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Protein

26S protease regulatory subunit 7 homolog

Gene

RPT1

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 bindingi250 – 2578ATPSequence analysis

GO - Molecular functioni

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

GO - Biological processi

  • ER-associated ubiquitin-dependent protein catabolic process Source: GO_Central
  • positive regulation of protein catabolic process Source: SGD
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  • proteasome regulatory particle assembly Source: SGD
  • ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31920-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 7 homolog
Alternative name(s):
Protein CIM5
Tat-binding homolog 3
Gene namesi
Name:RPT1
Synonyms:CIM5, YTA3
Ordered Locus Names:YKL145W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL145W.
SGDiS000001628. RPT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 46746726S protease regulatory subunit 7 homologPRO_0000084719Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei164 – 1641PhosphoserineCombined sources
Modified residuei231 – 2311PhosphoserineCombined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP33299.
PRIDEiP33299.

2D gel databases

SWISS-2DPAGEP33299.

PTM databases

iPTMnetiP33299.

Interactioni

Subunit structurei

Interacts with UBR1 and CIC1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DSK2P485103EBI-13910,EBI-6174
HSM3P383487EBI-13910,EBI-21152
PRE1P221412EBI-13910,EBI-13988
RAD23P326283EBI-13910,EBI-14668
RPN1P3876410EBI-13910,EBI-15913
RPT2P403277EBI-13910,EBI-13901
RPT3P332984EBI-13910,EBI-13905
RPT4P535493EBI-13910,EBI-18520
RPT5P332974EBI-13910,EBI-13920
RPT6Q019394EBI-13910,EBI-13914
UBR1P198122EBI-13910,EBI-19909

GO - Molecular functioni

Protein-protein interaction databases

BioGridi33991. 131 interactions.
DIPiDIP-2883N.
IntActiP33299. 83 interactions.
MINTiMINT-612502.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VLFX-ray3.80B/D381-467[»]
4A3VX-ray3.80B/D378-467[»]
4CR2electron microscopy7.70H1-467[»]
4CR3electron microscopy9.30H1-467[»]
4CR4electron microscopy8.80H1-467[»]
4JPOX-ray5.00C/D379-467[»]
5A5Belectron microscopy9.50H1-467[»]
ProteinModelPortaliP33299.
SMRiP33299. Positions 49-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074978.
HOGENOMiHOG000225143.
InParanoidiP33299.
KOiK03061.
OMAiFQVARCT.
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.

P33299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKEDWEKY KAPLEDDDKK PDDDKIVPLT EGDIQVLKSY GAAPYAAKLK
60 70 80 90 100
QTENDLKDIE ARIKEKAGVK ESDTGLAPSH LWDIMGDRQR LGEEHPLQVA
110 120 130 140 150
RCTKIIKGNG ESDETTTDNN NSGNSNSNSN QQSTDADEDD EDAKYVINLK
160 170 180 190 200
QIAKFVVGLG ERVSPTDIEE GMRVGVDRSK YNIELPLPPR IDPSVTMMTV
210 220 230 240 250
EEKPDVTYSD VGGCKDQIEK LREVVELPLL SPERFATLGI DPPKGILLYG
260 270 280 290 300
PPGTGKTLCA RAVANRTDAT FIRVIGSELV QKYVGEGARM VRELFEMART
310 320 330 340 350
KKACIIFFDE IDAVGGARFD DGAGGDNEVQ RTMLELITQL DGFDPRGNIK
360 370 380 390 400
VMFATNRPNT LDPALLRPGR IDRKVEFSLP DLEGRANIFR IHSKSMSVER
410 420 430 440 450
GIRWELISRL CPNSTGAELR SVCTEAGMFA IRARRKVATE KDFLKAVDKV
460
ISGYKKFSST SRYMQYN
Length:467
Mass (Da):51,983
Last modified:February 1, 1994 - v1
Checksum:i8454BBC9D549EC5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22817 Genomic DNA. Translation: CAA80470.1.
X73571 Genomic DNA. Translation: CAA51973.1.
Z28145 Genomic DNA. Translation: CAA81986.1.
BK006944 Genomic DNA. Translation: DAA09017.1.
PIRiS34354.
RefSeqiNP_012777.1. NM_001179711.1.

Genome annotation databases

EnsemblFungiiYKL145W; YKL145W; YKL145W.
GeneIDi853712.
KEGGisce:YKL145W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22817 Genomic DNA. Translation: CAA80470.1.
X73571 Genomic DNA. Translation: CAA51973.1.
Z28145 Genomic DNA. Translation: CAA81986.1.
BK006944 Genomic DNA. Translation: DAA09017.1.
PIRiS34354.
RefSeqiNP_012777.1. NM_001179711.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VLFX-ray3.80B/D381-467[»]
4A3VX-ray3.80B/D378-467[»]
4CR2electron microscopy7.70H1-467[»]
4CR3electron microscopy9.30H1-467[»]
4CR4electron microscopy8.80H1-467[»]
4JPOX-ray5.00C/D379-467[»]
5A5Belectron microscopy9.50H1-467[»]
ProteinModelPortaliP33299.
SMRiP33299. Positions 49-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33991. 131 interactions.
DIPiDIP-2883N.
IntActiP33299. 83 interactions.
MINTiMINT-612502.

PTM databases

iPTMnetiP33299.

2D gel databases

SWISS-2DPAGEP33299.

Proteomic databases

MaxQBiP33299.
PRIDEiP33299.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL145W; YKL145W; YKL145W.
GeneIDi853712.
KEGGisce:YKL145W.

Organism-specific databases

EuPathDBiFungiDB:YKL145W.
SGDiS000001628. RPT1.

Phylogenomic databases

GeneTreeiENSGT00550000074978.
HOGENOMiHOG000225143.
InParanoidiP33299.
KOiK03061.
OMAiFQVARCT.
OrthoDBiEOG7X3R1G.

Enzyme and pathway databases

BioCyciYEAST:G3O-31920-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

PROiP33299.

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. "S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase."
    Ghislain M., Udvardy A., Mann C.
    Nature 366:358-362(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 28383 / FL100 / VTT C-80102.
  2. "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.
  3. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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.
  6. "Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4."
    Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.
    EMBO J. 20:4423-4431(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIC1.
  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: BLOCKAGE OF N-TERMINUS.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPRS7_YEAST
AccessioniPrimary (citable) accession number: P33299
Secondary accession number(s): D6VX51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 6, 2016
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 105 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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.