PIN1
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Also known as: dod, PIN1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q13526
- Gene
- PIN1
- Ensembl
- ENSG00000127445
- Chromosome
- 19
- Canonical length
- 163 aa
- Protein class
- Cancer-related genes, Enzymes, Metabolic proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Cytosol
OverviewNCBI Gene
Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. This gene encodes one of the PPIases, which specifically binds to phosphorylated ser/thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. The conformational regulation catalyzed by this PPIase has a profound impact on key proteins involved in the regulation of cell growth, genotoxic and other stress responses, the immune response, induction and maintenance of pluripotency, germ cell development, neuronal differentiation, and survival. This enzyme also plays a key role in the pathogenesis of Alzheimer's disease and many cancers. Multiple alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Jun 2011]
Canonical amino-acid sequenceUniProt
163 residues, UniProt reviewed canonical sequence.
>Q13526|PIN1
1 MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL
61 LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG
121 DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTELocalizationUniProt · AlphaFold · HPA
Whether an antibody against PIN1 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)
- 0.31
- Highest tissue expression
- 256 nTPM
Expression across tissuesHPA
Tissue
- cerebral cortex: 256 nTPM
- amygdala: 194 nTPM
- hippocampal formation: 181 nTPM
- basal ganglia: 175 nTPM
- midbrain: 170 nTPM
- hypothalamus: 166 nTPM
Single-cell type
- late spermatids: 1,255 nCPM
- late primary spermatocytes: 339 nCPM
- early spermatids: 277 nCPM
- oocytes: 235 nCPM
- esophageal suprabasal cells: 207 nCPM
- decidual stromal cells: 191 nCPM
Immune cell
- eosinophil: 399 nTPM
- plasmacytoid DC: 318 nTPM
- basophil: 282 nTPM
- T-reg: 246 nTPM
- total PBMC: 215 nTPM
- intermediate monocyte: 202 nTPM
Brain region
- cerebral cortex: 199 nTPM
- pons: 190 nTPM
- medulla oblongata: 178 nTPM
- hypothalamus: 160 nTPM
- basal ganglia: 154 nTPM
- midbrain: 147 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)
- 0.54
- gnomAD pLI
- 0.74
- gnomAD missense Z
- 1.35
- DepMap mean gene effect
- 0.02
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cellular response to hypoxia
- negative regulation of amyloid-beta formation
- negative regulation of brown fat cell differentiation
- negative regulation of cell motility
- negative regulation of ERK1 and ERK2 cascade
- negative regulation of protein catabolic process
- negative regulation of SMAD protein signal transduction
- negative regulation of transforming growth factor beta receptor signaling pathway
- neuron differentiation
- positive regulation of canonical Wnt signaling pathway
- positive regulation of protein phosphorylation
- positive regulation of transcription by RNA polymerase II
- protein destabilization
- protein peptidyl-prolyl isomerization
- protein stabilization
- protein targeting to mitochondrion
- regulation of cytokinesis
- regulation of gene expression
- regulation of mitotic nuclear division
- regulation of protein localization to nucleus
- regulation of protein stability
- response to hypoxia
- Rho protein signal transduction
- synapse organization
Molecular functions
- beta-catenin binding
- cytoskeletal motor activity
- GTPase activating protein binding
- mitogen-activated protein kinase kinase binding
- peptidyl-prolyl cis-trans isomerase activity
- phosphoprotein binding
- phosphoserine residue binding
- phosphothreonine residue binding
- tau protein binding
- ubiquitin ligase activator activity
- cis-trans isomerase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Peptidyl-prolyl cis-trans isomerase, PpiC-type
- WW domain
- WW domain superfamily
- Peptidyl-prolyl cis-trans isomerase domain superfamily
- WW domain
- Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved site
- Peptidyl-prolyl cis-trans isomerase Pin1
- PPIC-type PPIASE domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PIN1 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 PIN1 as an antibody target. Whether an autoantibody or antibody against PIN1 could matter depends on whether native PIN1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PIN1 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 PIN1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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