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P21242 (PSA7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Probable proteasome subunit alpha type-7

EC=3.4.25.1
Alternative name(s):
Macropain subunit C1
Multicatalytic endopeptidase complex subunit C1
Proteasome component C1
Proteinase YSCE subunit 1
Gene names
Name:PRE10
Synonyms:PRC1, PRS1
Ordered Locus Names:YOR362C
ORF Names:O6650
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [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.

Sequence similarities

Belongs to the peptidase T1A family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRE1P221413EBI-13963,EBI-13988
SCL1P212436EBI-13963,EBI-13975

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.6
Chain2 – 288287Probable proteasome subunit alpha type-7
PRO_0000124102

Amino acid modifications

Modified residue21Blocked amino end (Thr) Ref.1
Modified residue21N-acetylthreonine Ref.6

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P21242 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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].
[5]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S PROTEASOME.
[8]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-288 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
[9]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-248 OF COMPLEX WITH THE 20S PROTEASOME.
[10]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
[11]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
[12]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
[13]"Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
Mol. Cell 37:728-735(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 5-248 IN COMPLEX WITH THE PROTEASOME.
[14]"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
M55436 mRNA. Translation: AAA35227.1.
Z75270 Genomic DNA. Translation: CAA99691.1.
BK006948 Genomic DNA. Translation: DAA11123.1.
PIRSNBYC1. S11182.
RefSeqNP_015007.1. NM_001183782.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20G/U2-288[»]
1G0UX-ray2.40F/T1-248[»]
1G65X-ray2.25F/T5-248[»]
1JD2X-ray3.001/F5-248[»]
1RYPX-ray1.90G/U5-248[»]
1VSYX-ray3.00G/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[»]
3L5QX-ray3.00L/X5-248[»]
3MG0X-ray2.68F/T5-248[»]
3MG4X-ray3.11F/T5-248[»]
3MG6X-ray2.60F/T1-248[»]
3MG7X-ray2.78F/T1-248[»]
3MG8X-ray2.59F/T1-248[»]
3NZJX-ray2.40F/T1-288[»]
3NZWX-ray2.50F/T1-288[»]
3NZXX-ray2.70F/T1-288[»]
3OEUX-ray2.60F/T7-248[»]
3OEVX-ray2.85F/T7-248[»]
3OKJX-ray2.70F/T5-248[»]
3SDIX-ray2.65F/T7-248[»]
3SDKX-ray2.70F/T7-248[»]
3SHJX-ray2.80F/T5-248[»]
3TDDX-ray2.70F/T5-248[»]
3UN4X-ray3.40F/T1-288[»]
3UN8X-ray2.70F/T1-288[»]
4B4Telectron microscopy7.40G1-288[»]
4C0Velectron microscopy9.80G1-288[»]
4EU2X-ray2.51G/U5-248[»]
4FZCX-ray2.80F/T5-248[»]
4FZGX-ray3.00F/T5-248[»]
4G4SX-ray2.49G1-288[»]
4GK7X-ray2.80F/T5-248[»]
4HNPX-ray2.80F/T5-248[»]
4HRCX-ray2.80F/T5-248[»]
4HRDX-ray2.80F/T5-248[»]
4INRX-ray2.70F/T1-288[»]
4INTX-ray2.90F/T1-288[»]
4INUX-ray3.10F/T1-288[»]
4J70X-ray2.80F/T1-288[»]
4JSQX-ray2.80F/T1-288[»]
4JSUX-ray2.90F/T1-288[»]
4JT0X-ray3.10F/T1-288[»]
4LQIX-ray2.70F/T5-248[»]
4NNNX-ray2.50F/T1-288[»]
4NNWX-ray2.60F/T1-288[»]
4NO1X-ray2.50F/T1-288[»]
4NO6X-ray3.00F/T1-288[»]
4NO8X-ray2.70F/T1-288[»]
4NO9X-ray2.90F/T1-288[»]
ProteinModelPortalP21242.
SMRP21242. Positions 5-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34747. 91 interactions.
DIPDIP-1526N.
IntActP21242. 29 interactions.
MINTMINT-411846.
STRING4932.YOR362C.

Proteomic databases

PaxDbP21242.
PeptideAtlasP21242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR362C; YOR362C; YOR362C.
GeneID854544.
KEGGsce:YOR362C.

Organism-specific databases

SGDS000005889. PRE10.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074912.
HOGENOMHOG000091086.
KOK02727.
OMAVPDGRHF.
OrthoDBEOG7SBP0C.

Enzyme and pathway databases

BioCycYEAST:G3O-33832-MONOMER.

Gene expression databases

GenevestigatorP21242.

Family and domain databases

InterProIPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21242.
NextBio976955.
PROP21242.

Entry information

Entry namePSA7_YEAST
AccessionPrimary (citable) accession number: P21242
Secondary accession number(s): D6W357
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references