Skip Header

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

UniProtKB - P04156 (PRIO_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Major prion protein

Gene

PRNP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. 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 similarity).By similarityCurated3 Publications

Miscellaneous

This protein is produced by a bicistronic gene which also produces the The alternative prion protein/AltPrP (AC F7VJQ1) from an overlapping reading frame.1 Publication
The alternative prion protein/AltPrP (AC F7VJQ1) and PRNP have no apparent direct functional relation since a mutation that removes the start codon of the AltPrP has no apparent effect on the biology of PRNP. In mouse and hamster, the alternative initiation AUG codon is absent and is replaced by a GUG codon.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi61Copper or zinc 11 Publication1
Metal bindingi62Copper or zinc 1; via amide nitrogen1 Publication1
Metal bindingi63Copper or zinc 1; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi69Copper or zinc 21 Publication1
Metal bindingi70Copper or zinc 2; via amide nitrogen1 Publication1
Metal bindingi71Copper or zinc 2; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi77Copper or zinc 31 Publication1
Metal bindingi78Copper or zinc 3; via amide nitrogen1 Publication1
Metal bindingi79Copper or zinc 3; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi85Copper or zinc 41 Publication1
Metal bindingi86Copper or zinc 4; via amide nitrogen1 Publication1
Metal bindingi87Copper or zinc 4; via amide nitrogen and carbonyl oxygen1 Publication1

GO - Molecular functioni

  • amyloid-beta binding Source: ARUK-UCL
  • ATP-dependent protein binding Source: Ensembl
  • chaperone binding Source: Ensembl
  • copper ion binding Source: UniProtKB
  • cupric ion binding Source: Ensembl
  • cuprous ion binding Source: CAFA
  • glycosaminoglycan binding Source: ARUK-UCL
  • identical protein binding Source: CAFA
  • ion channel binding Source: Ensembl
  • lamin binding Source: Ensembl
  • microtubule binding Source: UniProtKB
  • protease binding Source: ARUK-UCL
  • protein-containing complex binding Source: ARUK-UCL
  • signaling receptor activity Source: ARUK-UCL
  • tubulin binding Source: UniProtKB
  • type 5 metabotropic glutamate receptor binding Source: ARUK-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionPrion
Biological processCell cycle, Growth arrest
LigandCopper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-419037 NCAM1 interactions

Protein family/group databases

MoonDBiP04156 Predicted
TCDBi1.C.48.1.2 the prion peptide (prp) family

Names & Taxonomyi

Protein namesi
Recommended name:
Major prion protein
Short name:
PrP
Alternative name(s):
ASCR
PrP27-30
PrP33-35C
CD_antigen: CD230
Gene namesi
Name:PRNP
Synonyms:ALTPRP, PRIP, PRP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000171867.16
HGNCiHGNC:9449 PRNP
MIMi176640 gene
neXtProtiNX_P04156

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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 type 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.1 Publication
Creutzfeldt-Jakob disease (CJD)10 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionOccurs 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 animal 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.
See also OMIM:123400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_006470180V → I in CJD. 3 PublicationsCorresponds to variant dbSNP:rs74315408EnsemblClinVar.1
Natural variantiVAR_008749196E → K in CJD. 1 Publication1
Natural variantiVAR_006473200E → K in CJD. 3 PublicationsCorresponds to variant dbSNP:rs28933385EnsemblClinVar.1
Natural variantiVAR_008751203V → I in CJD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776593792Ensembl.1
Natural variantiVAR_006474208R → H in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315412EnsemblClinVar.1
Natural variantiVAR_006475210V → I in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315407EnsemblClinVar.1
Natural variantiVAR_008752211E → Q in CJD. 1 PublicationCorresponds to variant dbSNP:rs398122370EnsemblClinVar.1
Natural variantiVAR_006478232M → R in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315409EnsemblClinVar.1
Fatal familial insomnia (FFI)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.
See also OMIM:600072
Gerstmann-Straussler disease (GSD)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare inherited prion disease characterized by adult onset of memory loss, dementia, ataxia, and pathologic deposition of amyloid-like plaques in the brain. GSD presents with progressive limb and truncal ataxia, dysarthria, and cognitive decline in the thirties and forties, and the average disease duration is 7 years.
See also OMIM:137440
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_006465105P → L in GSD. 2 PublicationsCorresponds to variant dbSNP:rs11538758EnsemblClinVar.1
Natural variantiVAR_014264131G → V in GSD. 1 PublicationCorresponds to variant dbSNP:rs74315410EnsemblClinVar.1
Natural variantiVAR_008746187H → R in GSD. 1 PublicationCorresponds to variant dbSNP:rs74315413EnsemblClinVar.1
Natural variantiVAR_006472198F → S in GSD; atypical form with neurofibrillary tangles. 1 PublicationCorresponds to variant dbSNP:rs74315405EnsemblClinVar.1
Natural variantiVAR_008750202D → N in GSD. 1 PublicationCorresponds to variant dbSNP:rs761807915Ensembl.1
Natural variantiVAR_008753212Q → P in GSD. 1 PublicationCorresponds to variant dbSNP:rs751882709Ensembl.1
Natural variantiVAR_006476217Q → R in GSD; with neurofibrillary tangles. 1 PublicationCorresponds to variant dbSNP:rs74315406EnsemblClinVar.1
Huntington disease-like 1 (HDL1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Disease descriptionAutosomal dominant, early-onset neurodegenerative disorder with prominent psychiatric features.
See also OMIM:603218
Kuru (KURU)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionKuru 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.
See also OMIM:245300
Spongiform encephalopathy with neuropsychiatric features (SENF)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal 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.
See also OMIM:606688

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1M → S: Protein detected. No protein detected; when associated with S-8. 1 Publication1
Mutagenesisi8M → S: No protein detected; when associated with S-1. 1 Publication1

Keywords - Diseasei

Amyloidosis, Disease mutation

Organism-specific databases

DisGeNETi5621
GeneReviewsiPRNP
MalaCardsiPRNP
MIMi123400 phenotype
137440 phenotype
245300 phenotype
600072 phenotype
603218 phenotype
606688 phenotype
OpenTargetsiENSG00000171867
Orphaneti397606 Chronic diarrhea with hereditary sensory and autonomic neuropathy
280397 Familial Alzheimer-like prion disease
466 Fatal familial insomnia
356 Gerstmann-Straussler-Scheinker syndrome
157941 Huntington disease-like 1
282166 Inherited Creutzfeldt-Jakob disease
PharmGKBiPA33796

Chemistry databases

ChEMBLiCHEMBL4869
DrugBankiDB00759 Tetracycline

Polymorphism and mutation databases

BioMutaiPRNP
DMDMi130912

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
ChainiPRO_000002567523 – 230Major prion proteinAdd BLAST208
PropeptideiPRO_0000025676231 – 253Removed in mature formBy similarityAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi179 ↔ 2141 Publication
Glycosylationi181N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi197N-linked (GlcNAc...) asparagine1 Publication1
Lipidationi230GPI-anchor amidated serineBy similarity1

Post-translational modificationi

The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion.1 Publication
Isoform 2 is sumoylated with SUMO1.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Ubl conjugation

Proteomic databases

EPDiP04156
PaxDbiP04156
PeptideAtlasiP04156
PRIDEiP04156
ProteomicsDBi51667
51668 [P04156-2]

PTM databases

iPTMnetiP04156
PhosphoSitePlusiP04156
SwissPalmiP04156

Miscellaneous databases

PMAP-CutDBiP04156

Expressioni

Gene expression databases

BgeeiENSG00000171867
ExpressionAtlasiP04156 baseline and differential
GenevisibleiP04156 HS

Organism-specific databases

HPAiHPA042754
HPA043398

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 (PubMed:11524679, PubMed:11900542, PubMed:14623188, PubMed:17468747, PubMed:19204296, PubMed:19927125, PubMed:20375014, PubMed:20564047). 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 KIAA1191 (PubMed:21153684). Interacts with ADGRG6 (By similarity).By similarity9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • ATP-dependent protein binding Source: Ensembl
  • chaperone binding Source: Ensembl
  • identical protein binding Source: CAFA
  • ion channel binding Source: Ensembl
  • lamin binding Source: Ensembl
  • microtubule binding Source: UniProtKB
  • protease binding Source: ARUK-UCL
  • tubulin binding Source: UniProtKB
  • type 5 metabotropic glutamate receptor binding Source: ARUK-UCL
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111606, 72 interactors
CORUMiP04156
DIPiDIP-29933N
ELMiP04156
IntActiP04156, 94 interactors
MINTiP04156
STRINGi9606.ENSP00000368752

Chemistry databases

BindingDBiP04156

Structurei

Secondary structure

1253
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi63 – 67Combined sources5
Beta strandi70 – 73Combined sources4
Turni74 – 76Combined sources3
Beta strandi79 – 82Combined sources4
Beta strandi92 – 95Combined sources4
Beta strandi99 – 101Combined sources3
Beta strandi118 – 122Combined sources5
Beta strandi125 – 127Combined sources3
Beta strandi128 – 131Combined sources4
Beta strandi141 – 143Combined sources3
Helixi144 – 153Combined sources10
Helixi154 – 156Combined sources3
Beta strandi159 – 163Combined sources5
Helixi166 – 168Combined sources3
Turni171 – 173Combined sources3
Beta strandi178 – 181Combined sources4
Helixi185 – 187Combined sources3
Turni188 – 190Combined sources3
Turni193 – 195Combined sources3
Beta strandi212 – 215Combined sources4
Turni223 – 225Combined sources3
Turni228 – 230Combined sources3

3D structure databases

DisProtiDP00466
ProteinModelPortaliP04156
SMRiP04156
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04156

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati51 – 5919
Repeati60 – 6728
Repeati68 – 7538
Repeati76 – 8348
Repeati84 – 9158

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 230Interaction with GRB2, ERI3 and SYN1By similarityAdd BLAST208
Regioni23 – 38Interaction with ADGRG6By similarityAdd BLAST16
Regioni51 – 915 X 8 AA tandem repeats of P-H-G-G-G-W-G-QAdd BLAST41

Domaini

The normal, monomeric form, PRPN(C), has a mainly alpha-helical structure. Misfolding of this form produces a disease-associated, protease-resistant form, PRPN (Sc), accompanied by a large increase of the beta-sheet content and formation of amyloid fibrils. These fibrils consist of 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. In addition, the heparan-sulfate proteoglycan, GPC1, promotes the association of PRPN (C) to lipid rafts and appears to facilitate the conversion to PRPN (Sc).3 Publications
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.3 Publications

Sequence similaritiesi

Belongs to the prion family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IJMM Eukaryota
ENOG410YXUU LUCA
GeneTreeiENSGT00510000049083
HOVERGENiHBG008260
InParanoidiP04156
KOiK05634
OMAiGYPHNPG
OrthoDBiEOG091G0HMV
PhylomeDBiP04156
TreeFamiTF105188

Family and domain databases

Gene3Di1.10.790.10, 1 hit
InterProiView protein in InterPro
IPR000817 Prion
IPR036924 Prion/Doppel_b-ribbon_dom_sf
IPR022416 Prion/Doppel_prot_b-ribbon_dom
IPR025860 Prion_N_dom
PANTHERiPTHR10502:SF134 PTHR10502:SF134, 1 hit
PfamiView protein in Pfam
PF00377 Prion, 1 hit
PF11587 Prion_bPrPp, 1 hit
PRINTSiPR00341 PRION
SMARTiView protein in SMART
SM00157 PRP, 1 hit
SUPFAMiSSF54098 SSF54098, 1 hit
PROSITEiView protein in PROSITE
PS00291 PRION_1, 1 hit
PS00706 PRION_2, 1 hit

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P04156-1) [UniParc]FASTAAdd to basket
Also known as: PrP

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MANLGCWMLV LFVATWSDLG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP 
        60         70         80         90        100
PQGGGGWGQP HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHSQWN 
       110        120        130        140        150
KPSKPKTNMK HMAGAAAAGA VVGGLGGYML GSAMSRPIIH FGSDYEDRYY 
       160        170        180        190        200
RENMHRYPNQ VYYRPMDEYS NQNNFVHDCV NITIKQHTVT TTTKGENFTE 
       210        220        230        240        250
TDVKMMERVV EQMCITQYER ESQAYYQRGS SMVLFSSPPV ILLISFLIFL 

IVG
Length:253
Mass (Da):27,661
Last modified:November 1, 1986 - v1
Checksum:i43DB596BAAA66484
GO
Isoform 2 (identifier: P04156-2) [UniParc]FASTAAdd to basket
Also known as: PrP(M8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.

Show »
Length:246
Mass (Da):26,885
Checksum:i309B13B142A41566
GO
Isoform 3 (identifier: F7VJQ1-1) [UniParc]FASTAAdd to basket
Also known as: AltPrP
The sequence of this isoform can be found in the external entry F7VJQ1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:73
Mass (Da):8,691
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti118Missing in AAA19664 (PubMed:3014653).Curated1
Sequence conflicti118Missing in BAA00011 (PubMed:3014653).Curated1
Sequence conflicti169Y → H in ABD63004 (Ref. 6) Curated1
Sequence conflicti227Q → K in AAH22532 (PubMed:15489334).Curated1

Polymorphismi

The five tandem octapeptide repeats region is highly unstable. Insertions or deletions of octapeptide repeat units are associated to prion disease.1 Publication
A number of polymorphisms confer resistance to prion diseases (PubMed:1439789, PubMed:9482303, PubMed:19923577, PubMed:26061765). Val-127 has been selected for in response to the Kuru epidemic and confers resistance to prion disease by acting as a 'dominant negative' inhibitor of prion conversion (PubMed:26061765). Val-127 is not only itself resistant to conformational conversion, but also inhibits conversion of wild-type proteins. Confers protection against classical Creutzfeldt-Jakob disease (CJD) and Kuru in the heterozygous state, but can be infected with variant CJD prions, resulting from exposure to bovine spongiform encephalopathy prions. Confers complete resistance to all prion strains when homozygous (PubMed:26061765). Always associated with M-129 variant (PubMed:26061765). Val-129 confers relative protection against acquired, sporadic and some inherited prion diseases in the heterozygous state, possibly by preventing homodimerization (PubMed:1439789). Lys-219 confers relative protection against sporadic Creutzfeldt-Jakob disease (CJD) in the heterozygous state (PubMed:9482303).3 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01376356 – 63Missing 3 Publications8
Natural variantiVAR_006464102P → L in GSD and early-onset dementia. 5 PublicationsCorresponds to variant dbSNP:rs74315401EnsemblClinVar.1
Natural variantiVAR_006465105P → L in GSD. 2 PublicationsCorresponds to variant dbSNP:rs11538758EnsemblClinVar.1
Natural variantiVAR_006466117A → V Linked to development of dementing Gerstmann-Straussler disease. 1 PublicationCorresponds to variant dbSNP:rs74315402EnsemblClinVar.1
Natural variantiVAR_073722127G → V Polymorphism; variant that has been selected for in response to the Kuru epidemic and confers resistance to prion disease by acting as a 'dominant negative' inhibitor of prion conversion; is not only itself resistant to conformational conversion, but also inhibits conversion of wild-type proteins; confers protection against classical Creutzfeldt-Jakob disease (CJD) and Kuru in the heterozygous state, but can be infected with variant CJD prions, resulting from exposure to bovine spongiform encephalopathy prions; confers complete resistance to all prion strains when homozygous. Always associated with M-129 variant. 2 PublicationsCorresponds to variant dbSNP:rs267606980EnsemblClinVar.1
Natural variantiVAR_006467129M → V Polymorphism; confers relative protection against acquired, sporadic and some inherited prion diseases in the heterozygous state, possibly by preventing homodimerization; 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. 4 PublicationsCorresponds to variant dbSNP:rs1799990EnsemblClinVar.1
Natural variantiVAR_014264131G → V in GSD. 1 PublicationCorresponds to variant dbSNP:rs74315410EnsemblClinVar.1
Natural variantiVAR_006468171N → S in schizoaffective disorder. 1 PublicationCorresponds to variant dbSNP:rs16990018EnsemblClinVar.1
Natural variantiVAR_006469178D → N in FFI and CJD. 4 PublicationsCorresponds to variant dbSNP:rs74315403EnsemblClinVar.1
Natural variantiVAR_006470180V → I in CJD. 3 PublicationsCorresponds to variant dbSNP:rs74315408EnsemblClinVar.1
Natural variantiVAR_006471183T → A in SENF and early-onset dementia; induces loss of glycosylation at N-181. 3 PublicationsCorresponds to variant dbSNP:rs74315411EnsemblClinVar.1
Natural variantiVAR_008746187H → R in GSD. 1 PublicationCorresponds to variant dbSNP:rs74315413EnsemblClinVar.1
Natural variantiVAR_008748188T → K in early-onset dementia; dementia associated to prion diseases. 1 Publication1
Natural variantiVAR_008747188T → R1 PublicationCorresponds to variant dbSNP:rs372878791Ensembl.1
Natural variantiVAR_008749196E → K in CJD. 1 Publication1
Natural variantiVAR_006472198F → S in GSD; atypical form with neurofibrillary tangles. 1 PublicationCorresponds to variant dbSNP:rs74315405EnsemblClinVar.1
Natural variantiVAR_006473200E → K in CJD. 3 PublicationsCorresponds to variant dbSNP:rs28933385EnsemblClinVar.1
Natural variantiVAR_008750202D → N in GSD. 1 PublicationCorresponds to variant dbSNP:rs761807915Ensembl.1
Natural variantiVAR_008751203V → I in CJD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776593792Ensembl.1
Natural variantiVAR_006474208R → H in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315412EnsemblClinVar.1
Natural variantiVAR_006475210V → I in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315407EnsemblClinVar.1
Natural variantiVAR_008752211E → Q in CJD. 1 PublicationCorresponds to variant dbSNP:rs398122370EnsemblClinVar.1
Natural variantiVAR_008753212Q → P in GSD. 1 PublicationCorresponds to variant dbSNP:rs751882709Ensembl.1
Natural variantiVAR_006476217Q → R in GSD; with neurofibrillary tangles. 1 PublicationCorresponds to variant dbSNP:rs74315406EnsemblClinVar.1
Natural variantiVAR_006477219E → K Polymorphism; confers relative protection against sporadic Creutzfeldt-Jakob disease (CJD) in the heterozygous state. 2 PublicationsCorresponds to variant dbSNP:rs1800014EnsemblClinVar.1
Natural variantiVAR_006478232M → R in CJD. 1 PublicationCorresponds to variant dbSNP:rs74315409EnsemblClinVar.1
Natural variantiVAR_008754238P → S1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0390451 – 7Missing in isoform 2. Curated7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13899 mRNA Translation: AAA60182.1
X83416 Genomic DNA Translation: CAA58442.1
U29185 Genomic DNA Translation: AAC78725.1
AF076976 Genomic DNA Translation: AAD46098.1
AY008282 mRNA Translation: AAG21693.1
DQ408531 Genomic DNA Translation: ABD63004.1
AL133396 Genomic DNA No translation available.
BC012844 mRNA Translation: AAH12844.1
BC022532 mRNA Translation: AAH22532.1
D00015 mRNA Translation: BAA00011.1
M13667 mRNA Translation: AAA19664.1
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
CCDSiCCDS13080.1 [P04156-1]
PIRiA24173 UJHU
RefSeqiNP_000302.1, NM_000311.4 [P04156-1]
NP_001073590.1, NM_001080121.2 [P04156-1]
NP_001073591.1, NM_001080122.2 [P04156-1]
NP_001073592.1, NM_001080123.2 [P04156-1]
NP_001258490.1, NM_001271561.2
NP_898902.1, NM_183079.3 [P04156-1]
UniGeneiHs.472010
Hs.610285
Hs.721670

Genome annotation databases

EnsembliENST00000379440; ENSP00000368752; ENSG00000171867 [P04156-1]
ENST00000430350; ENSP00000399376; ENSG00000171867 [P04156-1]
GeneIDi5621
KEGGihsa:5621

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPRIO_HUMAN
AccessioniPrimary (citable) accession number: P04156
Secondary accession number(s): O60489
, P78446, Q15216, Q15221, Q27H91, Q5QPB4, Q8TBG0, Q96E70, Q9UP19
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: July 18, 2018
This is version 236 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  8. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health