Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

26S protease regulatory subunit 6A

Gene

RPT5

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 similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi222 – 2298ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity Source: SGD
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  2. proteasome regulatory particle assembly Source: SGD
  3. ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33646-MONOMER.
ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_230653. SCF-beta-TrCP mediated degradation of Emi1.
REACT_245870. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_245912. CDK-mediated phosphorylation and removal of Cdc6.
REACT_268441. Ubiquitin-dependent degradation of Cyclin D1.
REACT_83036. Orc1 removal from chromatin.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 6A
Alternative name(s):
Tat-binding protein homolog 1
Short name:
TBP-1
Gene namesi
Name:RPT5
Synonyms:YTA1
Ordered Locus Names:YOR117W
ORF Names:O3258, YOR3258W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

SGDiS000005643. RPT5.

Subcellular locationi

Cytoplasm Curated. Nucleus Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome regulatory particle, base subcomplex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 43443326S protease regulatory subunit 6APRO_0000084708Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei180 – 1801Phosphotyrosine1 Publication

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP33297.
PaxDbiP33297.
PeptideAtlasiP33297.
PRIDEiP33297.

Expressioni

Gene expression databases

GenevestigatoriP33297.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HSM3P383486EBI-13920,EBI-21152
NAS2P405556EBI-13920,EBI-14024
RPN1P387644EBI-13920,EBI-15913
RPN10P388862EBI-13920,EBI-15949
RPN14P531964EBI-13920,EBI-23691
RPT1P332994EBI-13920,EBI-13910
RPT3P332986EBI-13920,EBI-13905
RPT4P535497EBI-13920,EBI-18520

Protein-protein interaction databases

BioGridi34513. 374 interactions.
DIPiDIP-1590N.
IntActiP33297. 39 interactions.
MINTiMINT-383887.
STRINGi4932.YOR117W.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi356 – 36510Combined sources
Helixi376 – 3816Combined sources
Turni382 – 3854Combined sources
Helixi388 – 40417Combined sources
Beta strandi408 – 4103Combined sources
Helixi412 – 42716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WHKX-ray2.60A/B/C/D/E/F/G/H356-434[»]
3WHLX-ray4.00A/C/E/G356-434[»]
4CR2electron microscopy7.70M1-434[»]
4CR3electron microscopy9.30M1-434[»]
4CR4electron microscopy8.80M1-434[»]
ProteinModelPortaliP33297.
SMRiP33297. Positions 41-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiCOG1222.
GeneTreeiENSGT00730000111070.
HOGENOMiHOG000225143.
InParanoidiP33297.
KOiK03065.
OMAiTEIVHED.
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.

P33297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLEELDAQ TLPGDDELDQ EILNLSTQEL QTRAKLLDNE IRIFRSELQR
60 70 80 90 100
LSHENNVMLE KIKDNKEKIK NNRQLPYLVA NVVEVMDMNE IEDKENSEST
110 120 130 140 150
TQGGNVNLDN TAVGKAAVVK TSSRQTVFLP MVGLVDPDKL KPNDLVGVNK
160 170 180 190 200
DSYLILDTLP SEFDSRVKAM EVDEKPTETY SDVGGLDKQI EELVEAIVLP
210 220 230 240 250
MKRADKFKDM GIRAPKGALM YGPPGTGKTL LARACAAQTN ATFLKLAAPQ
260 270 280 290 300
LVQMYIGEGA KLVRDAFALA KEKAPTIIFI DELDAIGTKR FDSEKSGDRE
310 320 330 340 350
VQRTMLELLN QLDGFSSDDR VKVLAATNRV DVLDPALLRS GRLDRKIEFP
360 370 380 390 400
LPSEDSRAQI LQIHSRKMTT DDDINWQELA RSTDEFNGAQ LKAVTVEAGM
410 420 430
IALRNGQSSV KHEDFVEGIS EVQARKSKSV SFYA
Length:434
Mass (Da):48,256
Last modified:January 23, 2007 - v3
Checksum:iC215422033FCE830
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73569 Genomic DNA. Translation: CAA51971.1.
X90518 Genomic DNA. Translation: CAA62114.1.
X94335 Genomic DNA. Translation: CAA64037.1.
Z75025 Genomic DNA. Translation: CAA99315.1.
BK006948 Genomic DNA. Translation: DAA10892.1.
PIRiS46605.
RefSeqiNP_014760.3. NM_001183536.3.

Genome annotation databases

EnsemblFungiiYOR117W; YOR117W; YOR117W.
GeneIDi854284.
KEGGisce:YOR117W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73569 Genomic DNA. Translation: CAA51971.1.
X90518 Genomic DNA. Translation: CAA62114.1.
X94335 Genomic DNA. Translation: CAA64037.1.
Z75025 Genomic DNA. Translation: CAA99315.1.
BK006948 Genomic DNA. Translation: DAA10892.1.
PIRiS46605.
RefSeqiNP_014760.3. NM_001183536.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WHKX-ray2.60A/B/C/D/E/F/G/H356-434[»]
3WHLX-ray4.00A/C/E/G356-434[»]
4CR2electron microscopy7.70M1-434[»]
4CR3electron microscopy9.30M1-434[»]
4CR4electron microscopy8.80M1-434[»]
ProteinModelPortaliP33297.
SMRiP33297. Positions 41-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34513. 374 interactions.
DIPiDIP-1590N.
IntActiP33297. 39 interactions.
MINTiMINT-383887.
STRINGi4932.YOR117W.

Proteomic databases

MaxQBiP33297.
PaxDbiP33297.
PeptideAtlasiP33297.
PRIDEiP33297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR117W; YOR117W; YOR117W.
GeneIDi854284.
KEGGisce:YOR117W.

Organism-specific databases

SGDiS000005643. RPT5.

Phylogenomic databases

eggNOGiCOG1222.
GeneTreeiENSGT00730000111070.
HOGENOMiHOG000225143.
InParanoidiP33297.
KOiK03065.
OMAiTEIVHED.
OrthoDBiEOG7X3R1G.

Enzyme and pathway databases

BioCyciYEAST:G3O-33646-MONOMER.
ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_230653. SCF-beta-TrCP mediated degradation of Emi1.
REACT_245870. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_245912. CDK-mediated phosphorylation and removal of Cdc6.
REACT_268441. Ubiquitin-dependent degradation of Cyclin D1.
REACT_83036. Orc1 removal from chromatin.

Miscellaneous databases

NextBioi976260.
PROiP33297.

Gene expression databases

GenevestigatoriP33297.

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. "Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex."
    Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S., Schwarzlose C., Vetter I., Feldmann H.
    Yeast 10:1141-1155(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C836.
  2. "Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
    Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
    Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "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 ALA-2.
  7. "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].
  8. "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 TYR-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPRS6A_YEAST
AccessioniPrimary (citable) accession number: P33297
Secondary accession number(s): D6W2H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 138 of the entry and version 3 of the sequence. [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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

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 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.