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Protein

26S proteasome regulatory subunit RPN5

Gene

RPN5

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

Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.1 Publication

Miscellaneous

Present with 5710 molecules/cell in log phase SD medium.1 Publication

GO - Biological processi

  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  • protein deneddylation Source: SGD

Enzyme and pathway databases

BioCyciYEAST:G3O-29544-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-382556. ABC-family proteins mediated transport.
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-5689880. Ub-specific processing proteases.
R-SCE-6798695. Neutrophil degranulation.
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-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome regulatory subunit RPN5
Alternative name(s):
Proteasome non-ATPase subunit 5
Gene namesi
Name:RPN5
Synonyms:NAS5
Ordered Locus Names:YDL147W
ORF Names:D1572
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL147W.
SGDiS000002306. RPN5.

Subcellular locationi

GO - Cellular componenti

  • COP9 signalosome Source: SGD
  • nuclear proteasome complex Source: GO_Central
  • proteasome complex Source: SGD
  • proteasome regulatory particle, lid subcomplex Source: SGD
  • proteasome storage granule Source: SGD

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001738652 – 44526S proteasome regulatory subunit RPN5Add BLAST444

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ12250.
PRIDEiQ12250.

PTM databases

iPTMnetiQ12250.

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi31914. 610 interactors.
DIPiDIP-1578N.
IntActiQ12250. 47 interactors.
MINTiMINT-391026.

Structurei

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 35Combined sources4
Helixi37 – 41Combined sources5
Helixi42 – 44Combined sources3
Helixi49 – 68Combined sources20
Turni69 – 71Combined sources3
Helixi72 – 84Combined sources13
Helixi94 – 106Combined sources13
Helixi111 – 125Combined sources15
Helixi135 – 147Combined sources13
Helixi153 – 160Combined sources8
Turni161 – 164Combined sources4
Helixi165 – 167Combined sources3
Turni168 – 170Combined sources3
Helixi173 – 190Combined sources18
Helixi194 – 201Combined sources8
Helixi205 – 209Combined sources5
Helixi211 – 231Combined sources21
Helixi235 – 245Combined sources11
Helixi248 – 252Combined sources5
Helixi254 – 270Combined sources17
Helixi275 – 286Combined sources12
Helixi288 – 291Combined sources4
Helixi295 – 304Combined sources10
Helixi311 – 324Combined sources14
Turni326 – 328Combined sources3
Beta strandi331 – 334Combined sources4
Helixi337 – 356Combined sources20
Beta strandi357 – 361Combined sources5
Helixi362 – 369Combined sources8
Helixi373 – 385Combined sources13
Beta strandi392 – 394Combined sources3
Turni395 – 398Combined sources4
Beta strandi399 – 401Combined sources3
Helixi408 – 439Combined sources32

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-P409-442[»]
3JCKelectron microscopy3.50B1-445[»]
3JCOelectron microscopy4.80P1-445[»]
3JCPelectron microscopy4.60P1-445[»]
4CR2electron microscopy7.70P1-445[»]
4CR3electron microscopy9.30P1-445[»]
4CR4electron microscopy8.80P1-445[»]
5A5Belectron microscopy9.50P1-445[»]
5MPBelectron microscopy7.80P1-445[»]
5MPCelectron microscopy7.70P1-445[»]
5MPDelectron microscopy4.10P1-445[»]
5MPEelectron microscopy4.50P1-445[»]
5WVIelectron microscopy6.30P1-445[»]
5WVKelectron microscopy4.20P1-445[»]
ProteinModelPortaliQ12250.
SMRiQ12250.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini231 – 404PCIAdd BLAST174

Sequence similaritiesi

Belongs to the proteasome subunit p55 family.Curated

Phylogenomic databases

GeneTreeiENSGT00730000111110.
HOGENOMiHOG000194265.
InParanoidiQ12250.
KOiK03035.
OMAiWTQATIL.
OrthoDBiEOG092C2UIQ.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProiView protein in InterPro
IPR000717. PCI_dom.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
PfamiView protein in Pfam
PF01399. PCI. 1 hit.
SMARTiView protein in SMART
SM00088. PINT. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q12250-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRDAPIKAD KDYSQILKEE FPKIDSLAQN DCNSALDQLL VLEKKTRQAS
60 70 80 90 100
DLASSKEVLA KIVDLLASRN KWDDLNEQLT LLSKKHGQLK LSIQYMIQKV
110 120 130 140 150
MEYLKSSKSL DLNTRISVIE TIRVVTENKI FVEVERARVT KDLVEIKKEE
160 170 180 190 200
GKIDEAADIL CELQVETYGS MEMSEKIQFI LEQMELSILK GDYSQATVLS
210 220 230 240 250
RKILKKTFKN PKYESLKLEY YNLLVKISLH KREYLEVAQY LQEIYQTDAI
260 270 280 290 300
KSDEAKWKPV LSHIVYFLVL SPYGNLQNDL IHKIQNDNNL KKLESQESLV
310 320 330 340 350
KLFTTNELMR WPIVQKTYEP VLNEDDLAFG GEANKHHWED LQKRVIEHNL
360 370 380 390 400
RVISEYYSRI TLLRLNELLD LTESQTETYI SDLVNQGIIY AKVNRPAKIV
410 420 430 440
NFEKPKNSSQ LLNEWSHNVD ELLEHIETIG HLITKEEIMH GLQAK
Length:445
Mass (Da):51,768
Last modified:January 23, 2007 - v3
Checksum:iE5DC7F8E6AE27736
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97751 Genomic DNA. Translation: CAA66344.1.
Z74195 Genomic DNA. Translation: CAA98721.1.
BK006938 Genomic DNA. Translation: DAA11711.1.
PIRiS67695.
RefSeqiNP_010134.1. NM_001180207.1.

Genome annotation databases

EnsemblFungiiYDL147W; YDL147W; YDL147W.
GeneIDi851408.
KEGGisce:YDL147W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97751 Genomic DNA. Translation: CAA66344.1.
Z74195 Genomic DNA. Translation: CAA98721.1.
BK006938 Genomic DNA. Translation: DAA11711.1.
PIRiS67695.
RefSeqiNP_010134.1. NM_001180207.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-P409-442[»]
3JCKelectron microscopy3.50B1-445[»]
3JCOelectron microscopy4.80P1-445[»]
3JCPelectron microscopy4.60P1-445[»]
4CR2electron microscopy7.70P1-445[»]
4CR3electron microscopy9.30P1-445[»]
4CR4electron microscopy8.80P1-445[»]
5A5Belectron microscopy9.50P1-445[»]
5MPBelectron microscopy7.80P1-445[»]
5MPCelectron microscopy7.70P1-445[»]
5MPDelectron microscopy4.10P1-445[»]
5MPEelectron microscopy4.50P1-445[»]
5WVIelectron microscopy6.30P1-445[»]
5WVKelectron microscopy4.20P1-445[»]
ProteinModelPortaliQ12250.
SMRiQ12250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31914. 610 interactors.
DIPiDIP-1578N.
IntActiQ12250. 47 interactors.
MINTiMINT-391026.

PTM databases

iPTMnetiQ12250.

Proteomic databases

MaxQBiQ12250.
PRIDEiQ12250.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL147W; YDL147W; YDL147W.
GeneIDi851408.
KEGGisce:YDL147W.

Organism-specific databases

EuPathDBiFungiDB:YDL147W.
SGDiS000002306. RPN5.

Phylogenomic databases

GeneTreeiENSGT00730000111110.
HOGENOMiHOG000194265.
InParanoidiQ12250.
KOiK03035.
OMAiWTQATIL.
OrthoDBiEOG092C2UIQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29544-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-382556. ABC-family proteins mediated transport.
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-5689880. Ub-specific processing proteases.
R-SCE-6798695. Neutrophil degranulation.
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-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiPR:Q12250.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProiView protein in InterPro
IPR000717. PCI_dom.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
PfamiView protein in Pfam
PF01399. PCI. 1 hit.
SMARTiView protein in SMART
SM00088. PINT. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRPN5_YEAST
AccessioniPrimary (citable) accession number: Q12250
Secondary accession number(s): D6VRK1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 23, 2007
Last modified: May 10, 2017
This is version 141 of the entry and version 3 of the sequence. See 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.