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Protein

26S protease regulatory subunit 4 homolog

Gene

RPT2

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). Has ATPase activity.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi223 – 2308ATPSequence analysis

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29438-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 4 homolog
Alternative name(s):
Tat-binding homolog 5
Gene namesi
Name:RPT2
Synonyms:YHS4, YTA5
Ordered Locus Names:YDL007W
ORF Names:D2920
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL007W.
SGDiS000002165. RPT2.

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

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi229 – 2291K → Q: 73% loss of ATPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 43743626S protease regulatory subunit 4 homologPRO_0000084685Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Cross-linki234 – 234Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki255 – 255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki290 – 290Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Ubl conjugation

Proteomic databases

MaxQBiP40327.
PRIDEiP40327.

PTM databases

iPTMnetiP40327.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RPN1P387646EBI-13901,EBI-15913
RPT1P332997EBI-13901,EBI-13910

GO - Molecular functioni

Protein-protein interaction databases

BioGridi32047. 196 interactions.
DIPiDIP-6282N.
IntActiP40327. 33 interactions.
MINTiMINT-632695.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JCOelectron microscopy4.80I1-437[»]
3JCPelectron microscopy4.60I1-437[»]
4CR2electron microscopy7.70I1-437[»]
4CR3electron microscopy9.30I1-437[»]
4CR4electron microscopy8.80I1-437[»]
5A5Belectron microscopy9.50I1-437[»]
ProteinModelPortaliP40327.
SMRiP40327. Positions 75-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074818.
HOGENOMiHOG000225143.
InParanoidiP40327.
KOiK03062.
OMAiIHTRKMT.
OrthoDBiEOG092C19WS.

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.

P40327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQGVSSGQD KKKKKGSNQK PKYEPPVQSK FGRKKRKGGP ATAEKLPNIY
60 70 80 90 100
PSTRCKLKLL RMERIKDHLL LEEEFVSNSE ILKPFEKKQE EEKKQLEEIR
110 120 130 140 150
GNPLSIGTLE EIIDDDHAIV TSPTMPDYYV SILSFVDKEL LEPGCSVLLH
160 170 180 190 200
HKTMSIVGVL QDDADPMVSV MKMDKSPTES YSDIGGLESQ IQEIKESVEL
210 220 230 240 250
PLTHPELYEE MGIKPPKGVI LYGAPGTGKT LLAKAVANQT SATFLRIVGS
260 270 280 290 300
ELIQKYLGDG PRLCRQIFKV AGENAPSIVF IDEIDAIGTK RYDSNSGGER
310 320 330 340 350
EIQRTMLELL NQLDGFDDRG DVKVIMATNK IETLDPALIR PGRIDRKILF
360 370 380 390 400
ENPDLSTKKK ILGIHTSKMN LSEDVNLETL VTTKDDLSGA DIQAMCTEAG
410 420 430
LLALRERRMQ VTAEDFKQAK ERVMKNKVEE NLEGLYL
Length:437
Mass (Da):48,828
Last modified:January 23, 2007 - v3
Checksum:iEB735354C3A0EBD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti347 – 3471K → N in AAA97498 (PubMed:7721833).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81070 Genomic DNA. Translation: CAA56957.1.
L17040 Genomic DNA. Translation: AAA97498.1.
Z48432 Genomic DNA. Translation: CAA88352.1.
Z74055 Genomic DNA. Translation: CAA98563.1.
BK006938 Genomic DNA. Translation: DAA11841.1.
PIRiS46613.
RefSeqiNP_010277.1. NM_001180066.1.

Genome annotation databases

EnsemblFungiiYDL007W; YDL007W; YDL007W.
GeneIDi851557.
KEGGisce:YDL007W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81070 Genomic DNA. Translation: CAA56957.1.
L17040 Genomic DNA. Translation: AAA97498.1.
Z48432 Genomic DNA. Translation: CAA88352.1.
Z74055 Genomic DNA. Translation: CAA98563.1.
BK006938 Genomic DNA. Translation: DAA11841.1.
PIRiS46613.
RefSeqiNP_010277.1. NM_001180066.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JCOelectron microscopy4.80I1-437[»]
3JCPelectron microscopy4.60I1-437[»]
4CR2electron microscopy7.70I1-437[»]
4CR3electron microscopy9.30I1-437[»]
4CR4electron microscopy8.80I1-437[»]
5A5Belectron microscopy9.50I1-437[»]
ProteinModelPortaliP40327.
SMRiP40327. Positions 75-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32047. 196 interactions.
DIPiDIP-6282N.
IntActiP40327. 33 interactions.
MINTiMINT-632695.

PTM databases

iPTMnetiP40327.

Proteomic databases

MaxQBiP40327.
PRIDEiP40327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL007W; YDL007W; YDL007W.
GeneIDi851557.
KEGGisce:YDL007W.

Organism-specific databases

EuPathDBiFungiDB:YDL007W.
SGDiS000002165. RPT2.

Phylogenomic databases

GeneTreeiENSGT00550000074818.
HOGENOMiHOG000225143.
InParanoidiP40327.
KOiK03062.
OMAiIHTRKMT.
OrthoDBiEOG092C19WS.

Enzyme and pathway databases

BioCyciYEAST:G3O-29438-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

PROiP40327.

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...

Entry informationi

Entry nameiPRS4_YEAST
AccessioniPrimary (citable) accession number: P40327
Secondary accession number(s): D6VRY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 151 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.