P04156 (PRIO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-anchor › GPI-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 annimal 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]: Heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births. 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 process	Cell cycle Growth arrest
Cellular component	Amyloid Cell membrane Cytoplasm Golgi apparatus Membrane Nucleus
Coding sequence diversity	Alternative initiation Polymorphism
Disease	Disease mutation
Domain	Repeat Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Prion
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon 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: Compara 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: Compara 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: Compara response to copper ion Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB extrinsic to membrane Traceable author statement PubMed 16004966. Source: UniProtKB membrane raft Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	copper ion binding Inferred from direct assay Ref.29. Source: UniProtKB microtubule binding Inferred from direct assay PubMed 16004966. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		12	EBI-977302,EBI-977302
FAM64A	Q9BSJ6	5	EBI-977302,EBI-2568609
HOXA1	P49639	4	EBI-977302,EBI-740785
MPG	P29372	4	EBI-977302,EBI-1043398
PLK3	Q9H4B4	4	EBI-977302,EBI-751877

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Chain

23 – 230

208

Major prion protein

PRO_0000025675

Propeptide

231 – 253

23

Removed in mature form By similarity

PRO_0000025676

Regions

Repeat

51 – 59

9

1

Repeat

60 – 67

8

2

Repeat

68 – 75

8

3

Repeat

76 – 83

8

4

Repeat

84 – 91

8

5

Region

23 – 230

208

Interaction with GRB2, ERI3 and SYN1 By similarity

Region

51 – 91

41

5 X 8 AA tandem repeats of P-H-G-G-G-W-G-Q

Sites

Metal binding

61

1

Copper or zinc 1

Metal binding

62

1

Copper or zinc 1; via amide nitrogen

Metal binding

63

1

Copper or zinc 1; via amide nitrogen and carbonyl oxygen

Metal binding

69

1

Copper or zinc 2 Probable

Metal binding

70

1

Copper or zinc 2; via amide nitrogen Probable

Metal binding

71

1

Copper or zinc 2; via amide nitrogen and carbonyl oxygen Probable

Metal binding

77

1

Copper or zinc 3 Probable

Metal binding

78

1

Copper or zinc 3; via amide nitrogen Probable

Metal binding

79

1

Copper or zinc 3; via amide nitrogen and carbonyl oxygen Probable

Metal binding

85

1

Copper or zinc 4 Probable

Metal binding

86

1

Copper or zinc 4; via amide nitrogen Probable

Metal binding

87

1

Copper or zinc 4; via amide nitrogen and carbonyl oxygen Probable

Amino acid modifications

Lipidation

230

1

GPI-anchor amidated serine By similarity

Glycosylation

181

1

N-linked (GlcNAc...)

Glycosylation

197

1

N-linked (GlcNAc...) Ref.19

Disulfide bond

179 ↔ 214

Ref.30

Natural variations

Alternative sequence

1 – 7

7

Missing in isoform 2.

VSP_039045

Natural variant

56 – 63

8

Missing.

VAR_013763

Natural variant

102

1

P → L in GSD and early-onset dementia. Ref.36 Ref.37 Ref.48 Ref.49 Ref.54

VAR_006464

Natural variant

105

1

P → L in GSD. Ref.44 Ref.45

VAR_006465

Natural variant

117

1

A → V Linked to development of dementing Gerstmann-Straussler disease. Ref.37

VAR_006466

Natural variant

129

1

M → 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 variant

131

1

G → V in GSD. Ref.56

VAR_014264

Natural variant

171

1

N → S in schizoaffective disorder. Ref.11
Corresponds to variant rs16990018 [ dbSNP | Ensembl ].

VAR_006468

Natural variant

178

1

D → N in FFI and CJD. Ref.35 Ref.38 Ref.39

VAR_006469

Natural variant

180

1

V → I in CJD. Ref.42

VAR_006470

Natural variant

183

1

T → A in familial spongiform encephalopathy. Ref.54

VAR_006471

Natural variant

187

1

H → R in GSD. Ref.4

VAR_008746

Natural variant

188

1

T → K in early-onset dementia; dementia associated to prion diseases. Ref.54

VAR_008748

Natural variant

188

1

T → R. Ref.53

VAR_008747

Natural variant

196

1

E → K in CJD. Ref.55

VAR_008749

Natural variant

198

1

F → S in GSD; atypical form with neurofibrillary tangles. Ref.35

VAR_006472

Natural variant

200

1

E → K in CJD. Ref.25 Ref.40 Ref.46 Ref.47

VAR_006473

Natural variant

202

1

D → N in GSD. Ref.52

VAR_008750

Natural variant

203

1

V → I in CJD; it could be an extremely rare polymorphism. Ref.55

VAR_008751

Natural variant

208

1

R → H in CJD. Ref.50 Ref.51

VAR_006474

Natural variant

210

1

V → I in CJD. Ref.43

VAR_006475

Natural variant

211

1

E → Q in CJD. Ref.55

VAR_008752

Natural variant

212

1

Q → P in GSD. Ref.52

VAR_008753

Natural variant

217

1

Q → R in GSD; with neurofibrillary tangles. Ref.41

VAR_006476

Natural variant

219

1

E → K. Ref.49
Corresponds to variant rs1800014 [ dbSNP | Ensembl ].

VAR_006477

Natural variant

232

1

M → R in CJD. Ref.42

VAR_006478

Natural variant

238

1

P → S. Ref.53

VAR_008754

Experimental info

Mutagenesis

1

1

M → S: Protein detected. No protein detected; when associated with S-8. Ref.18

Mutagenesis

8

1

M → S: No protein detected; when associated with S-1. Ref.18

Sequence conflict

118

1

Missing in AAA19664. Ref.9

Sequence conflict

118

1

Missing in BAA00011. Ref.9

Sequence conflict

169

1

Y → H in ABD63004. Ref.6

Sequence conflict

227

1

Q → K in AAH22532. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

253

Helix Strand Turn

Details...

Beta strand

63 – 66

4

Beta strand

70 – 73

4

Turn

74 – 76

3

Beta strand

78 – 82

5

Beta strand

125 – 127

3

Beta strand

128 – 131

4

Beta strand

141 – 143

3

Helix

144 – 153

10

Helix

154 – 156

3

Beta strand

159 – 163

5

Helix

165 – 169

5

Helix

172 – 192

21

Turn

193 – 195

3

Helix

200 – 226

27

Turn

228 – 230

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1986. Version 1. Checksum: 43DB596BAAA66484	FASTA	253	27,661
	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
	Isoform 2 (PrP(M8)) [UniParc]. Checksum: 309B13B142A41566	FASTA	246	26,885
	10 20 30 40 50 60 MLVLFVATWS DLGLCKKRPK PGGWNTGGSR YPGQGSPGGN RYPPQGGGGW GQPHGGGWGQ 70 80 90 100 110 120 PHGGGWGQPH GGGWGQPHGG GWGQGGGTHS QWNKPSKPKT NMKHMAGAAA AGAVVGGLGG 130 140 150 160 170 180 YMLGSAMSRP IIHFGSDYED RYYRENMHRY PNQVYYRPMD EYSNQNNFVH DCVNITIKQH 190 200 210 220 230 240 TVTTTTKGEN FTETDVKMME RVVEQMCITQ YERESQAYYQ RGSSMVLFSS PPVILLISFL IFLIVG

References

	« Hide 'large scale' referencesShow '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. , 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, ZINK-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, MASS SPECTROMETRY. 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. , 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.

Web resources

The Official Mad Cow Disease Home Page

GeneReviews

Wikipedia

PRNP entry

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.

IPI

IPI00022284.
IPI00956325.

PIR

UJHU. A24173.

RefSeq

NP_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.

UniGene

Hs.472010.
Hs.597483.
Hs.610285.
Hs.721670.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E1G	NMR	-	A	125-228	[»]
1E1J	NMR	-	A	125-228	[»]
1E1P	NMR	-	A	125-228	[»]
1E1S	NMR	-	A	125-228	[»]
1E1U	NMR	-	A	125-228	[»]
1E1W	NMR	-	A	125-228	[»]
1FKC	NMR	-	A	90-231	[»]
1FO7	NMR	-	A	90-231	[»]
1H0L	NMR	-	A	121-230	[»]
1HJM	NMR	-	A	125-228	[»]
1HJN	NMR	-	A	125-228	[»]
1I4M	X-ray	2.00	A	119-226	[»]
1OEH	NMR	-	A	61-68	[»]
1OEI	NMR	-	A	61-84	[»]
1QLX	NMR	-	A	23-230	[»]
1QLZ	NMR	-	A	23-230	[»]
1QM0	NMR	-	A	90-230	[»]
1QM1	NMR	-	A	90-230	[»]
1QM2	NMR	-	A	121-230	[»]
1QM3	NMR	-	A	121-230	[»]
2IV4	NMR	-	A	180-195	[»]
2IV5	NMR	-	A	173-195	[»]
2IV6	NMR	-	A	173-195	[»]
2K1D	NMR	-	A	90-231	[»]
2KUN	NMR	-	A	90-231	[»]
2LBG	NMR	-	A	110-136	[»]
2LEJ	NMR	-	A	90-231	[»]
2LFT	NMR	-	A	90-231	[»]
2LSB	NMR	-	A	90-231	[»]
2LV1	NMR	-	A	90-231	[»]
2OL9	X-ray	0.85	A	170-175	[»]
2W9E	X-ray	2.90	A	119-231	[»]
3HAF	X-ray	2.26	A	90-231	[»]
3HAK	X-ray	1.80	A	125-227	[»]
3HEQ	X-ray	1.80	A/B	90-231	[»]
3HER	X-ray	1.85	A/B	90-231	[»]
3HES	X-ray	2.00	A/B	90-231	[»]
3HJ5	X-ray	3.10	A/B	90-231	[»]
3HJX	X-ray	2.00	A	126-231	[»]
3MD4	X-ray	1.15	A/B	127-132	[»]
3MD5	X-ray	1.40	A/B	127-132	[»]
3NHC	X-ray	1.57	A/B	127-132	[»]
3NHD	X-ray	1.92	A/B	127-132	[»]
3NVF	X-ray	1.80	A	138-143	[»]
4DGI	X-ray	2.40	A	120-230	[»]
4E1H	X-ray	1.40	A/C/E/G/I/K	177-182	[»]
			B/D/F/H/J/L	211-216	[»]
4E1I	X-ray	2.03	A/C/E/G/I/K	177-182	[»]
			B/D/F/H/J/L	211-216	[»]

DisProt

DP00466.

ProteinModelPortal

P04156.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29933N.

IntAct

P04156. 57 interactions.

MINT

MINT-1420984.

PTM databases

PhosphoSite

P04156.

Polymorphism databases

DMDM

130912.

Proteomic databases

PaxDb

P04156.

PRIDE

P04156.

Protocols and materials databases

DNASU

5621.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379440; ENSP00000368752; ENSG00000171867.
ENST00000430350; ENSP00000399376; ENSG00000171867.
ENST00000457586; ENSP00000415284; ENSG00000171867.

GeneID

5621.

KEGG

hsa:5621.

UCSC

uc002wkt.1. human.

Organism-specific databases

CTD

5621.

GeneCards

GC20P004615.

HGNC

HGNC:9449. PRNP.

HPA

HPA042754.

MIM

123400. phenotype.
137440. phenotype.
176640. gene.
245300. phenotype.
600072. phenotype.
603218. phenotype.
606688. phenotype.

neXtProt

NX_P04156.

Orphanet

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.

PharmGKB

PA33796.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41716.

HOVERGEN

HBG008260.

InParanoid

P04156.

KO

K05634.

OMA

GYPHNPG.

OrthoDB

EOG4HDSW2.

PhylomeDB

P04156.

Enzyme and pathway databases

Pathway_Interaction_DB

glypican_1pathway. Glypican 1 network.

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

P04156.

Bgee

P04156.

Genevestigator

P04156.

GermOnline

ENSG00000171867. Homo sapiens.

Family and domain databases

Gene3D

1.10.790.10. 1 hit.

InterPro

IPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
IPR025860. Prion_N_dom.
[Graphical view]

PANTHER

PTHR11522. PTHR11522. 1 hit.

Pfam

PF00377. Prion. 1 hit.
PF11587. Prion_bPrPp. 1 hit.
[Graphical view]

PRINTS

PR00341. PRION.

SMART

SM00157. PRP. 1 hit.
[Graphical view]

SUPFAM

SSF54098. Prion. 1 hit.

PROSITE

PS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P04156.

ChEMBL

CHEMBL4869.

ChiTaRS

PRNP. human.

DrugBank

DB00759. Tetracycline.

EvolutionaryTrace

P04156.

GenomeRNAi

5621.

NextBio

21844.

PMAP-CutDB

P04156.

SOURCE

Search...

Entry information

Entry name

PRIO_HUMAN

Accession

Primary (citable) accession number: P04156
Secondary accession number(s): O60489 , 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:	May 1, 2013
This is version 177 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.