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Protein

Major prion protein

Gene

PRNP

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

PrionUniRule annotationImported

Keywords - Ligandi

CopperSAAS annotation, Metal-bindingSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Major prion proteinUniRule annotation
Gene namesi
Name:PRNPImported
ORF Names:hCG_1785425Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

  • Cell membrane SAAS annotation; Lipid-anchorGPI-anchor SAAS annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei112 – 13120HelicalSequence analysisAdd
BLAST
Transmembranei232 – 25221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Cell membraneUniRule annotationSAAS annotation, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 253231Major prion proteinSequence analysisPRO_5007703993Add
BLAST

Keywords - PTMi

Disulfide bondSAAS annotation

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.SAAS annotation

Protein-protein interaction databases

STRINGi9606.ENSP00000368752.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini113 – 12816Prion/Doppel_prot_b-ribbon_domInterPro annotationAdd
BLAST
Domaini200 – 21819Prion/Doppel_prot_b-ribbon_domInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the prion family.UniRule annotationSAAS annotation

Keywords - Domaini

RepeatSAAS annotation, SignalSequence analysis, Transmembrane, Transmembrane helixSequence analysis

Phylogenomic databases

eggNOGiENOG410IJMM. Eukaryota.
ENOG410YXUU. LUCA.
GeneTreeiENSGT00510000049083.
HOVERGENiHBG008260.
KOiK05634.
OMAiHNPGYPH.

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]
PANTHERiPTHR10502:SF11. PTHR10502:SF11. 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.

Q53YK7-1 [UniParc]FASTAAdd to basket

« 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:May 24, 2005 - v1
Checksum:i43DB596BAAA66484
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY569456 mRNA. Translation: AAS80162.1.
HM459606 Genomic DNA. Translation: ADO16981.1.
AB300823 mRNA. Translation: BAG32276.1.
CH471133 Genomic DNA. Translation: EAX10449.1.
CH471133 Genomic DNA. Translation: EAX10450.1.
RefSeqiNP_000302.1. NM_000311.3.
NP_001073590.1. NM_001080121.1.
NP_001073591.1. NM_001080122.1.
NP_001073592.1. NM_001080123.1.
NP_898902.1. NM_183079.2.
UniGeneiHs.472010.
Hs.610285.
Hs.721670.

Genome annotation databases

GeneIDi5621.
KEGGihsa:5621.
UCSCiuc002wkx.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY569456 mRNA. Translation: AAS80162.1.
HM459606 Genomic DNA. Translation: ADO16981.1.
AB300823 mRNA. Translation: BAG32276.1.
CH471133 Genomic DNA. Translation: EAX10449.1.
CH471133 Genomic DNA. Translation: EAX10450.1.
RefSeqiNP_000302.1. NM_000311.3.
NP_001073590.1. NM_001080121.1.
NP_001073591.1. NM_001080122.1.
NP_001073592.1. NM_001080123.1.
NP_898902.1. NM_183079.2.
UniGeneiHs.472010.
Hs.610285.
Hs.721670.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000368752.

Protocols and materials databases

DNASUi5621.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5621.
KEGGihsa:5621.
UCSCiuc002wkx.4. human.

Organism-specific databases

CTDi5621.
PharmGKBiPA33796.

Phylogenomic databases

eggNOGiENOG410IJMM. Eukaryota.
ENOG410YXUU. LUCA.
GeneTreeiENSGT00510000049083.
HOVERGENiHBG008260.
KOiK05634.
OMAiHNPGYPH.

Miscellaneous databases

ChiTaRSiPRNP. human.
GenomeRNAii5621.

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]
PANTHERiPTHR10502:SF11. PTHR10502:SF11. 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

  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Analysis of the Sequence and Polymorphism of Human PrPc Mature Protein Gene."
    Cui X., Wang Z., Chen J.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Cloning, Prokaryotic Expression and Antigenic Analysis of Resistant Core of Human PrP in E. coli."
    Cui X., Wang Z., Chen J.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE.
  5. "Hypoxia induces expression of a GPI-anchorless splice variant of the prion protein."
    Kikuchi Y., Kakeya T., Nakajima O., Sakai A., Ikeda K., Yamaguchi N., Yamazaki T., Tanamoto K., Matsuda H., Sawada J., Takatori K.
    FEBS J. 275:2965-2976(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  6. "Molecular Characterization of PrP Gene isolated from Pakistani Population."
    Jabeen R., Awan A.R., Nadeem A., Firyal S., Hussain T., Babar M.E.
    Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ53YK7_HUMAN
AccessioniPrimary (citable) accession number: Q53YK7
Entry historyi
Integrated into UniProtKB/TrEMBL: May 24, 2005
Last sequence update: May 24, 2005
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

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 one 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.