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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
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  • 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-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 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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001738082 – 94526S proteasome regulatory subunit RPN2Add BLAST944

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei801PhosphothreonineCombined sources1
Modified residuei932PhosphothreonineCombined sources1

Post-translational modificationi

N-acetylated by NAT1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP32565.
PRIDEiP32565.

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 interactors.
DIPiDIP-4638N.
IntActiP32565. 65 interactors.
MINTiMINT-539880.

Structurei

Secondary structure

1945
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 12Combined sources6
Helixi18 – 40Combined sources23
Helixi43 – 50Combined sources8
Helixi58 – 72Combined sources15
Helixi75 – 85Combined sources11
Helixi86 – 88Combined sources3
Helixi96 – 119Combined sources24
Helixi123 – 125Combined sources3
Helixi131 – 147Combined sources17
Helixi150 – 159Combined sources10
Helixi163 – 173Combined sources11
Helixi179 – 195Combined sources17
Helixi200 – 216Combined sources17
Beta strandi217 – 219Combined sources3
Helixi222 – 232Combined sources11
Helixi235 – 246Combined sources12
Helixi251 – 264Combined sources14
Helixi267 – 279Combined sources13
Helixi284 – 289Combined sources6
Helixi293 – 306Combined sources14
Helixi311 – 320Combined sources10
Helixi326 – 339Combined sources14
Turni340 – 343Combined sources4
Helixi347 – 351Combined sources5
Helixi353 – 358Combined sources6
Helixi362 – 374Combined sources13
Turni379 – 381Combined sources3
Helixi382 – 386Combined sources5
Turni387 – 389Combined sources3
Helixi398 – 411Combined sources14
Turni412 – 416Combined sources5
Helixi417 – 430Combined sources14
Helixi437 – 453Combined sources17
Helixi460 – 471Combined sources12
Helixi475 – 489Combined sources15
Helixi495 – 507Combined sources13
Helixi511 – 524Combined sources14
Turni525 – 527Combined sources3
Helixi529 – 532Combined sources4
Helixi533 – 541Combined sources9
Helixi545 – 558Combined sources14
Turni559 – 561Combined sources3
Helixi565 – 577Combined sources13
Helixi581 – 594Combined sources14
Beta strandi596 – 598Combined sources3
Helixi602 – 605Combined sources4
Turni606 – 608Combined sources3
Helixi609 – 611Combined sources3
Helixi615 – 628Combined sources14
Beta strandi630 – 632Combined sources3
Helixi635 – 645Combined sources11
Helixi650 – 663Combined sources14
Turni669 – 671Combined sources3
Helixi675 – 687Combined sources13
Beta strandi689 – 691Combined sources3
Helixi693 – 706Combined sources14
Helixi709 – 711Combined sources3
Beta strandi713 – 715Combined sources3
Turni720 – 722Combined sources3
Helixi727 – 736Combined sources10
Turni737 – 741Combined sources5
Helixi743 – 752Combined sources10
Beta strandi753 – 755Combined sources3
Beta strandi757 – 762Combined sources6
Turni763 – 766Combined sources4
Beta strandi767 – 769Combined sources3
Beta strandi772 – 775Combined sources4
Turni779 – 782Combined sources4
Beta strandi866 – 869Combined sources4
Helixi878 – 881Combined sources4
Beta strandi886 – 894Combined sources9
Beta strandi898 – 908Combined sources11
Helixi920 – 924Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JCOelectron microscopy4.80N1-945[»]
3JCPelectron microscopy4.60N1-945[»]
4ADYX-ray2.70A/B2-945[»]
4CR2electron microscopy7.70N1-945[»]
4CR3electron microscopy9.30N1-945[»]
4CR4electron microscopy8.80N1-945[»]
5A5Belectron microscopy9.50N1-945[»]
ProteinModelPortaliP32565.
SMRiP32565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati366 – 399PC 1Add BLAST34
Repeati403 – 440PC 2Add BLAST38
Repeati445 – 479PC 3Add BLAST35
Repeati480 – 514PC 4Add BLAST35
Repeati516 – 549PC 5Add BLAST34
Repeati550 – 585PC 6Add BLAST36
Repeati586 – 618PC 7Add BLAST33
Repeati620 – 654PC 8Add BLAST35
Repeati655 – 692PC 9Add BLAST38
Repeati698 – 734PC 10Add BLAST37

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00550000074915.
HOGENOMiHOG000189403.
InParanoidiP32565.
KOiK03032.
OMAiLWAEIAN.
OrthoDBiEOG092C0PBV.

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)DescriptionActionsGraphical viewLength
Sequence conflicti333 – 334SV → RL in AAA87613 (PubMed:7565784).Curated2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JCOelectron microscopy4.80N1-945[»]
3JCPelectron microscopy4.60N1-945[»]
4ADYX-ray2.70A/B2-945[»]
4CR2electron microscopy7.70N1-945[»]
4CR3electron microscopy9.30N1-945[»]
4CR4electron microscopy8.80N1-945[»]
5A5Belectron microscopy9.50N1-945[»]
ProteinModelPortaliP32565.
SMRiP32565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP32565.

Proteomic databases

MaxQBiP32565.
PRIDEiP32565.

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.
OMAiLWAEIAN.
OrthoDBiEOG092C0PBV.

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-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

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...

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: November 30, 2016
This is version 148 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.