P60891 (PRPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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	Magnesium.
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 structure	Homodimer. The active form is probably an hexamer composed of 3 homodimers. Ref.10
Involvement in disease	Defects in PRPS1 are the cause of phosphoribosylpyrophosphate synthetase superactivity (PRPS1 superactivity) [MIM:300661]; also known as PRPS-related gout. It is a familial disorder characterized by excessive purine production, gout and uric acid urolithiasis. Defects in PRPS1 are the cause of Charcot-Marie-Tooth disease X-linked recessive type 5 (CMTX5) [MIM:311070]; also known as optic atrophy-polyneuropathy-deafness or Rosenberg-Chutorian syndrome. CMTX5 is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. 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. Ref.15 Defects in PRPS1 are the cause of ARTS syndrome (ARTS) [MIM:301835]; also known as fatal ataxia X-linked with deafness and loss of vision. ARTS is 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. Ref.14 Defects in PRPS1 are the cause of deafness X-linked type 1 (DFNX1) [MIM:304500]; also known as congenital sensorineural deafness X-linked 2 (DFN2). It is a form of deafness characterized by progressive, severe-to-profound sensorineural hearing loss in males. Females manifest mild to moderate hearing loss. Ref.16
Sequence similarities	Belongs to the ribose-phosphate pyrophosphokinase family.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Coding sequence diversity	Polymorphism
Disease	Charcot-Marie-Tooth disease Deafness Disease mutation Gout Neuropathy Non-syndromic deafness
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	5-phosphoribose 1-diphosphate biosynthetic process Traceable author statement. Source: Reactome hypoxanthine biosynthetic process Inferred from mutant phenotype Ref.14. Source: UniProtKB nervous system development Inferred from mutant phenotype Ref.15. Source: UniProtKB nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine nucleotide biosynthetic process Inferred from mutant phenotype. Source: UniProtKB pyrimidine nucleotide biosynthetic process Non-traceable author statement Ref.14. Source: UniProtKB ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro urate biosynthetic process Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from direct assay Ref.10. Source: UniProtKB kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from physical interaction Ref.10. Source: UniProtKB ribose phosphate diphosphokinase activity Inferred from direct assay Ref.10Ref.15. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 318

317

Ribose-phosphate pyrophosphokinase 1

PRO_0000141071

Regions

Nucleotide binding

96 – 101

6

ATP

Region

212 – 227

16

Binding of phosphoribosylpyrophosphate Potential

Sites

Metal binding

128

1

Magnesium Potential

Metal binding

130

1

Magnesium Potential

Metal binding

139

1

Magnesium Potential

Metal binding

143

1

Magnesium Potential

Binding site

130

1

ATP

Natural variations

Natural variant

43

1

E → D in CMTX5. Ref.15

VAR_036941

Natural variant

52

1

D → H in PRPS1 superactivity. Ref.12

VAR_016044

Natural variant

65

1

D → N in DFNX1. Ref.16

VAR_063522

Natural variant

87

1

A → T in DFNX1. Ref.16

VAR_063523

Natural variant

114

1

N → S in PRPS1 superactivity. Ref.11 Ref.12

VAR_004163

Natural variant

115

1

M → T in CMTX5. Ref.15

VAR_036942

Natural variant

129

1

L → I in PRPS1 superactivity. Ref.12

VAR_016045

Natural variant

133

1

Q → P in ARTS. Ref.14

VAR_036943

Natural variant

152

1

L → P in ARTS. Ref.14

VAR_036944

Natural variant

183

1

D → H in PRPS1 superactivity. Ref.11 Ref.12

VAR_004164

Natural variant

190

1

A → V in PRPS1 superactivity. Ref.12

VAR_016046

Natural variant

193

1

H → Q in PRPS1 superactivity. Ref.12

VAR_016047

Natural variant

203

1

D → H in a breast cancer sample; somatic mutation. Ref.13

VAR_036593

Natural variant

219

1

V → G in a breast cancer sample; somatic mutation. Ref.13

VAR_036594

Natural variant

231

1

H → D in a colorectal cancer sample; somatic mutation. Ref.13

VAR_036595

Natural variant

290

1

I → T in DFNX1. Ref.16

VAR_063524

Natural variant

306

1

G → R in DFNX1. Ref.16

VAR_063525

Experimental info

Mutagenesis

132

1

S → A: Reduces catalytic activity. Ref.10

Mutagenesis

132

1

S → F: No effect on catalytic activity. Ref.10

Mutagenesis

144

1

N → H: No effect on catalytic activity. Ref.10

Mutagenesis

146

1

Y → F: No effect on catalytic activity. Ref.10

Mutagenesis

146

1

Y → M: Reduces catalytic activity. Ref.10

Secondary structure

1

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318

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

14 – 23

10

Beta strand

30 – 34

5

Beta strand

36 – 38

3

Beta strand

40 – 44

5

Beta strand

52 – 56

5

Helix

63 – 78

16

Turn

79 – 81

3

Beta strand

82 – 91

10

Turn

93 – 96

4

Beta strand

101 – 104

4

Helix

108 – 119

12

Beta strand

123 – 128

6

Helix

132 – 137

6

Beta strand

142 – 145

4

Helix

148 – 156

9

Helix

162 – 164

3

Beta strand

166 – 171

6

Helix

172 – 174

3

Helix

175 – 185

11

Beta strand

188 – 194

7

Beta strand

205 – 209

5

Beta strand

214 – 225

12

Helix

227 – 238

12

Beta strand

241 – 251

11

Helix

257 – 263

7

Beta strand

266 – 272

7

Helix

278 – 283

6

Beta strand

287 – 290

4

Helix

293 – 305

13

Helix

310 – 312

3

Sequences

	Sequence		Length	Mass (Da)
	P60891 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 46D017E969908BA0	FASTA	318	34,834
	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

References

	« Hide 'large scale' referencesShow '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: 2155397] [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: 1650777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 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(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[6]	"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: 1314091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-41.
[7]	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, LACK OF N-TERMINAL ACETYLATION, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[8]	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.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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: 16939420] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH AMP, SUBUNIT, MUTAGENESIS OF SER-132; ASN-144 AND TYR-146.
[11]	"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.
[12]	"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: 7593598] [Abstract] Cited for: VARIANTS PRPS1 SUPERACTIVITY HIS-52; SER-114; ILE-129; HIS-183; VAL-190 AND GLN-193.
[13]	"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. , 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: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-203; GLY-219 AND ASP-231.
[14]	"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: 17701896] [Abstract] Cited for: VARIANTS ARTS PRO-133 AND PRO-152.
[15]	"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: 17701900] [Abstract] Cited for: VARIANTS CMTX5 ASP-43 AND THR-115.
[16]	"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: 20021999] [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.
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.

IPI

IPI00219616.

PIR

KIHUR1. JX0159.

RefSeq

NP_001191331.1. NM_001204402.1.
NP_002755.1. NM_002764.3.

UniGene

Hs.56.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P60891.

SMR

P60891. Positions 3-317.

ModBase

Search...

Protein-protein interaction databases

IntAct

P60891. 4 interactions.

STRING

P60891.

PTM databases

PhosphoSite

P60891.

Polymorphism databases

DMDM

46397477.

2D gel databases

UCD-2DPAGE

P60891.

Proteomic databases

PRIDE

P60891.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000372435; ENSP00000361512; ENSG00000147224.

GeneID

5631.

KEGG

hsa:5631.

UCSC

uc004ene.2. human.

Organism-specific databases

CTD

5631.

GeneCards

GC0XP106871.

H-InvDB

HIX0016976.

HGNC

HGNC:9462. PRPS1.

MIM

300661. phenotype.
301835. phenotype.
304500. phenotype.
311070. phenotype.
311850. gene.

neXtProt

NX_P60891.

Orphanet

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.

PharmGKB

PA33817.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16107.

HOGENOM

HBG519284.

HOVERGEN

HBG001520.

InParanoid

P60891.

OMA

TIPQDGH.

OrthoDB

EOG4SQWX5.

PhylomeDB

P60891.

Enzyme and pathway databases

Reactome

REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P60891.

Bgee

P60891.

CleanEx

HS_PRPS1.

Genevestigator

P60891.

GermOnline

ENSG00000147224. Homo sapiens.

Family and domain databases

InterPro

IPR000842. PRib_PP_synth_CS.
IPR000836. PRibTrfase.
IPR005946. Rib-P_diPkinase.
[Graphical view]

KO

K00948.

Pfam

PF00156. Pribosyltran. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01251. RibP_PPkin. 1 hit.

PROSITE

PS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

21886.

SOURCE

Search...

Entry information

Entry name

PRPS1_HUMAN

Accession

Primary (citable) accession number: P60891
Secondary accession number(s): B1ALA8, D3DUX6, P09329

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.