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Protein

26S proteasome regulatory subunit RPN6

Gene

RPN6

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

Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.3 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • structural molecule activity Source: SGD

GO - Biological processi

  • proteasome assembly Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-29500-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 proteasome regulatory subunit RPN6
Alternative name(s):
Proteasome non-ATPase subunit 4
Gene namesi
Name:RPN6
Synonyms:NAS4
Ordered Locus Names:YDL097C
ORF Names:D2381
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL097C.
SGDiS000002255. RPN6.

Subcellular locationi

GO - Cellular componenti

  • proteasome regulatory particle, lid subcomplex Source: UniProtKB
  • proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321F → L in rpn6-2; temperature-sensitive mutant that shows defects in proteasome assembly when incubated at 37 degrees Celsius; when associated with P-377. 1 Publication
Mutagenesisi377 – 3771L → P in rpn6-2; temperature-sensitive mutant that shows defects in proteasome assembly when incubated at 37 degrees Celsius; when associated with L-132. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 43443326S proteasome regulatory subunit RPN6PRO_0000173860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources1 Publication

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ12377.
PeptideAtlasiQ12377.

PTM databases

iPTMnetiQ12377.

Interactioni

Subunit structurei

Component of the lid subcomplex of the 19S proteasome regulatory particle complex (also named PA700 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPN5Q122507EBI-308,EBI-15935
RPN8Q087234EBI-308,EBI-36176
RPN9Q040624EBI-308,EBI-15944

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi31965. 157 interactions.
DIPiDIP-1581N.
IntActiQ12377. 33 interactions.
MINTiMINT-396028.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-Q407-431[»]
3JCKelectron microscopy3.50C1-434[»]
4CR2electron microscopy7.70Q1-434[»]
4CR3electron microscopy9.30Q1-434[»]
4CR4electron microscopy8.80Q1-434[»]
5A5Belectron microscopy9.50Q1-434[»]
ProteinModelPortaliQ12377.
SMRiQ12377. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini229 – 401173PCIAdd
BLAST

Sequence similaritiesi

Belongs to the proteasome subunit S9 family.Curated
Contains 1 PCI domain.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063301.
HOGENOMiHOG000210093.
InParanoidiQ12377.
KOiK03036.
OMAiHENIEWA.
OrthoDBiEOG7W9S45.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 2 hits.
InterProiIPR000717. PCI_dom.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48452. SSF48452. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12377-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLPGSKLEE ARRLVNEKQY NEAEQVYLSL LDKDSSQSSA AAGASVDDKR
60 70 80 90 100
RNEQETSILE LGQLYVTMGA KDKLREFIPH STEYMMQFAK SKTVKVLKTL
110 120 130 140 150
IEKFEQVPDS LDDQIFVCEK SIEFAKREKR VFLKHSLSIK LATLHYQKKQ
160 170 180 190 200
YKDSLALIND LLREFKKLDD KPSLVDVHLL ESKVYHKLRN LAKSKASLTA
210 220 230 240 250
ARTAANSIYC PTQTVAELDL MSGILHCEDK DYKTAFSYFF ESFESYHNLT
260 270 280 290 300
THNSYEKACQ VLKYMLLSKI MLNLIDDVKN ILNAKYTKET YQSRGIDAMK
310 320 330 340 350
AVAEAYNNRS LLDFNTALKQ YEKELMGDEL TRSHFNALYD TLLESNLCKI
360 370 380 390 400
IEPFECVEIS HISKIIGLDT QQVEGKLSQM ILDKIFYGVL DQGNGWLYVY
410 420 430
ETPNQDATYD SALELVGQLN KVVDQLFEKA SVLY
Length:434
Mass (Da):49,774
Last modified:January 23, 2007 - v3
Checksum:iA8B1F7E6F73A4024
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95644 Genomic DNA. Translation: CAA64916.1.
Z74145 Genomic DNA. Translation: CAA98664.1.
BK006938 Genomic DNA. Translation: DAA11763.1.
PIRiS67639.
RefSeqiNP_010186.1. NM_001180156.1.

Genome annotation databases

EnsemblFungiiYDL097C; YDL097C; YDL097C.
GeneIDi851461.
KEGGisce:YDL097C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95644 Genomic DNA. Translation: CAA64916.1.
Z74145 Genomic DNA. Translation: CAA98664.1.
BK006938 Genomic DNA. Translation: DAA11763.1.
PIRiS67639.
RefSeqiNP_010186.1. NM_001180156.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-Q407-431[»]
3JCKelectron microscopy3.50C1-434[»]
4CR2electron microscopy7.70Q1-434[»]
4CR3electron microscopy9.30Q1-434[»]
4CR4electron microscopy8.80Q1-434[»]
5A5Belectron microscopy9.50Q1-434[»]
ProteinModelPortaliQ12377.
SMRiQ12377. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31965. 157 interactions.
DIPiDIP-1581N.
IntActiQ12377. 33 interactions.
MINTiMINT-396028.

PTM databases

iPTMnetiQ12377.

Proteomic databases

MaxQBiQ12377.
PeptideAtlasiQ12377.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL097C; YDL097C; YDL097C.
GeneIDi851461.
KEGGisce:YDL097C.

Organism-specific databases

EuPathDBiFungiDB:YDL097C.
SGDiS000002255. RPN6.

Phylogenomic databases

GeneTreeiENSGT00530000063301.
HOGENOMiHOG000210093.
InParanoidiQ12377.
KOiK03036.
OMAiHENIEWA.
OrthoDBiEOG7W9S45.

Enzyme and pathway databases

BioCyciYEAST:G3O-29500-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

NextBioi968741.
PROiQ12377.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 2 hits.
InterProiIPR000717. PCI_dom.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48452. SSF48452. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames."
    Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G., Jimenez A., Remacha M.A.
    Yeast 12:1377-1384(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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 SER-2.
  5. "cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome."
    Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A., DeMartino G.N., Tanahashi N., Tanaka K.
    Gene 203:241-250(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Rpn6p, a proteasome subunit from Saccharomyces cerevisiae, is essential for the assembly and activity of the 26 S proteasome."
    Santamaria P.G., Finley D., Ballesta J.P., Remacha M.
    J. Biol. Chem. 278:6687-6695(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Functional analysis of Rpn6p, a lid component of the 26 S proteasome, using temperature-sensitive rpn6 mutants of the yeast Saccharomyces cerevisiae."
    Isono E., Saito N., Kamata N., Saeki Y., Toh-E A.
    J. Biol. Chem. 280:6537-6547(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, MUTAGENESIS OF PHE-132 AND LEU-377.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiRPN6_YEAST
AccessioniPrimary (citable) accession number: Q12377
Secondary accession number(s): D6VRQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 16800 molecules/cell in log phase SD medium.1 Publication

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.