Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Major prion protein  

UniProtKB / Swiss-Prot ID :  PRIO_HUMAN

Gene Name (Synonyms) : 
PRNP, PRIP, PRP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor, GPI-anchor. Golgi apparatus. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of CU(2+), to vesicles in para- and perinuclear regions, where both proteins underg 

Protein Function :  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 Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity). 

Protein Sequence MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHG...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
56Missing. VAR_013763
102P -> L (in GSD and early-onset dementia). VAR_006464
105P -> L (in GSD). VAR_006465
117A -> V (linked to development ofdementing Gerstmann-Straussler disease).
129M -> V (polymorphism; determines thedisease phenotype in patients who have a
131G -> V (in GSD). VAR_014264
171N -> S (in schizoaffective disorder;dbSNP:rs16990018).
178D -> N (in FFI and CJD). VAR_006469
180V -> I (in CJD). VAR_006470
183T -> A (in familial spongiformencephalopathy).
187H -> R (in GSD). VAR_008746
188T -> K (in early-onset dementia; dementiaassociated to prion diseases).
188T -> R. VAR_008747
196E -> K (in CJD). VAR_008749
198F -> S (in GSD; atypical form withneurofibrillary tangles).
200E -> K (in CJD). VAR_006473
202D -> N (in GSD). VAR_008750
203V -> I (in CJD; it could be an extremelyrare polymorphism).
208R -> H (in CJD). VAR_006474
210V -> I (in CJD). VAR_006475
211E -> Q (in CJD). VAR_008752
212Q -> P (in GSD). VAR_008753
217Q -> R (in GSD; with neurofibrillarytangles).
219E -> K (in dbSNP:rs1800014). VAR_006477
232M -> R (in CJD). VAR_006478
238P -> S. VAR_008754
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
44HydroxyprolineGQGSPGGNR
CCCCCCCCC
62.63HPRD
Link-
96noneGGGTHSQWN
CCCCCCCCC
22.67HPRD
Link-
111noneTNMKHMAGA
CCCCCCCCC
10.68HPRD
Link-
179S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)FVHDCVNIT
EEEEEEEEE
1.20HPRD
Link
181N-linked (Glc...)HDCVNITIK
EEEEEEEEE
31.83HPRD
Link
181N-linked (GlcNAc...).HDCVNITIK
EEEEEEEEE
31.83UniProtKB
Link
197N-linked (Glc...)TKGENFTET
CCCCCCHHH
58.78HPRD
Link
197N-linked (GlcNAc...)TKGENFTET
CCCCCCHHH
58.78SysPTM
Link
197N-linked (GlcNAc...).TKGENFTET
CCCCCCHHH
58.78UniProtKB
Link
214S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)VEQMCITQY
HHHHHHHHH
2.81HPRD
Link
230GPI-anchor amidated serineYQRGSSMVL
HHCCCCEEE
19.90HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
Q8IV54_HUMANphysical interactionMINT-2876863MINT16713569
PRIO_HUMANcolocalization
physical interaction
physical interaction
physical interaction
colocalization
EBI-977412
EBI-977636
EBI-978
intact16286452
16286452
16286452
16286452
16286452
BAT3_HUMANphysical interactionEBI-735477
intact16169070
A4_HUMANphysical interactionEBI-979744
intact16286452
PSA3_HUMANphysical interactionEBI-953386
intact16713569
APLP1_HUMANin vivoHPRD:01453HPRD15146195
APLP2_HUMANin vivoHPRD:01453HPRD15146195
GRB2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01453HPRD11571277
APOE_HUMANin vivoHPRD:01453HPRD15146195
NCA11_HUMANin vivoHPRD:01453HPRD15146195
CH60_HUMANin vitro
in vivo
HPRD:01453HPRD8676499
DPP6_HUMANin vivoHPRD:01453HPRD15146195
GRP78_HUMANin vivoHPRD:01453HPRD15146195
MAG_HUMANin vivoHPRD:01453HPRD15146195
PLMN_HUMANin vivoHPRD:01453HPRD11100730
PSA3_HUMANyeast 2-hybridHPRD:01453HPRD16713569
T22D4_HUMANyeast 2-hybridHPRD:01453HPRD16713569
BAT3_HUMANyeast 2-hybridHPRD:01453HPRD16169070
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Disease Reference
Kegg disease
H00061 Prion diseases; Creutzfeldt-Jacob disease (CJD); Gerstmann-Straussler disease (GSD); Gerstmann-Strau
H01243 Huntington's disease-like syndrome
OMIM disease
Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humansNote=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
scrapie in sheep and goat
bovine spongiform encephalopathy (BSE) in cattle
transmissible mink encephalopathy (TME)
chronic wasting disease (CWD) of mule deer and elk
(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. 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
123400
600072Fatal familial insomnia (FFI)
137440Gerstmann-Straussler disease (GSD)
603218Huntington disease-like 1 (HDL1)
245300Kuru (KURU)
606688Spongiform encephalopathy with neuropsychiatric features (SENF)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures