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Reviewed, UniProtKB/Swiss-Prot P04156 (PRIO_HUMAN)

Last modified July 7, 2009. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

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

General annotation (Comments)

Function

The physiological function of PrP is not known.

Subunit structure

PrP has a tendency to aggregate yielding polymers called "rods". Interacts with GRB2, PRNPIP and SYN1 By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor. Golgi apparatus By similarity.

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.

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 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.25 Ref.26 Ref.28 Ref.29 Ref.32 Ref.33 Ref.36 Ref.37 Ref.41

Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:123400]. CJD 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. Ref.25 Ref.26 Ref.28 Ref.29 Ref.32 Ref.33 Ref.36 Ref.37 Ref.41

Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:600072]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia. Ref.24

Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:137440]. GSD is a 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. Ref.4 Ref.22 Ref.27 Ref.30 Ref.31 Ref.34 Ref.35 Ref.38 Ref.42

Defects in PRNP are the cause of Huntington disease-like 1 (HDL1) [MIM:603218]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.

Defects in PRNP are the cause of 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.

Defects in PRNP are the cause of prion disease with protracted course [MIM:606688]; an 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.

Sequence similarities

Belongs to the prion family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-977302,EBI-977302
AldocP050631EBI-977302,EBI-444845From a different organism.
APPP050671EBI-977302,EBI-77613
Hnrnpa2b1O885691EBI-977302,EBI-299636From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

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

Amino acid modifications

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

Natural variations

Natural variant56 – 638Missing Ref.2 Ref.10 Ref.12
VAR_013763
Natural variant1021P → L in GSD and early-onset dementia.
VAR_006464
Natural variant1051P → L in GSD. Ref.30 Ref.31
VAR_006465
Natural variant1171A → V Linked to development of dementing Gerstmann-Straussler disease. Ref.23
VAR_006466
Natural variant1291M → V Polymorphism; determines the disease phenotype in patients who have a PrP mutation at position 178. Patients with M-129 develop FFI, those with V-129 develop CJD. dbSNP rs1799990. Ref.23
VAR_006467
Natural variant1311G → V in GSD. Ref.42
VAR_014264
Natural variant1711N → S in schizoaffective disorder. dbSNP rs16990018. Ref.11
VAR_006468
Natural variant1781D → N in FFI and CJD.
VAR_006469
Natural variant1801V → I in CJD. Ref.28
VAR_006470
Natural variant1831T → A in familial spongiform encephalopathy. Ref.40
VAR_006471
Natural variant1871H → R in GSD. Ref.4
VAR_008746
Natural variant1881T → K in early-onset dementia; dementia associated to prion diseases. Ref.40 Ref.39
VAR_008748
Natural variant1881T → R Ref.40 Ref.39
VAR_008747
Natural variant1961E → K in CJD. Ref.41
VAR_008749
Natural variant1981F → S in GSD; atypical form with neurofibrillary tangles.
VAR_006472
Natural variant2001E → K in CJD. Ref.26 Ref.32 Ref.33
VAR_006473
Natural variant2021D → N in GSD. Ref.38
VAR_008750
Natural variant2031V → I in CJD; it could be an extremely rare polymorphism. Ref.41
VAR_008751
Natural variant2081R → H in CJD. Ref.36 Ref.37
VAR_006474
Natural variant2101V → I in CJD. Ref.29
VAR_006475
Natural variant2111E → Q in CJD. Ref.41
VAR_008752
Natural variant2121Q → P in GSD. Ref.38
VAR_008753
Natural variant2171Q → R in GSD; with neurofibrillary tangles. Ref.27
VAR_006476
Natural variant2191E → K: dbSNP rs1800014. Ref.35
VAR_006477
Natural variant2321M → R in CJD. Ref.28
VAR_006478
Natural variant2381P → S Ref.39
VAR_008754

Experimental info

Sequence conflict1181Missing in AAA19664. Ref.9
Sequence conflict1181Missing in BAA00011. Ref.9
Sequence conflict1691Y → H in ABD63004. Ref.6
Sequence conflict2271Q → K in AAH22532. Ref.8

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P04156-1 [UniParc].

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

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

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

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

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

       250 
ILLISFLIFL IVG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a human prion protein cDNA."
Kretzschmar H.A., Stowring L.E., Westaway D., Stubblebine W.H., Prusiner S.B., Dearmond S.J.
DNA 5:315-324(1986) [PubMed: 3755672] [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: 1678248] [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: 9799790] [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: 10581485] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GSD ARG-187.
Tissue: Blood.
[5]"Cloning of human prostate prion protein cDNA."
Hryb D.J., Reynolds T.A., Nakhla A.M., Kahn S.M., Khan S.M., Romas N.A., Rosner W.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Prostate.
[6]"Analysis and comparison of several mammalian prion protein genes Prnp."
Zhang J., Liu Y., Chen H., Jiang H., Lu W., Zhu X., Xie Q., Cai X., Liu X.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed: 11780052] [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: 15489334] [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: 3014653] [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: 1363802] [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: 9384372] [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: 7485229] [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: 1672107] [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: 1683708] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-91.
[15]"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: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197, MASS SPECTROMETRY.
[16]"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: 10954699] [Abstract]
Cited for: STRUCTURE BY NMR OF 90-231 OF MUTANT LYS-200.
[17]"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: 10618385] [Abstract]
Cited for: STRUCTURE BY NMR OF 23-230.
[18]"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: 10900000] [Abstract]
Cited for: STRUCTURE BY NMR OF 118-221.
[19]"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: 14623188] [Abstract]
Cited for: STRUCTURE BY NMR OF 61-68.
[20]"Mutations and polymorphisms in the prion protein gene."
Palmer M.S., Collinge J.
Hum. Mutat. 2:168-173(1993) [PubMed: 8364585] [Abstract]
Cited for: REVIEW ON VARIANTS.
[21]"Genetic and infectious prion diseases."
Prusiner S.B.
Arch. Neurol. 50:1129-1153(1993) [PubMed: 8105771] [Abstract]
Cited for: REVIEW ON VARIANTS.
[22]"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: 2564168] [Abstract]
Cited for: VARIANT GSD LEU-102.
[23]"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: 2783132] [Abstract]
Cited for: VARIANTS LEU-102; VAL-117 AND VAL-129.
[24]"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: 1347910] [Abstract]
Cited for: VARIANT FFI ASN-178.
[25]"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: 1671440] [Abstract]
Cited for: VARIANT CJD ASN-178.
[26]"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: 1975028] [Abstract]
Cited for: VARIANT CJD LYS-200.
[27]"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: 1363810] [Abstract]
Cited for: VARIANT GSD ARG-217.
[28]"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: 8461023] [Abstract]
Cited for: VARIANTS CJD ILE-180 AND ARG-232.
[29]"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: 7902693] [Abstract]
Cited for: VARIANT CJD ILE-210.
[30]"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: 7902972] [Abstract]
Cited for: VARIANT GSD LEU-105.
[31]"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: 7699395] [Abstract]
Cited for: VARIANT GSD LEU-105.
[32]"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: 7906019] [Abstract]
Cited for: VARIANT CJD LYS-200.
[33]"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: 7913755] [Abstract]
Cited for: VARIANT CJD LYS-200.
[34]"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: 7783876] [Abstract]
Cited for: VARIANT GSD LEU-102.
[35]"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: 8797472] [Abstract]
Cited for: VARIANT GSD LEU-102, VARIANT LYS-219.
[36]"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: 8909447] [Abstract]
Cited for: VARIANT CJD HIS-208.
[37]"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: 9266722] [Abstract]
Cited for: VARIANT CJD HIS-208.
[38]"Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity."
Piccardo P., Dlouhy S.R., Lievens P.M., Young K., Bird T.D., Nochlin D., Dickson D.W., Vinters H.V., Zimmerman T.R., Mackenzie I.R., Kish S.J., Ang L.C., De Carli C., Pocchiari M., Brown P., Gibbs C.J. Jr., Gajdusek D.C., Bugiani O. expand/collapse author list , Ironside J., Tagliavini F., Ghetti B.
J. Neuropathol. Exp. Neurol. 57:979-988(1998) [PubMed: 9786248] [Abstract]
Cited for: VARIANTS GSD ASN-202 AND PRO-212.
[39]"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: 10987652] [Abstract]
Cited for: VARIANTS ARG-188 AND SER-238.
[40]"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: 10631141] [Abstract]
Cited for: VARIANTS EARLY-ONSET DEMENTIA LEU-102; ALA-183 AND LYS-188.
[41]"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: 10790216] [Abstract]
Cited for: VARIANTS CJD LYS-196; ILE-203 AND GLN-211.
[42]"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: 11709001] [Abstract]
Cited for: VARIANT GSD VAL-131.
+Additional computationally mapped references.

Cross-references

Sequence databases

M13899 mRNA. Translation: AAA60182.1.
X83416 Genomic DNA. Translation: CAA58442.1.
U29185 Genomic DNA. Translation: AAC78725.1.
AY008282 mRNA. Translation: AAG21693.1.
AF076976 Genomic DNA. Translation: AAD46098.1.
DQ408531 Genomic DNA. Translation: ABD63004.1.
AL133396 Genomic DNA. Translation: CAB75503.1.
BC012844 mRNA. Translation: AAH12844.1.
BC022532 mRNA. Translation: AAH22532.1.
M13667 mRNA. Translation: AAA19664.1.
D00015 mRNA. Translation: BAA00011.1.
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.
IPIIPI00022284.
PIRUJHU. A24173.
RefSeqNP_000302.1.
NP_001073590.1.
NP_001073591.1.
NP_001073592.1.
NP_898902.1.
UniGeneHs.472010
Hs.610285
Hs.714553

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1E1GNMR-A125-228[»]
1E1JNMR-A125-228[»]
1E1PNMR-A125-228[»]
1E1SNMR-A125-228[»]
1E1UNMR-A125-228[»]
1E1WNMR-A125-228[»]
1FKCNMR-A90-231[»]
1FO7NMR-A90-231[»]
1H0LNMR-A121-230[»]
1HJMNMR-A125-228[»]
1HJNNMR-A125-228[»]
1I4MX-ray2.00A119-226[»]
1OEHNMR-A61-68[»]
1OEINMR-A61-84[»]
1QLXNMR-A23-230[»]
1QLZNMR-A23-230[»]
1QM0NMR-A90-230[»]
1QM1NMR-A90-230[»]
1QM2NMR-A121-230[»]
1QM3NMR-A121-230[»]
2K1DNMR-A90-231[»]
2W9EX-ray2.90A119-231[»]
DisProtDP00466.
ModBaseSearch...

Protein-protein interaction databases

IntActP04156. 10 interactions.

Proteomic databases

PRIDEP04156.

Genome annotation databases

EnsemblENSG00000171867. Homo sapiens. [Contig view]
GeneID5621.
KEGGhsa:5621.
UCSCuc002wku.1. human.

Organism-specific databases

GeneCardsGC20P004615.
H-InvDBHIX0015613.
HGNCHGNC:9449. PRNP.
MIM123400. phenotype.
137440. phenotype.
176640. gene.
245300. phenotype.
600072. phenotype.
603218. phenotype.
606688. phenotype.
Orphanet204. Creutzfeldt-Jakob disease.
356. Gerstmann-Straussler-Scheinker syndrome.
157941. Huntington disease-like 1.
466. Insomnia, familial fatal.
PharmGKBPA33796.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP04156.
OMAP04156. PNQVYYR.

Enzyme and pathway databases

Pathway_Interaction_DBglypican_1pathway. Glypican 1 network.

Gene expression databases

ArrayExpressP04156.
BgeeP04156.
GermOnlineENSG00000171867. Homo sapiens.

Family and domain databases

InterProIPR000817. Prion.
[Graphical view]
Gene3DG3DSA:1.10.790.10. Prion. 1 hit.
PANTHERPTHR11522. Prion. 1 hit.
PfamPF00377. Prion. 1 hit.
PF03991. Prion_octapep. 5 hits.
[Graphical view]
PRINTSPR00341. PRION.
SMARTSM00157. PRP. 1 hit.
[Graphical view]
PROSITEPS00291. PRION_1. 1 hit.
PS00706. PRION_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00759. Tetracycline.
NextBio21844.
PMAP-CutDBP04156.
SOURCESearch...

Entry information

Entry namePRIO_HUMAN
AccessionPrimary (citable) accession number: P04156
Secondary accession number(s): O60489 expand/collapse secondary AC list , P78446, Q15216, Q15221, Q27H91, Q8TBG0, Q96E70, Q9UP19
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: July 7, 2009
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human cell differentiation molecules

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

Human chromosome 20

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents