum; 4M0P; -.
PDBsum; 4M0U; -.
ProteinModelPortal; P60891; -.
SMR; P60891; -.
BioGrid; 111615; 53.
DIP; DIP-61999N; -.
IntAct; P60891; 18.
STRING; 9606.ENSP00000361512; -.
BindingDB; P60891; -.
ChEMBL; CHEMBL2638; -.
iPTMnet; P60891; -.
PhosphoSitePlus; P60891; -.
SwissPalm; P60891; -.
BioMuta; PRPS1; -.
DMDM; 46397477; -.
UCD-2DPAGE; P60891; -.
EPD; P60891; -.
MaxQB; P60891; -.
PaxDb; P60891; -.
PeptideAtlas; P60891; -.
PRIDE; P60891; -.
DNASU; 5631; -.
Ensembl; ENST00000372435; ENSP00000361512; ENSG00000147224. [P60891-1]
GeneID; 5631; -.
KEGG; hsa:5631; -.
UCSC; uc004ene.5; human. [P60891-1]
CTD; 5631; -.
DisGeNET; 5631; -.
EuPathDB; HostDB:ENSG00000147224.10; -.
GeneCards; PRPS1; -.
GeneReviews; PRPS1; -.
HGNC; HGNC:9462; PRPS1.
MalaCards; PRPS1; -.
MIM; 300661; phenotype.
MIM; 301835; phenotype.
MIM; 304500; phenotype.
MIM; 311070; phenotype.
MIM; 311850; gene.
neXtProt; NX_P60891; -.
OpenTargets; ENSG00000147224; -.
Orphanet; 1187; Lethal ataxia with deafness and optic atrophy.
Orphanet; 411536; Mild phosphoribosylpyrophosphate synthetase superactivity.
Orphanet; 411543; Severe phosphoribosylpyrophosphate synthetase superactivity.
Orphanet; 99014; X-linked Charcot-Marie-Tooth disease type 5.
Orphanet; 90625; X-linked non-syndromic sensorineural deafness type DFN.
PharmGKB; PA33817; -.
eggNOG; KOG1448; Eukaryota.
eggNOG; COG0462; LUCA.
GeneTree; ENSGT00550000074583; -.
HOGENOM; HOG000210451; -.
HOVERGEN; HBG001520; -.
InParanoid; P60891; -.
KO; K00948; -.
OMA; FGWARQD; -.
OrthoDB; EOG091G0ZG8; -.
PhylomeDB; P60891; -.
TreeFam; TF106366; -.
BioCyc; MetaCyc:HS07410-MONOMER; -.
BRENDA; 2.7.6.1; 2681.
Reactome; R-HSA-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
UniPathway; UPA00087; UER00172.
ChiTaRS; PRPS1; human.
EvolutionaryTrace; P60891; -.
GenomeRNAi; 5631; -.
PRO; PR:P60891; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000147224; -.
CleanEx; HS_PRPS1; -.
ExpressionAtlas; P60891; baseline and differential.
Genevisible; P60891; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:Ensembl.
GO; GO:0043531; F:ADP binding; IEA:Ensembl.
GO; GO:0016208; F:AMP binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
GO; GO:0019003; F:GDP binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IDA:UniProtKB.
GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; TAS:Reactome.
GO; GO:0006167; P:AMP biosynthetic process; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0046101; P:hypoxanthine biosynthetic process; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
GO; GO:0006144; P:purine nucleobase metabolic process; IMP:UniProtKB.
GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:UniProtKB.
GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; NAS:UniProtKB.
GO; GO:0034418; P:urate biosynthetic process; IMP:UniProtKB.
CDD; cd06223; PRTases_typeI; 1.
HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
InterPro; IPR000842; PRib_PP_synth_CS.
InterPro; IPR029099; Pribosyltran_N.
InterPro; IPR000836; PRibTrfase_dom.
InterPro; IPR029057; PRTase-like.
InterPro; IPR005946; Rib-P_diPkinase.
Pfam; PF14572; Pribosyl_synth; 1.
Pfam; PF13793; Pribosyltran_N; 1.
SUPFAM; SSF53271; SSF53271; 1.
TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PROSITE; PS00114; PRPP_SYNTHASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding;
Charcot-Marie-Tooth disease; Complete proteome; Deafness;
Direct protein sequencing; Disease mutation; Gout; Kinase; Magnesium;
Mental retardation; Metal-binding; Neurodegeneration; Neuropathy;
Non-syndromic deafness; Nucleotide biosynthesis; Nucleotide-binding;
Polymorphism; Reference proteome; Retinitis pigmentosa; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.8}.
CHAIN 2 318 Ribose-phosphate pyrophosphokinase 1.
/FTId=PRO_0000141071.
NP_BIND 96 101 ATP.
REGION 212 227 Binding of phosphoribosylpyrophosphate.
{ECO:0000255}.
METAL 128 128 Magnesium. {ECO:0000255}.
METAL 130 130 Magnesium. {ECO:0000255}.
METAL 139 139 Magnesium. {ECO:0000255}.
METAL 143 143 Magnesium. {ECO:0000255}.
BINDING 130 130 ATP.
VAR_SEQ 1 67 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056028.
VARIANT 16 16 S -> P (probable disease-associated
mutation found in patients with
phosphoribosyl pyrophosphate synthetase I
deficiency; dbSNP:rs869025594).
{ECO:0000269|PubMed:25491489}.
/FTId=VAR_072719.
VARIANT 43 43 E -> D (in CMTX5; dbSNP:rs80338731).
{ECO:0000269|PubMed:17701900}.
/FTId=VAR_036941.
VARIANT 52 52 D -> H (in PRPS1 superactivity;
dbSNP:rs137852542).
{ECO:0000269|PubMed:7593598}.
/FTId=VAR_016044.
VARIANT 65 65 D -> N (in DFNX1; dbSNP:rs180177151).
{ECO:0000269|PubMed:20021999}.
/FTId=VAR_063522.
VARIANT 87 87 A -> T (in DFNX1; dbSNP:rs180177152).
{ECO:0000269|PubMed:20021999}.
/FTId=VAR_063523.
VARIANT 114 114 N -> S (in PRPS1 superactivity;
dbSNP:rs137852540).
{ECO:0000269|PubMed:7593598,
ECO:0000269|Ref.12}.
/FTId=VAR_004163.
VARIANT 115 115 M -> T (in CMTX5; dbSNP:rs80338732).
{ECO:0000269|PubMed:17701900}.
/FTId=VAR_036942.
VARIANT 129 129 L -> I (in PRPS1 superactivity;
dbSNP:rs137852543).
{ECO:0000269|PubMed:7593598}.
/FTId=VAR_016045.
VARIANT 133 133 Q -> P (in ARTS; dbSNP:rs80338675).
{ECO:0000269|PubMed:17701896}.
/FTId=VAR_036943.
VARIANT 142 142 V -> L (probable disease-associated
mutation found in a patient with an
intermediate phenotype between ARTS and
PRPS1 superactivity; normal PRPP
synthetase activity in fibroblasts; loss
of activity in erythrocytes;
dbSNP:rs398122855).
{ECO:0000269|PubMed:22246954}.
/FTId=VAR_078489.
VARIANT 152 152 L -> P (in ARTS; dbSNP:rs80338676).
{ECO:0000269|PubMed:17701896}.
/FTId=VAR_036944.
VARIANT 183 183 D -> H (in PRPS1 superactivity;
dbSNP:rs137852541).
{ECO:0000269|PubMed:7593598,
ECO:0000269|Ref.12}.
/FTId=VAR_004164.
VARIANT 190 190 A -> V (in PRPS1 superactivity;
dbSNP:rs137852544).
{ECO:0000269|PubMed:7593598}.
/FTId=VAR_016046.
VARIANT 193 193 H -> Q (in PRPS1 superactivity;
dbSNP:rs137852545).
{ECO:0000269|PubMed:7593598}.
/FTId=VAR_016047.
VARIANT 203 203 D -> H (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036593.
VARIANT 219 219 V -> G (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036594.
VARIANT 231 231 H -> D (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036595.
VARIANT 290 290 I -> T (in DFNX1; dbSNP:rs180177153).
{ECO:0000269|PubMed:20021999}.
/FTId=VAR_063524.
VARIANT 306 306 G -> R (in DFNX1; dbSNP:rs180177154).
{ECO:0000269|PubMed:20021999}.
/FTId=VAR_063525.
MUTAGEN 132 132 S->A: Reduces catalytic activity.
{ECO:0000269|PubMed:16939420}.
MUTAGEN 132 132 S->F: No effect on catalytic activity.
{ECO:0000269|PubMed:16939420}.
MUTAGEN 144 144 N->H: No effect on catalytic activity.
{ECO:0000269|PubMed:16939420}.
MUTAGEN 146 146 Y->F: No effect on catalytic activity.
{ECO:0000269|PubMed:16939420}.
MUTAGEN 146 146 Y->M: Reduces catalytic activity.
{ECO:0000269|PubMed:16939420}.
CONFLICT 82 82 A -> G (in Ref. 3; BAG35584).
{ECO:0000305}.
CONFLICT 122 122 D -> G (in Ref. 3; BAG35584).
{ECO:0000305}.
CONFLICT 278 278 E -> G (in Ref. 3; BAG35584).
{ECO:0000305}.
STRAND 4 8 {ECO:0000244|PDB:3S5J}.
HELIX 14 22 {ECO:0000244|PDB:3S5J}.
STRAND 30 34 {ECO:0000244|PDB:3S5J}.
STRAND 36 38 {ECO:0000244|PDB:2H06}.
STRAND 40 44 {ECO:0000244|PDB:3S5J}.
STRAND 52 56 {ECO:0000244|PDB:3S5J}.
HELIX 63 79 {ECO:0000244|PDB:3S5J}.
STRAND 83 91 {ECO:0000244|PDB:3S5J}.
TURN 93 96 {ECO:0000244|PDB:3S5J}.
STRAND 101 104 {ECO:0000244|PDB:2H06}.
HELIX 108 119 {ECO:0000244|PDB:3S5J}.
STRAND 122 128 {ECO:0000244|PDB:3S5J}.
HELIX 132 137 {ECO:0000244|PDB:3S5J}.
STRAND 142 145 {ECO:0000244|PDB:3S5J}.
HELIX 148 158 {ECO:0000244|PDB:3S5J}.
HELIX 162 164 {ECO:0000244|PDB:3S5J}.
STRAND 166 171 {ECO:0000244|PDB:3S5J}.
HELIX 172 174 {ECO:0000244|PDB:3S5J}.
HELIX 175 185 {ECO:0000244|PDB:3S5J}.
STRAND 188 194 {ECO:0000244|PDB:3S5J}.
STRAND 205 209 {ECO:0000244|PDB:3S5J}.
STRAND 214 225 {ECO:0000244|PDB:3S5J}.
HELIX 227 238 {ECO:0000244|PDB:3S5J}.
STRAND 242 251 {ECO:0000244|PDB:3S5J}.
TURN 254 256 {ECO:0000244|PDB:4LYG}.
HELIX 257 263 {ECO:0000244|PDB:3S5J}.
STRAND 267 272 {ECO:0000244|PDB:3S5J}.
HELIX 278 282 {ECO:0000244|PDB:3S5J}.
STRAND 287 290 {ECO:0000244|PDB:3S5J}.
HELIX 293 305 {ECO:0000244|PDB:3S5J}.
HELIX 310 313 {ECO:0000244|PDB:3S5J}.
SEQUENCE 318 AA; 34834 MW; 46D017E969908BA0 CRC64;
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIGESVRG EDVYIVQSGC
GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG
ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLKWIRENIS EWRNCTIVSP DAGGAKRVTS
IADRLNVDFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG
ATRVYAILTH GIFSGPAISR INNACFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI
RRTHNGESVS YLFSHVPL


Related products :

Catalog number Product name Quantity
EIAAB32525 Homo sapiens,Human,Phosphoribosyl pyrophosphate synthase II,PPRibP,PRPS2,PRS-II,Ribose-phosphate pyrophosphokinase 2
EIAAB32523 Homo sapiens,Human,Phosphoribosyl pyrophosphate synthase I,PPRibP,PRPS1,PRS-I,Ribose-phosphate pyrophosphokinase 1
18-003-44258 Ribose-phosphate pyrophosphokinase 2 - EC 2.7.6.1; Phosphoribosyl pyrophosphate synthetase II; PRS-II; PPRibP Polyclonal 0.1 mg Protein A
18-003-44259 Ribose-phosphate pyrophosphokinase 2 - EC 2.7.6.1; Phosphoribosyl pyrophosphate synthetase II; PRS-II; PPRibP Polyclonal 0.1 mg Protein A
EIAAB32529 Homo sapiens,Human,Phosphoribosyl pyrophosphate synthase 1-like 1,Phosphoribosyl pyrophosphate synthase III,PRPS1L1,PRPS1-like 1,PRPS3,PRPSL,PRS-III,Ribose-phosphate pyrophosphokinase 3
EIAAB32522 Phosphoribosyl pyrophosphate synthase I,Prps1,PRS-I,Rat,Rattus norvegicus,Ribose-phosphate pyrophosphokinase 1
EIAAB32526 Mouse,Mus musculus,Phosphoribosyl pyrophosphate synthase II,Prps2,PRS-II,Ribose-phosphate pyrophosphokinase 2
EIAAB32521 Mouse,Mus musculus,Phosphoribosyl pyrophosphate synthase I,Prps1,PRS-I,Ribose-phosphate pyrophosphokinase 1
EIAAB32528 Phosphoribosyl pyrophosphate synthase II,Prps2,PRS-II,Rat,Rattus norvegicus,Ribose-phosphate pyrophosphokinase 2
EIAAB32524 Bos taurus,Bovine,Phosphoribosyl pyrophosphate synthase I,PRPS1,PRS-I,Ribose-phosphate pyrophosphokinase 1
EIAAB32527 Chicken,Gallus gallus,Phosphoribosyl pyrophosphate synthase II,PRPS2,PRS-II,RCJMB04_30f3,Ribose-phosphate pyrophosphokinase 2
PRPS2_RAT Rat ELISA Kit FOR Ribose-phosphate pyrophosphokinase 2 96T
CSB-EL018776RA Rat Ribose-phosphate pyrophosphokinase 1(PRPS1) ELISA kit 96T
CSB-EL018779RA Rat Ribose-phosphate pyrophosphokinase 2(PRPS2) ELISA kit 96T
G7945 Ribose-phosphate pyrophosphokinase 1 (PRPS1), Rat, ELISA Kit 96T
G7949 Ribose-phosphate pyrophosphokinase 2 (PRPS2), Rat, ELISA Kit 96T
PRPS2_MOUSE Mouse ELISA Kit FOR Ribose-phosphate pyrophosphokinase 2 96T
CSB-EL018779CH Chicken Ribose-phosphate pyrophosphokinase 2(PRPS2) ELISA kit 96T
G7950 Ribose-phosphate pyrophosphokinase 3 (PRPS1L1), Human, ELISA Kit 96T
G7948 Ribose-phosphate pyrophosphokinase 2 (PRPS2), Mouse, ELISA Kit 96T
CSB-EL018779HU Human Ribose-phosphate pyrophosphokinase 2(PRPS2) ELISA kit 96T
CSB-EL018777HU Human Ribose-phosphate pyrophosphokinase 3(PRPS1L1) ELISA kit 96T
CSB-EL018776BO Bovine Ribose-phosphate pyrophosphokinase 1(PRPS1) ELISA kit 96T
CSB-EL018776MO Mouse Ribose-phosphate pyrophosphokinase 1(PRPS1) ELISA kit 96T
CSB-EL018779MO Mouse Ribose-phosphate pyrophosphokinase 2(PRPS2) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur