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P04156 (PRIO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 188. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Major prion protein

Short name=PrP
Alternative name(s):
ASCR
PrP27-30
PrP33-35C
CD_antigen=CD230
Gene names
Name:PRNP
Synonyms:PRIP, PRP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). 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. Ref.15 Ref.20 Ref.23

Subunit structure

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. 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. Ref.22 Ref.23 Ref.24 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.35

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor. Golgi apparatus. Note: Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of CU2+, to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. Ref.18 Ref.20

Isoform 2: Cytoplasm. Nucleus. Note: Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus. Ref.18 Ref.20

Domain

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). Ref.22 Ref.23 Ref.28 Ref.29 Ref.33 Ref.35

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. Ref.22 Ref.23 Ref.28 Ref.29 Ref.33 Ref.35

Post-translational modification

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

Isoform 2 is sumoylated with SUMO1 By similarity.

Polymorphism

The five tandem octapeptide repeats region is highly unstable. Insertions or deletions of octapeptide repeat units are associated to prion disease.

Involvement in disease

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. Ref.20 Ref.39 Ref.40 Ref.42 Ref.43 Ref.46 Ref.47 Ref.50 Ref.51 Ref.55

Creutzfeldt-Jakob disease (CJD) [MIM:123400]: Occurs 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.39 Ref.40 Ref.42 Ref.43 Ref.46 Ref.47 Ref.50 Ref.51 Ref.55

Fatal familial insomnia (FFI) [MIM:600072]: Autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.35 Ref.38

Gerstmann-Straussler disease (GSD) [MIM:137440]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.20 Ref.35 Ref.36 Ref.41 Ref.44 Ref.45 Ref.48 Ref.49 Ref.52 Ref.56

Huntington disease-like 1 (HDL1) [MIM:603218]: Autosomal dominant, early-onset neurodegenerative disorder with prominent psychiatric features.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Kuru (KURU) [MIM:245300]: Kuru 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:606688]: Autosomal 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Miscellaneous

This protein is produced by a bicistronic gene which also produces the The alternative prion protein/AltPrP from an overlapping reading frame.

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.

Sequence similarities

Belongs to the prion family.

Ontologies

Keywords
   Biological processCell cycle
Growth arrest
   Cellular componentAmyloid
Cell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative initiation
Polymorphism
   DiseaseAmyloidosis
Disease mutation
   DomainRepeat
Signal
   LigandCopper
Metal-binding
Zinc
   Molecular functionPrion
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

cell cycle arrest

Inferred from electronic annotation. Source: UniProtKB-KW

cellular copper ion homeostasis

Non-traceable author statement PubMed 16004966. Source: UniProtKB

learning or memory

Inferred from electronic annotation. Source: Ensembl

metabolic process

Traceable author statement Ref.1. Source: ProtInc

negative regulation of T cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of activated T cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of calcineurin-NFAT signaling cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of interferon-gamma production

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of interleukin-17 production

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of interleukin-2 production

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to copper ion

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

anchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Traceable author statement PubMed 16004966. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

extrinsic component of membrane

Traceable author statement PubMed 16004966. Source: UniProtKB

membrane raft

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncopper ion binding

Inferred from direct assay Ref.29. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 16286452Ref.35PubMed 21920025. Source: IntAct

microtubule binding

Inferred from direct assay PubMed 16004966. Source: UniProtKB

tubulin binding

Inferred from direct assay PubMed 16004966. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P04156-1)

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.
Isoform 2 (identifier: P04156-2)

Also known as: PrP(M8);

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 230208Major prion protein
PRO_0000025675
Propeptide231 – 25323Removed in mature form By similarity
PRO_0000025676

Regions

Repeat51 – 5991
Repeat60 – 6782
Repeat68 – 7583
Repeat76 – 8384
Repeat84 – 9185
Region23 – 230208Interaction with GRB2, ERI3 and SYN1 By similarity
Region51 – 91415 X 8 AA tandem repeats of P-H-G-G-G-W-G-Q

Sites

Metal binding611Copper or zinc 1
Metal binding621Copper or zinc 1; via amide nitrogen
Metal binding631Copper or zinc 1; via amide nitrogen and carbonyl oxygen
Metal binding691Copper or zinc 2 Probable
Metal binding701Copper or zinc 2; via amide nitrogen Probable
Metal binding711Copper or zinc 2; via amide nitrogen and carbonyl oxygen Probable
Metal binding771Copper or zinc 3 Probable
Metal binding781Copper or zinc 3; via amide nitrogen Probable
Metal binding791Copper or zinc 3; via amide nitrogen and carbonyl oxygen Probable
Metal binding851Copper or zinc 4 Probable
Metal binding861Copper or zinc 4; via amide nitrogen Probable
Metal binding871Copper or zinc 4; via amide nitrogen and carbonyl oxygen Probable

Amino acid modifications

Lipidation2301GPI-anchor amidated serine By similarity
Glycosylation1811N-linked (GlcNAc...)
Glycosylation1971N-linked (GlcNAc...) Ref.19
Disulfide bond179 ↔ 214 Ref.30

Natural variations

Alternative sequence1 – 77Missing in isoform 2.
VSP_039045
Natural variant56 – 638Missing.
VAR_013763
Natural variant1021P → L in GSD and early-onset dementia. Ref.36 Ref.37 Ref.48 Ref.49 Ref.54
VAR_006464
Natural variant1051P → L in GSD. Ref.44 Ref.45
VAR_006465
Natural variant1171A → V Linked to development of dementing Gerstmann-Straussler disease. Ref.37
VAR_006466
Natural variant1291M → V Polymorphism; 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. Ref.35 Ref.37
Corresponds to variant rs1799990 [ dbSNP | Ensembl ].
VAR_006467
Natural variant1311G → V in GSD. Ref.56
VAR_014264
Natural variant1711N → S in schizoaffective disorder. Ref.11
Corresponds to variant rs16990018 [ dbSNP | Ensembl ].
VAR_006468
Natural variant1781D → N in FFI and CJD. Ref.35 Ref.38 Ref.39
VAR_006469
Natural variant1801V → I in CJD. Ref.42
VAR_006470
Natural variant1831T → A in familial spongiform encephalopathy. Ref.54
VAR_006471
Natural variant1871H → R in GSD. Ref.4
VAR_008746
Natural variant1881T → K in early-onset dementia; dementia associated to prion diseases. Ref.54
VAR_008748
Natural variant1881T → R. Ref.53
VAR_008747
Natural variant1961E → K in CJD. Ref.55
VAR_008749
Natural variant1981F → S in GSD; atypical form with neurofibrillary tangles. Ref.35
VAR_006472
Natural variant2001E → K in CJD. Ref.25 Ref.40 Ref.46 Ref.47
VAR_006473
Natural variant2021D → N in GSD. Ref.52
VAR_008750
Natural variant2031V → I in CJD; it could be an extremely rare polymorphism. Ref.55
VAR_008751
Natural variant2081R → H in CJD. Ref.50 Ref.51
VAR_006474
Natural variant2101V → I in CJD. Ref.43
VAR_006475
Natural variant2111E → Q in CJD. Ref.55
VAR_008752
Natural variant2121Q → P in GSD. Ref.52
VAR_008753
Natural variant2171Q → R in GSD; with neurofibrillary tangles. Ref.41
VAR_006476
Natural variant2191E → K. Ref.49
Corresponds to variant rs1800014 [ dbSNP | Ensembl ].
VAR_006477
Natural variant2321M → R in CJD. Ref.42
VAR_006478
Natural variant2381P → S. Ref.53
VAR_008754

Experimental info

Mutagenesis11M → S: Protein detected. No protein detected; when associated with S-8. Ref.18
Mutagenesis81M → S: No protein detected; when associated with S-1. Ref.18
Sequence conflict1181Missing in AAA19664. Ref.9
Sequence conflict1181Missing in BAA00011. Ref.9
Sequence conflict1691Y → H in ABD63004. Ref.6
Sequence conflict2271Q → K in AAH22532. Ref.8

Secondary structure

.................................... 253
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 43DB596BAAA66484

FASTA25327,661
        10         20         30         40         50         60 
MANLGCWMLV LFVATWSDLG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGGWGQP 

        70         80         90        100        110        120 
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHSQWN KPSKPKTNMK HMAGAAAAGA 

       130        140        150        160        170        180 
VVGGLGGYML GSAMSRPIIH FGSDYEDRYY RENMHRYPNQ VYYRPMDEYS NQNNFVHDCV 

       190        200        210        220        230        240 
NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCITQYER ESQAYYQRGS SMVLFSSPPV 

       250 
ILLISFLIFL IVG 

« Hide

Isoform 2 (PrP(M8)) [UniParc].

Checksum: 309B13B142A41566
Show »

FASTA24626,885

References

« Hide 'large scale' references
[1]"Molecular cloning of a human prion protein cDNA."
Kretzschmar H.A., Stowring L.E., Westaway D., Stubblebine W.H., Prusiner S.B., Dearmond S.J.
DNA 5:315-324(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic structure of the human prion protein gene."
Puckett C., Concannon P., Casey C., Hood L.E.
Am. J. Hum. Genet. 49:320-329(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT 56-GLY--GLY-63 DEL.
Tissue: Brain.
[3]"Complete genomic sequence and analysis of the prion protein gene region from three mammalian species."
Lee I.Y., Westaway D., Smit A.F.A., Wang K., Seto J., Chen L., Acharya C., Ankener M., Baskin D., Cooper C., Yao H., Prusiner S.B., Hood L.E.
Genome Res. 8:1022-1037(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Novel PRNP sequence variant associated with familial encephalopathy."
Cervenakova L., Buetefisch C., Lee H.S., Taller I., Stone G., Gibbs C.J. Jr., Brown P., Hallett M., Goldfarb L.G.
Am. J. Med. Genet. 88:653-656(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GSD ARG-187.
Tissue: Blood.
[5]"Cloning of human prostate prion protein cDNA."
Hryb D.J., Reynolds T.A., Nakhla A.M., Kahn S.M., Khan S.M., Romas N.A., Rosner W.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Prostate.
[6]"Analysis and comparison of several mammalian prion protein genes Prnp."
Zhang J., Liu Y., Chen H., Jiang H., Lu W., Zhu X., Xie Q., Cai X., Liu X.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Ovary.
[9]"Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications."
Liao Y.-C.J., Lebo R.V., Clawson G.A., Smuckler E.A.
Science 233:364-367(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-253.
[10]"Deletion in the prion protein gene in a demented patient."
Diedrich J.F., Knopman D.S., List J.F., Olson K., Frey W.H., Emory C.R., Sung J.H., Haase A.T.
Hum. Mol. Genet. 1:443-444(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-232, VARIANT 56-GLY--GLY-63 DEL.
Tissue: Brain.
[11]"A prion-linked psychiatric disorder."
Samaia H.B., Mari J.J., Vallada H.P., Moura R.P., Simpson A.J.G., Brentani R.R.
Nature 390:241-241(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-253, VARIANT SCHIZOAFFECTIVE DISORDER SER-171.
[12]"SSCP analysis and sequencing of the human prion protein gene (PRNP) detects two different 24 bp deletions in an atypical Alzheimer's disease family."
Perry R.T., Go R.C., Harrell L.E., Acton R.T.
Am. J. Med. Genet. 60:12-18(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-85, VARIANT 56-GLY--GLY-63 DEL.
[13]"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."
Tagliavini F., Prelli F., Ghiso J., Bugiani O., Serban D., Prusiner S.B., Farlow M.R., Ghetti B., Frangione B.
EMBO J. 10:513-519(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 58-85 AND 111-150.
[14]"Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene."
Goldfarb L.G., Brown P., McCombie W.R., Goldgaber D., Swergold G.D., Wills P.R., Cervenakova L., Baron H., Gibbs C.J. Jr., Gajdusek D.C.
Proc. Natl. Acad. Sci. U.S.A. 88:10926-10930(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-91.
[15]"Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfate."
Mani K., Cheng F., Havsmark B., Jonsson M., Belting M., Fransson L.A.
J. Biol. Chem. 278:38956-38965(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-BINDING, FUNCTION.
[16]"The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4."
Chattopadhyay M., Walter E.D., Newell D.J., Jackson P.J., Aronoff-Spencer E., Peisach J., Gerfen G.J., Bennett B., Antholine W.E., Millhauser G.L.
J. Am. Chem. Soc. 127:12647-12656(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-BINDING.
[17]"The prion protein is a combined zinc and copper binding protein: Zn2+ alters the distribution of Cu2+ coordination modes."
Walter E.D., Stevens D.J., Visconte M.P., Millhauser G.L.
J. Am. Chem. Soc. 129:15440-15441(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-BINDING, ZINC-BINDING.
[18]"Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative initiation of translation."
Juanes M.E., Elvira G., Garcia-Grande A., Calero M., Gasset M.
J. Biol. Chem. 284:2787-2794(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION (ISOFORM 2), SUBCELLULAR LOCATION, MUTAGENESIS OF MET-1 AND MET-8.
[19]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197.
Tissue: Leukemic T-cell.
[20]"Glypican-1 mediates both prion protein lipid raft association and disease isoform formation."
Taylor D.R., Whitehouse I.J., Hooper N.M.
PLoS Pathog. 5:E1000666-E1000666(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISEASE ASSOCIATION.
[21]"Early onset prion disease from octarepeat expansion correlates with copper or zinc binding properties."
Stevens D.J., Walter E.D., Rodriguez A., Draper D., Davies P., Brown D.R., Millhauser G.L.
PLoS Pathog. 5:E1000390-E1000390(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-BINDING.
[22]"Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3."
Adrover M., Pauwels K., Prigent S., de Chiara C., Xu Z., Chapuis C., Pastore A., Rezaei H.
J. Biol. Chem. 285:21004-21012(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, DOMAIN.
[23]"Copper (II) promotes the formation of soluble neurotoxic PrP oligomers in acidic environment."
Wu D., Zhang W., Luo Q., Luo K., Huang L., Wang W., Huang T., Chen R., Lin Y., Pang D., Xiao G.
J. Cell. Biochem. 111:627-633(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-BINDING, CIRCULAR DICHROISM, DOMAIN, FUNCTION, SUBUNIT.
[24]"Characterizing the novel protein p33MONOX."
Mishra M., Inoue N., Heese K.
Mol. Cell. Biochem. 350:127-134(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIAA1191.
[25]"Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases."
Zhang Y., Swietnicki W., Zagorski M.G., Surewicz W.K., Soennichsen F.D.
J. Biol. Chem. 275:33650-33654(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 90-231 OF MUTANT LYS-200.
[26]"NMR solution structure of the human prion protein."
Zahn R., Liu A., Luhrs T., Riek R., von Schroetter C., Lopez Garcia F., Billeter M., Calzolai L., Wider G., Wuethrich K.
Proc. Natl. Acad. Sci. U.S.A. 97:145-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 23-230.
[27]"NMR structures of three single-residue variants of the human prion protein."
Calzolai L., Lysek D.A., Guntert P., von Schroetter C., Riek R., Zahn R., Wuethrich K.
Proc. Natl. Acad. Sci. U.S.A. 97:8340-8345(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 118-221.
[28]"Crystal structure of the human prion protein reveals a mechanism for oligomerization."
Knaus K.J., Morillas M., Swietnicki W., Malone M., Surewicz W.K., Yee V.C.
Nat. Struct. Biol. 8:770-774(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 119-226, DOMAIN, SUBUNIT.
[29]"Molecular features of the copper binding sites in the octarepeat domain of the prion protein."
Burns C.S., Aronoff-Spencer E., Dunham C.M., Lario P., Avdievich N.I., Antholine W.E., Olmstead M.M., Vrielink A., Gerfen G.J., Peisach J., Scott W.G., Millhauser G.L.
Biochemistry 41:3991-4001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.75 ANGSTROMS) OF 61-65 IN COMPLEX WITH COPPER ION, DOMAIN, SUBUNIT.
[30]"The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site."
Zahn R.
J. Mol. Biol. 334:477-488(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 61-68, DISULFIDE BOND, SUBUNIT.
[31]"Mutations and polymorphisms in the prion protein gene."
Palmer M.S., Collinge J.
Hum. Mutat. 2:168-173(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[32]"Genetic and infectious prion diseases."
Prusiner S.B.
Arch. Neurol. 50:1129-1153(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[33]"Atomic structures of amyloid cross-beta spines reveal varied steric zippers."
Sawaya M.R., Sambashivan S., Nelson R., Ivanova M.I., Sievers S.A., Apostol M.I., Thompson M.J., Balbirnie M., Wiltzius J.J., McFarlane H.T., Madsen A.O., Riekel C., Eisenberg D.
Nature 447:453-457(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS) OF 170-175, SUBUNIT, DOMAIN.
[34]"Crystal structure of human prion protein bound to a therapeutic antibody."
Antonyuk S.V., Trevitt C.R., Strange R.W., Jackson G.S., Sangar D., Batchelor M., Cooper S., Fraser C., Jones S., Georgiou T., Khalili-Shirazi A., Clarke A.R., Hasnain S.S., Collinge J.
Proc. Natl. Acad. Sci. U.S.A. 106:2554-2558(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 119-231 IN COMPLEX WITH FAB FRAGMENT OF MONOCLONAL ANTIBODY ICSM 18, SUBUNIT.
[35]"Conformational diversity in prion protein variants influences intermolecular beta-sheet formation."
Lee S., Antony L., Hartmann R., Knaus K.J., Surewicz K., Surewicz W.K., Yee V.C.
EMBO J. 29:251-262(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 125-227 OF VARIANT VAL-129; VARIANT FFI/CJD ASN-178 AND VARIANT GSD SER-198, SUBUNIT, DOMAIN.
[36]"Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome."
Hsiao K., Baker H.F., Crow T.J., Poulter M., Owen F., Terwilliger J.D., Westaway D., Ott J., Pursiner S.B.
Nature 338:342-345(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD LEU-102.
[37]"Pro-->Leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome."
Doh-Ura K., Tateishi J., Sasaki H., Kitamoto T., Sakaki Y.
Biochem. Biophys. Res. Commun. 163:974-979(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-102; VAL-117 AND VAL-129.
[38]"Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178."
Medori R., Montagna P., Tritschler H.J., Leblanc A., Cortelli P., Tinuper P., Lugaresi E., Gambetti P.
Neurology 42:669-670(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FFI ASN-178.
[39]"New mutation in scrapie amyloid precursor gene (at codon 178) in Finnish Creutzfeldt-Jakob kindred."
Goldfarb L.G., Haltia M., Brown P., Nieto A., Kovanen J., McCombie W.R., Trapp S., Gajdusek D.C.
Lancet 337:425-425(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CJD ASN-178.
[40]"Mutation in codon 200 of scrapie amyloid protein gene in two clusters of Creutzfeldt-Jakob disease in Slovakia."
Goldfarb L., Mitrova E., Brown P., Toh B.K., Gajdusek D.C.
Lancet 336:514-515(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CJD LYS-200.
[41]"Mutant prion proteins in Gerstmann-Straussler-Scheinker disease with neurofibrillary tangles."
Hsiao K., Dlouhy S.R., Farlow M.R., Cass C., da Costa M., Conneally P.M., Hodes M.E., Ghetti B., Prusiner S.B.
Nat. Genet. 1:68-71(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD ARG-217.
[42]"Novel missense variants of prion protein in Creutzfeldt-Jakob disease or Gerstmann-Straussler syndrome."
Kitamoto T., Ohta M., Doh-Ura K., Hitoshi S., Terao Y., Tateishi J.
Biochem. Biophys. Res. Commun. 191:709-714(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CJD ILE-180 AND ARG-232.
[43]"A new point mutation of the prion protein gene in Creutzfeldt-Jakob disease."
Pocchiari M., Salvatore M., Cutruzzola F., Genuardi M., Allcatelli C.T., Masullo C., Macchi G., Alema G., Galgani S., Xi Y.G., Petraroli R., Silvestrini M.C., Brunori M.
Ann. Neurol. 34:802-807(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CJD ILE-210.
[44]"A missense mutation at codon 105 with codon 129 polymorphism of the prion protein gene in a new variant of Gerstmann-Straussler-Scheinker disease."
Yamada M., Itoh Y., Fujigasaki H., Naruse S., Kaneko K., Kitamoto T., Tateishi J., Otomo E., Hayakawa M., Tanaka J., Matsushita M., Miyatake T.
Neurology 43:2723-2724(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD LEU-105.
[45]"A variant of Gerstmann-Straussler-Scheinker disease carrying codon 105 mutation with codon 129 polymorphism of the prion protein gene: a clinicopathological study."
Itoh Y., Yamada M., Hayakawa M., Shozawa T., Tanaka J., Matsushita M., Kitamoto T., Tateishi J., Otomo E.
J. Neurol. Sci. 127:77-86(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD LEU-105.
[46]"Japanese family with Creutzfeldt-Jakob disease with codon 200 point mutation of the prion protein gene."
Inoue I., Kitamoto T., Doh-Ura K., Shii H., Goto I., Tateishi J.
Neurology 44:299-301(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CJD LYS-200.
[47]"Mutation in codon 200 and polymorphism in codon 129 of the prion protein gene in Libyan Jews with Creutzfeldt-Jakob disease."
Gabizon R., Rosenman H., Meiner Z., Kahana I., Kahana E., Shugart Y., Ott J., Prusiner S.B.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 343:385-390(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CJD LYS-200.
[48]"Gerstmann-Straussler-Scheinker disease with mutation at codon 102 and methionine at codon 129 of PRNP in previously unreported patients."
Young K., Jones C.K., Piccardo P., Lazzarini A., Golbe L.I., Zimmerman T.R., Dickson D.W., McLachlan D.C., St George-Hyslop P.H., Lennox A.
Neurology 45:1127-1134(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD LEU-102.
[49]"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)."
Barbanti P., Fabbrini G., Salvatore M., Petraroli R., Cardone F., Maras B., Equestre M., Macchi G., Lenzi G.L., Pocchiari M.
Neurology 47:734-741(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD LEU-102, VARIANT LYS-219.
[50]"Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease."
Mastrianni J.A., Iannicola C., Myers R.M., Dearmond S., Prusiner S.B.
Neurology 47:1305-1312(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CJD HIS-208.
[51]"Familial spongiform encephalopathy associated with a novel prion protein gene mutation."
Nitrini R., Rosemberg S., Passos-Bueno M.R., da Silva L.S., Iughetti P., Papadopoulos M., Carrilho P.M., Caramelli P., Albrecht S., Zatz M., Leblanc A.
Ann. Neurol. 42:138-146(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CJD HIS-208.
[52]"Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity."
Piccardo P., Dlouhy S.R., Lievens P.M., Young K., Bird T.D., Nochlin D., Dickson D.W., Vinters H.V., Zimmerman T.R., Mackenzie I.R., Kish S.J., Ang L.C., De Carli C., Pocchiari M., Brown P., Gibbs C.J. Jr., Gajdusek D.C., Bugiani O. expand/collapse author list , Ironside J., Tagliavini F., Ghetti B.
J. Neuropathol. Exp. Neurol. 57:979-988(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD ASN-202 AND PRO-212.
[53]"Molecular genetics of human prion diseases in Germany."
Windl O., Giese A., Schulz-Schaeffer W., Zerr I., Skworc K., Arendt S., Oberdieck C., Bodemer M., Poser S., Kretzschmar H.A.
Hum. Genet. 105:244-252(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-188 AND SER-238.
[54]"High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes."
Finckh U., Mueller-Thomsen T., Mann U., Eggers C., Marksteiner J., Meins W., Binetti G., Alberici A., Hock C., Nitsch R.M., Gal A.
Am. J. Hum. Genet. 66:110-117(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EARLY-ONSET DEMENTIA LEU-102; ALA-183 AND LYS-188.
[55]"Identification of three novel mutations (E196K, V203I, E211Q) in the prion protein gene (PRNP) in inherited prion diseases with Creutzfeldt-Jakob disease phenotype."
Peoc'h K., Manivet P., Beaudry P., Attane F., Besson G., Didier H., Delasnerie-Laupretre N., Laplanche J.-L.
Hum. Mutat. 15:482-482(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CJD LYS-196; ILE-203 AND GLN-211.
[56]"A new PRNP mutation (G131V) associated with Gerstmann-Straussler-Scheinker disease."
Panegyres P.K., Toufexis K., Kakulas B.A., Cernevakova L., Brown P., Ghetti B., Piccardo P., Dlouhy S.R.
Arch. Neurol. 58:1899-1902(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD VAL-131.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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. Translation: CAB75503.1.
AL133396 Genomic DNA. Translation: CAI19053.1.
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.
PIRUJHU. A24173.
RefSeqNP_000302.1. NM_000311.3.
NP_001073590.1. NM_001080121.1.
NP_001073591.1. NM_001080122.1.
NP_001073592.1. NM_001080123.1.
NP_898902.1. NM_183079.2.
UniGeneHs.472010.
Hs.610285.
Hs.721670.

3D structure databases

PDBe
RCSB PDB
PDBj
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-A61-68[»]
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[»]
DisProtDP00466.
ProteinModelPortalP04156.
SMRP04156. Positions 2-28, 57-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111606. 59 interactions.
DIPDIP-29933N.
IntActP04156. 65 interactions.
MINTMINT-1420984.

Chemistry

BindingDBP04156.
ChEMBLCHEMBL4869.
DrugBankDB00759. Tetracycline.

PTM databases

PhosphoSiteP04156.

Polymorphism databases

DMDM130912.

Proteomic databases

PaxDbP04156.
PRIDEP04156.

Protocols and materials databases

DNASU5621.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379440; ENSP00000368752; ENSG00000171867. [P04156-1]
ENST00000430350; ENSP00000399376; ENSG00000171867. [P04156-1]
GeneID5621.
KEGGhsa:5621.
UCSCuc002wkt.1. human. [P04156-1]

Organism-specific databases

CTD5621.
GeneCardsGC20P004615.
HGNCHGNC:9449. PRNP.
HPAHPA042754.
MIM123400. phenotype.
137440. phenotype.
176640. gene.
245300. phenotype.
600072. phenotype.
603218. phenotype.
606688. phenotype.
neXtProtNX_P04156.
Orphanet280397. Familial Alzheimer-like prion disease.
466. Fatal familial insomnia.
356. Gerstmann-Straussler-Scheinker syndrome.
157941. Huntington disease-like 1.
282166. Inherited Creutzfeldt-Jakob disease.
PharmGKBPA33796.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41716.
HOVERGENHBG008260.
InParanoidP04156.
KOK05634.
OMAGYPHNPG.
OrthoDBEOG7DRJ4Q.
PhylomeDBP04156.
TreeFamTF105188.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressP04156.
BgeeP04156.
GenevestigatorP04156.

Family and domain databases

Gene3D1.10.790.10. 1 hit.
InterProIPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
IPR025860. Prion_N_dom.
[Graphical view]
PANTHERPTHR11522. PTHR11522. 1 hit.
PfamPF00377. Prion. 1 hit.
PF11587. Prion_bPrPp. 1 hit.
[Graphical view]
PRINTSPR00341. PRION.
SMARTSM00157. PRP. 1 hit.
[Graphical view]
SUPFAMSSF54098. SSF54098. 1 hit.
PROSITEPS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRNP. human.
EvolutionaryTraceP04156.
GenomeRNAi5621.
NextBio21844.
PMAP-CutDBP04156.
PROP04156.
SOURCESearch...

Entry information

Entry namePRIO_HUMAN
AccessionPrimary (citable) accession number: P04156
Secondary accession number(s): O60489 expand/collapse secondary AC list , P78446, Q15216, Q15221, Q27H91, Q5QPB4, Q8TBG0, Q96E70, Q9UP19
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: April 16, 2014
This is version 188 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries