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Protein

26S protease regulatory subunit 8 homolog

Gene

RPT6

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

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1968ATP

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • protein domain specific binding Source: SGD

GO - Biological processi

  • chromatin remodeling Source: SGD
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: SGD
  • nonfunctional rRNA decay Source: SGD
  • nucleotide-excision repair Source: SGD
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
  • proteasome regulatory particle assembly Source: SGD
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30558-MONOMER.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 8 homolog
Alternative name(s):
Protein CIM3
Protein SUG1
Tat-binding protein TBY1
Gene namesi
Name:RPT6
Synonyms:CIM3, CRL3, SUG1, TBPY, TBY1
Ordered Locus Names:YGL048C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL048C.
SGDiS000003016. RPT6.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 40540426S protease regulatory subunit 8 homologPRO_0000084730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ01939.
PeptideAtlasiQ01939.

Interactioni

Subunit structurei

May form a homodimer or a heterodimer with a related family member. Interacts with OLA1, TMA17, and UBR1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD23P326284EBI-13914,EBI-14668
RPN1P387643EBI-13914,EBI-15913
RPN14P531966EBI-13914,EBI-23691
RPT1P332994EBI-13914,EBI-13910
RPT3P332985EBI-13914,EBI-13905
SSA1P105912EBI-13914,EBI-8591
UBR1P198124EBI-13914,EBI-19909
UFD4P332023EBI-13914,EBI-20010

GO - Molecular functioni

  • protein domain specific binding Source: SGD

Protein-protein interaction databases

BioGridi33200. 150 interactions.
DIPiDIP-979N.
IntActiQ01939. 56 interactions.
MINTiMINT-568023.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CR2electron microscopy7.70J1-405[»]
4CR3electron microscopy9.30J1-405[»]
4CR4electron microscopy8.80J1-405[»]
5A5Belectron microscopy9.50J1-405[»]
ProteinModelPortaliQ01939.
SMRiQ01939. Positions 24-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074947.
HOGENOMiHOG000225143.
InParanoidiQ01939.
KOiK03066.
OMAiVMGTKKV.
OrthoDBiEOG7X3R1G.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q01939-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAAVTSSNI VLETHESGIK PYFEQKIQET ELKIRSKTEN VRRLEAQRNA
60 70 80 90 100
LNDKVRFIKD ELRLLQEPGS YVGEVIKIVS DKKVLVKVQP EGKYIVDVAK
110 120 130 140 150
DINVKDLKAS QRVCLRSDSY MLHKVLENKA DPLVSLMMVE KVPDSTYDMV
160 170 180 190 200
GGLTKQIKEI KEVIELPVKH PELFESLGIA QPKGVILYGP PGTGKTLLAR
210 220 230 240 250
AVAHHTDCKF IRVSGAELVQ KYIGEGSRMV RELFVMAREH APSIIFMDEI
260 270 280 290 300
DSIGSTRVEG SGGGDSEVQR TMLELLNQLD GFETSKNIKI IMATNRLDIL
310 320 330 340 350
DPALLRPGRI DRKIEFPPPS VAARAEILRI HSRKMNLTRG INLRKVAEKM
360 370 380 390 400
NGCSGADVKG VCTEAGMYAL RERRIHVTQE DFELAVGKVM NKNQETAISV

AKLFK
Length:405
Mass (Da):45,272
Last modified:January 23, 2007 - v4
Checksum:i9C59E92A0794F60F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411V → G in CAA47023 (PubMed:1614516).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66400 Genomic DNA. Translation: CAA47023.1.
L01626 Genomic DNA. Translation: AAA35138.1.
Z72570 Genomic DNA. Translation: CAA96750.1.
AY693135 Genomic DNA. Translation: AAT93154.1.
BK006941 Genomic DNA. Translation: DAA08053.1.
PIRiS64052.
RefSeqiNP_011467.1. NM_001180913.1.

Genome annotation databases

EnsemblFungiiYGL048C; YGL048C; YGL048C.
GeneIDi852834.
KEGGisce:YGL048C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66400 Genomic DNA. Translation: CAA47023.1.
L01626 Genomic DNA. Translation: AAA35138.1.
Z72570 Genomic DNA. Translation: CAA96750.1.
AY693135 Genomic DNA. Translation: AAT93154.1.
BK006941 Genomic DNA. Translation: DAA08053.1.
PIRiS64052.
RefSeqiNP_011467.1. NM_001180913.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CR2electron microscopy7.70J1-405[»]
4CR3electron microscopy9.30J1-405[»]
4CR4electron microscopy8.80J1-405[»]
5A5Belectron microscopy9.50J1-405[»]
ProteinModelPortaliQ01939.
SMRiQ01939. Positions 24-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33200. 150 interactions.
DIPiDIP-979N.
IntActiQ01939. 56 interactions.
MINTiMINT-568023.

Proteomic databases

MaxQBiQ01939.
PeptideAtlasiQ01939.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL048C; YGL048C; YGL048C.
GeneIDi852834.
KEGGisce:YGL048C.

Organism-specific databases

EuPathDBiFungiDB:YGL048C.
SGDiS000003016. RPT6.

Phylogenomic databases

GeneTreeiENSGT00550000074947.
HOGENOMiHOG000225143.
InParanoidiQ01939.
KOiK03066.
OMAiVMGTKKV.
OrthoDBiEOG7X3R1G.

Enzyme and pathway databases

BioCyciYEAST:G3O-30558-MONOMER.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi972403.
PROiQ01939.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4."
    Swaffield J.C., Bromberg J.F., Johnston S.A.
    Nature 357:698-700(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Isolation of a yeast gene encoding a protein homologous to the human Tat-binding protein TBP-1."
    Goyer C., Lee H.S., Malo D., Sonenberg N.
    DNA Cell Biol. 11:579-585(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
    Feuermann M., de Montigny J., Potier S., Souciet J.-L.
    Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. "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 THR-2.
  8. "The proteasome is linked to cycloheximide resistance in yeast: CRL3 is a subunit of the 26S proteasome."
    Gerlinger U.-M., Wolf D.H., Hilt W.
    Enzyme Protein 48:317-317(1995)
    Cited for: CHARACTERIZATION.
  9. "Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome."
    Rubin D.M., Coux O., Wefes I., Hengartner C., Young R.A., Goldberg A.L., Finley D.
    Nature 379:655-657(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  10. "Physical association of ubiquitin ligases and the 26S proteasome."
    Xie Y., Varshavsky A.
    Proc. Natl. Acad. Sci. U.S.A. 97:2497-2502(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBR1.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network."
    Guerrero C., Tagwerker C., Kaiser P., Huang L.
    Mol. Cell. Proteomics 5:366-378(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OLA1.
  13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.
  14. Cited for: FUNCTION, INTERACTION WITH TMA17.

Entry informationi

Entry nameiPRS8_YEAST
AccessioniPrimary (citable) accession number: Q01939
Secondary accession number(s): D6VU92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 158 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4700 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. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.