Proteasome component PRE5 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40302 (PSA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 127. History...

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

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Proteasome component PRE5
EC=3.4.25.1

Alternative name(s):
Macropain subunit PRE5
Multicatalytic endopeptidase complex subunit PRE5
Proteinase YSCE subunit PRE5

Gene names

Name:	PRE5
Ordered Locus Names:	YMR314W
ORF Names:	YM9924.06

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Protein existence	Evidence 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 7210 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: SGD proteasomal ubiquitin-independent protein catabolic process Inferred from direct assay. Source: SGD
Cellular component	mitochondrion Inferred by curator Ref.8. Source: SGD nuclear outer membrane-endoplasmic reticulum membrane network Inferred by curator Ref.8. Source: SGD nucleus Inferred by curator Ref.8. Source: SGD proteasome core complex, alpha-subunit complex Inferred from direct assay Ref.8. Source: SGD proteasome storage granule Inferred from direct assay. 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRE10	P21242	3	EBI-13955,EBI-13963

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 234

234

Proteasome component PRE5

PRO_0000124076

Amino acid modifications

Modified residue

Phosphoserine Ref.6 Ref.7

Modified residue

Phosphothreonine Ref.7

Secondary structure

234

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P40302 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: C43CBCC1C6B9E39E
Show »

FASTA

234

25,604

        10         20         30         40         50         60 
MFRNNYDGDT VTFSPTGRLF QVEYALEAIK QGSVTVGLRS NTHAVLVALK RNADELSSYQ 

        70         80         90        100        110        120 
KKIIKCDEHM GLSLAGLAPD ARVLSNYLRQ QCNYSSLVFN RKLAVERAGH LLCDKAQKNT 

       130        140        150        160        170        180 
QSYGGRPYGV GLLIIGYDKS GAHLLEFQPS GNVTELYGTA IGARSQGAKT YLERTLDTFI 

       190        200        210        220        230 
KIDGNPDELI KAGVEAISQS LRDESLTVDN LSIAIVGKDT PFTIYDGEAV AKYI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core." Heinemeyer W., Troendle N., Albrecht G., Wolf D.H. Biochemistry 33:12229-12237(1994) [PubMed: 7918444] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 141-149 AND 220-228. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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.
[5]	"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].
[6]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY. Strain: ADR376.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND THR-16, MASS SPECTROMETRY.
[8]	"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 COMPLEX WITH THE 20S PROTEASOME.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L34347 Genomic DNA. Translation: AAA53544.1.
Z54141 Genomic DNA. Translation: CAA90832.1.
AY557978 Genomic DNA. Translation: AAS56304.1.
BK006946 Genomic DNA. Translation: DAA10215.1.

PIR

A55904.

RefSeq

NP_014045.1. NM_001182825.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FNT	X-ray	3.20	F/T	1-234	[»]
1G0U	X-ray	2.40	E/S	1-234	[»]
1G65	X-ray	2.25	E/S	2-234	[»]
1JD2	X-ray	3.00	E/Z	2-234	[»]
1RYP	X-ray	1.90	F/T	2-234	[»]
1VSY	X-ray	3.00	F/T	1-234	[»]
1Z7Q	X-ray	3.22	F/T	1-234	[»]
2F16	X-ray	2.80	E/S	2-234	[»]
2FAK	X-ray	2.80	E/S	2-234	[»]
2GPL	X-ray	2.81	E/S	2-234	[»]
2ZCY	X-ray	2.90	E/S	1-234	[»]
3BDM	X-ray	2.70	E/S	1-234	[»]
3D29	X-ray	2.60	E/S	2-234	[»]
3DY3	X-ray	2.81	E/S	2-234	[»]
3DY4	X-ray	2.80	E/S	2-234	[»]
3E47	X-ray	3.00	E/S	2-234	[»]
3GPJ	X-ray	2.70	E/S	2-234	[»]
3GPT	X-ray	2.41	E/S	2-234	[»]
3GPW	X-ray	2.50	E/S	2-234	[»]
3HYE	X-ray	2.50	E/S	2-234	[»]
3L5Q	X-ray	3.00	K/W	1-234	[»]
3MG0	X-ray	2.68	E/S	2-234	[»]
3MG4	X-ray	3.11	E/S	2-234	[»]
3MG6	X-ray	2.60	E/S	1-234	[»]
3MG7	X-ray	2.78	E/S	1-234	[»]
3MG8	X-ray	2.59	E/S	1-234	[»]
3NZJ	X-ray	2.40	E/S	1-234	[»]
3NZW	X-ray	2.50	E/S	1-234	[»]
3NZX	X-ray	2.70	E/S	1-234	[»]
3OEU	X-ray	2.60	E/S	2-234	[»]
3OEV	X-ray	2.85	E/S	2-234	[»]
3OKJ	X-ray	2.70	E/S	2-234	[»]
3TDD	X-ray	2.70	E/S	2-234	[»]

ProteinModelPortal

P40302.

SMR

P40302. Positions 2-234.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1528N.

IntAct

P40302. 39 interactions.

MINT

MINT-400436.

STRING

P40302.

Protein family/group databases

MEROPS

T01.976.

2D gel databases

UCD-2DPAGE

P40302.

Proteomic databases

PeptideAtlas

P40302.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YMR314W; YMR314W; YMR314W.

GeneID

855362.

KEGG

sce:YMR314W.

NMPDR

fig|4932.3.peg.5104.

Organism-specific databases

CYGD

YMR314w.

SGD

S000004931. PRE5.

Phylogenomic databases

eggNOG

fuNOG05813.

GeneTree

EFGT00050000002415.

HOGENOM

HBG499923.

OMA

KGPHIYQ.

OrthoDB

EOG4X6GJH.

Gene expression databases

ArrayExpress

P40302.

Genevestigator

P40302.

GermOnline

YMR314W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]

K02725.

Pfam

PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]

SMART

SM00948. Proteasome_A_N. 1 hit.
[Graphical view]

PROSITE

PS00388. PROTEASOME_A_1. 1 hit.
PS51475. PROTEASOME_A_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

979136.

Entry information

Entry name

PSA1_YEAST

Accession

Primary (citable) accession number: P40302
Secondary accession number(s): D6W0E1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents