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Protein

26S proteasome regulatory subunit RPN7

Gene

RPN7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.By similarity

GO - Molecular functioni

  • structural molecule activity Source: SGD

GO - Biological processi

  • ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-34248-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 RPN7
Gene namesi
Name:RPN7
Ordered Locus Names:YPR108W
ORF Names:P8283.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR108W.
SGDiS000006312. RPN7.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
  • proteasome regulatory particle, lid subcomplex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 42942826S proteasome regulatory subunit RPN7PRO_0000173845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei77 – 771PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06103.
PeptideAtlasiQ06103.

PTM databases

iPTMnetiQ06103.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RPN3P400168EBI-15940,EBI-15927

Protein-protein interaction databases

BioGridi36274. 61 interactions.
DIPiDIP-2880N.
IntActiQ06103. 29 interactions.
MINTiMINT-531082.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-R397-422[»]
3JCKelectron microscopy3.50D1-429[»]
4CR2electron microscopy7.70R1-429[»]
4CR3electron microscopy9.30R1-429[»]
4CR4electron microscopy8.80R1-429[»]
5A5Belectron microscopy9.50R1-429[»]
ProteinModelPortaliQ06103.
SMRiQ06103. Positions 23-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati131 – 16434TPRAdd
BLAST
Domaini221 – 392172PCIAdd
BLAST

Sequence similaritiesi

Contains 1 PCI domain.Curated
Contains 1 TPR repeat.PROSITE-ProRule annotation

Keywords - Domaini

TPR repeat

Phylogenomic databases

GeneTreeiENSGT00510000046608.
HOGENOMiHOG000214998.
InParanoidiQ06103.
KOiK03037.
OMAiYVCMIAL.
OrthoDBiEOG7DFXP0.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 2 hits.
InterProiIPR000717. PCI_dom.
IPR019585. Rpn7/CSN1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
PF10602. RPN7. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q06103-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDVEEKSQE VEYVDPTVNR VPNYEVSEKA FLLTQSKVSI EQRKEAAEFV
60 70 80 90 100
LAKIKEEEMA PYYKYLCEEY LVNNGQSDLE HDEKSDSLNE WIKFDQELYN
110 120 130 140 150
ELCKKNESKI KELNEKIQKL EEDDEGELEQ AQAWINLGEY YAQIGDKDNA
160 170 180 190 200
EKTLGKSLSK AISTGAKIDV MLTIARLGFF YNDQLYVKEK LEAVNSMIEK
210 220 230 240 250
GGDWERRNRY KTYYGIHCLA VRNFKEAAKL LVDSLATFTS IELTSYESIA
260 270 280 290 300
TYASVTGLFT LERTDLKSKV IDSPELLSLI STTAALQSIS SLTISLYASD
310 320 330 340 350
YASYFPYLLE TYANVLIPCK YLNRHADFFV REMRRKVYAQ LLESYKTLSL
360 370 380 390 400
KSMASAFGVS VAFLDNDLGK FIPNKQLNCV IDRVNGIVET NRPDNKNAQY
410 420
HLLVKQGDGL LTKLQKYGAA VRLTGSDRV
Length:429
Mass (Da):48,959
Last modified:January 23, 2007 - v3
Checksum:iB21B66CD818E636D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81S → G in AAT92788 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32445 Genomic DNA. Translation: AAB68078.1.
AY692769 Genomic DNA. Translation: AAT92788.1.
BK006949 Genomic DNA. Translation: DAA11522.1.
PIRiS59773.
RefSeqiNP_015433.1. NM_001184205.1.

Genome annotation databases

EnsemblFungiiYPR108W; YPR108W; YPR108W.
GeneIDi856223.
KEGGisce:YPR108W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32445 Genomic DNA. Translation: AAB68078.1.
AY692769 Genomic DNA. Translation: AAT92788.1.
BK006949 Genomic DNA. Translation: DAA11522.1.
PIRiS59773.
RefSeqiNP_015433.1. NM_001184205.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-R397-422[»]
3JCKelectron microscopy3.50D1-429[»]
4CR2electron microscopy7.70R1-429[»]
4CR3electron microscopy9.30R1-429[»]
4CR4electron microscopy8.80R1-429[»]
5A5Belectron microscopy9.50R1-429[»]
ProteinModelPortaliQ06103.
SMRiQ06103. Positions 23-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36274. 61 interactions.
DIPiDIP-2880N.
IntActiQ06103. 29 interactions.
MINTiMINT-531082.

PTM databases

iPTMnetiQ06103.

Proteomic databases

MaxQBiQ06103.
PeptideAtlasiQ06103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR108W; YPR108W; YPR108W.
GeneIDi856223.
KEGGisce:YPR108W.

Organism-specific databases

EuPathDBiFungiDB:YPR108W.
SGDiS000006312. RPN7.

Phylogenomic databases

GeneTreeiENSGT00510000046608.
HOGENOMiHOG000214998.
InParanoidiQ06103.
KOiK03037.
OMAiYVCMIAL.
OrthoDBiEOG7DFXP0.

Enzyme and pathway databases

BioCyciYEAST:G3O-34248-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

PROiQ06103.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 2 hits.
InterProiIPR000717. PCI_dom.
IPR019585. Rpn7/CSN1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
PF10602. RPN7. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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-8 AND SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiRPN7_YEAST
AccessioniPrimary (citable) accession number: Q06103
Secondary accession number(s): D6W4A6, E9P8W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 137 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 51900 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.