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Protein

26S protease regulatory subunit 6B homolog

Gene

RPT3

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 bindingi213 – 2208ATPSequence analysis

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct

GO - Biological processi

  • 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-29942-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 6B homolog
Alternative name(s):
Protein YNT1
Tat-binding homolog 2
Gene namesi
Name:RPT3
Synonyms:YNT1, YTA2
Ordered Locus Names:YDR394W
ORF Names:D9509.14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR394W.
SGDiS000002802. RPT3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • 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
Chaini1 – 42842826S protease regulatory subunit 6B homologPRO_0000084697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Post-translational modificationi

N-acetylated by NAT3.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP33298.
PeptideAtlasiP33298.

PTM databases

iPTMnetiP33298.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-13905,EBI-13905
NAS6P500869EBI-13905,EBI-14028
RAD23P326283EBI-13905,EBI-14668
RPN12P324963EBI-13905,EBI-15953
RPT1P332994EBI-13905,EBI-13910
RPT5P332976EBI-13905,EBI-13920
RPT6Q019395EBI-13905,EBI-13914

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi32456. 157 interactions.
DIPiDIP-1587N.
IntActiP33298. 44 interactions.
MINTiMINT-383865.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi351 – 3599Combined sources
Helixi368 – 3736Combined sources
Helixi380 – 39617Combined sources
Beta strandi400 – 4023Combined sources
Helixi404 – 4129Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DZNX-ray2.20B/D/F348-428[»]
2DZOX-ray3.00B/D348-428[»]
4CR2electron microscopy7.70K1-428[»]
4CR3electron microscopy9.30K1-428[»]
4CR4electron microscopy8.80K1-428[»]
5A5Belectron microscopy9.50K1-428[»]
ProteinModelPortaliP33298.
SMRiP33298. Positions 48-428.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33298.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074962.
HOGENOMiHOG000225143.
InParanoidiP33298.
KOiK03063.
OMAiDNDHAIV.
OrthoDBiEOG7RNK8W.

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.

P33298-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEELGIVTPV EKAVEEKPAV KSYASLLAQL NGTVNNNSAL SNVNSDIYFK
60 70 80 90 100
LKKLEKEYEL LTLQEDYIKD EQRHLKRELK RAQEEVKRIQ SVPLVIGQFL
110 120 130 140 150
EPIDQNTGIV SSTTGMSYVV RILSTLDREL LKPSMSVALH RHSNALVDIL
160 170 180 190 200
PPDSDSSISV MGENEKPDVT YADVGGLDMQ KQEIREAVEL PLVQADLYEQ
210 220 230 240 250
IGIDPPRGVL LYGPPGTGKT MLVKAVANST KAAFIRVNGS EFVHKYLGEG
260 270 280 290 300
PRMVRDVFRL ARENAPSIIF IDEVDSIATK RFDAQTGSDR EVQRILIELL
310 320 330 340 350
TQMDGFDQST NVKVIMATNR ADTLDPALLR PGRLDRKIEF PSLRDRRERR
360 370 380 390 400
LIFGTIASKM SLAPEADLDS LIIRNDSLSG AVIAAIMQEA GLRAVRKNRY
410 420
VILQSDLEEA YATQVKTDNT VDKFDFYK
Length:428
Mass (Da):47,894
Last modified:October 5, 2010 - v2
Checksum:iE12F0995A60732BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti342 – 3421S → Y in CAA51972 (PubMed:7754704).Curated
Sequence conflicti342 – 3421S → Y in AAA81916 (PubMed:7803857).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73570 Genomic DNA. Translation: CAA51972.1.
U06229 Genomic DNA. Translation: AAA81916.1.
U32274 Genomic DNA. Translation: AAB64836.1.
BK006938 Genomic DNA. Translation: DAA12238.1.
PIRiS69678.
RefSeqiNP_010682.3. NM_001180702.3.

Genome annotation databases

EnsemblFungiiYDR394W; YDR394W; YDR394W.
GeneIDi852003.
KEGGisce:YDR394W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73570 Genomic DNA. Translation: CAA51972.1.
U06229 Genomic DNA. Translation: AAA81916.1.
U32274 Genomic DNA. Translation: AAB64836.1.
BK006938 Genomic DNA. Translation: DAA12238.1.
PIRiS69678.
RefSeqiNP_010682.3. NM_001180702.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DZNX-ray2.20B/D/F348-428[»]
2DZOX-ray3.00B/D348-428[»]
4CR2electron microscopy7.70K1-428[»]
4CR3electron microscopy9.30K1-428[»]
4CR4electron microscopy8.80K1-428[»]
5A5Belectron microscopy9.50K1-428[»]
ProteinModelPortaliP33298.
SMRiP33298. Positions 48-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32456. 157 interactions.
DIPiDIP-1587N.
IntActiP33298. 44 interactions.
MINTiMINT-383865.

PTM databases

iPTMnetiP33298.

Proteomic databases

MaxQBiP33298.
PeptideAtlasiP33298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR394W; YDR394W; YDR394W.
GeneIDi852003.
KEGGisce:YDR394W.

Organism-specific databases

EuPathDBiFungiDB:YDR394W.
SGDiS000002802. RPT3.

Phylogenomic databases

GeneTreeiENSGT00550000074962.
HOGENOMiHOG000225143.
InParanoidiP33298.
KOiK03063.
OMAiDNDHAIV.
OrthoDBiEOG7RNK8W.

Enzyme and pathway databases

BioCyciYEAST:G3O-29942-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

EvolutionaryTraceiP33298.
PROiP33298.

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. "Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue."
    Campbell C.L., Tanaka N., White K.H., Thorsness P.E.
    Mol. Biol. Cell 5:899-905(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [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. "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 1-6, ACETYLATION AT MET-1.
  6. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPRS6B_YEAST
AccessioniPrimary (citable) accession number: P33298
Secondary accession number(s): D6VT28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 5, 2010
Last modified: June 8, 2016
This is version 152 of the entry and version 2 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.