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Reviewed, UniProtKB/Swiss-Prot P21242 (PSA3_YEAST)

Last modified November 3, 2009. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 C1
    EC=3.4.25.1
Alternative name(s):
    Macropain subunit C1
    Proteinase YSCE subunit 1
    Multicatalytic endopeptidase complex subunit C1
Gene names
Name: PRE10
Synonyms: PRC1, PRS1
Ordered Locus Names: YOR362C
ORF Names: O6650
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Post-translational modification

The alpha and beta forms are probably products of the same gene with different post-translational modifications.

Miscellaneous

Present with 12000 molecules/cell in log phase SD medium. Ref.3

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 288287Proteasome component C1
PRO_0000124102

Amino acid modifications

Modified residue21Blocked amino end (Thr) Ref.1
Modified residue2781Phosphothreonine Ref.4
Modified residue2791Phosphothreonine Ref.4

Secondary structure

................................... 288
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21242-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1E51D904CF336747

FASTA28831,536
        10         20         30         40         50         60 
MTSIGTGYDL SNSVFSPDGR NFQVEYAVKA VENGTTSIGI KCNDGVVFAV EKLITSKLLV 

        70         80         90        100        110        120 
PQKNVKIQVV DRHIGCVYSG LIPDGRHLVN RGREEAASFK KLYKTPIPIP AFADRLGQYV 

       130        140        150        160        170        180 
QAHTLYNSVR PFGVSTIFGG VDKNGAHLYM LEPSGSYWGY KGAATGKGRQ SAKAELEKLV 

       190        200        210        220        230        240 
DHHPEGLSAR EAVKQAAKII YLAHEDNKEK DFELEISWCS LSETNGLHKF VKGDLLQEAI 

       250        260        270        280 
DFAQKEINGD DDEDEDDSDN VMSSDDENAP VATNANATTD QEGDIHLE 

« Hide

References

« Hide 'large scale' references
[1]"Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits."
Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A., Tamura T., Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A., Nakanishi S., Ichihara A.
J. Biol. Chem. 265:16604-16613(1990) [PubMed: 1697860] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 106-135; 180-195 AND 200-209, CLEAVAGE OF INITIATOR METHIONINE.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [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 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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278 AND THR-279, 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 5-248 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 1-288 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 1-248 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 5-248 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 5-248 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 5-248 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
+Additional computationally mapped references.

Cross-references

Sequence databases

M55436 mRNA. Translation: AAA35227.1.
Z75270 Genomic DNA. Translation: CAA99691.1.
PIRSNBYC1. S11182.
RefSeqNP_015007.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20G/U2-288[»]
1G0UX-ray2.40F/T1-248[»]
1G65X-ray2.25F/T5-248[»]
1JD2X-ray3.001/F5-247[»]
1RYPX-ray1.90G/U5-248[»]
1Z7QX-ray3.22G/U1-288[»]
2F16X-ray2.80F/T5-248[»]
2FAKX-ray2.80F/T5-248[»]
2GPLX-ray2.81F/T5-248[»]
2ZCYX-ray2.90F/T2-288[»]
3BDMX-ray2.70F/T2-288[»]
3D29X-ray2.60F/T5-248[»]
3DY3X-ray2.81F/T5-248[»]
3DY4X-ray2.80F/T5-248[»]
3E47X-ray3.00F/T5-248[»]
3GPJX-ray2.70F/T5-248[»]
3GPTX-ray2.41F/T5-248[»]
3GPWX-ray2.50F/T5-248[»]
3HYEX-ray2.50F/T5-248[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1526N.
IntActP21242. 34 interactions.
STRINGP21242.

Protein family/group databases

MEROPST01.977.

Proteomic databases

PeptideAtlasP21242.
PRIDEP21242.

Genome annotation databases

EnsemblYOR362C; YOR362C; YOR362C; Saccharomyces cerevisiae. [Genome view]
GeneID854544.
GenomeReviewsGene locus YOR362C in contig Y13140_GR.
KEGGsce:YOR362C.
NMPDRfig|4932.3.peg.6126.

Organism-specific databases

CYGDYOR362c.
SGDS000005889. PRE10.

Phylogenomic databases

HOGENOMP21242.
OMALSWVGEI.

Enzyme and pathway databases

BRENDA3.4.25.1. 250.

Gene expression databases

ArrayExpressP21242.
GenevestigatorP21242.
GermOnlineYOR362C. 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

NextBio976955.

Entry information

Entry namePSA3_YEAST
AccessionPrimary (citable) accession number: P21242
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 113 of the entry and version 2 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

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