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P04156

- PRIO_HUMAN

UniProt

P04156 - PRIO_HUMAN

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Protein

Major prion protein

Gene

PRNP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Copper or zinc 1
Metal bindingi62 – 621Copper or zinc 1; via amide nitrogen
Metal bindingi63 – 631Copper or zinc 1; via amide nitrogen and carbonyl oxygen
Metal bindingi69 – 691Copper or zinc 2Curated
Metal bindingi70 – 701Copper or zinc 2; via amide nitrogenCurated
Metal bindingi71 – 711Copper or zinc 2; via amide nitrogen and carbonyl oxygenCurated
Metal bindingi77 – 771Copper or zinc 3Curated
Metal bindingi78 – 781Copper or zinc 3; via amide nitrogenCurated
Metal bindingi79 – 791Copper or zinc 3; via amide nitrogen and carbonyl oxygenCurated
Metal bindingi85 – 851Copper or zinc 4Curated
Metal bindingi86 – 861Copper or zinc 4; via amide nitrogenCurated
Metal bindingi87 – 871Copper or zinc 4; via amide nitrogen and carbonyl oxygenCurated

GO - Molecular functioni

  1. copper ion binding Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. microtubule binding Source: UniProtKB
  4. tubulin binding Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cell cycle arrest Source: UniProtKB-KW
  3. cellular copper ion homeostasis Source: UniProtKB
  4. learning or memory Source: Ensembl
  5. metabolic process Source: ProtInc
  6. negative regulation of activated T cell proliferation Source: BHF-UCL
  7. negative regulation of apoptotic process Source: Ensembl
  8. negative regulation of calcineurin-NFAT signaling cascade Source: BHF-UCL
  9. negative regulation of interferon-gamma production Source: BHF-UCL
  10. negative regulation of interleukin-17 production Source: BHF-UCL
  11. negative regulation of interleukin-2 production Source: BHF-UCL
  12. negative regulation of protein phosphorylation Source: BHF-UCL
  13. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  14. negative regulation of T cell receptor signaling pathway Source: BHF-UCL
  15. protein homooligomerization Source: InterPro
  16. regulation of potassium ion transmembrane transport Source: Ensembl
  17. regulation of protein localization Source: Ensembl
  18. response to cadmium ion Source: Ensembl
  19. response to copper ion Source: Ensembl
  20. response to oxidative stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Prion

Keywords - Biological processi

Cell cycle, Growth arrest

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_18312. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Major prion protein
Short name:
PrP
Alternative name(s):
ASCR
PrP27-30
PrP33-35C
CD_antigen: CD230
Gene namesi
Name:PRNP
Synonyms:ALTPRP, PRIP, PRP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9449. PRNP.

Subcellular locationi

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

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. extrinsic component of membrane Source: UniProtKB
  7. Golgi apparatus Source: UniProtKB
  8. membrane raft Source: UniProtKB
  9. nucleus Source: UniProtKB-KW
  10. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

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.
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.9 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291M → 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. 1 Publication
Corresponds to variant rs1799990 [ dbSNP | Ensembl ].
VAR_006467
Natural varianti178 – 1781D → N in FFI and CJD. 2 Publications
VAR_006469
Natural varianti180 – 1801V → I in CJD. 1 Publication
VAR_006470
Natural varianti196 – 1961E → K in CJD. 1 Publication
VAR_008749
Natural varianti200 – 2001E → K in CJD. 3 Publications
VAR_006473
Natural varianti203 – 2031V → I in CJD; it could be an extremely rare polymorphism. 1 Publication
VAR_008751
Natural varianti208 – 2081R → H in CJD. 2 Publications
VAR_006474
Natural varianti210 – 2101V → I in CJD. 1 Publication
VAR_006475
Natural varianti211 – 2111E → Q in CJD. 1 Publication
VAR_008752
Natural varianti232 – 2321M → R in CJD. 1 Publication
VAR_006478
Fatal familial insomnia (FFI) [MIM:600072]: Autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291M → 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. 1 Publication
Corresponds to variant rs1799990 [ dbSNP | Ensembl ].
VAR_006467
Natural varianti178 – 1781D → N in FFI and CJD. 2 Publications
VAR_006469
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.9 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021P → L in GSD and early-onset dementia. 5 Publications
VAR_006464
Natural varianti105 – 1051P → L in GSD. 2 Publications
VAR_006465
Natural varianti131 – 1311G → V in GSD. 1 Publication
VAR_014264
Natural varianti187 – 1871H → R in GSD. 1 Publication
VAR_008746
Natural varianti198 – 1981F → S in GSD; atypical form with neurofibrillary tangles.
VAR_006472
Natural varianti202 – 2021D → N in GSD. 1 Publication
VAR_008750
Natural varianti212 – 2121Q → P in GSD. 1 Publication
VAR_008753
Natural varianti217 – 2171Q → R in GSD; with neurofibrillary tangles. 1 Publication
VAR_006476
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.
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.
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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11M → S: Protein detected. No protein detected; when associated with S-8. 1 Publication
Mutagenesisi8 – 81M → S: No protein detected; when associated with S-1. 1 Publication

Keywords - Diseasei

Amyloidosis, Disease mutation

Organism-specific databases

MIMi123400. phenotype.
137440. phenotype.
245300. phenotype.
600072. phenotype.
603218. phenotype.
606688. phenotype.
Orphaneti397606. Chronic diarrhea with hereditary sensory and autonomic neuropathy.
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.
PharmGKBiPA33796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 230208Major prion proteinPRO_0000025675Add
BLAST
Propeptidei231 – 25323Removed in mature formBy similarityPRO_0000025676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi179 ↔ 2141 Publication
Glycosylationi181 – 1811N-linked (GlcNAc...)
Glycosylationi197 – 1971N-linked (GlcNAc...)1 Publication
Lipidationi230 – 2301GPI-anchor amidated serineBy similarity

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
Isoform 2 is sumoylated with SUMO1.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Ubl conjugation

Proteomic databases

MaxQBiP04156.
PaxDbiP04156.
PRIDEiP04156.

PTM databases

PhosphoSiteiP04156.

Miscellaneous databases

PMAP-CutDBP04156.

Expressioni

Gene expression databases

BgeeiP04156.
ExpressionAtlasiP04156. baseline and differential.
GenevestigatoriP04156.

Organism-specific databases

HPAiHPA042754.

Interactioni

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. 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.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself17EBI-977302,EBI-977302
APPP050673EBI-977302,EBI-77613
APPP05067-42EBI-977302,EBI-302641
FAM64AQ9BSJ65EBI-977302,EBI-2568609
Grm5P31424-24EBI-8830282,EBI-8830305From a different organism.
HOXA1P496394EBI-977302,EBI-740785
MAPTP106362EBI-977302,EBI-366182
MPGP293724EBI-977302,EBI-1043398
PLK3Q9H4B44EBI-977302,EBI-751877
PRNPP102795EBI-977302,EBI-7430632From a different organism.
PRNPP239073EBI-977302,EBI-7670302From a different organism.
PrnpP049253EBI-977302,EBI-768613From a different organism.

Protein-protein interaction databases

BioGridi111606. 60 interactions.
DIPiDIP-29933N.
IntActiP04156. 65 interactions.
MINTiMINT-1420984.

Structurei

Secondary structure

1
253
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi63 – 675
Beta strandi70 – 734
Turni74 – 763
Beta strandi79 – 824
Beta strandi118 – 1225
Beta strandi125 – 1273
Beta strandi128 – 1314
Beta strandi141 – 1433
Helixi144 – 15310
Helixi154 – 1563
Beta strandi159 – 1635
Helixi166 – 1683
Turni171 – 1733
Beta strandi178 – 1814
Helixi185 – 1873
Turni188 – 1903
Turni193 – 1953
Beta strandi212 – 2154
Turni223 – 2253
Turni228 – 2303

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00466.
ProteinModelPortaliP04156.
SMRiP04156. Positions 2-28, 90-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04156.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati51 – 5991
Repeati60 – 6782
Repeati68 – 7583
Repeati76 – 8384
Repeati84 – 9185

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 230208Interaction with GRB2, ERI3 and SYN1By similarityAdd
BLAST
Regioni51 – 91415 X 8 AA tandem repeats of P-H-G-G-G-W-G-QAdd
BLAST

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).
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.

Sequence similaritiesi

Belongs to the prion family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG41716.
HOVERGENiHBG008260.
InParanoidiP04156.
KOiK05634.
OMAiHNPGYPH.
OrthoDBiEOG7DRJ4Q.
PhylomeDBiP04156.
TreeFamiTF105188.

Family and domain databases

Gene3Di1.10.790.10. 1 hit.
InterProiIPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
IPR025860. Prion_N_dom.
[Graphical view]
PANTHERiPTHR11522. PTHR11522. 1 hit.
PfamiPF00377. Prion. 1 hit.
PF11587. Prion_bPrPp. 1 hit.
[Graphical view]
PRINTSiPR00341. PRION.
SMARTiSM00157. PRP. 1 hit.
[Graphical view]
SUPFAMiSSF54098. SSF54098. 1 hit.
PROSITEiPS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P04156-1) [UniParc]FASTAAdd to Basket

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
Checksum:i43DB596BAAA66484
GO
Isoform 2 (identifier: P04156-2) [UniParc]FASTAAdd to Basket

Also known as: PrP(M8)

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

Show »
Length:246
Mass (Da):26,885
Checksum:i309B13B142A41566
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181Missing in AAA19664. (PubMed:3014653)Curated
Sequence conflicti118 – 1181Missing in BAA00011. (PubMed:3014653)Curated
Sequence conflicti169 – 1691Y → H in ABD63004. 1 PublicationCurated
Sequence conflicti227 – 2271Q → K in AAH22532. (PubMed:15489334)Curated

Polymorphismi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 638Missing.3 Publications
VAR_013763
Natural varianti102 – 1021P → L in GSD and early-onset dementia. 5 Publications
VAR_006464
Natural varianti105 – 1051P → L in GSD. 2 Publications
VAR_006465
Natural varianti117 – 1171A → V Linked to development of dementing Gerstmann-Straussler disease. 1 Publication
VAR_006466
Natural varianti129 – 1291M → 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. 1 Publication
Corresponds to variant rs1799990 [ dbSNP | Ensembl ].
VAR_006467
Natural varianti131 – 1311G → V in GSD. 1 Publication
VAR_014264
Natural varianti171 – 1711N → S in schizoaffective disorder. 1 Publication
Corresponds to variant rs16990018 [ dbSNP | Ensembl ].
VAR_006468
Natural varianti178 – 1781D → N in FFI and CJD. 2 Publications
VAR_006469
Natural varianti180 – 1801V → I in CJD. 1 Publication
VAR_006470
Natural varianti183 – 1831T → A in familial spongiform encephalopathy. 1 Publication
VAR_006471
Natural varianti187 – 1871H → R in GSD. 1 Publication
VAR_008746
Natural varianti188 – 1881T → K in early-onset dementia; dementia associated to prion diseases. 1 Publication
VAR_008748
Natural varianti188 – 1881T → R.1 Publication
VAR_008747
Natural varianti196 – 1961E → K in CJD. 1 Publication
VAR_008749
Natural varianti198 – 1981F → S in GSD; atypical form with neurofibrillary tangles.
VAR_006472
Natural varianti200 – 2001E → K in CJD. 3 Publications
VAR_006473
Natural varianti202 – 2021D → N in GSD. 1 Publication
VAR_008750
Natural varianti203 – 2031V → I in CJD; it could be an extremely rare polymorphism. 1 Publication
VAR_008751
Natural varianti208 – 2081R → H in CJD. 2 Publications
VAR_006474
Natural varianti210 – 2101V → I in CJD. 1 Publication
VAR_006475
Natural varianti211 – 2111E → Q in CJD. 1 Publication
VAR_008752
Natural varianti212 – 2121Q → P in GSD. 1 Publication
VAR_008753
Natural varianti217 – 2171Q → R in GSD; with neurofibrillary tangles. 1 Publication
VAR_006476
Natural varianti219 – 2191E → K.1 Publication
Corresponds to variant rs1800014 [ dbSNP | Ensembl ].
VAR_006477
Natural varianti232 – 2321M → R in CJD. 1 Publication
VAR_006478
Natural varianti238 – 2381P → S.1 Publication
VAR_008754

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 77Missing in isoform 2. CuratedVSP_039045

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. 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.
CCDSiCCDS13080.1. [P04156-1]
PIRiA24173. UJHU.
RefSeqiNP_000302.1. NM_000311.3. [P04156-1]
NP_001073590.1. NM_001080121.1. [P04156-1]
NP_001073591.1. NM_001080122.1. [P04156-1]
NP_001073592.1. NM_001080123.1. [P04156-1]
NP_898902.1. NM_183079.2. [P04156-1]
UniGeneiHs.472010.
Hs.610285.
Hs.721670.

Genome annotation databases

EnsembliENST00000379440; ENSP00000368752; ENSG00000171867. [P04156-1]
ENST00000430350; ENSP00000399376; ENSG00000171867. [P04156-1]
GeneIDi5621.
KEGGihsa:5621.
UCSCiuc002wkt.1. human. [P04156-1]

Polymorphism databases

DMDMi130912.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

The Official Mad Cow Disease Home Page
Wikipedia

PRNP entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. 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 .
CCDSi CCDS13080.1. [P04156-1 ]
PIRi A24173. UJHU.
RefSeqi NP_000302.1. NM_000311.3. [P04156-1 ]
NP_001073590.1. NM_001080121.1. [P04156-1 ]
NP_001073591.1. NM_001080122.1. [P04156-1 ]
NP_001073592.1. NM_001080123.1. [P04156-1 ]
NP_898902.1. NM_183079.2. [P04156-1 ]
UniGenei Hs.472010.
Hs.610285.
Hs.721670.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 77-84 [» ]
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 [» ]
2M8T 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 [» ]
4KML X-ray 1.50 A 24-231 [» ]
4N9O X-ray 1.50 A 90-231 [» ]
DisProti DP00466.
ProteinModelPortali P04156.
SMRi P04156. Positions 2-28, 90-231.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111606. 60 interactions.
DIPi DIP-29933N.
IntActi P04156. 65 interactions.
MINTi MINT-1420984.

Chemistry

BindingDBi P04156.
ChEMBLi CHEMBL4869.
DrugBanki DB00759. Tetracycline.

PTM databases

PhosphoSitei P04156.

Polymorphism databases

DMDMi 130912.

Proteomic databases

MaxQBi P04156.
PaxDbi P04156.
PRIDEi P04156.

Protocols and materials databases

DNASUi 5621.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379440 ; ENSP00000368752 ; ENSG00000171867 . [P04156-1 ]
ENST00000430350 ; ENSP00000399376 ; ENSG00000171867 . [P04156-1 ]
GeneIDi 5621.
KEGGi hsa:5621.
UCSCi uc002wkt.1. human. [P04156-1 ]

Organism-specific databases

CTDi 5621.
GeneCardsi GC20P004615.
GeneReviewsi PRNP.
HGNCi HGNC:9449. PRNP.
HPAi HPA042754.
MIMi 123400. phenotype.
137440. phenotype.
176640. gene.
245300. phenotype.
600072. phenotype.
603218. phenotype.
606688. phenotype.
neXtProti NX_P04156.
Orphaneti 397606. Chronic diarrhea with hereditary sensory and autonomic neuropathy.
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.
PharmGKBi PA33796.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41716.
HOVERGENi HBG008260.
InParanoidi P04156.
KOi K05634.
OMAi HNPGYPH.
OrthoDBi EOG7DRJ4Q.
PhylomeDBi P04156.
TreeFami TF105188.

Enzyme and pathway databases

Reactomei REACT_18312. NCAM1 interactions.

Miscellaneous databases

ChiTaRSi PRNP. human.
EvolutionaryTracei P04156.
GenomeRNAii 5621.
NextBioi 21844.
PMAP-CutDB P04156.
PROi P04156.
SOURCEi Search...

Gene expression databases

Bgeei P04156.
ExpressionAtlasi P04156. baseline and differential.
Genevestigatori P04156.

Family and domain databases

Gene3Di 1.10.790.10. 1 hit.
InterProi IPR000817. Prion.
IPR022416. Prion/Doppel_prot_b-ribbon_dom.
IPR025860. Prion_N_dom.
[Graphical view ]
PANTHERi PTHR11522. PTHR11522. 1 hit.
Pfami PF00377. Prion. 1 hit.
PF11587. Prion_bPrPp. 1 hit.
[Graphical view ]
PRINTSi PR00341. PRION.
SMARTi SM00157. PRP. 1 hit.
[Graphical view ]
SUPFAMi SSF54098. SSF54098. 1 hit.
PROSITEi PS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-232, VARIANT 56-GLY--GLY-63 DEL.
    Tissue: Brain.
  11. 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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS) OF 170-175, SUBUNIT, DOMAIN.
  34. 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. 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. Cited for: VARIANT CJD HIS-208.
  52. Cited for: VARIANTS GSD ASN-202 AND PRO-212.
  53. 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.

Entry informationi

Entry nameiPRIO_HUMAN
AccessioniPrimary (citable) accession number: P04156
Secondary accession number(s): O60489
, P78446, Q15216, Q15221, Q27H91, Q5QPB4, Q8TBG0, Q96E70, Q9UP19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: October 29, 2014
This is version 194 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

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.

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3