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P11908 (PRPS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribose-phosphate pyrophosphokinase 2

EC=2.7.6.1
Alternative name(s):
PPRibP
Phosphoribosyl pyrophosphate synthase II
Short name=PRS-II
Gene names
Name:PRPS2
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. Competitively or non-competitively inhibited by ADP, 2,3-bisphosphoglyceride or GDP. 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 By similarity.

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Sequence caution

The sequence AAH30019.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process5-phosphoribose 1-diphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

AMP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing compound metabolic process

Traceable author statement Ref.1. Source: ProtInc

organ regeneration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentribose phosphate diphosphokinase complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionADP binding

Inferred from electronic annotation. Source: Ensembl

AMP binding

Inferred from electronic annotation. Source: Ensembl

ATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GDP binding

Inferred from electronic annotation. Source: Ensembl

carbohydrate binding

Inferred from electronic annotation. Source: Ensembl

kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: Ensembl

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

ribose phosphate diphosphokinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11908-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P11908-2)

The sequence of this isoform differs from the canonical sequence as follows:
     102-102: K → KVGE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 318317Ribose-phosphate pyrophosphokinase 2 HAMAP-Rule MF_00583_B
PRO_0000141074

Regions

Nucleotide binding96 – 1016ATP By similarity
Region212 – 22716Binding of phosphoribosylpyrophosphate Potential

Sites

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

Natural variations

Alternative sequence1021K → KVGE in isoform 2.
VSP_027769

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 72A2873408250C31

FASTA31834,769
        10         20         30         40         50         60 
MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC 

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

       130        140        150        160        170        180 
ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLQWIRENIA EWKNCIIVSP DAGGAKRVTS 

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

       250        260        270        280        290        300 
ATKVYAILTH GIFSGPAISR INNAAFEAVV VTNTIPQEDK MKHCTKIQVI DISMILAEAI 

       310 
RRTHNGESVS YLFSHVPL 

« Hide

Isoform 2 [UniParc].

Checksum: EDD88B9D33A55A37
Show »

FASTA32135,054

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of human cDNA for phosphoribosyl pyrophosphate synthetase subunit II."
Iizasa T., Taira M., Shimada H., Ishijima S., Tatibana M.
FEBS Lett. 244:47-50(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[2]"Deduced amino acid sequence from human phosphoribosylpyrophosphate synthetase subunit II cDNA."
Iizasa T., Taira M., Shimada H., Tatibana M.
Adv. Exp. Med. Biol. 253A:519-523(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[3]"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] (ISOFORMS 1 AND 2).
Tissue: Testis and Uterus.
[4]"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 [GENOMIC DNA] OF 1-40.
Tissue: Leukocyte.
[5]Bienvenut W.V., Calvo F., Bensaad K., Vousden K.H., Matallanas D., Cooper W.N., Kolch W., Lourenco F., Olson M.F.
Submitted (DEC-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-29; 34-49; 85-96; 164-196; 205-214; 244-282 AND 287-318, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma, Mammary carcinoma and Osteosarcoma.
[6]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00971 mRNA. Translation: CAA68785.1.
BC030019 mRNA. Translation: AAH30019.2. Different initiation.
BC040483 mRNA. Translation: AAH40483.3.
BC110875 mRNA. Translation: AAI10876.2.
BC119662 mRNA. Translation: AAI19663.1.
BC119663 mRNA. Translation: AAI19664.1.
D28134 Genomic DNA. Translation: BAA05676.1.
CCDSCCDS14150.1. [P11908-1]
CCDS43918.1. [P11908-2]
PIRKIHUR2. S02778.
RefSeqNP_001034180.1. NM_001039091.2. [P11908-2]
NP_002756.1. NM_002765.4. [P11908-1]
UniGeneHs.654581.

3D structure databases

ProteinModelPortalP11908.
SMRP11908. Positions 3-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111617. 9 interactions.
IntActP11908. 1 interaction.
MINTMINT-5000929.
STRING9606.ENSP00000381504.

PTM databases

PhosphoSiteP11908.

Polymorphism databases

DMDM125583.

2D gel databases

REPRODUCTION-2DPAGEIPI00219617.
P11908.

Proteomic databases

MaxQBP11908.
PaxDbP11908.
PRIDEP11908.

Protocols and materials databases

DNASU5634.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380668; ENSP00000370043; ENSG00000101911. [P11908-1]
ENST00000398491; ENSP00000381504; ENSG00000101911. [P11908-2]
GeneID5634.
KEGGhsa:5634.
UCSCuc004cva.3. human. [P11908-2]
uc004cvb.3. human. [P11908-1]

Organism-specific databases

CTD5634.
GeneCardsGC0XP012719.
HGNCHGNC:9465. PRPS2.
MIM311860. gene.
neXtProtNX_P11908.
PharmGKBPA33820.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0462.
HOGENOMHOG000210451.
HOVERGENHBG001520.
KOK00948.
OMATINDHLM.
PhylomeDBP11908.
TreeFamTF106366.

Enzyme and pathway databases

BioCycMetaCyc:HS02317-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00087; UER00172.

Gene expression databases

ArrayExpressP11908.
BgeeP11908.
CleanExHS_PRPS2.
GenevestigatorP11908.

Family and domain databases

Gene3D3.40.50.2020. 2 hits.
HAMAPMF_00583_B. RibP_PPkinase_B.
InterProIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
TIGRFAMsTIGR01251. ribP_PPkin. 1 hit.
PROSITEPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi5634.
NextBio21892.
PROP11908.
SOURCESearch...

Entry information

Entry namePRPS2_HUMAN
AccessionPrimary (citable) accession number: P11908
Secondary accession number(s): Q0VDH9 expand/collapse secondary AC list , Q0VDI0, Q15245, Q2TAK7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 157 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome X

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