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P40016 (RPN3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
26S proteasome regulatory subunit RPN3
Gene names
Name:RPN3
Synonyms:SUN2
Ordered Locus Names:YER021W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively By similarity.

Post-translational modification

N-acetylated by NAT1. Ref.5

Miscellaneous

Present with 16700 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the proteasome subunit S3 family.

Contains 1 PCI domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPN7Q061038EBI-15927,EBI-15940

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 52352226S proteasome regulatory subunit RPN3
PRO_0000173827

Regions

Domain343 – 447105PCI

Amino acid modifications

Modified residue21N-acetylalanine Ref.5
Modified residue4541Phosphoserine Ref.7

Experimental info

Sequence conflict3551G → S no nucleotide entry Ref.1
Sequence conflict3551G → S in BAA11208. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P40016 [UniParc].

Last modified October 5, 2010. Version 5.
Checksum: B08B58663DDA85DC

FASTA52360,393
        10         20         30         40         50         60 
MASTAVMMDV DSSGVNDLHH SEKKYAEEDQ VQELLKVLNE ISKTTLTLDP RYIWRSLKDL 

        70         80         90        100        110        120 
SSLRNQELLN AETLCFTVNV LYPDSSSFKK NLLKFITSNH KSSVPGSAEL RNSYPASFYS 

       130        140        150        160        170        180 
VNTEKKTIEV TAEINCFMHL LVQLFLWDSK ELEQLVEFNR KVVIPNLLCY YNLRSLNLIN 

       190        200        210        220        230        240 
AKLWFYIYLS HETLARSSEE INSDNQNIIL RSTMMKFLKI ASLKHDNETK AMLINLILRD 

       250        260        270        280        290        300 
FLNNGEVDSA SDFISKLEYP HTDVSSSLEA RYFFYLSKIN AIQLDYSTAN EYIIAAIRKA 

       310        320        330        340        350        360 
PHNSKSLGFL QQSNKLHCCI QLLMGDIPEL SFFHQSNMQK SLLPYYHLTK AVKLGDLKKF 

       370        380        390        400        410        420 
TSTITKYKQL LLKDDTYQLC VRLRSNVIKT GIRIISLTYK KISLRDICLK LNLDSEQTVE 

       430        440        450        460        470        480 
YMVSRAIRDG VIEAKINHED GFIETTELLN IYDSEDPQQV FDERIKFANQ LHDEYLVSMR 

       490        500        510        520 
YPEDKKTQQN EKSENGENDD DTLDGDLMDD MSDISDLDDL GFL 

« Hide

References

« Hide 'large scale' references
[1]"A multicopy suppressor of nin1-1 of the yeast Saccharomyces cerevisiae is a counterpart of the Drosophila melanogaster diphenol oxidase A2 gene, Dox-A2."
Kawamura M., Kominami K., Takeuchi J., Toh-e A.
Mol. Gen. Genet. 251:146-152(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1."
Kominami K., Okura N., Kawamura M., Demartino G.N., Slaughter C.A., Shimbara N., Chung C.H., Fujimuro M., Yokosawa H., Shimizu Y., Tanahashi N., Tanaka K., Toh-e A.
Mol. Biol. Cell 8:171-187(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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 2-8, ACETYLATION AT ALA-2.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"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-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Near-atomic resolution structural model of the yeast 26S proteasome."
Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G., Sakata E., Nickell S., Plitzko J.M., Villa E., Baumeister W., Forster F.
Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D78023 Genomic DNA. Translation: BAA11208.1.
U18778 Genomic DNA. Translation: AAB64554.1.
BK006939 Genomic DNA. Translation: DAA07674.1.
PIRS50479.
RefSeqNP_010938.1. NM_001178912.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J47electron microscopy-S455-478[»]
4CR2electron microscopy7.70S1-523[»]
4CR3electron microscopy9.30S1-523[»]
4CR4electron microscopy8.80S1-523[»]
ProteinModelPortalP40016.
SMRP40016. Positions 126-478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36755. 114 interactions.
DIPDIP-1322N.
IntActP40016. 32 interactions.
MINTMINT-401279.
STRING4932.YER021W.

Proteomic databases

MaxQBP40016.
PaxDbP40016.
PeptideAtlasP40016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER021W; YER021W; YER021W.
GeneID856742.
KEGGsce:YER021W.

Organism-specific databases

SGDS000000823. RPN3.

Phylogenomic databases

eggNOGNOG251646.
GeneTreeENSGT00490000043406.
HOGENOMHOG000193909.
KOK03033.
OMAEAKINHE.
OrthoDBEOG7PVX27.

Enzyme and pathway databases

BioCycYEAST:G3O-30205-MONOMER.

Gene expression databases

GenevestigatorP40016.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR013586. 26S_Psome_reg_C.
IPR013143. PAM.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01399. PCI. 1 hit.
PF08375. Rpn3_C. 1 hit.
[Graphical view]
SMARTSM00753. PAM. 1 hit.
SM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982876.
PROP40016.

Entry information

Entry nameRPN3_YEAST
AccessionPrimary (citable) accession number: P40016
Secondary accession number(s): D3DLS0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 5, 2010
Last modified: June 11, 2014
This is version 112 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references