PRPSAP2
Phosphoribosyl pyrophosphate synthase-associated protein 2
Also known as: KPRB_HUMAN, PAP41
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- O60256
- Gene
- PRPSAP2
- Ensembl
- ENSG00000141127
- Chromosome
- 17
- Canonical length
- 369 aa
- Protein class
- Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Cytosol
OverviewNCBI Gene
This gene encodes a protein that associates with the enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes the formation of phosphoribosylpyrophosphate which is a substrate for synthesis of purine and pyrimidine nucleotides, histidine, tryptophan and NAD. PRS exists as a complex with two catalytic subunits and two associated subunits. This gene encodes a non-catalytic associated subunit of PRS. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2011]
Canonical amino-acid sequenceUniProt
369 residues, UniProt reviewed canonical sequence.
>O60256|PRPSAP2
1 MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ VYQEPNRETR
61 VQIQESVRGK DVFIIQTVSK DVNTTIMELL IMVYACKTSC AKSIIGVIPY FPYSKQCKMR
121 KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV DNLRASPFLL QYIQEEIPDY
181 RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS
241 LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG
301 LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY
361 LFRNIGLDDLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PRPSAP2 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)
- 0.28
- Highest tissue expression
- 54 nTPM
Expression across tissuesHPA
Tissue
- tonsil: 54 nTPM
- lymph node: 48 nTPM
- retina: 43 nTPM
- cerebellum: 37 nTPM
- spinal cord: 36 nTPM
- testis: 30 nTPM
Single-cell type
- plasma cells: 90 nCPM
- late spermatids: 87 nCPM
- differentiating spermatogonia: 87 nCPM
- proximal tubule cells: 80 nCPM
- late primary spermatocytes: 77 nCPM
- rod photoreceptor cells: 71 nCPM
Immune cell
- naive CD4 T-cell: 46 nTPM
- memory B-cell: 44 nTPM
- naive B-cell: 40 nTPM
- NK-cell: 37 nTPM
- T-reg: 36 nTPM
- naive CD8 T-cell: 35 nTPM
Brain region
- cerebellum: 78 nTPM
- white matter: 73 nTPM
- medulla oblongata: 56 nTPM
- spinal cord: 53 nTPM
- hypothalamus: 51 nTPM
- hippocampal formation: 50 nTPM
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)
- 0.77
- gnomAD pLI
- 0
- gnomAD missense Z
- 2.6
- DepMap mean gene effect
- 0.03
- DepMap dependency class
- none
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
- bone development
- nucleobase-containing compound metabolic process
- purine nucleotide biosynthetic process
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PRPSAP2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PRPSAP2 as an antibody target. Whether an autoantibody or antibody against PRPSAP2 could matter depends on whether native PRPSAP2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PRPSAP2 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label PRPSAP2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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