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Protein

Major prion protein

Gene

PRNP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu2+ or ZN2+ for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).By similarityCurated3 Publications

Miscellaneous

This protein is produced by a bicistronic gene which also produces the alternative prion protein/AltPrP (AC F7VJQ1) from an overlapping reading frame.1 Publication
The alternative prion protein/AltPrP (AC F7VJQ1) and PRNP have no apparent direct functional relation since a mutation that removes the start codon of the AltPrP has no apparent effect on the biology of PRNP. In mouse and hamster, the alternative initiation AUG codon is absent and is replaced by a GUG codon.Curated

Caution

An isoform was shown to be localized to both the cytoplasm and the nucleus and to be sumoylated with SUMO1 (PubMed:19059915). The article has later been withdrawn by the authors.1 Publication1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi61Copper or zinc 11 Publication1
Metal bindingi62Copper or zinc 1; via amide nitrogen1 Publication1
Metal bindingi63Copper or zinc 1; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi69Copper or zinc 21 Publication1
Metal bindingi70Copper or zinc 2; via amide nitrogen1 Publication1
Metal bindingi71Copper or zinc 2; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi77Copper or zinc 31 Publication1
Metal bindingi78Copper or zinc 3; via amide nitrogen1 Publication1
Metal bindingi79Copper or zinc 3; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi85Copper or zinc 41 Publication1
Metal bindingi86Copper or zinc 4; via amide nitrogen1 Publication1
Metal bindingi87Copper or zinc 4; via amide nitrogen and carbonyl oxygen1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • amyloid-beta binding Source: ARUK-UCL
  • ATP-dependent protein binding Source: GO_Central
  • chaperone binding Source: GO_Central
  • copper ion binding Source: UniProtKB
  • cupric ion binding Source: GO_Central
  • cuprous ion binding Source: CAFA
  • glycosaminoglycan binding Source: ARUK-UCL
  • identical protein binding Source: CAFA
  • ion channel binding Source: GO_Central
  • lamin binding Source: GO_Central
  • microtubule binding Source: UniProtKB
  • protease binding Source: ARUK-UCL
  • protein-containing complex binding Source: ARUK-UCL
  • signaling receptor activity Source: ARUK-UCL
  • tubulin binding Source: UniProtKB
  • type 5 metabotropic glutamate receptor binding Source: ARUK-UCL

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionPrion
Biological processCell cycle, Growth arrest
LigandCopper, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-419037 NCAM1 interactions

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P04156 Predicted

Transport Classification Database

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TCDBi
1.C.48.1.2 the prion peptide (prp) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Major prion protein
Short name:
PrP
Alternative name(s):
ASCR
PrP27-30
PrP33-35C
CD_antigen: CD230
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PRNP
Synonyms:ALTPRP, PRIP, PRP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000171867.16

Human Gene Nomenclature Database

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HGNCi
HGNC:9449 PRNP

Online Mendelian Inheritance in Man (OMIM)

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MIMi
176640 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P04156

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Cell membrane, Golgi apparatus, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.1 Publication
Creutzfeldt-Jakob disease (CJD)10 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionOccurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected animal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.
See also OMIM:123400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_006470180V → I in CJD. 3 PublicationsCorresponds to variant dbSNP:rs74315408EnsemblClinVar.1
Natural variantiVAR_008749196E → K in CJD. 1 Publication1
Natural variantiVAR_006473200E → K in CJD. 3 PublicationsCorresponds to variant dbSNP:rs28933385EnsemblClinVar.1
Natural variantiVAR_008751203V → I in CJD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776593792Ensembl.1
Natural variantiVAR_006474208R → H in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315412EnsemblClinVar.1
Natural variantiVAR_006475210V → I in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315407EnsemblClinVar.1
Natural variantiVAR_008752211E → Q in CJD. 1 PublicationCorresponds to variant dbSNP:rs398122370EnsemblClinVar.1
Natural variantiVAR_006478232M → R in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315409EnsemblClinVar.1
Fatal familial insomnia (FFI)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.
See also OMIM:600072
Gerstmann-Straussler disease (GSD)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare inherited prion disease characterized by adult onset of memory loss, dementia, ataxia, and pathologic deposition of amyloid-like plaques in the brain. GSD presents with progressive limb and truncal ataxia, dysarthria, and cognitive decline in the thirties and forties, and the average disease duration is 7 years.
See also OMIM:137440
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_006465105P → L in GSD. 2 PublicationsCorresponds to variant dbSNP:rs11538758EnsemblClinVar.1
Natural variantiVAR_014264131G → V in GSD. 1 PublicationCorresponds to variant dbSNP:rs74315410EnsemblClinVar.1
Natural variantiVAR_008746187H → R in GSD. 1 PublicationCorresponds to variant dbSNP:rs74315413EnsemblClinVar.1
Natural variantiVAR_006472198F → S in GSD; atypical form with neurofibrillary tangles. 1 PublicationCorresponds to variant dbSNP:rs74315405EnsemblClinVar.1
Natural variantiVAR_008750202D → N in GSD. 1 PublicationCorresponds to variant dbSNP:rs761807915Ensembl.1
Natural variantiVAR_008753212Q → P in GSD. 1 PublicationCorresponds to variant dbSNP:rs751882709Ensembl.1
Natural variantiVAR_006476217Q → R in GSD; with neurofibrillary tangles. 1 PublicationCorresponds to variant dbSNP:rs74315406EnsemblClinVar.1
Huntington disease-like 1 (HDL1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant, early-onset neurodegenerative disorder with prominent psychiatric features.
See also OMIM:603218
Kuru (KURU)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionKuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.
See also OMIM:245300
Spongiform encephalopathy with neuropsychiatric features (SENF)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.
See also OMIM:606688

Keywords - Diseasei

Amyloidosis, Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
5621

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
PRNP

MalaCards human disease database

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MalaCardsi
PRNP
MIMi123400 phenotype
137440 phenotype
245300 phenotype
600072 phenotype
603218 phenotype
606688 phenotype

Open Targets

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OpenTargetsi
ENSG00000171867

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
280397 Familial Alzheimer-like prion disease
466 Fatal familial insomnia
356 Gerstmann-Straussler-Scheinker syndrome
157941 Huntington disease-like 1
282166 Inherited Creutzfeldt-Jakob disease
454745 Kuru
397606 PrP systemic amyloidosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33796

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4869

Drug and drug target database

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DrugBanki
DB00759 Tetracycline

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PRNP

Domain mapping of disease mutations (DMDM)

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DMDMi
130912

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22By similarityAdd BLAST22
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002567523 – 230Major prion proteinAdd BLAST208
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000025676231 – 253Removed in mature formBy similarityAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi179 ↔ 2141 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi181N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi197N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi230GPI-anchor amidated serineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P04156

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P04156

PeptideAtlas

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PeptideAtlasi
P04156

PRoteomics IDEntifications database

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PRIDEi
P04156

ProteomicsDB human proteome resource

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ProteomicsDBi
51667
51668

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P04156

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P04156

SwissPalm database of S-palmitoylation events

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SwissPalmi
P04156

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P04156

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000171867 Expressed in 242 organ(s), highest expression level in Brodmann (1909) area 23

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P04156 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P04156 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA042754
HPA043398

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer and homodimer. Has a tendency to aggregate into amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Soluble oligomers may represent an intermediate stage on the path to fibril formation. Copper binding may promote oligomerization (PubMed:11524679, PubMed:11900542, PubMed:14623188, PubMed:17468747, PubMed:19204296, PubMed:19927125, PubMed:20375014, PubMed:20564047). Interacts with GRB2, APP, ERI3/PRNPIP and SYN1. Mislocalized cytosolically exposed PrP interacts with MGRN1; this interaction alters MGRN1 subcellular location and causes lysosomal enlargement (By similarity). Interacts with KIAA1191 (PubMed:21153684). Interacts with ADGRG6 (By similarity).By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111606, 72 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P04156

Database of interacting proteins

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DIPi
DIP-29933N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P04156

Protein interaction database and analysis system

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IntActi
P04156, 94 interactors

Molecular INTeraction database

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MINTi
P04156

STRING: functional protein association networks

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STRINGi
9606.ENSP00000368752

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P04156

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1253
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00466

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P04156

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P04156

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P04156

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati51 – 5919
Repeati60 – 6728
Repeati68 – 7538
Repeati76 – 8348
Repeati84 – 9158

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni23 – 230Interaction with GRB2, ERI3 and SYN1By similarityAdd BLAST208
Regioni23 – 38Interaction with ADGRG6By similarityAdd BLAST16
Regioni51 – 915 X 8 AA tandem repeats of P-H-G-G-G-W-G-QAdd BLAST41

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The normal, monomeric form, PRPN(C), has a mainly alpha-helical structure. Misfolding of this form produces a disease-associated, protease-resistant form, PRPN (Sc), accompanied by a large increase of the beta-sheet content and formation of amyloid fibrils. These fibrils consist of a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization. In addition, the heparan-sulfate proteoglycan, GPC1, promotes the association of PRPN (C) to lipid rafts and appears to facilitate the conversion to PRPN (Sc).3 Publications
Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization.3 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the prion family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IJMM Eukaryota
ENOG410YXUU LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00510000049083

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG008260

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P04156

KEGG Orthology (KO)

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KOi
K05634

Identification of Orthologs from Complete Genome Data

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OMAi
HNPGYPH

Database of Orthologous Groups

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OrthoDBi
EOG091G0HMV

Database for complete collections of gene phylogenies

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PhylomeDBi
P04156

TreeFam database of animal gene trees

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TreeFami
TF105188

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.790.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000817 Prion
IPR036924 Prion/Doppel_b-ribbon_dom_sf
IPR022416 Prion/Doppel_prot_b-ribbon_dom
IPR025860 Prion_N_dom

The PANTHER Classification System

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PANTHERi
PTHR10502:SF134 PTHR10502:SF134, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00377 Prion, 1 hit
PF11587 Prion_bPrPp, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00341 PRION

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00157 PRP, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54098 SSF54098, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00291 PRION_1, 1 hit
PS00706 PRION_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P04156-1) [UniParc]FASTAAdd to basket
Also known as: PrP

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MANLGCWMLV LFVATWSDLG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP
60 70 80 90 100
PQGGGGWGQP HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHSQWN
110 120 130 140 150
KPSKPKTNMK HMAGAAAAGA VVGGLGGYML GSAMSRPIIH FGSDYEDRYY
160 170 180 190 200
RENMHRYPNQ VYYRPMDEYS NQNNFVHDCV NITIKQHTVT TTTKGENFTE
210 220 230 240 250
TDVKMMERVV EQMCITQYER ESQAYYQRGS SMVLFSSPPV ILLISFLIFL

IVG
Length:253
Mass (Da):27,661
Last modified:November 1, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i43DB596BAAA66484
GO
Isoform 3 (identifier: F7VJQ1-1) [UniParc]FASTAAdd to basket
Also known as: AltPrP
The sequence of this isoform can be found in the external entry F7VJQ1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:73
Mass (Da):8,691
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2A2V1A2A2V1_HUMAN
Major prion protein
PRNP
249Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
X6RKS3X6RKS3_HUMAN
Major prion protein
PRNP
217Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti118Missing in AAA19664 (PubMed:3014653).Curated1
Sequence conflicti118Missing in BAA00011 (PubMed:3014653).Curated1
Sequence conflicti169Y → H in ABD63004 (Ref. 6) Curated1
Sequence conflicti227Q → K in AAH22532 (PubMed:15489334).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

The five tandem octapeptide repeats region is highly unstable. Insertions or deletions of octapeptide repeat units are associated to prion disease.1 Publication
A number of polymorphisms confer resistance to prion diseases (PubMed:1439789, PubMed:9482303, PubMed:19923577, PubMed:26061765). Val-127 has been selected for in response to the Kuru epidemic and confers resistance to prion disease by acting as a 'dominant negative' inhibitor of prion conversion (PubMed:26061765). Val-127 is not only itself resistant to conformational conversion, but also inhibits conversion of wild-type proteins. Confers protection against classical Creutzfeldt-Jakob disease (CJD) and Kuru in the heterozygous state, but can be infected with variant CJD prions, resulting from exposure to bovine spongiform encephalopathy prions. Confers complete resistance to all prion strains when homozygous (PubMed:26061765). Always associated with M-129 variant (PubMed:26061765). Val-129 confers relative protection against acquired, sporadic and some inherited prion diseases in the heterozygous state, possibly by preventing homodimerization (PubMed:1439789). Lys-219 confers relative protection against sporadic Creutzfeldt-Jakob disease (CJD) in the heterozygous state (PubMed:9482303).3 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01376356 – 63Missing 3 Publications8
Natural variantiVAR_006464102P → L in GSD and early-onset dementia. 5 PublicationsCorresponds to variant dbSNP:rs74315401EnsemblClinVar.1
Natural variantiVAR_006465105P → L in GSD. 2 PublicationsCorresponds to variant dbSNP:rs11538758EnsemblClinVar.1
Natural variantiVAR_006466117A → V Linked to development of dementing Gerstmann-Straussler disease. 1 PublicationCorresponds to variant dbSNP:rs74315402EnsemblClinVar.1
Natural variantiVAR_073722127G → V Polymorphism; variant that has been selected for in response to the Kuru epidemic and confers resistance to prion disease by acting as a 'dominant negative' inhibitor of prion conversion; is not only itself resistant to conformational conversion, but also inhibits conversion of wild-type proteins; confers protection against classical Creutzfeldt-Jakob disease (CJD) and Kuru in the heterozygous state, but can be infected with variant CJD prions, resulting from exposure to bovine spongiform encephalopathy prions; confers complete resistance to all prion strains when homozygous. Always associated with M-129 variant. 2 PublicationsCorresponds to variant dbSNP:rs267606980EnsemblClinVar.1
Natural variantiVAR_006467129M → V Polymorphism; confers relative protection against acquired, sporadic and some inherited prion diseases in the heterozygous state, possibly by preventing homodimerization; determines the disease phenotype in patients who have a PrP mutation at position 178; patients with M-129 develop FFI, those with V-129 develop CJD. 4 PublicationsCorresponds to variant dbSNP:rs1799990EnsemblClinVar.1
Natural variantiVAR_014264131G → V in GSD. 1 PublicationCorresponds to variant dbSNP:rs74315410EnsemblClinVar.1
Natural variantiVAR_006468171N → S in schizoaffective disorder. 1 PublicationCorresponds to variant dbSNP:rs16990018EnsemblClinVar.1
Natural variantiVAR_006469178D → N in FFI and CJD. 4 PublicationsCorresponds to variant dbSNP:rs74315403EnsemblClinVar.1
Natural variantiVAR_006470180V → I in CJD. 3 PublicationsCorresponds to variant dbSNP:rs74315408EnsemblClinVar.1
Natural variantiVAR_006471183T → A in SENF and early-onset dementia; induces loss of glycosylation at N-181. 3 PublicationsCorresponds to variant dbSNP:rs74315411EnsemblClinVar.1
Natural variantiVAR_008746187H → R in GSD. 1 PublicationCorresponds to variant dbSNP:rs74315413EnsemblClinVar.1
Natural variantiVAR_008748188T → K in early-onset dementia; dementia associated to prion diseases. 1 Publication1
Natural variantiVAR_008747188T → R1 PublicationCorresponds to variant dbSNP:rs372878791Ensembl.1
Natural variantiVAR_008749196E → K in CJD. 1 Publication1
Natural variantiVAR_006472198F → S in GSD; atypical form with neurofibrillary tangles. 1 PublicationCorresponds to variant dbSNP:rs74315405EnsemblClinVar.1
Natural variantiVAR_006473200E → K in CJD. 3 PublicationsCorresponds to variant dbSNP:rs28933385EnsemblClinVar.1
Natural variantiVAR_008750202D → N in GSD. 1 PublicationCorresponds to variant dbSNP:rs761807915Ensembl.1
Natural variantiVAR_008751203V → I in CJD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776593792Ensembl.1
Natural variantiVAR_006474208R → H in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315412EnsemblClinVar.1
Natural variantiVAR_006475210V → I in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315407EnsemblClinVar.1
Natural variantiVAR_008752211E → Q in CJD. 1 PublicationCorresponds to variant dbSNP:rs398122370EnsemblClinVar.1
Natural variantiVAR_008753212Q → P in GSD. 1 PublicationCorresponds to variant dbSNP:rs751882709Ensembl.1
Natural variantiVAR_006476217Q → R in GSD; with neurofibrillary tangles. 1 PublicationCorresponds to variant dbSNP:rs74315406EnsemblClinVar.1
Natural variantiVAR_006477219E → K Polymorphism; confers relative protection against sporadic Creutzfeldt-Jakob disease (CJD) in the heterozygous state. 2 PublicationsCorresponds to variant dbSNP:rs1800014EnsemblClinVar.1
Natural variantiVAR_006478232M → R in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315409EnsemblClinVar.1
Natural variantiVAR_008754238P → S1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M13899 mRNA Translation: AAA60182.1
X83416 Genomic DNA Translation: CAA58442.1
U29185 Genomic DNA Translation: AAC78725.1
AF076976 Genomic DNA Translation: AAD46098.1
AY008282 mRNA Translation: AAG21693.1
DQ408531 Genomic DNA Translation: ABD63004.1
AL133396 Genomic DNA No translation available.
BC012844 mRNA Translation: AAH12844.1
BC022532 mRNA Translation: AAH22532.1
D00015 mRNA Translation: BAA00011.1
M13667 mRNA Translation: AAA19664.1
M81929 Genomic DNA Translation: AAB59442.1
M81930 Genomic DNA Translation: AAB59443.1
AF030575 Genomic DNA Translation: AAC05365.1
S80732 Genomic DNA Translation: AAB50648.2
S80743 Genomic DNA Translation: AAB50649.2
S71208 Genomic DNA Translation: AAB20521.1
S71210 Genomic DNA Translation: AAB20522.1
S71212 Genomic DNA Translation: AAB20523.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS13080.1 [P04156-1]

Protein sequence database of the Protein Information Resource

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PIRi
A24173 UJHU

NCBI Reference Sequences

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RefSeqi
NP_000302.1, NM_000311.4 [P04156-1]
NP_001073590.1, NM_001080121.2 [P04156-1]
NP_001073591.1, NM_001080122.2 [P04156-1]
NP_001073592.1, NM_001080123.2 [P04156-1]
NP_001258490.1, NM_001271561.2
NP_898902.1, NM_183079.3 [P04156-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.472010
Hs.610285
Hs.721670

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000379440; ENSP00000368752; ENSG00000171867 [P04156-1]
ENST00000430350; ENSP00000399376; ENSG00000171867 [P04156-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5621

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5621

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

The Official Mad Cow Disease Home Page
Wikipedia

PRNP entry

Protein Spotlight

The shape of harm - Issue 179 of May 2016

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13899 mRNA Translation: AAA60182.1
X83416 Genomic DNA Translation: CAA58442.1
U29185 Genomic DNA Translation: AAC78725.1
AF076976 Genomic DNA Translation: AAD46098.1
AY008282 mRNA Translation: AAG21693.1
DQ408531 Genomic DNA Translation: ABD63004.1
AL133396 Genomic DNA No translation available.
BC012844 mRNA Translation: AAH12844.1
BC022532 mRNA Translation: AAH22532.1
D00015 mRNA Translation: BAA00011.1
M13667 mRNA Translation: AAA19664.1
M81929 Genomic DNA Translation: AAB59442.1
M81930 Genomic DNA Translation: AAB59443.1
AF030575 Genomic DNA Translation: AAC05365.1
S80732 Genomic DNA Translation: AAB50648.2
S80743 Genomic DNA Translation: AAB50649.2
S71208 Genomic DNA Translation: AAB20521.1
S71210 Genomic DNA Translation: AAB20522.1
S71212 Genomic DNA Translation: AAB20523.1
CCDSiCCDS13080.1 [P04156-1]
PIRiA24173 UJHU
RefSeqiNP_000302.1, NM_000311.4 [P04156-1]
NP_001073590.1, NM_001080121.2 [P04156-1]
NP_001073591.1, NM_001080122.2 [P04156-1]
NP_001073592.1, NM_001080123.2 [P04156-1]
NP_001258490.1, NM_001271561.2
NP_898902.1, NM_183079.3 [P04156-1]
UniGeneiHs.472010
Hs.610285
Hs.721670

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E1GNMR-A125-228[»]
1E1JNMR-A125-228[»]
1E1PNMR-A125-228[»]
1E1SNMR-A125-228[»]
1E1UNMR-A125-228[»]
1E1WNMR-A125-228[»]
1FKCNMR-A90-231[»]
1FO7NMR-A90-231[»]
1H0LNMR-A121-230[»]
1HJMNMR-A125-228[»]
1HJNNMR-A125-228[»]
1I4MX-ray2.00A119-226[»]
1OEHNMR-A77-84[»]
1OEINMR-A61-84[»]
1QLXNMR-A23-230[»]
1QLZNMR-A23-230[»]
1QM0NMR-A90-230[»]
1QM1NMR-A90-230[»]
1QM2NMR-A121-230[»]
1QM3NMR-A121-230[»]
2IV4NMR-A180-195[»]
2IV5NMR-A173-195[»]
2IV6NMR-A173-195[»]
2K1DNMR-A90-231[»]
2KUNNMR-A90-231[»]
2LBGNMR-A110-136[»]
2LEJNMR-A90-231[»]
2LFTNMR-A90-231[»]
2LSBNMR-A90-231[»]
2LV1NMR-A90-231[»]
2M8TNMR-A90-231[»]
2OL9X-ray0.85A170-175[»]
2W9EX-ray2.90A119-231[»]
3HAFX-ray2.26A90-231[»]
3HAKX-ray1.80A125-227[»]
3HEQX-ray1.80A/B90-231[»]
3HERX-ray1.85A/B90-231[»]
3HESX-ray2.00A/B90-231[»]
3HJ5X-ray3.10A/B90-231[»]
3HJXX-ray2.00A126-231[»]
3MD4X-ray1.15A/B127-132[»]
3MD5X-ray1.40A/B127-132[»]
3NHCX-ray1.57A/B127-132[»]
3NHDX-ray1.92A/B127-132[»]
3NVFX-ray1.80A138-143[»]
4DGIX-ray2.40A120-230[»]
4E1HX-ray1.40A/C/E/G/I/K177-182[»]
B/D/F/H/J/L211-216[»]
4E1IX-ray2.03A/C/E/G/I/K177-182[»]
B/D/F/H/J/L211-216[»]
4KMLX-ray1.50A24-231[»]
4N9OX-ray1.50A90-231[»]
5L6RNMR-A90-226[»]
5YJ4NMR-A91-231[»]
5YJ5NMR-A91-231[»]
DisProtiDP00466
ProteinModelPortaliP04156
SMRiP04156
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111606, 72 interactors
CORUMiP04156
DIPiDIP-29933N
ELMiP04156
IntActiP04156, 94 interactors
MINTiP04156
STRINGi9606.ENSP00000368752

Chemistry databases

BindingDBiP04156
ChEMBLiCHEMBL4869
DrugBankiDB00759 Tetracycline

Protein family/group databases

MoonDBiP04156 Predicted
TCDBi1.C.48.1.2 the prion peptide (prp) family

PTM databases

iPTMnetiP04156
PhosphoSitePlusiP04156
SwissPalmiP04156

Polymorphism and mutation databases

BioMutaiPRNP
DMDMi130912

Proteomic databases

EPDiP04156
PaxDbiP04156
PeptideAtlasiP04156
PRIDEiP04156
ProteomicsDBi51667
51668

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5621
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379440; ENSP00000368752; ENSG00000171867 [P04156-1]
ENST00000430350; ENSP00000399376; ENSG00000171867 [P04156-1]
GeneIDi5621
KEGGihsa:5621

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5621
DisGeNETi5621
EuPathDBiHostDB:ENSG00000171867.16

GeneCards: human genes, protein and diseases

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GeneCardsi
PRNP
GeneReviewsiPRNP
HGNCiHGNC:9449 PRNP
HPAiHPA042754
HPA043398
MalaCardsiPRNP
MIMi123400 phenotype
137440 phenotype
176640 gene
245300 phenotype
600072 phenotype
603218 phenotype
606688 phenotype
neXtProtiNX_P04156
OpenTargetsiENSG00000171867
Orphaneti280397 Familial Alzheimer-like prion disease
466 Fatal familial insomnia
356 Gerstmann-Straussler-Scheinker syndrome
157941 Huntington disease-like 1
282166 Inherited Creutzfeldt-Jakob disease
454745 Kuru
397606 PrP systemic amyloidosis
PharmGKBiPA33796

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IJMM Eukaryota
ENOG410YXUU LUCA
GeneTreeiENSGT00510000049083
HOVERGENiHBG008260
InParanoidiP04156
KOiK05634
OMAiHNPGYPH
OrthoDBiEOG091G0HMV
PhylomeDBiP04156
TreeFamiTF105188

Enzyme and pathway databases

ReactomeiR-HSA-419037 NCAM1 interactions

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
PRNP human
EvolutionaryTraceiP04156

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
5621
PMAP-CutDBiP04156

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000171867 Expressed in 242 organ(s), highest expression level in Brodmann (1909) area 23
ExpressionAtlasiP04156 baseline and differential
GenevisibleiP04156 HS

Family and domain databases

Gene3Di1.10.790.10, 1 hit
InterProiView protein in InterPro
IPR000817 Prion
IPR036924 Prion/Doppel_b-ribbon_dom_sf
IPR022416 Prion/Doppel_prot_b-ribbon_dom
IPR025860 Prion_N_dom
PANTHERiPTHR10502:SF134 PTHR10502:SF134, 1 hit
PfamiView protein in Pfam
PF00377 Prion, 1 hit
PF11587 Prion_bPrPp, 1 hit
PRINTSiPR00341 PRION
SMARTiView protein in SMART
SM00157 PRP, 1 hit
SUPFAMiSSF54098 SSF54098, 1 hit
PROSITEiView protein in PROSITE
PS00291 PRION_1, 1 hit
PS00706 PRION_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPRIO_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P04156
Secondary accession number(s): O60489
, P78446, Q15216, Q15221, Q27H91, Q5QPB4, Q8TBG0, Q96E70, Q9UP19
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: December 5, 2018
This is version 240 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  4. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  8. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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