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Reviewed, UniProtKB/Swiss-Prot P23638 (PSA4_YEAST)

Last modified November 3, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Proteasome component Y13
    EC=3.4.25.1
Alternative name(s):
    Macropain subunit Y13
    Proteinase YSCE subunit 13
    Multicatalytic endopeptidase complex subunit Y13
Gene names
Name: PRE9
Synonyms: PRS5
Ordered Locus Names: YGR135W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.

Catalytic activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.

Subcellular location

Cytoplasm. Nucleus.

Miscellaneous

Present with 17100 molecules/cell in log phase SD medium. Ref.3

Sequence similarities

Belongs to the peptidase T1A family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRE10P212421EBI-13967,EBI-13963
PRE8P236391EBI-13967,EBI-13959

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Proteasome component Y13
PRO_0000124116

Amino acid modifications

Cross-link199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4

Secondary structure

....................................... 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23638-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: B43BB05233A01A9E

FASTA25828,714
        10         20         30         40         50         60 
MGSRRYDSRT TIFSPEGRLY QVEYALESIS HAGTAIGIMA SDGIVLAAER KVTSTLLEQD 

        70         80         90        100        110        120 
TSTEKLYKLN DKIAVAVAGL TADAEILINT ARIHAQNYLK TYNEDIPVEI LVRRLSDIKQ 

       130        140        150        160        170        180 
GYTQHGGLRP FGVSFIYAGY DDRYGYQLYT SNPSGNYTGW KAISVGANTS AAQTLLQMDY 

       190        200        210        220        230        240 
KDDMKVDDAI ELALKTLSKT TDSSALTYDR LEFATIRKGA NDGEVYQKIF KPQEIKDILV 

       250 
KTGITKKDED EEADEDMK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and functional analysis of three subunits of yeast proteasome."
Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K.
Mol. Cell. Biol. 11:344-353(1991) [PubMed: 1898763] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 73-92; 120-139 AND 200-236.
Strain: ATCC 26786 / X2180-1A.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed: 14557538] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-199, MASS SPECTROMETRY.
[5]"Structure of 20S proteasome from yeast at 2.4-A resolution."
Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R.
Nature 386:463-471(1997) [PubMed: 9087403] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S PROTEASOME.
[6]"Structural basis for the activation of 20S proteasomes by 11S regulators."
Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P.
Nature 408:115-120(2000) [PubMed: 11081519] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-245 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
[7]"A gated channel into the proteasome core particle."
Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R., Glickman M.H., Finley D.
Nat. Struct. Biol. 7:1062-1067(2000) [PubMed: 11062564] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-245 OF COMPLEX WITH THE 20S PROTEASOME.
[8]"TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome."
Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.
Chem. Biol. 13:607-614(2006) [PubMed: 16793518] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
[9]"Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding."
Groll M., Huber R., Potts B.C.M.
J. Am. Chem. Soc. 128:5136-5141(2006) [PubMed: 16608349] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
[10]"Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome."
Groll M., Berkers C.R., Ploegh H.L., Ovaa H.
Structure 14:451-456(2006) [PubMed: 16531229] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
+Additional computationally mapped references.

Cross-references

Sequence databases

M63851 Genomic DNA. Translation: AAA34907.1.
X56730 Genomic DNA. Translation: CAA40054.1.
Z72920 Genomic DNA. Translation: CAA97148.1.
PIRSNBYY3. S12940.
RefSeqNP_011651.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20C/Q1-245[»]
1G0UX-ray2.40B/P1-245[»]
1G65X-ray2.25B/P2-245[»]
1JD2X-ray3.00B/W2-245[»]
1RYPX-ray1.90C/Q2-245[»]
1Z7QX-ray3.22C/Q1-258[»]
2F16X-ray2.80B/P2-245[»]
2FAKX-ray2.80B/P2-245[»]
2GPLX-ray2.81B/P2-245[»]
2ZCYX-ray2.90B/P1-258[»]
3BDMX-ray2.70B/P1-258[»]
3D29X-ray2.60B/P2-245[»]
3DY3X-ray2.81B/P2-245[»]
3DY4X-ray2.80B/P2-245[»]
3E47X-ray3.00B/P2-245[»]
3GPJX-ray2.70B/P2-245[»]
3GPTX-ray2.41B/P2-245[»]
3GPWX-ray2.50B/P2-245[»]
3HYEX-ray2.50B/P2-245[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2823N.
IntActP23638. 19 interactions.
STRINGP23638.

Protein family/group databases

MEROPST01.973.

Proteomic databases

PeptideAtlasP23638.
PRIDEP23638.

Genome annotation databases

EnsemblYGR135W; YGR135W; YGR135W; Saccharomyces cerevisiae. [Genome view]
GeneID853036.
GenomeReviewsGene locus YGR135W in contig Y13135_GR.
KEGGsce:YGR135W.
NMPDRfig|4932.3.peg.2770.

Organism-specific databases

CYGDYGR135w.
SGDS000003367. PRE9.

Phylogenomic databases

HOGENOMP23638.
OMAMARRYDS.

Enzyme and pathway databases

BRENDA3.4.25.1. 250.

Gene expression databases

ArrayExpressP23638.
GenevestigatorP23638.
GermOnlineYGR135W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000426. Proteasome_asu_CS.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
PROSITEPS00388. PROTEASOME_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio972935.

Entry information

Entry namePSA4_YEAST
AccessionPrimary (citable) accession number: P23638
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 3, 2009
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VII

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents