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Protein

26S proteasome regulatory subunit RPN8

Gene

RPN8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.1 Publication

GO - Biological processi

  • ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-33752-MONOMER.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-5668541. TNFR2 non-canonical NF-kB pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiM67.973.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome regulatory subunit RPN8
Gene namesi
Name:RPN8
Ordered Locus Names:YOR261C
ORF Names:O5360
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR261C.
SGDiS000005787. RPN8.

Subcellular locationi

GO - Cellular componenti

  • proteasome regulatory particle, lid subcomplex Source: SGD
  • proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 33833726S proteasome regulatory subunit RPN8PRO_0000213951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei314 – 3141PhosphoserineCombined sources
Modified residuei317 – 3171PhosphoserineCombined sources
Modified residuei319 – 3191PhosphoserineCombined sources
Modified residuei327 – 3271PhosphothreonineCombined sources

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ08723.
PeptideAtlasiQ08723.

PTM databases

iPTMnetiQ08723.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HSM3P383485EBI-36176,EBI-21152
RPN11P435887EBI-36176,EBI-11219
RPN12P324965EBI-36176,EBI-15953
RPN5Q122507EBI-36176,EBI-15935
RPN6Q123774EBI-36176,EBI-308
RPN9Q040626EBI-36176,EBI-15944

Protein-protein interaction databases

BioGridi34651. 79 interactions.
DIPiDIP-1574N.
IntActiQ08723. 28 interactions.
MINTiMINT-405204.

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Helixi12 – 2413Combined sources
Beta strandi34 – 407Combined sources
Beta strandi42 – 5312Combined sources
Beta strandi56 – 594Combined sources
Beta strandi62 – 687Combined sources
Helixi70 – 8314Combined sources
Beta strandi87 – 948Combined sources
Helixi103 – 1119Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi133 – 14210Combined sources
Turni145 – 1484Combined sources
Beta strandi151 – 1577Combined sources
Beta strandi159 – 1613Combined sources
Helixi165 – 17814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-U188-308[»]
3JCKelectron microscopy3.50E1-338[»]
4CR2electron microscopy7.70U1-338[»]
4CR3electron microscopy9.30U1-338[»]
4CR4electron microscopy8.80U1-338[»]
4O8XX-ray1.99A2-178[»]
4O8YX-ray1.95A2-178[»]
4OCLX-ray2.40A/D1-176[»]
4OCMX-ray1.99A/D1-176[»]
4OCNX-ray2.25A/D1-176[»]
4OWPX-ray2.35A1-186[»]
5A5Belectron microscopy9.50U1-338[»]
ProteinModelPortaliQ08723.
SMRiQ08723. Positions 3-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M67A family.Curated
Contains 1 MPN (JAB/Mov34) domain.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063075.
HOGENOMiHOG000209236.
InParanoidiQ08723.
KOiK03038.
OMAiHNYVESM.
OrthoDBiEOG7GQZ5S.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q08723-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLQHEKVTI APLVLLSALD HYERTQTKEN KRCVGVILGD ANSSTIRVTN
60 70 80 90 100
SFALPFEEDE KNSDVWFLDH NYIENMNEMC KKINAKEKLI GWYHSGPKLR
110 120 130 140 150
ASDLKINELF KKYTQNNPLL LIVDVKQQGV GLPTDAYVAI EQVKDDGTST
160 170 180 190 200
EKTFLHLPCT IEAEEAEEIG VEHLLRDVRD QAAGGLSIRL TNQLKSLKGL
210 220 230 240 250
QSKLKDVVEY LDKVINKELP INHTILGKLQ DVFNLLPNLG TPDDDEIDVE
260 270 280 290 300
NHDRINISNN LQKALTVKTN DELMVIYISN LVRSIIAFDD LIENKIQNKK
310 320 330
IQEQRVKDKQ SKVSDDSESE SGDKEATAPL IQRKNKKN
Length:338
Mass (Da):38,313
Last modified:January 23, 2007 - v3
Checksum:i6EE6009545A3D0EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1261K → E in AAS56365 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75169 Genomic DNA. Translation: CAA99483.1.
AY558039 Genomic DNA. Translation: AAS56365.1.
BK006948 Genomic DNA. Translation: DAA11028.1.
PIRiS67158.
RefSeqiNP_014904.3. NM_001183680.3.

Genome annotation databases

EnsemblFungiiYOR261C; YOR261C; YOR261C.
GeneIDi854435.
KEGGisce:YOR261C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75169 Genomic DNA. Translation: CAA99483.1.
AY558039 Genomic DNA. Translation: AAS56365.1.
BK006948 Genomic DNA. Translation: DAA11028.1.
PIRiS67158.
RefSeqiNP_014904.3. NM_001183680.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-U188-308[»]
3JCKelectron microscopy3.50E1-338[»]
4CR2electron microscopy7.70U1-338[»]
4CR3electron microscopy9.30U1-338[»]
4CR4electron microscopy8.80U1-338[»]
4O8XX-ray1.99A2-178[»]
4O8YX-ray1.95A2-178[»]
4OCLX-ray2.40A/D1-176[»]
4OCMX-ray1.99A/D1-176[»]
4OCNX-ray2.25A/D1-176[»]
4OWPX-ray2.35A1-186[»]
5A5Belectron microscopy9.50U1-338[»]
ProteinModelPortaliQ08723.
SMRiQ08723. Positions 3-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34651. 79 interactions.
DIPiDIP-1574N.
IntActiQ08723. 28 interactions.
MINTiMINT-405204.

Protein family/group databases

MEROPSiM67.973.

PTM databases

iPTMnetiQ08723.

Proteomic databases

MaxQBiQ08723.
PeptideAtlasiQ08723.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR261C; YOR261C; YOR261C.
GeneIDi854435.
KEGGisce:YOR261C.

Organism-specific databases

EuPathDBiFungiDB:YOR261C.
SGDiS000005787. RPN8.

Phylogenomic databases

GeneTreeiENSGT00530000063075.
HOGENOMiHOG000209236.
InParanoidiQ08723.
KOiK03038.
OMAiHNYVESM.
OrthoDBiEOG7GQZ5S.

Enzyme and pathway databases

BioCyciYEAST:G3O-33752-MONOMER.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-5668541. TNFR2 non-canonical NF-kB pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi976670.
PROiQ08723.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1 and VPH1."
    Poirey R., Jauniaux J.-C.
    Yeast 13:483-487(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "N-terminal modifications of the 19S regulatory particle subunits of the yeast proteasome."
    Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.
    Arch. Biochem. Biophys. 409:341-348(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-9, ACETYLATION AT SER-2.
  6. "The regulatory particle of the Saccharomyces cerevisiae proteasome."
    Glickman M.H., Rubin D.M., Fried V.A., Finley D.
    Mol. Cell. Biol. 18:3149-3162(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-317; SER-319 AND THR-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiRPN8_YEAST
AccessioniPrimary (citable) accession number: Q08723
Secondary accession number(s): D6W2W2, Q6Q5I7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 19800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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.