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Protein

26S proteasome regulatory subunit 8 homolog

Gene

RPT6

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

Functioni

The 26S proteasome 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

Miscellaneous

Present with 4700 molecules/cell in log phase SD medium.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi189 – 196ATP8

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • proteasome-activating ATPase activity Source: GO_Central
  • protein domain specific binding Source: SGD
  • TBP-class protein binding Source: GO_Central

GO - Biological processi

  • chromatin remodeling Source: SGD
  • negative regulation of DNA binding transcription factor activity Source: SGD
  • nonfunctional rRNA decay Source: SGD
  • nucleotide-excision repair Source: SGD
  • positive regulation of DNA binding transcription factor activity Source: SGD
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly 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
  • ubiquitin-dependent ERAD pathway Source: GO_Central

Keywordsi

LigandATP-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-187577 SCF(Skp2)-mediated degradation of p27/p21
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-68949 Orc1 removal from chromatin
R-SCE-69017 CDK-mediated phosphorylation and removal of Cdc6
R-SCE-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-SCE-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-SCE-983168 Antigen processing: Ubiquitination & Proteasome degradation

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome 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

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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000847302 – 40526S proteasome regulatory subunit 8 homologAdd BLAST404

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonine1 Publication1

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ01939
PaxDbiQ01939
PRIDEiQ01939

PTM databases

CarbonylDBiQ01939
iPTMnetiQ01939

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

Show more details

GO - Molecular functioni

  • protein domain specific binding Source: SGD
  • TBP-class protein binding Source: GO_Central

Protein-protein interaction databases

BioGridi33200, 715 interactors
ComplexPortaliCPX-2262 26S Proteasome complex
DIPiDIP-979N
IntActiQ01939, 104 interactors
MINTiQ01939
STRINGi4932.YGL048C

Structurei

3D structure databases

ProteinModelPortaliQ01939
SMRiQ01939
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074947
HOGENOMiHOG000225143
InParanoidiQ01939
KOiK03066
OMAiHGNNQEA
OrthoDBiEOG092C19WS

Family and domain databases

InterProiView protein in InterPro
IPR005937 26S_Psome_P45-like
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR027417 P-loop_NTPase
IPR035261 PSMC5
PANTHERiPTHR23073:SF12 PTHR23073:SF12, 1 hit
PfamiView protein in Pfam
PF00004 AAA, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01242 26Sp45, 1 hit
PROSITEiView protein in PROSITE
PS00674 AAA, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti41V → G in CAA47023 (PubMed:1614516).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiPRS8_YEAST
AccessioniPrimary (citable) accession number: Q01939
Secondary accession number(s): D6VU92
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 179 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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