Proteasome component C11 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P22141 (PSB2_YEAST)

Last modified November 24, 2009. Version 108. History...

Clusters with 100%, 90%, 50% identity |

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

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Names and origin

Protein names

Recommended name:
    Proteasome component C11
    EC=3.4.25.1
Alternative name(s):
    Macropain subunit C11
    Proteinase YSCE subunit 11
    Multicatalytic endopeptidase complex subunit C11

Gene names

Name:	PRE1
Ordered Locus Names:	YER012W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. This subunit has a chymotrypsin-like 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 21800 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the peptidase T1B family.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ascospore formation Traceable author statement. Source: SGD response to stress Traceable author statement. Source: SGD ubiquitin-dependent protein catabolic process Inferred from genetic interaction. Source: SGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: SGD proteasome core complex, beta-subunit complex Ref.6 Inferred from physical interaction. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
PRE10	P21242	1	EBI-13988,EBI-13963
RPT1	P33299	1	EBI-13988,EBI-13910
RPT6	Q01939	1	EBI-13988,EBI-13914
SEM1	O94742	1	EBI-13988,EBI-31337

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 198

198

Proteasome component C11

PRO_0000148055

Amino acid modifications

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphoserine Ref.5

Experimental info

Sequence conflict

183

I → T Ref.1

Sequence conflict

188

G → R Ref.1

Secondary structure

198

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P22141-1 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: ED43D319A5895B40
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FASTA

198

22,517

        10         20         30         40         50         60 
MDIILGIRVQ DSVILASSKA VTRGISVLKD SDDKTRQLSP HTLMSFAGEA GDTVQFAEYI 

        70         80         90        100        110        120 
QANIQLYSIR EDYELSPQAV SSFVRQELAK SIRSRRPYQV NVLIGGYDKK KNKPELYQID 

       130        140        150        160        170        180 
YLGTKVELPY GAHGYSGFYT FSLLDHHYRP DMTTEEGLDL LKLCVQELEK RMPMDFKGVI 

       190 
VKIVDKDGIR QVDDFQAQ

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival." Heinemeyer W., Kleinschmidt J.A., Saidowsky J., Escher C., Wolf D.H. EMBO J. 10:555-562(1991) [PubMed: 2001673] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"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. Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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: 14562106] [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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-82, MASS SPECTROMETRY.
[6]	"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 (1.90 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
[7]	"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 COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
[8]	"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 COMPLEX WITH THE 20S PROTEASOME.
[9]	"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 COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
[10]	"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 COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
[11]	"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 COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X56812 Genomic DNA. Translation: CAA40149.1.
U18778 Genomic DNA. Translation: AAB64545.1.
AY557807 Genomic DNA. Translation: AAS56133.1.

PIR

S50470.

RefSeq

NP_010928.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FNT	X-ray	3.20	K/Y	1-198	[»]
1G0U	X-ray	2.40	J/X	1-198	[»]
1G65	X-ray	2.25	J/X	1-198	[»]
1JD2	X-ray	3.00	J/Q	1-198	[»]
1RYP	X-ray	1.90	K/Y	1-198	[»]
1Z7Q	X-ray	3.22	K/Y	1-198	[»]
2F16	X-ray	2.80	J/X	1-198	[»]
2FAK	X-ray	2.80	J/X	1-198	[»]
2GPL	X-ray	2.81	J/X	1-198	[»]
2ZCY	X-ray	2.90	J/X	1-198	[»]
3BDM	X-ray	2.70	J/X	1-198	[»]
3D29	X-ray	2.60	J/X	1-198	[»]
3DY3	X-ray	2.81	J/X	1-198	[»]
3DY4	X-ray	2.80	J/X	1-198	[»]
3E47	X-ray	3.00	J/X	1-198	[»]
3GPJ	X-ray	2.70	J/X	1-198	[»]
3GPT	X-ray	2.41	J/X	1-198	[»]
3GPW	X-ray	2.50	J/X	1-198	[»]
3HYE	X-ray	2.50	J/X	1-198	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2808N.

IntAct

P22141. 26 interactions.

STRING

P22141.

Protein family/group databases

MEROPS

T01.984.

Proteomic databases

PeptideAtlas

P22141.

PRIDE

P22141.

Genome annotation databases

Ensembl

YER012W; YER012W; YER012W; Saccharomyces cerevisiae. [Genome view]

GeneID

856731.

KEGG

sce:YER012W.

NMPDR

fig|4932.3.peg.1987.

Organism-specific databases

CYGD

YER012w.

SGD

S000000814. PRE1.

Phylogenomic databases

HOGENOM

P22141.

OMA

RMPIDFK

OrthoDB

EOG937SXH

Enzyme and pathway databases

BRENDA

3.4.25.1. 250.

Gene expression databases

ArrayExpress

P22141.

Genevestigator

P22141.

GermOnline

YER012W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
[Graphical view]

Pfam

PF00227. Proteasome. 1 hit.
[Graphical view]

PROSITE

PS00854. PROTEASOME_B. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

982843.

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Entry information

Entry name

PSB2_YEAST

Accession

Primary (citable) accession number: P22141

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	February 1, 1995
Last modified:	November 24, 2009
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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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 V

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents