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MGI:Prnp

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Contents

Species (Taxon ID) Mus musculus (house mouse) (taxon:10090)
Gene Name(s) Prnp ( synonyms: CD230, Prn-i, Prn-p, PrP, PrPC, PrPSc, Sinc )
Protein Name(s) prion protein,
External Links
MGI MGI:97769

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0001933

negative regulation of protein phosphorylation

MGI:MGI:4943618
PMID:20145049[1]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0005507

copper ion binding

MGI:MGI:2652950
PMID:12500977[2]

IDA: Inferred from Direct Assay

F

From MGI

GO:0005507

copper ion binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P04156

F

From MGI

GO:0005515

protein binding

MGI:MGI:2153789
PMID:11571277[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q8C460
UniProtKB:Q60631
UniProtKB:O88935-1

F

From MGI

GO:0005624

membrane fraction

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P13852

C

From MGI

GO:0005634

nucleus

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:F5GY30

C

From MGI

GO:0005730

nucleolus

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:F5GY30

C

From MGI

GO:0005737

cytoplasm

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P13852

C

From MGI

GO:0005783

endoplasmic reticulum

MGI:MGI:2175940
PMID:11756421[4]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005794

Golgi apparatus

MGI:MGI:2175940
PMID:11756421[4]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005886

plasma membrane

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P13852

C

From MGI

GO:0005886

plasma membrane

MGI:MGI:4821089
PMID:9837873[5]

IDA: Inferred from Direct Assay

C

From MGI

GO:0006139

nucleobase-containing compound metabolic process

MGI:MGI:2386138
PMID:12206674[6]

TAS: Traceable Author Statement

P

From MGI

GO:0006878

cellular copper ion homeostasis

MGI:MGI:2175940
PMID:11756421[4]

TAS: Traceable Author Statement

P

From MGI

GO:0006916

anti-apoptosis

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P13852

P

From MGI

GO:0006979

response to oxidative stress

MGI:MGI:2652950
PMID:12500977[2]

IDA: Inferred from Direct Assay

P

From MGI

GO:0007611

learning or memory

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P13852

P

From MGI

GO:0008017

microtubule binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P04156

F

From MGI

GO:0015631

tubulin binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P04156

F

From MGI

GO:0016020

membrane

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0472

C

From MGI

GO:0016020

membrane

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR000817
InterPro:IPR022416

C

From MGI

GO:0031225

anchored to membrane

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0336

C

From MGI

GO:0032689

negative regulation of interferon-gamma production

MGI:MGI:4943618
PMID:20145049[1]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0032700

negative regulation of interleukin-17 production

MGI:MGI:4943618
PMID:20145049[1]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0032703

negative regulation of interleukin-2 production

MGI:MGI:4943618
PMID:20145049[1]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0042802

identical protein binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P04156

F

From MGI

GO:0043008

ATP-dependent protein binding

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P13852

F

From MGI

GO:0043066

negative regulation of apoptotic process

MGI:MGI:3579917
PMID:15753097[7]

IGI: Inferred from Genetic Interaction

MGI:MGI:99702

P

From MGI

GO:0043231

intracellular membrane-bounded organelle

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:F5GY30

C

From MGI

GO:0043433

negative regulation of sequence-specific DNA binding transcription factor activity

MGI:MGI:4943618
PMID:20145049[1]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0045121

membrane raft

MGI:MGI:2182534
PMID:12091459[8]

TAS: Traceable Author Statement

C

From MGI

GO:0045121

membrane raft

MGI:MGI:2674181
PMID:12927782[9]

IDA: Inferred from Direct Assay

C

From MGI

GO:0046007

negative regulation of activated T cell proliferation

MGI:MGI:4943618
PMID:20145049[1]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0046686

response to cadmium ion

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P13852

P

From MGI

GO:0046688

response to copper ion

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P13852

P

From MGI

GO:0046872

metal ion binding

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0479

F

From MGI

GO:0050860

negative regulation of T cell receptor signaling pathway

MGI:MGI:4943618
PMID:20145049[1]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0051087

chaperone binding

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P13852

F

From MGI

GO:0051260

protein homooligomerization

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR000817
InterPro:IPR022416

P

From MGI

GO:0070885

negative regulation of calcineurin-NFAT signaling cascade

MGI:MGI:4943618
PMID:20145049[1]

IMP: Inferred from Mutant Phenotype

P

From MGI


Notes

References

See Help:References for how to manage references in GONUTS.
  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 Hu W et al. (2010) Pharmacological prion protein silencing accelerates central nervous system autoimmune disease via T cell receptor signalling. Brain 133: 375-88 PubMed GONUTS page
  2. 2.0 2.1 Rachidi W et al. (2003) Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery. J Biol Chem 278: 9064-72 PubMed GONUTS page
  3. Spielhaupter C & Schätzl HM (2001) PrPC directly interacts with proteins involved in signaling pathways. J Biol Chem 276: 44604-12 PubMed GONUTS page
  4. 4.0 4.1 4.2 Lorenz H et al. (2002) Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases. J Biol Chem 277: 8508-16 PubMed GONUTS page
  5. Pauly PC & Harris DA (1998) Copper stimulates endocytosis of the prion protein. J Biol Chem 273: 33107-10 PubMed GONUTS page
  6. Nandi PK et al. (2002) Unusual property of prion protein unfolding in neutral salt solution. Biochemistry 41: 11017-24 PubMed GONUTS page
  7. Li A & Harris DA (2005) Mammalian prion protein suppresses Bax-induced cell death in yeast. J Biol Chem 280: 17430-4 PubMed GONUTS page
  8. Shaked Y et al. (2002) The binding of prion proteins to serum components is affected by detergent extraction conditions. J Neurochem 82: 1-5 PubMed GONUTS page
  9. Rouvinski A et al. (2003) Both raft- and non-raft proteins associate with CHAPS-insoluble complexes: some APP in large complexes. Biochem Biophys Res Commun 308: 750-8 PubMed GONUTS page
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