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Protein

26S protease subunit RPT4

Gene

RPT4

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

  • 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

  • ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  • nucleotide-excision repair 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 regulatory particle assembly Source: SGD
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33750-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 subunit RPT4
Alternative name(s):
26S protease subunit SUG2
Proteasomal cap subunit
Gene namesi
Name:RPT4
Synonyms:CRL13, PCS1, SUG2
Ordered Locus Names:YOR259C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR259C.
SGDiS000005785. RPT4.

Subcellular locationi

GO - Cellular componenti

  • cytosolic proteasome complex Source: GO_Central
  • nuclear proteasome complex Source: GO_Central
  • nucleus Source: SGD
  • proteasome regulatory particle, base subcomplex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 43743626S protease subunit RPT4PRO_0000084737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP53549.

PTM databases

iPTMnetiP53549.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RPT1P332993EBI-18520,EBI-13910
RPT5P332977EBI-18520,EBI-13920

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi34649. 147 interactions.
DIPiDIP-1589N.
IntActiP53549. 27 interactions.
MINTiMINT-397407.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CR2electron microscopy7.70L1-437[»]
4CR3electron microscopy9.30L1-437[»]
4CR4electron microscopy8.80L1-437[»]
5A5Belectron microscopy9.50L1-437[»]
ProteinModelPortaliP53549.
SMRiP53549. Positions 67-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074826.
HOGENOMiHOG000225143.
InParanoidiP53549.
KOiK03064.
OMAiYNMTSFE.
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.

P53549-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEEQDPLLA GLGETSGDNH TQQSHEQQPE QPQETEEHHE EEPSRVDPEQ
60 70 80 90 100
EAHNKALNQF KRKLLEHRRY DDQLKQRRQN IRDLEKLYDK TENDIKALQS
110 120 130 140 150
IGQLIGEVMK ELSEEKYIVK ASSGPRYIVG VRNSVDRSKL KKGVRVTLDI
160 170 180 190 200
TTLTIMRILP RETDPLVYNM TSFEQGEITF DGIGGLTEQI RELREVIELP
210 220 230 240 250
LKNPEIFQRV GIKPPKGVLL YGPPGTGKTL LAKAVAATIG ANFIFSPASG
260 270 280 290 300
IVDKYIGESA RIIREMFAYA KEHEPCIIFM DEVDAIGGRR FSEGTSADRE
310 320 330 340 350
IQRTLMELLT QMDGFDNLGQ TKIIMATNRP DTLDPALLRP GRLDRKVEIP
360 370 380 390 400
LPNEAGRLEI FKIHTAKVKK TGEFDFEAAV KMSDGFNGAD IRNCATEAGF
410 420 430
FAIRDDRDHI NPDDLMKAVR KVAEVKKLEG TIEYQKL
Length:437
Mass (Da):49,408
Last modified:January 23, 2007 - v4
Checksum:i0EA42A599E2B2E2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211A → P in AAA85134 (PubMed:8955118).Curated
Sequence conflicti135 – 1351V → A in AAA85134 (PubMed:8955118).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43720 Genomic DNA. Translation: AAA85134.1.
U93262 Genomic DNA. Translation: AAB51594.1.
Z75167 Genomic DNA. Translation: CAA99481.1.
BK006948 Genomic DNA. Translation: DAA11026.1.
PIRiS67156.
RefSeqiNP_014902.3. NM_001183678.3.

Genome annotation databases

EnsemblFungiiYOR259C; YOR259C; YOR259C.
GeneIDi854433.
KEGGisce:YOR259C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43720 Genomic DNA. Translation: AAA85134.1.
U93262 Genomic DNA. Translation: AAB51594.1.
Z75167 Genomic DNA. Translation: CAA99481.1.
BK006948 Genomic DNA. Translation: DAA11026.1.
PIRiS67156.
RefSeqiNP_014902.3. NM_001183678.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CR2electron microscopy7.70L1-437[»]
4CR3electron microscopy9.30L1-437[»]
4CR4electron microscopy8.80L1-437[»]
5A5Belectron microscopy9.50L1-437[»]
ProteinModelPortaliP53549.
SMRiP53549. Positions 67-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34649. 147 interactions.
DIPiDIP-1589N.
IntActiP53549. 27 interactions.
MINTiMINT-397407.

PTM databases

iPTMnetiP53549.

Proteomic databases

MaxQBiP53549.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR259C; YOR259C; YOR259C.
GeneIDi854433.
KEGGisce:YOR259C.

Organism-specific databases

EuPathDBiFungiDB:YOR259C.
SGDiS000005785. RPT4.

Phylogenomic databases

GeneTreeiENSGT00550000074826.
HOGENOMiHOG000225143.
InParanoidiP53549.
KOiK03064.
OMAiYNMTSFE.
OrthoDBiEOG7X3R1G.

Enzyme and pathway databases

BioCyciYEAST:G3O-33750-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

PROiP53549.

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. "Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26 S proteasome."
    Russell S.J., Sathyanarayana U.G., Johnston S.A.
    J. Biol. Chem. 271:32810-32817(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A proteasome cap subunit required for spindle pole body duplication in yeast."
    McDonald H.B., Byers B.
    J. Cell Biol. 137:539-553(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1 and VPH1."
    Poirey R., Jauniaux J.-C.
    Yeast 13:483-487(1997) [PubMed] [Europe PMC] [Abstract]
    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 2-10, ACETYLATION AT SER-2.
  7. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPRS10_YEAST
AccessioniPrimary (citable) accession number: P53549
Secondary accession number(s): D6W2W0, Q08718
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 143 of the entry and version 4 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

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.