Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Major prion protein

Gene

Prnp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu2+ or ZN2+ for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains.By similarity4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Copper or zinc 1By similarity
Metal bindingi61 – 611Copper or zinc 1; via amide nitrogenBy similarity
Metal bindingi62 – 621Copper or zinc 1; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi68 – 681Copper or zinc 2By similarity
Metal bindingi69 – 691Copper or zinc 2; via amide nitrogenBy similarity
Metal bindingi70 – 701Copper or zinc 2; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi76 – 761Copper or zinc 3By similarity
Metal bindingi77 – 771Copper or zinc 3; via amide nitrogenBy similarity
Metal bindingi78 – 781Copper or zinc 3; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi84 – 841Copper or zinc 4By similarity
Metal bindingi85 – 851Copper or zinc 4; via amide nitrogenBy similarity
Metal bindingi86 – 861Copper or zinc 4; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Prion

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_236183. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Major prion protein
Short name:
PrP
Alternative name(s):
PrP27-30
PrP33-35C
CD_antigen: CD230
Gene namesi
Name:Prnp
Synonyms:Prn-p, Prp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:97769. Prnp.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Amyloid, Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.

Disruption phenotypei

No obvious phenotype. Mice develop chronic demyelinating polyneuropathy after 60 weeks. Mice show abnormally low iron levels throughout the body, and are mildly anemic. Iron accumulates in duodenum enterocytes, suggesting impaired transport from the intestine to the blood.6 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011P → L: No effect on interaction with GRB2. 1 Publication
Mutagenesisi104 – 1041P → L: No effect on interaction with GRB2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 230208Major prion proteinPRO_0000025697Add
BLAST
Propeptidei231 – 25424Removed in mature formBy similarityPRO_0000025698Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Hydroxyproline1 Publication
Disulfide bondi178 ↔ 213
Glycosylationi180 – 1801N-linked (GlcNAc...)Curated
Glycosylationi196 – 1961N-linked (GlcNAc...)1 Publication
Lipidationi230 – 2301GPI-anchor amidated serineBy similarity

Post-translational modificationi

N-glycosylated.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Hydroxylation, Lipoprotein

Proteomic databases

MaxQBiP04925.
PaxDbiP04925.
PRIDEiP04925.

PTM databases

PhosphoSiteiP04925.

Miscellaneous databases

PMAP-CutDBP04925.

Expressioni

Tissue specificityi

Highly expressed in the brain, lung, kidney and heart. Expressed at low levels in the liver and spleen.2 Publications

Gene expression databases

BgeeiP04925.
CleanExiMM_PRNP.
ExpressionAtlasiP04925. baseline and differential.
GenevestigatoriP04925.

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 APP. Interacts with KIAA1191 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-768613,EBI-768613
Grb2Q606317EBI-768613,EBI-1688
PRNPP041563EBI-768613,EBI-977302From a different organism.

Protein-protein interaction databases

BioGridi202389. 38 interactions.
DIPiDIP-4N.
IntActiP04925. 11 interactions.
MINTiMINT-214988.

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni121 – 1233Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi127 – 1293Combined sources
Helixi143 – 15210Combined sources
Helixi153 – 1553Combined sources
Beta strandi160 – 1623Combined sources
Helixi165 – 1673Combined sources
Beta strandi168 – 1703Combined sources
Helixi171 – 19222Combined sources
Helixi199 – 22224Combined sources
Turni224 – 2285Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AG2NMR-A123-225[»]
1XYXNMR-A120-231[»]
1Y15NMR-A120-231[»]
1Y16NMR-A120-231[»]
2K5ONMR-A120-231[»]
2KFMNMR-A120-231[»]
2KFONMR-A120-231[»]
2KU5NMR-A120-231[»]
2KU6NMR-A120-231[»]
2L1DNMR-A120-231[»]
2L1ENMR-A120-231[»]
2L1HNMR-A120-231[»]
2L1KNMR-A120-231[»]
2L39NMR-A118-231[»]
2L40NMR-A120-231[»]
3NVGX-ray1.48A137-142[»]
3NVHX-ray1.61A137-143[»]
4H88X-ray1.90A120-230[»]
4J8RX-ray2.30I/J67-82[»]
4MA7X-ray1.97A116-229[»]
4MA8X-ray2.20C116-229[»]
DisProtiDP00265.
ProteinModelPortaliP04925.
SMRiP04925. Positions 2-28, 89-232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04925.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati51 – 5881
Repeati59 – 6682
Repeati67 – 7483
Repeati75 – 8284
Repeati83 – 9085

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 231209Interaction with GRB2, ERI3 and SYN1Add
BLAST
Regioni51 – 90405 X 8 AA tandem repeats of P-H-G-G-G-W-G-QAdd
BLAST

Domaini

The normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing 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 (By similarity).By similarity
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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the prion family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG41716.
HOGENOMiHOG000232077.
HOVERGENiHBG008260.
InParanoidiP04925.
KOiK05634.
OMAiQVYYRPV.
OrthoDBiEOG7DRJ4Q.
PhylomeDBiP04925.
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]

Sequencei

Sequence statusi: Complete.

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

P04925-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANLGYWLLA LFVTMWTDVG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP
60 70 80 90 100
PQGGTWGQPH GGGWGQPHGG SWGQPHGGSW GQPHGGGWGQ GGGTHNQWNK
110 120 130 140 150
PSKPKTNLKH VAGAAAAGAV VGGLGGYMLG SAMSRPMIHF GNDWEDRYYR
160 170 180 190 200
ENMYRYPNQV YYRPVDQYSN QNNFVHDCVN ITIKQHTVTT TTKGENFTET
210 220 230 240 250
DVKMMERVVE QMCVTQYQKE SQAYYDGRRS SSTVLFSSPP VILLISFLIF

LIVG
Length:254
Mass (Da):27,977
Last modified:January 1, 1990 - v2
Checksum:iD5331E6321826CC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331M → V in AAA39996. (PubMed:3462700)Curated
Sequence conflicti133 – 1331M → V in AAA39999. (PubMed:3923361)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti108 – 1081L → F Linked to long incubation time.
Natural varianti189 – 1891T → V Linked to long incubation time.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18070 Genomic DNA. Translation: AAA39997.1.
M18071 Genomic DNA. Translation: AAA39998.1.
M13685 mRNA. Translation: AAA39996.1.
U29186 Genomic DNA. Translation: AAC02804.1.
BC006703 mRNA. Translation: AAH06703.1.
M30384 mRNA. Translation: AAA39999.1.
CCDSiCCDS16766.1.
PIRiA29669. A23544.
RefSeqiNP_001265185.1. NM_001278256.1.
NP_035300.1. NM_011170.3.
UniGeneiMm.648.

Genome annotation databases

EnsembliENSMUST00000091288; ENSMUSP00000088833; ENSMUSG00000079037.
GeneIDi19122.
KEGGimmu:19122.
UCSCiuc008mly.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18070 Genomic DNA. Translation: AAA39997.1.
M18071 Genomic DNA. Translation: AAA39998.1.
M13685 mRNA. Translation: AAA39996.1.
U29186 Genomic DNA. Translation: AAC02804.1.
BC006703 mRNA. Translation: AAH06703.1.
M30384 mRNA. Translation: AAA39999.1.
CCDSiCCDS16766.1.
PIRiA29669. A23544.
RefSeqiNP_001265185.1. NM_001278256.1.
NP_035300.1. NM_011170.3.
UniGeneiMm.648.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AG2NMR-A123-225[»]
1XYXNMR-A120-231[»]
1Y15NMR-A120-231[»]
1Y16NMR-A120-231[»]
2K5ONMR-A120-231[»]
2KFMNMR-A120-231[»]
2KFONMR-A120-231[»]
2KU5NMR-A120-231[»]
2KU6NMR-A120-231[»]
2L1DNMR-A120-231[»]
2L1ENMR-A120-231[»]
2L1HNMR-A120-231[»]
2L1KNMR-A120-231[»]
2L39NMR-A118-231[»]
2L40NMR-A120-231[»]
3NVGX-ray1.48A137-142[»]
3NVHX-ray1.61A137-143[»]
4H88X-ray1.90A120-230[»]
4J8RX-ray2.30I/J67-82[»]
4MA7X-ray1.97A116-229[»]
4MA8X-ray2.20C116-229[»]
DisProtiDP00265.
ProteinModelPortaliP04925.
SMRiP04925. Positions 2-28, 89-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202389. 38 interactions.
DIPiDIP-4N.
IntActiP04925. 11 interactions.
MINTiMINT-214988.

Chemistry

BindingDBiP04925.
ChEMBLiCHEMBL3698.

PTM databases

PhosphoSiteiP04925.

Proteomic databases

MaxQBiP04925.
PaxDbiP04925.
PRIDEiP04925.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091288; ENSMUSP00000088833; ENSMUSG00000079037.
GeneIDi19122.
KEGGimmu:19122.
UCSCiuc008mly.2. mouse.

Organism-specific databases

CTDi5621.
MGIiMGI:97769. Prnp.

Phylogenomic databases

eggNOGiNOG41716.
HOGENOMiHOG000232077.
HOVERGENiHBG008260.
InParanoidiP04925.
KOiK05634.
OMAiQVYYRPV.
OrthoDBiEOG7DRJ4Q.
PhylomeDBiP04925.
TreeFamiTF105188.

Enzyme and pathway databases

ReactomeiREACT_236183. NCAM1 interactions.

Miscellaneous databases

ChiTaRSiPrnp. mouse.
EvolutionaryTraceiP04925.
NextBioi295714.
PMAP-CutDBP04925.
PROiP04925.
SOURCEiSearch...

Gene expression databases

BgeeiP04925.
CleanExiMM_PRNP.
ExpressionAtlasiP04925. baseline and differential.
GenevestigatoriP04925.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Distinct prion proteins in short and long scrapie incubation period mice."
    Westaway D., Goodman P.A., Mirenda C.A., McKinley M.P., Carlson G.A., Prusiner S.B.
    Cell 51:651-662(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: I/LnJ and NZW.
  2. "Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent."
    Locht C., Chesebro B., Race R., Keith J.M.
    Proc. Natl. Acad. Sci. U.S.A. 83:6372-6376(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Molecular pathology of scrapie-associated fibril protein (PrP) in mouse brain affected by the ME7 strain of scrapie."
    Hope J., Multhaup G., Reekie L.J.D., Kimberlin R.H., Beyreuther K.
    Eur. J. Biochem. 172:271-277(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  4. "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].
    Strain: NZW.
    Tissue: Brain.
  5. "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].
  6. "Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain."
    Chesebro B., Race R., Wehrly K., Nishio J., Bloom M., Lechner D., Bergstrom S., Robbins K., Mayer L., Keith J.M., Garon C., Haase A.
    Nature 315:331-333(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-164.
  7. Cited for: DISRUPTION PHENOTYPE.
  8. "Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus."
    Lledo P.M., Tremblay P., DeArmond S.J., Prusiner S.B., Nicoll R.A.
    Proc. Natl. Acad. Sci. U.S.A. 93:2403-2407(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Copper stimulates endocytosis of the prion protein."
    Pauly P.C., Harris D.A.
    J. Biol. Chem. 273:33107-33110(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo."
    Gill A.C., Ritchie M.A., Hunt L.G., Steane S.E., Davies K.G., Bocking S.P., Rhie A.G.O., Bennett A.D., Hope J.
    EMBO J. 19:5324-5331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION AT PRO-44.
  11. "PrPC directly interacts with proteins involved in signaling pathways."
    Spielhaupter C., Schaetzl H.M.
    J. Biol. Chem. 276:44604-44612(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH GRB2; ERI3 AND SYN1, MUTAGENESIS OF PRO-101 AND PRO-104.
  12. "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, SUBCELLULAR LOCATION, FUNCTION.
  13. "Copper-dependent co-internalization of the prion protein and glypican-1."
    Cheng F., Lindqvist J., Haigh C.L., Brown D.R., Mani K.
    J. Neurochem. 98:1445-1457(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, COPPER-BINDING.
  14. "Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis."
    Steele A.D., Emsley J.G., Ozdinler P.H., Lindquist S., Macklis J.D.
    Proc. Natl. Acad. Sci. U.S.A. 103:3416-3421(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, GLYCOSYLATION, FUNCTION, TISSUE SPECIFICITY.
  15. "Functional depletion of mahogunin by cytosolically exposed prion protein contributes to neurodegeneration."
    Chakrabarti O., Hegde R.S.
    Cell 137:1136-1147(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MGRN1.
  16. "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-196.
  17. "Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers."
    Lauren J., Gimbel D.A., Nygaard H.B., Gilbert J.W., Strittmatter S.M.
    Nature 457:1128-1132(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, INTERACTION WITH APP, FUNCTION.
  18. "Prion protein (PrP) knock-out mice show altered iron metabolism: a functional role for PrP in iron uptake and transport."
    Singh A., Kong Q., Luo X., Petersen R.B., Meyerson H., Singh N.
    PLoS ONE 4:E6115-E6115(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, GLYCOSYLATION, TISSUE SPECIFICITY.
  19. "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.
  20. Cited for: DISRUPTION PHENOTYPE.
  21. "NMR structure of the mouse prion protein domain PrP(121-321)."
    Riek R., Hornemann S., Wider G., Bileter M., Glockshuber R., Wuethrich K.
    Nature 382:180-182(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 120-230.
  22. "NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)."
    Riek R., Hornemann S., Wider G., Glockshuber R., Wuethrich K.
    FEBS Lett. 413:282-288(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-231.

Entry informationi

Entry nameiPRIO_MOUSE
AccessioniPrimary (citable) accession number: P04925
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 1, 1990
Last modified: February 4, 2015
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.