PRNP | ENSG00000171867 | NCBI 5621

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Network Configuration

Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.

Context Genes (max 20):

Interaction Source:

Pathway Categories (for ONTOLOGY source):

Baseline Cell Type:

Baseline Cell Context(s): Comma-separated if multiple.

Target Cell Type:

Target Cell Context(s): Comma-separated if multiple.

Legend:

Query Gene
Node Color (Target Cell CSI, relative to current network):
- Very High
- High
- Medium
- Low
- Very Low
- CSI N/A
Node Size: Proportional to Target Cell CSI magnitude
STRING PPI Edge
Shared Pathway Edge (ONTOLOGY)

Loading network (please wait)...

Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

Description
Proteins

## Summary [PRNP](/details-gene/5621) encodes the major prion protein, a glycosylphosphatidylinositol (GPI)-anchored cell surface protein most famously implicated in the pathogenesis of fatal neurodegenerative transmissible spongiform encephalopathies (TSEs), or prion diseases. These include Creutzfeldt-Jakob disease ([176640](https://omim.org/entry/176640)), Gerstmann-Sträussler-Scheinker disease ([137440](https://omim.org/entry/137440)), and fatal familial insomnia ([600072](https://omim.org/entry/600072)). While its misfolded, pathogenic isoform is the causative agent of these conditions, the native protein is expressed in a wide range of tissues and appears to play diverse physiological roles. Expression data indicates significant roles for [PRNP](/details-gene/5621) in both the central nervous system, particularly in various cortical neuron subtypes, and the adaptive immune system, with notably high significance in memory and cytotoxic T lymphocytes. Its molecular functions are broad, encompassing copper ion homeostasis, signal transduction, neuroprotection, and regulation of synaptic processes. ## Cellular Roles and Expression Landscape The expression profile of [PRNP](/details-gene/5621) highlights its importance in two distinct biological systems: the immune system and the central nervous system. **Overall**, the gene shows the highest significance in specific subsets of the adaptive immune system. It is a particularly strong marker for [central memory CD8-positive, alpha-beta T cell](/details-cell/CL0000907)s and [CD8-positive, alpha-beta cytotoxic T cell](/details-cell/CL0000794)s. Its presence in [group 3 innate lymphoid cell](/details-cell/CL0001071)s and [activated CD8-positive, alpha-beta T cell, human](/details-cell/CL0001049)s further underscores a consistent role within the lymphocytic lineage, potentially modulating cell activation and long-term memory. Concurrently, [PRNP](/details-gene/5621) is highly significant across a range of neuronal cell types, consistent with its well-established role in neurobiology. It is prominently expressed in multiple cortical interneuron populations, including [sncg GABAergic cortical interneuron](/details-cell/CL4023015)s, [lamp5 GABAergic cortical interneuron](/details-cell/CL4023011)s, and [sst GABAergic cortical interneuron](/details-cell/CL4023017)s. Its expression is also notable in excitatory neurons, such as [L2/3 intratelencephalic projecting glutamatergic neuron](/details-cell/CL4030059)s. This broad neuronal expression pattern suggests a fundamental role in maintaining neuronal health and function. Beyond these primary domains, [PRNP](/details-gene/5621) shows moderate significance in other cell types, including [skin fibroblast](/details-cell/CL0002620)s and [endothelial cell of lymphatic vessel](/details-cell/CL0002138)s, indicating a broader, though less pronounced, role in stromal and vascular tissues. ## Pathways and Molecular Function Functional annotation reveals the diverse activities of the [PRNP](/details-gene/5621) protein, extending far beyond its role in prion pathology. Its involvement in nervous system development and function is strongly supported by its association with Reactome pathways like `[Axon guidance](/details-gene/R-HSA-422475)` and `[Nervous system development](/details-gene/R-HSA-9675108)`. This is consistent with GO annotations related to synaptic plasticity and maintenance, such as `[dendritic spine maintenance](/details-cell/GO:0097062)` and `[negative regulation of long-term synaptic potentiation](/details-cell/GO:1900272)`. In line with its high expression in T cells, [PRNP](/details-gene/5621) is implicated in the negative regulation of immune responses. GO terms such as `[negative regulation of activated t cell proliferation](/details-cell/GO:0046007)`, `[negative regulation of t cell receptor signaling pathway](/details-cell/GO:0050860)`, and negative regulation of interleukin production (`[GO:0032700](/details-cell/GO:0032700)`, `[GO:0032703](/details-cell/GO:0032703)`) suggest it may function as a molecular brake to control T cell-mediated immunity. At the molecular level, [PRNP](/details-gene/5621) exhibits multiple binding activities. Its well-documented ability to bind metal ions is reflected in the `[copper ion binding](/details-cell/GO:0005507)` annotation. Furthermore, its capacity for `[amyloid-beta binding](/details-cell/GO:0001540)` suggests a potential role in the pathology of Alzheimer's disease, linking it to a broader class of protein misfolding disorders. The protein's function as a scaffold or adaptor is indicated by its involvement in `[protein homooligomerization](/details-cell/GO:0051260)` and its `[molecular adaptor activity](/details-cell/GO:0060090)`, enabling it to participate in diverse signaling complexes at the cell surface. ## Research Directions The dual prominence of [PRNP](/details-gene/5621) in both the immune and nervous systems, coupled with its extensive functional annotations, opens several avenues for future investigation. Understanding how a single protein executes distinct functions in such different cellular contexts is a key challenge. **Proposed Hypotheses:** 1. Given its high expression in memory and cytotoxic T cells and its annotated role in negative regulation of T cell signaling, **`[PRNP](/details-gene/5621)` functions as an inhibitory co-receptor on CD8+ T cells, modulating TCR signaling strength to prevent excessive activation and maintain immune homeostasis.** Loss of [PRNP](/details-gene/5621) on T cells may lead to a lower threshold for activation and a heightened inflammatory response. 2. The pathogenic conversion of the prion protein in neurons disrupts not only cell-autonomous functions but also critical neuro-immune crosstalk. **The native form of `[PRNP](/details-gene/5621)` expressed on neurons is essential for maintaining synaptic integrity by mediating signals from CNS-resident immune cells; this protective interaction is lost upon pathogenic misfolding, accelerating neurodegeneration.** **Experimental Approach:** To test the first hypothesis regarding [PRNP](/details-gene/5621)'s role in T cell regulation, a definitive experiment would involve the specific deletion of [PRNP](/details-gene/5621) in human primary CD8+ T cells using CRISPR-Cas9. These `[PRNP](/details-gene/5621)`-knockout T cells, alongside unmodified controls, could be stimulated *in vitro* via their T cell receptor (TCR). Key readouts would include: (i) proliferation rates, assessed by cell trace violet dilution via flow cytometry; (ii) effector cytokine production (e.g., IFN-gamma, TNF-alpha), measured by ELISA and intracellular staining; and (iii) activation of proximal TCR signaling components (e.g., phosphorylation of LCK, ZAP70, and SLP-76), analyzed by Phosflow or Western blot. An observed hyper-responsive phenotype in knockout cells would support the hypothesis that [PRNP](/details-gene/5621) is a negative regulator of T cell function. **Therapeutic Potential:** As the central pathogenic agent in TSEs, [PRNP](/details-gene/5621) is a primary therapeutic target. The therapeutic strategy is focused on **inhibition** of its pathogenic conversion or **depletion** of the protein altogether. Several approaches are being explored, including antisense oligonucleotides (ASOs) designed to reduce `[PRNP](/details-gene/5621)` mRNA levels, which has shown promise in animal models. Other strategies include small molecules that stabilize the native protein's conformation or monoclonal antibodies that bind the cellular prion protein and prevent its recruitment into pathogenic aggregates. Given the protein's physiological roles, a reduction rather than complete ablation may represent a safer long-term therapeutic strategy.

Disclaimer: This in-silico analysis is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Alternative prion protein
Major prion protein

Genular Protein ID: 705335050

Symbol: APRIO_HUMAN

Name: Alternative prion protein

UniProtKB Accession Codes:

F7VJQ1

Database IDs:

Citations:

PubMed ID: 11780052

Title: The DNA sequence and comparative analysis of human chromosome 20.

PubMed ID: 11780052

DOI: 10.1038/414865a

PubMed ID: 21478263

Title: An overlapping reading frame in the PRNP gene encodes a novel polypeptide distinct from the prion protein.

PubMed ID: 21478263

DOI: 10.1096/fj.10-173815

Sequence Information:

Length: 73
Mass: 8691
Checksum: 4360C28341A4CA52
Sequence:

MEHWGQPIPG AGQPWRQPLP TSGRWWLGAA SWWWLGAASW WWLGAAPWWW LGTASWWWLG 
SRRWHPQSVE QAE

Genular Protein ID: 44896081

Symbol: PRIO_HUMAN

Name: Major prion protein

UniProtKB Accession Codes:

P04156 O60489 P78446 Q15216 Q15221 Q27H91 Q5QPB4 Q8TBG0 Q96E70 Q9UP19

Database IDs:

Citations:

PubMed ID: 3755672

Title: Molecular cloning of a human prion protein cDNA.

PubMed ID: 3755672

DOI: 10.1089/dna.1986.5.315

PubMed ID: 1678248

Title: Genomic structure of the human prion protein gene.

PubMed ID: 1678248

PubMed ID: 9799790

Title: Complete genomic sequence and analysis of the prion protein gene region from three mammalian species.

PubMed ID: 9799790

DOI: 10.1101/gr.8.10.1022

PubMed ID: 10581485

Title: Novel PRNP sequence variant associated with familial encephalopathy.

PubMed ID: 10581485

DOI: 10.1002/(sici)1096-8628(19991215)88:6<653::aid-ajmg14>3.0.co;2-e

PubMed ID: 11780052

Title: The DNA sequence and comparative analysis of human chromosome 20.

PubMed ID: 11780052

DOI: 10.1038/414865a

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 3014653

Title: Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications.

PubMed ID: 3014653

DOI: 10.1126/science.3014653

PubMed ID: 1363802

Title: Deletion in the prion protein gene in a demented patient.

PubMed ID: 1363802

DOI: 10.1093/hmg/1.6.443

PubMed ID: 9384372

Title: A prion-linked psychiatric disorder.

PubMed ID: 9384372

DOI: 10.1038/36757

PubMed ID: 7485229

Title: SSCP analysis and sequencing of the human prion protein gene (PRNP) detects two different 24 bp deletions in an atypical Alzheimer's disease family.

PubMed ID: 7485229

DOI: 10.1002/ajmg.1320600104

PubMed ID: 1672107

Title: Amyloid protein of Gerstmann-Straussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58.

PubMed ID: 1672107

DOI: 10.1002/j.1460-2075.1991.tb07977.x

PubMed ID: 1683708

Title: Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene.

PubMed ID: 1683708

DOI: 10.1073/pnas.88.23.10926

PubMed ID: 9792871

Title: A Huntington disease-like neurodegenerative disorder maps to chromosome 20p.

PubMed ID: 9792871

DOI: 10.1086/302093

PubMed ID: 12732622

Title: Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfate.

PubMed ID: 12732622

DOI: 10.1074/jbc.m300394200

PubMed ID: 12214108

Title: The Thr183Ala mutation, not the loss of the first glycosylation site, alters the physical properties of the prion protein.

PubMed ID: 12214108

DOI: 10.3233/jad-2000-2104

PubMed ID: 16144413

Title: The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4.

PubMed ID: 16144413

DOI: 10.1021/ja053254z

PubMed ID: 18034490

Title: The prion protein is a combined zinc and copper binding protein: Zn2+ alters the distribution of Cu2+ coordination modes.

PubMed ID: 18034490

DOI: 10.1021/ja077146j

PubMed ID: 19059915

Title: Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative initiation of translation.

PubMed ID: 19059915

DOI: 10.1074/jbc.m804051200

PubMed ID: 29222195

Title: Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative initiation of translation.

PubMed ID: 29222195

DOI: 10.1074/jbc.w117.000658

PubMed ID: 19349973

Title: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.

PubMed ID: 19349973

DOI: 10.1038/nbt.1532

PubMed ID: 19936054

Title: Glypican-1 mediates both prion protein lipid raft association and disease isoform formation.

PubMed ID: 19936054

DOI: 10.1371/journal.ppat.1000666

PubMed ID: 19381258

Title: Early onset prion disease from octarepeat expansion correlates with copper or zinc binding properties.

PubMed ID: 19381258

DOI: 10.1371/journal.ppat.1000390

PubMed ID: 20375014

Title: Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3.

PubMed ID: 20375014

DOI: 10.1074/jbc.m110.111815

PubMed ID: 20564047

Title: Copper (II) promotes the formation of soluble neurotoxic PrP oligomers in acidic environment.

PubMed ID: 20564047

DOI: 10.1002/jcb.22743

PubMed ID: 21478263

Title: An overlapping reading frame in the PRNP gene encodes a novel polypeptide distinct from the prion protein.

PubMed ID: 21478263

DOI: 10.1096/fj.10-173815

PubMed ID: 21153684

Title: Characterizing the novel protein p33MONOX.

PubMed ID: 21153684

DOI: 10.1007/s11010-010-0690-4

PubMed ID: 10954699

Title: Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases.

PubMed ID: 10954699

DOI: 10.1074/jbc.c000483200

PubMed ID: 10618385

Title: NMR solution structure of the human prion protein.

PubMed ID: 10618385

DOI: 10.1073/pnas.97.1.145

PubMed ID: 10900000

Title: NMR structures of three single-residue variants of the human prion protein.

PubMed ID: 10900000

DOI: 10.1073/pnas.97.15.8340

PubMed ID: 11524679

Title: Crystal structure of the human prion protein reveals a mechanism for oligomerization.

PubMed ID: 11524679

DOI: 10.1038/nsb0901-770

PubMed ID: 11900542

Title: Molecular features of the copper binding sites in the octarepeat domain of the prion protein.

PubMed ID: 11900542

DOI: 10.1021/bi011922x

PubMed ID: 14623188

Title: The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site.

PubMed ID: 14623188

DOI: 10.1016/j.jmb.2003.09.048

PubMed ID: 8364585

Title: Mutations and polymorphisms in the prion protein gene.

PubMed ID: 8364585

DOI: 10.1002/humu.1380020303

PubMed ID: 8105771

Title: Genetic and infectious prion diseases.

PubMed ID: 8105771

DOI: 10.1001/archneur.1993.00540110011002

PubMed ID: 17468747

Title: Atomic structures of amyloid cross-beta spines reveal varied steric zippers.

PubMed ID: 17468747

DOI: 10.1038/nature05695

PubMed ID: 19204296

Title: Crystal structure of human prion protein bound to a therapeutic antibody.

PubMed ID: 19204296

DOI: 10.1073/pnas.0809170106

PubMed ID: 19927125

Title: Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.

PubMed ID: 19927125

DOI: 10.1038/emboj.2009.333

PubMed ID: 2564168

Title: Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome.

PubMed ID: 2564168

DOI: 10.1038/338342a0

PubMed ID: 2783132

Title: Pro-->Leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome.

PubMed ID: 2783132

DOI: 10.1016/0006-291x(89)92317-6

PubMed ID: 1347910

Title: Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178.

PubMed ID: 1347910

DOI: 10.1212/wnl.42.3.669

PubMed ID: 1671440

Title: New mutation in scrapie amyloid precursor gene (at codon 178) in Finnish Creutzfeldt-Jakob kindred.

PubMed ID: 1671440

DOI: 10.1016/0140-6736(91)91198-4

PubMed ID: 1975028

Title: Mutation in codon 200 of scrapie amyloid protein gene in two clusters of Creutzfeldt-Jakob disease in Slovakia.

PubMed ID: 1975028

DOI: 10.1016/0140-6736(90)92073-q

PubMed ID: 1363810

Title: Mutant prion proteins in Gerstmann-Straussler-Scheinker disease with neurofibrillary tangles.

PubMed ID: 1363810

DOI: 10.1038/ng0492-68

PubMed ID: 1439789

Title: Fatal familial insomnia and familial Creutzfeldt-Jakob disease: disease phenotype determined by a DNA polymorphism.

PubMed ID: 1439789

DOI: 10.1126/science.1439789

PubMed ID: 8461023

Title: Novel missense variants of prion protein in Creutzfeldt-Jakob disease or Gerstmann-Straussler syndrome.

PubMed ID: 8461023

DOI: 10.1006/bbrc.1993.1275

PubMed ID: 7902693

Title: A new point mutation of the prion protein gene in Creutzfeldt-Jakob disease.

PubMed ID: 7902693

DOI: 10.1002/ana.410340608

PubMed ID: 7902972

Title: A missense mutation at codon 105 with codon 129 polymorphism of the prion protein gene in a new variant of Gerstmann-Straussler-Scheinker disease.

PubMed ID: 7902972

DOI: 10.1212/wnl.43.12.2723-a

PubMed ID: 7699395

Title: A variant of Gerstmann-Straussler-Scheinker disease carrying codon 105 mutation with codon 129 polymorphism of the prion protein gene: a clinicopathological study.

PubMed ID: 7699395

DOI: 10.1016/0022-510x(94)90138-4

PubMed ID: 7906019

Title: Japanese family with Creutzfeldt-Jakob disease with codon 200 point mutation of the prion protein gene.

PubMed ID: 7906019

DOI: 10.1212/wnl.44.2.299

PubMed ID: 7913755

Title: Mutation in codon 200 and polymorphism in codon 129 of the prion protein gene in Libyan Jews with Creutzfeldt-Jakob disease.

PubMed ID: 7913755

DOI: 10.1098/rstb.1994.0033

PubMed ID: 7783876

Title: Gerstmann-Straussler-Scheinker disease with mutation at codon 102 and methionine at codon 129 of PRNP in previously unreported patients.

PubMed ID: 7783876

DOI: 10.1212/wnl.45.6.1127

PubMed ID: 8797472

Title: Polymorphism at codon 129 or codon 219 of PRNP and clinical heterogeneity in a previously unreported family with Gerstmann-Straussler-Scheinker disease (PrP-P102L mutation).

PubMed ID: 8797472

DOI: 10.1212/wnl.47.3.734

PubMed ID: 8909447

Title: Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease.

PubMed ID: 8909447

DOI: 10.1212/wnl.47.5.1305

PubMed ID: 9266722

Title: Familial spongiform encephalopathy associated with a novel prion protein gene mutation.

PubMed ID: 9266722

DOI: 10.1002/ana.410420203

PubMed ID: 9786248

Title: Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity.

PubMed ID: 9786248

DOI: 10.1097/00005072-199810000-00010

PubMed ID: 9482303

Title: Protective prion protein polymorphisms against sporadic Creutzfeldt-Jakob disease.

PubMed ID: 9482303

DOI: 10.1016/s0140-6736(05)78358-6

PubMed ID: 10987652

Title: Molecular genetics of human prion diseases in Germany.

PubMed ID: 10987652

DOI: 10.1007/s004399900124

PubMed ID: 10631141

Title: High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes.

PubMed ID: 10631141

DOI: 10.1086/302702

PubMed ID: 10790216

Title: Identification of three novel mutations (E196K, V203I, E211Q) in the prion protein gene (PRNP) in inherited prion diseases with Creutzfeldt-Jakob disease phenotype.

PubMed ID: 10790216

DOI: 10.1002/(sici)1098-1004(200005)15:5<482::aid-humu16>3.0.co;2-1

PubMed ID: 11709001

Title: A new PRNP mutation (G131V) associated with Gerstmann-Straussler-Scheinker disease.

PubMed ID: 11709001

DOI: 10.1001/archneur.58.11.1899

PubMed ID: 12690204

Title: Balancing selection at the prion protein gene consistent with prehistoric kurulike epidemics.

PubMed ID: 12690204

DOI: 10.1126/science.1083320

PubMed ID: 19923577

Title: A novel protective prion protein variant that colocalizes with kuru exposure.

PubMed ID: 19923577

DOI: 10.1056/nejmoa0809716

PubMed ID: 26061765

Title: A naturally occurring variant of the human prion protein completely prevents prion disease.

PubMed ID: 26061765

DOI: 10.1038/nature14510

Sequence Information:

Length: 253
Mass: 27661
Checksum: 43DB596BAAA66484
Sequence:

MANLGCWMLV LFVATWSDLG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGGWGQP 
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHSQWN KPSKPKTNMK HMAGAAAAGA 
VVGGLGGYML GSAMSRPIIH FGSDYEDRYY RENMHRYPNQ VYYRPMDEYS NQNNFVHDCV 
NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCITQYER ESQAYYQRGS SMVLFSSPPV 
ILLISFLIFL IVG

	Overall overall
	Acute kidney failure MONDO0002492
	Adrenal gland UBERON0002369
	Alzheimer disease MONDO0004975
	Amyotrophic lateral sclerosis MONDO0004976
	Basal cell carcinoma MONDO0020804
	Bipolar disorder MONDO0004985
	Bipolar I disorder MONDO0001866
	Blood UBERON0000178
	\|— Blood COVID-19 UBERON0000178_MONDO0100096
	\|— Blood Cytomegalovirus infection UBERON0000178_MONDO0005132
	\|— Blood Healthy UBERON0000178_PATO0000461
	Body of stomach UBERON0001161
	Bone marrow UBERON0002371
	\|— Bone marrow Healthy UBERON0002371_PATO0000461
	Brain UBERON0000955
	Breast UBERON0000310
	\|— Breast cancer MONDO0007254
	Bronchus UBERON0002185
	Caudate lobe of liver UBERON0001117
	Cerebellum UBERON0002037
	\|— Cerebellum Healthy UBERON0002037_PATO0000461
	Cerebral cortex UBERON0000956
	\|— Cerebral cortex Healthy UBERON0000956_PATO0000461
	Cerebrospinal fluid UBERON0001359
	Choroid plexus UBERON0001886
	Colon UBERON0001155
	\|— Colon Healthy UBERON0001155_PATO0000461
	Colorectal cancer MONDO0005575
	Cortex of kidney UBERON0001225
	\|— Cortex of kidney Healthy UBERON0001225_PATO0000461
	COVID-19 MONDO0100096
	Crohn disease MONDO0005011
	Cytomegalovirus infection MONDO0005132
	Dementia MONDO0001627
	Dental pulp UBERON0001754
	Dorsolateral prefrontal cortex UBERON0009834
	\|— Dorsolateral prefrontal cortex Bipolar disorder UBERON0009834_MONDO0004985
	\|— Dorsolateral prefrontal cortex Bipolar I disorder UBERON0009834_MONDO0001866
	\|— Dorsolateral prefrontal cortex Dementia UBERON0009834_MONDO0001627
	\|— Dorsolateral prefrontal cortex Healthy UBERON0009834_PATO0000461
	\|— Dorsolateral prefrontal cortex Schizophrenia UBERON0009834_MONDO0005090
	\|— Dorsolateral prefrontal cortex Vascular dementia UBERON0009834_MONDO0004648
	Duodenum UBERON0002114
	\|— Duodenum Healthy UBERON0002114_PATO0000461
	Fovea centralis UBERON0001786
	\|— Fovea centralis Healthy UBERON0001786_PATO0000461
	Frontal cortex UBERON0001870
	Glioblastoma MONDO0018177
	Healthy PATO0000461
	Heart left ventricle UBERON0002084
	\|— Heart left ventricle Healthy UBERON0002084_PATO0000461
	Heart right ventricle UBERON0002080
	Hippocampal formation UBERON0002421
	\|— Hippocampal formation Healthy UBERON0002421_PATO0000461
	Hypothalamus UBERON0001898
	\|— Hypothalamus Healthy UBERON0001898_PATO0000461
	Ileum UBERON0002116
	\|— Ileum Healthy UBERON0002116_PATO0000461
	\|— Ileum lamina propria UBERON8600035
	Interventricular septum UBERON0002094
	Islet of Langerhans UBERON0000006
	Isolated focal cortical dysplasia type II MONDO0011818
	Kidney UBERON0002113
	\|— Kidney Healthy UBERON0002113_PATO0000461
	Leukoencephalopathy, diffuse hereditary, with spheroids 1 MONDO0800027
	Liver UBERON0002107
	\|— Liver Healthy UBERON0002107_PATO0000461
	Lung UBERON0002048
	\|— Lung Healthy UBERON0002048_PATO0000461
	\|— Lung adenocarcinoma MONDO0005061
	Lymph node UBERON0000029
	Malignant ovarian serous tumor MONDO0024885
	Medial orbital frontal cortex UBERON0022352
	Mesenteric lymph node UBERON0002509
	\|— Mesenteric lymph node Healthy UBERON0002509_PATO0000461
	Midbrain UBERON0001891
	\|— Midbrain Healthy UBERON0001891_PATO0000461
	Nasopharynx UBERON0001728
	Neocortex UBERON0001950
	\|— Neocortex Healthy UBERON0001950_PATO0000461
	Neuroblastoma MONDO0005072
	Occipital cortex UBERON0016540
	Ovary UBERON0000992
	\|— Ovary Healthy UBERON0000992_PATO0000461
	Parkinson disease MONDO0005180
	Peripheral region of retina UBERON0013682
	\|— Peripheral region of retina Healthy UBERON0013682_PATO0000461
	Placenta UBERON0001987
	Pleural effusion UBERON0000175
	Pons UBERON0000988
	\|— Pons Healthy UBERON0000988_PATO0000461
	Prefrontal cortex UBERON0000451
	\|— Prefrontal cortex Healthy UBERON0000451_PATO0000461
	Primary motor cortex UBERON0001384
	\|— Primary motor cortex Healthy UBERON0001384_PATO0000461
	Renal medulla UBERON0000362
	Respiratory airway UBERON0001005
	\|— Respiratory airway COVID-19 UBERON0001005_MONDO0100096
	Retina UBERON0000966
	\|— Retina Healthy UBERON0000966_PATO0000461
	Right atrium auricular region UBERON0006631
	Schizophrenia MONDO0005090
	Sigmoid colon UBERON0001159
	Skin of body UBERON0002097
	\|— Skin of body Healthy UBERON0002097_PATO0000461
	Small cell lung carcinoma MONDO0008433
	Spleen UBERON0002106
	\|— Spleen Healthy UBERON0002106_PATO0000461
	Stomach UBERON0000945
	Substantia nigra pars compacta UBERON0001965
	Telencephalon UBERON0001893
	\|— Telencephalon Healthy UBERON0001893_PATO0000461
	Thalamic complex UBERON0010225
	\|— Thalamic complex Healthy UBERON0010225_PATO0000461
	Transverse colon UBERON0001157
	UBERON0005290 UBERON0005290
	\|— UBERON0005290 Healthy UBERON0005290_PATO0000461
	UBERON8440012 UBERON8440012
	\|— UBERON8440012 Healthy UBERON8440012_PATO0000461
	Vascular dementia MONDO0004648

Details for: PRNP

Cell Significance Landscape

Associated with

Significant Cells

Network Configuration

Legend:

Other Information

The DNA sequence and comparative analysis of human chromosome 20. PubMed ID: 11780052

An overlapping reading frame in the PRNP gene encodes a novel polypeptide distinct from the prion protein. PubMed ID: 21478263

Molecular cloning of a human prion protein cDNA. PubMed ID: 3755672

Genomic structure of the human prion protein gene. PubMed ID: 1678248

Complete genomic sequence and analysis of the prion protein gene region from three mammalian species. PubMed ID: 9799790

Novel PRNP sequence variant associated with familial encephalopathy. PubMed ID: 10581485

The DNA sequence and comparative analysis of human chromosome 20. PubMed ID: 11780052

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications. PubMed ID: 3014653

Deletion in the prion protein gene in a demented patient. PubMed ID: 1363802

A prion-linked psychiatric disorder. PubMed ID: 9384372

SSCP analysis and sequencing of the human prion protein gene (PRNP) detects two different 24 bp deletions in an atypical Alzheimer's disease family. PubMed ID: 7485229

Amyloid protein of Gerstmann-Straussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. PubMed ID: 1672107

Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene. PubMed ID: 1683708

A Huntington disease-like neurodegenerative disorder maps to chromosome 20p. PubMed ID: 9792871

Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfate. PubMed ID: 12732622

The Thr183Ala mutation, not the loss of the first glycosylation site, alters the physical properties of the prion protein. PubMed ID: 12214108

The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4. PubMed ID: 16144413

The prion protein is a combined zinc and copper binding protein: Zn2+ alters the distribution of Cu2+ coordination modes. PubMed ID: 18034490

Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative initiation of translation. PubMed ID: 19059915

Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative initiation of translation. PubMed ID: 29222195

Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. PubMed ID: 19349973

Glypican-1 mediates both prion protein lipid raft association and disease isoform formation. PubMed ID: 19936054

Early onset prion disease from octarepeat expansion correlates with copper or zinc binding properties. PubMed ID: 19381258

Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3. PubMed ID: 20375014

Copper (II) promotes the formation of soluble neurotoxic PrP oligomers in acidic environment. PubMed ID: 20564047

An overlapping reading frame in the PRNP gene encodes a novel polypeptide distinct from the prion protein. PubMed ID: 21478263

Characterizing the novel protein p33MONOX. PubMed ID: 21153684

Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. PubMed ID: 10954699

NMR solution structure of the human prion protein. PubMed ID: 10618385

NMR structures of three single-residue variants of the human prion protein. PubMed ID: 10900000

Crystal structure of the human prion protein reveals a mechanism for oligomerization. PubMed ID: 11524679

Molecular features of the copper binding sites in the octarepeat domain of the prion protein. PubMed ID: 11900542

The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site. PubMed ID: 14623188

Mutations and polymorphisms in the prion protein gene. PubMed ID: 8364585

Genetic and infectious prion diseases. PubMed ID: 8105771

Atomic structures of amyloid cross-beta spines reveal varied steric zippers. PubMed ID: 17468747

Crystal structure of human prion protein bound to a therapeutic antibody. PubMed ID: 19204296

Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. PubMed ID: 19927125

Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. PubMed ID: 2564168

Pro--&gt;Leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome. PubMed ID: 2783132

Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178. PubMed ID: 1347910

New mutation in scrapie amyloid precursor gene (at codon 178) in Finnish Creutzfeldt-Jakob kindred. PubMed ID: 1671440

Mutation in codon 200 of scrapie amyloid protein gene in two clusters of Creutzfeldt-Jakob disease in Slovakia. PubMed ID: 1975028

Mutant prion proteins in Gerstmann-Straussler-Scheinker disease with neurofibrillary tangles. PubMed ID: 1363810

Fatal familial insomnia and familial Creutzfeldt-Jakob disease: disease phenotype determined by a DNA polymorphism. PubMed ID: 1439789

Novel missense variants of prion protein in Creutzfeldt-Jakob disease or Gerstmann-Straussler syndrome. PubMed ID: 8461023

A new point mutation of the prion protein gene in Creutzfeldt-Jakob disease. PubMed ID: 7902693

A missense mutation at codon 105 with codon 129 polymorphism of the prion protein gene in a new variant of Gerstmann-Straussler-Scheinker disease. PubMed ID: 7902972

A variant of Gerstmann-Straussler-Scheinker disease carrying codon 105 mutation with codon 129 polymorphism of the prion protein gene: a clinicopathological study. PubMed ID: 7699395

Japanese family with Creutzfeldt-Jakob disease with codon 200 point mutation of the prion protein gene. PubMed ID: 7906019

Mutation in codon 200 and polymorphism in codon 129 of the prion protein gene in Libyan Jews with Creutzfeldt-Jakob disease. PubMed ID: 7913755

Gerstmann-Straussler-Scheinker disease with mutation at codon 102 and methionine at codon 129 of PRNP in previously unreported patients. PubMed ID: 7783876

Polymorphism at codon 129 or codon 219 of PRNP and clinical heterogeneity in a previously unreported family with Gerstmann-Straussler-Scheinker disease (PrP-P102L mutation). PubMed ID: 8797472

Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease. PubMed ID: 8909447

Familial spongiform encephalopathy associated with a novel prion protein gene mutation. PubMed ID: 9266722

Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity. PubMed ID: 9786248

Protective prion protein polymorphisms against sporadic Creutzfeldt-Jakob disease. PubMed ID: 9482303

Molecular genetics of human prion diseases in Germany. PubMed ID: 10987652

High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes. PubMed ID: 10631141

Identification of three novel mutations (E196K, V203I, E211Q) in the prion protein gene (PRNP) in inherited prion diseases with Creutzfeldt-Jakob disease phenotype. PubMed ID: 10790216

A new PRNP mutation (G131V) associated with Gerstmann-Straussler-Scheinker disease. PubMed ID: 11709001

Balancing selection at the prion protein gene consistent with prehistoric kurulike epidemics. PubMed ID: 12690204

A novel protective prion protein variant that colocalizes with kuru exposure. PubMed ID: 19923577

A naturally occurring variant of the human prion protein completely prevents prion disease. PubMed ID: 26061765

PubMed ID: 11780052

PubMed ID: 21478263

PubMed ID: 3755672

PubMed ID: 1678248

PubMed ID: 9799790

PubMed ID: 10581485

PubMed ID: 11780052

PubMed ID: 15489334

PubMed ID: 3014653

PubMed ID: 1363802

PubMed ID: 9384372

PubMed ID: 7485229

PubMed ID: 1672107

PubMed ID: 1683708

PubMed ID: 9792871

PubMed ID: 12732622

PubMed ID: 12214108

PubMed ID: 16144413

PubMed ID: 18034490

PubMed ID: 19059915

PubMed ID: 29222195

PubMed ID: 19349973

PubMed ID: 19936054

PubMed ID: 19381258

PubMed ID: 20375014

PubMed ID: 20564047

PubMed ID: 21478263

PubMed ID: 21153684

PubMed ID: 10954699

PubMed ID: 10618385

PubMed ID: 10900000

PubMed ID: 11524679

PubMed ID: 11900542

PubMed ID: 14623188

PubMed ID: 8364585

PubMed ID: 8105771

PubMed ID: 17468747

PubMed ID: 19204296

PubMed ID: 19927125

PubMed ID: 2564168

PubMed ID: 2783132

PubMed ID: 1347910

PubMed ID: 1671440

PubMed ID: 1975028

PubMed ID: 1363810

PubMed ID: 1439789

PubMed ID: 8461023

PubMed ID: 7902693

PubMed ID: 7902972

PubMed ID: 7699395

PubMed ID: 7906019

PubMed ID: 7913755

PubMed ID: 7783876

PubMed ID: 8797472

PubMed ID: 8909447

PubMed ID: 9266722

PubMed ID: 9786248

PubMed ID: 9482303

PubMed ID: 10987652

PubMed ID: 10631141

PubMed ID: 10790216

PubMed ID: 11709001

PubMed ID: 12690204

PubMed ID: 19923577

PubMed ID: 26061765