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Protein

26S proteasome regulatory subunit RPN2

Gene

RPN2

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

GO - Molecular functioni

  • enzyme regulator activity Source: InterPro
  • protein binding, bridging Source: SGD

GO - Biological processi

  • proteasome assembly Source: SGD
  • regulation of protein catabolic process Source: InterPro
  • ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-31340-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 RPN2
Gene namesi
Name:RPN2
Synonyms:SEN3
Ordered Locus Names:YIL075C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL075C.
SGDiS000001337. RPN2.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
  • proteasome regulatory particle, base subcomplex Source: SGD
  • proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 94594426S proteasome regulatory subunit RPN2PRO_0000173808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources1 Publication
Modified residuei801 – 8011PhosphothreonineCombined sources
Modified residuei932 – 9321PhosphothreonineCombined sources

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP32565.
PeptideAtlasiP32565.

PTM databases

iPTMnetiP32565.

Interactioni

Subunit structurei

Interacts with UBR1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RPN13O135633EBI-15919,EBI-32948
UBR1P198122EBI-15919,EBI-19909

GO - Molecular functioni

  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi34917. 100 interactions.
DIPiDIP-4638N.
IntActiP32565. 65 interactions.
MINTiMINT-539880.

Structurei

Secondary structure

1
945
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 126Combined sources
Helixi18 – 4023Combined sources
Helixi43 – 508Combined sources
Helixi58 – 7215Combined sources
Helixi75 – 8511Combined sources
Helixi86 – 883Combined sources
Helixi96 – 11924Combined sources
Helixi123 – 1253Combined sources
Helixi131 – 14717Combined sources
Helixi150 – 15910Combined sources
Helixi163 – 17311Combined sources
Helixi179 – 19517Combined sources
Helixi200 – 21617Combined sources
Beta strandi217 – 2193Combined sources
Helixi222 – 23211Combined sources
Helixi235 – 24612Combined sources
Helixi251 – 26414Combined sources
Helixi267 – 27913Combined sources
Helixi284 – 2896Combined sources
Helixi293 – 30614Combined sources
Helixi311 – 32010Combined sources
Helixi326 – 33914Combined sources
Turni340 – 3434Combined sources
Helixi347 – 3515Combined sources
Helixi353 – 3586Combined sources
Helixi362 – 37413Combined sources
Turni379 – 3813Combined sources
Helixi382 – 3865Combined sources
Turni387 – 3893Combined sources
Helixi398 – 41114Combined sources
Turni412 – 4165Combined sources
Helixi417 – 43014Combined sources
Helixi437 – 45317Combined sources
Helixi460 – 47112Combined sources
Helixi475 – 48915Combined sources
Helixi495 – 50713Combined sources
Helixi511 – 52414Combined sources
Turni525 – 5273Combined sources
Helixi529 – 5324Combined sources
Helixi533 – 5419Combined sources
Helixi545 – 55814Combined sources
Turni559 – 5613Combined sources
Helixi565 – 57713Combined sources
Helixi581 – 59414Combined sources
Beta strandi596 – 5983Combined sources
Helixi602 – 6054Combined sources
Turni606 – 6083Combined sources
Helixi609 – 6113Combined sources
Helixi615 – 62814Combined sources
Beta strandi630 – 6323Combined sources
Helixi635 – 64511Combined sources
Helixi650 – 66314Combined sources
Turni669 – 6713Combined sources
Helixi675 – 68713Combined sources
Beta strandi689 – 6913Combined sources
Helixi693 – 70614Combined sources
Helixi709 – 7113Combined sources
Beta strandi713 – 7153Combined sources
Turni720 – 7223Combined sources
Helixi727 – 73610Combined sources
Turni737 – 7415Combined sources
Helixi743 – 75210Combined sources
Beta strandi753 – 7553Combined sources
Beta strandi757 – 7626Combined sources
Turni763 – 7664Combined sources
Beta strandi767 – 7693Combined sources
Beta strandi772 – 7754Combined sources
Turni779 – 7824Combined sources
Beta strandi866 – 8694Combined sources
Helixi878 – 8814Combined sources
Beta strandi886 – 8949Combined sources
Beta strandi898 – 90811Combined sources
Helixi920 – 9245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ADYX-ray2.70A/B2-945[»]
4CR2electron microscopy7.70N1-945[»]
4CR3electron microscopy9.30N1-945[»]
4CR4electron microscopy8.80N1-945[»]
5A5Belectron microscopy9.50N1-945[»]
ProteinModelPortaliP32565.
SMRiP32565. Positions 4-836, 855-925.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati366 – 39934PC 1Add
BLAST
Repeati403 – 44038PC 2Add
BLAST
Repeati445 – 47935PC 3Add
BLAST
Repeati480 – 51435PC 4Add
BLAST
Repeati516 – 54934PC 5Add
BLAST
Repeati550 – 58536PC 6Add
BLAST
Repeati586 – 61833PC 7Add
BLAST
Repeati620 – 65435PC 8Add
BLAST
Repeati655 – 69238PC 9Add
BLAST
Repeati698 – 73437PC 10Add
BLAST

Sequence similaritiesi

Belongs to the proteasome subunit S1 family.Curated
Contains 10 PC repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00550000074915.
HOGENOMiHOG000189403.
InParanoidiP32565.
KOiK03032.
OMAiVPTCDLD.
OrthoDBiEOG7X9GGC.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR016642. 26S_Psome_Rpn2.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PfamiPF01851. PC_rep. 3 hits.
[Graphical view]
PIRSFiPIRSF015947. 26S_Psome_Rpn2. 1 hit.
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P32565-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLTTAAPLL ALLRENQDSV KTYALESINN VVDQLWSEIS NELPDIEALY
60 70 80 90 100
DDDTFSDREM AALIASKVYY NLGEYESAVK YALAAKDRFD IDEKSQFVET
110 120 130 140 150
IVSKSIEMYV QEASKQYTKD EQFYTKDIID PKLTSIFERM IEKCLKASEL
160 170 180 190 200
KLALGIALEG YRLDIIESAL KSKLDQDSTS ENVKIINYLL TLAITTVTNS
210 220 230 240 250
KFRSSILRKS FDFLMNMPNC DYLTLNKVVV NLNDAGLALQ LFKKLKEEND
260 270 280 290 300
EGLSAQIAFD LVSSASQQLL EILVTELTAQ GYDPALLNIL SGLPTCDYYN
310 320 330 340 350
TFLLNNKNID IGLLNKSKSS LDGKFSLFHT AVSVANGFMH AGTTDNSFIK
360 370 380 390 400
ANLPWLGKAQ NWAKFTATAS LGVIHKGNLL EGKKVMAPYL PGSRASSRFI
410 420 430 440 450
KGGSLYGLGL IYAGFGRDTT DYLKNIIVEN SGTSGDEDVD VLLHGASLGI
460 470 480 490 500
GLAAMGSANI EVYEALKEVL YNDSATSGEA AALGMGLCML GTGKPEAIHD
510 520 530 540 550
MFTYSQETQH GNITRGLAVG LALINYGRQE LADDLITKML ASDESLLRYG
560 570 580 590 600
GAFTIALAYA GTGNNSAVKR LLHVAVSDSN DDVRRAAVIA LGFVLLRDYT
610 620 630 640 650
TVPRIVQLLS KSHNAHVRCG TAFALGIACA GKGLQSAIDV LDPLTKDPVD
660 670 680 690 700
FVRQAAMIAL SMILIQQTEK LNPQVADINK NFLSVITNKH QEGLAKFGAC
710 720 730 740 750
VAQGIMNAGG RNVTIQLENA DTGTLDTKSV VGLVMFSQFW YWFPLAHFLS
760 770 780 790 800
LSFTPTTVIG IRGSDQAIPK FQMNCYAKED AFSYPRMYEE ASGKEVEKVA
810 820 830 840 850
TAVLSTTARA KARAKKTKKE KGPNEEEKKK EHEEKEKERE TNKKGIKETK
860 870 880 890 900
ENDEEFYKNK YSSKPYKVDN MTRILPQQSR YISFIKDDRF VPVRKFKGNN
910 920 930 940
GVVVLRDREP KEPVALIETV RQMKDVNAPL PTPFKVDDNV DFPSA
Length:945
Mass (Da):104,232
Last modified:January 23, 2007 - v4
Checksum:i881E78EBC6BD934F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti333 – 3342SV → RL in AAA87613 (PubMed:7565784).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06321 Genomic DNA. Translation: AAA87613.1.
Z37997 Genomic DNA. Translation: CAA86095.1.
BK006942 Genomic DNA. Translation: DAA08475.1.
PIRiS48369.
RefSeqiNP_012190.1. NM_001179425.1.

Genome annotation databases

EnsemblFungiiYIL075C; YIL075C; YIL075C.
GeneIDi854735.
KEGGisce:YIL075C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06321 Genomic DNA. Translation: AAA87613.1.
Z37997 Genomic DNA. Translation: CAA86095.1.
BK006942 Genomic DNA. Translation: DAA08475.1.
PIRiS48369.
RefSeqiNP_012190.1. NM_001179425.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ADYX-ray2.70A/B2-945[»]
4CR2electron microscopy7.70N1-945[»]
4CR3electron microscopy9.30N1-945[»]
4CR4electron microscopy8.80N1-945[»]
5A5Belectron microscopy9.50N1-945[»]
ProteinModelPortaliP32565.
SMRiP32565. Positions 4-836, 855-925.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34917. 100 interactions.
DIPiDIP-4638N.
IntActiP32565. 65 interactions.
MINTiMINT-539880.

PTM databases

iPTMnetiP32565.

Proteomic databases

MaxQBiP32565.
PeptideAtlasiP32565.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL075C; YIL075C; YIL075C.
GeneIDi854735.
KEGGisce:YIL075C.

Organism-specific databases

EuPathDBiFungiDB:YIL075C.
SGDiS000001337. RPN2.

Phylogenomic databases

GeneTreeiENSGT00550000074915.
HOGENOMiHOG000189403.
InParanoidiP32565.
KOiK03032.
OMAiVPTCDLD.
OrthoDBiEOG7X9GGC.

Enzyme and pathway databases

BioCyciYEAST:G3O-31340-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

NextBioi977437.
PROiP32565.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR016642. 26S_Psome_Rpn2.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PfamiPF01851. PC_rep. 3 hits.
[Graphical view]
PIRSFiPIRSF015947. 26S_Psome_Rpn2. 1 hit.
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo."
    Demarini D.J., Papa F.R., Swaminathan S., Ursic D., Rasmussen T.P., Culbertson M.R., Hochstrasser M.
    Mol. Cell. Biol. 15:6311-6321(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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. "The regulatory particle of the Saccharomyces cerevisiae proteasome."
    Glickman M.H., Rubin D.M., Fried V.A., Finley D.
    Mol. Cell. Biol. 18:3149-3162(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Physical association of ubiquitin ligases and the 26S proteasome."
    Xie Y., Varshavsky A.
    Proc. Natl. Acad. Sci. U.S.A. 97:2497-2502(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBR1.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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 THR-801 AND THR-932, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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 nameiRPN2_YEAST
AccessioniPrimary (citable) accession number: P32565
Secondary accession number(s): D6VVK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4750 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: 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.