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P04925

- PRIO_MOUSE

UniProt

P04925 - PRIO_MOUSE

Protein

Major prion protein

Gene

Prnp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
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    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. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Molecular functioni

    Prion

    Keywords - Ligandi

    Copper, Metal-binding, Zinc

    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. endoplasmic reticulum Source: MGI
    3. Golgi apparatus Source: MGI
    4. membrane Source: MGI
    5. membrane raft Source: MGI
    6. nucleolus Source: Ensembl
    7. plasma membrane Source: UniProtKB

    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

    ArrayExpressiP04925.
    BgeeiP04925.
    CleanExiMM_PRNP.
    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 – 1233
    Beta strandi124 – 1263
    Beta strandi127 – 1293
    Helixi143 – 15210
    Helixi153 – 1553
    Beta strandi160 – 1623
    Helixi165 – 1673
    Beta strandi168 – 1703
    Helixi171 – 19222
    Helixi199 – 22224
    Turni224 – 2285

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiHNPGYPH.
    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

    MANLGYWLLA LFVTMWTDVG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP    50
    PQGGTWGQPH GGGWGQPHGG SWGQPHGGSW GQPHGGGWGQ GGGTHNQWNK 100
    PSKPKTNLKH VAGAAAAGAV VGGLGGYMLG SAMSRPMIHF GNDWEDRYYR 150
    ENMYRYPNQV YYRPVDQYSN QNNFVHDCVN ITIKQHTVTT TTKGENFTET 200
    DVKMMERVVE QMCVTQYQKE SQAYYDGRRS SSTVLFSSPP VILLISFLIF 250
    LIVG 254
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS16766.1.
    PIRi A29669. A23544.
    RefSeqi NP_001265185.1. NM_001278256.1.
    NP_035300.1. NM_011170.3.
    UniGenei Mm.648.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AG2 NMR - A 123-225 [» ]
    1XYX NMR - A 120-231 [» ]
    1Y15 NMR - A 120-231 [» ]
    1Y16 NMR - A 120-231 [» ]
    2K5O NMR - A 120-231 [» ]
    2KFM NMR - A 120-231 [» ]
    2KFO NMR - A 120-231 [» ]
    2KU5 NMR - A 120-231 [» ]
    2KU6 NMR - A 120-231 [» ]
    2L1D NMR - A 120-231 [» ]
    2L1E NMR - A 120-231 [» ]
    2L1H NMR - A 120-231 [» ]
    2L1K NMR - A 120-231 [» ]
    2L39 NMR - A 118-231 [» ]
    2L40 NMR - A 120-231 [» ]
    3NVG X-ray 1.48 A 137-142 [» ]
    3NVH X-ray 1.61 A 137-143 [» ]
    4H88 X-ray 1.90 A 120-230 [» ]
    4J8R X-ray 2.30 I/J 67-82 [» ]
    4MA7 X-ray 1.97 A 116-229 [» ]
    4MA8 X-ray 2.20 C 116-229 [» ]
    DisProti DP00265.
    ProteinModelPortali P04925.
    SMRi P04925. Positions 2-28, 89-232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202389. 38 interactions.
    DIPi DIP-4N.
    IntActi P04925. 11 interactions.
    MINTi MINT-214988.

    Chemistry

    BindingDBi P04925.
    ChEMBLi CHEMBL3698.

    PTM databases

    PhosphoSitei P04925.

    Proteomic databases

    MaxQBi P04925.
    PaxDbi P04925.
    PRIDEi P04925.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000091288 ; ENSMUSP00000088833 ; ENSMUSG00000079037 .
    GeneIDi 19122.
    KEGGi mmu:19122.
    UCSCi uc008mly.2. mouse.

    Organism-specific databases

    CTDi 5621.
    MGIi MGI:97769. Prnp.

    Phylogenomic databases

    eggNOGi NOG41716.
    HOGENOMi HOG000232077.
    HOVERGENi HBG008260.
    InParanoidi P04925.
    KOi K05634.
    OMAi HNPGYPH.
    OrthoDBi EOG7DRJ4Q.
    PhylomeDBi P04925.
    TreeFami TF105188.

    Miscellaneous databases

    ChiTaRSi PRNP. mouse.
    EvolutionaryTracei P04925.
    NextBioi 295714.
    PMAP-CutDB P04925.
    PROi P04925.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04925.
    Bgeei P04925.
    CleanExi MM_PRNP.
    Genevestigatori P04925.

    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

    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: October 1, 2014
    This is version 161 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