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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

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-382556. ABC-family proteins mediated transport.
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-5689880. Ub-specific processing proteases.
R-SCE-6798695. Neutrophil degranulation.
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-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002139512 – 33826S proteasome regulatory subunit RPN8Add BLAST337

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei314PhosphoserineCombined sources1
Modified residuei317PhosphoserineCombined sources1
Modified residuei319PhosphoserineCombined sources1
Modified residuei327PhosphothreonineCombined sources1

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ08723.
PRIDEiQ08723.

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. 81 interactors.
DIPiDIP-1574N.
IntActiQ08723. 28 interactors.
MINTiMINT-405204.

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 10Combined sources4
Helixi12 – 24Combined sources13
Beta strandi34 – 40Combined sources7
Beta strandi42 – 53Combined sources12
Beta strandi56 – 59Combined sources4
Beta strandi62 – 68Combined sources7
Helixi70 – 83Combined sources14
Beta strandi87 – 94Combined sources8
Helixi103 – 111Combined sources9
Beta strandi115 – 117Combined sources3
Beta strandi119 – 123Combined sources5
Beta strandi129 – 131Combined sources3
Beta strandi133 – 142Combined sources10
Turni145 – 148Combined sources4
Beta strandi151 – 157Combined sources7
Beta strandi159 – 161Combined sources3
Helixi165 – 178Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-U188-308[»]
3JCKelectron microscopy3.50E1-338[»]
3JCOelectron microscopy4.80U1-338[»]
3JCPelectron microscopy4.60U1-338[»]
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.
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.
OMAiNHTILGK.
OrthoDBiEOG092C3ND9.

Family and domain databases

CDDicd08062. MPN_RPN7_8. 1 hit.
InterProiIPR000555. JAMM/MPN+_dom.
IPR033858. MPN_RPN7_8.
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)DescriptionActionsGraphical viewLength
Sequence conflicti126K → E in AAS56365 (PubMed:17322287).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-U188-308[»]
3JCKelectron microscopy3.50E1-338[»]
3JCOelectron microscopy4.80U1-338[»]
3JCPelectron microscopy4.60U1-338[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34651. 81 interactors.
DIPiDIP-1574N.
IntActiQ08723. 28 interactors.
MINTiMINT-405204.

Protein family/group databases

MEROPSiM67.973.

PTM databases

iPTMnetiQ08723.

Proteomic databases

MaxQBiQ08723.
PRIDEiQ08723.

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.
OMAiNHTILGK.
OrthoDBiEOG092C3ND9.

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-382556. ABC-family proteins mediated transport.
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-5689880. Ub-specific processing proteases.
R-SCE-6798695. Neutrophil degranulation.
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-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ08723.

Family and domain databases

CDDicd08062. MPN_RPN7_8. 1 hit.
InterProiIPR000555. JAMM/MPN+_dom.
IPR033858. MPN_RPN7_8.
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...

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: November 30, 2016
This is version 145 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.