PPIL1
Peptidyl-prolyl cis-trans isomerase-like 1
Also known as: CYPL1, PPIL1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9Y3C6
- Gene
- PPIL1
- Ensembl
- ENSG00000137168
- Chromosome
- 6
- Canonical length
- 166 aa
- Protein class
- Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins
- Subcellular location
- Nucleoli
OverviewNCBI Gene
This gene is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a highly conserved, ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. Based on similarity to other PPIases, this protein could accelerate the folding of proteins and might catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
166 residues, UniProt reviewed canonical sequence.
>Q9Y3C6|PPIL1
1 MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF
61 MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ
121 WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PPIL1 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)
- 0.26
- Highest tissue expression
- 41 nTPM
Expression across tissuesHPA
Tissue
- heart muscle: 41 nTPM
- choroid plexus: 32 nTPM
- thyroid gland: 31 nTPM
- retina: 27 nTPM
- basal ganglia: 26 nTPM
- hypothalamus: 25 nTPM
Single-cell type
- oocytes: 88 nCPM
- migrating cytotrophoblasts: 82 nCPM
- extravillous trophoblasts: 75 nCPM
- cytotrophoblasts: 71 nCPM
- differentiating spermatogonia: 69 nCPM
- esophageal basal cells: 52 nCPM
Immune cell
- MAIT T-cell: 20 nTPM
- naive CD8 T-cell: 16 nTPM
- gdT-cell: 15 nTPM
- memory CD8 T-cell: 14 nTPM
- naive CD4 T-cell: 14 nTPM
- memory CD4 T-cell: 12 nTPM
Brain region
- hypothalamus: 30 nTPM
- spinal cord: 27 nTPM
- choroid plexus: 27 nTPM
- medulla oblongata: 26 nTPM
- pons: 26 nTPM
- cerebellum: 24 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about PPIL1.
Disease | AllUniProt
Conditions PPIL1 is implicated in, by any mechanism.
- Pontocerebellar hypoplasia 14 (PCH14) MIM:619301
Disease | GeneticClinVar
10 pathogenic / likely-pathogenic of 43 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Congenital pontocerebellar hypoplasia
- Pontocerebellar hypoplasia, type 14
- Neurodevelopmental disorder
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)
- 0.81
- gnomAD pLI
- 0.12
- gnomAD missense Z
- 0.58
- DepMap mean gene effect
- -0.65
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 8% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- embryonic brain development
- mRNA splicing, via spliceosome
- protein folding
- protein peptidyl-prolyl isomerization
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain
- Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site
- Cyclophilin-type peptidyl-prolyl cis-trans isomerase
- Cyclophilin-like domain superfamily
- Cyclophilin-type peptidyl-prolyl cis-trans isomerase, cyclophilin A-like
- Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PPIL1 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 PPIL1 as an antibody target. Whether an autoantibody or antibody against PPIL1 could matter depends on whether native PPIL1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PPIL1 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 PPIL1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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