PRPS2

Protein identityUniProt · HPA

UniProt accession

P11908

Gene

PRPS2

Ensembl

ENSG00000101911

Chromosome

X

Canonical length

318 aa

Protein class

Enzymes, Metabolic proteins, Predicted intracellular proteins

Subcellular location

Nuclear speckles,Vesicles,Basal body

Quaternary structure

Homodimer

OverviewNCBI Gene

This gene encodes a phosphoribosyl pyrophosphate synthetase that plays a central role in the synthesis of purines and pyrimidines. The encoded protein catalyzes the synthesis of 5-phosphoribosyl 1-pyrophosphate from ATP and D-ribose 5-phosphate. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Mar 2010]

Canonical amino-acid sequenceUniProt

318 residues, UniProt reviewed canonical sequence.

>P11908|PRPS2
     1  MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC
    61  GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG
   121  ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLQWIRENIA EWKNCIIVSP DAGGAKRVTS
   181  IADRLNVEFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG
   241  ATKVYAILTH GIFSGPAISR INNAAFEAVV VTNTIPQEDK MKHCTKIQVI DISMILAEAI
   301  RRTHNGESVS YLFSHVPL

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PRPS2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.24

Highest tissue expression

171 nTPM

Expression across tissuesHPA

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.34

gnomAD pLI

0.94

gnomAD missense Z

3.05

DepMap mean gene effect

0.12

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• 5-phosphoribose 1-diphosphate biosynthetic process
• nucleobase-containing compound metabolic process
• pentose-phosphate shunt
• purine nucleotide biosynthetic process
• ribonucleoside monophosphate biosynthetic process

Molecular functions

• ATP binding
• identical protein binding
• kinase activity
• magnesium ion binding
• protein homodimerization activity
• ribose phosphate diphosphokinase activity

Cellular components

• cytoplasm
• cytosol

Protein domainsUniProt · Pfam · InterPro

• Phosphoribosyltransferase domain
• Phosphoribosyl pyrophosphate synthetase, conserved site
• Ribose-phosphate pyrophosphokinase
• Phosphoribosyltransferase-like
• Ribose-phosphate pyrophosphokinase, N-terminal domain
• Ribose-phosphate pyrophosphokinase, bacterial-type
• N-terminal domain of ribose phosphate pyrophosphokinase
• Phosphoribosyl synthetase-associated domain

KeywordsUniProt

• ATP-binding
• Kinase
• Magnesium
• Metal-binding
• Nucleotide biosynthesis
• Nucleotide-binding
• Transferase

InteractionsUniProt · HPA

Protein binding partners of PRPS2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• PARP1
• PRPS1
• PRPSAP1