Proteasome component Y7 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P23639 (PSA2_YEAST)

Last modified February 9, 2010. Version 111. 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 Y7
    EC=3.4.25.1
Alternative name(s):
    Macropain subunit Y7
    Proteinase YSCE subunit 7
    Multicatalytic endopeptidase complex subunit Y7

Gene names

Name:	PRE8
Synonyms:	PRS4
Ordered Locus Names:	YML092C

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	250 AA.
Sequence status	Complete.
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.
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 7060 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the peptidase T1A 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	ubiquitin-dependent protein catabolic process Traceable author statement. Source: SGD
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex, alpha-subunit complex Ref.6 Inferred from physical interaction. 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...

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Binary interactions

With	Entry	#Exp.	IntAct
GLN1	P32288	1	EBI-13959,EBI-7665
PRE10	P21242	1	EBI-13959,EBI-13963
PRE9	P23638	1	EBI-13959,EBI-13967
SCL1	P21243	1	EBI-13959,EBI-13975
VAC14	Q06708	1	EBI-13959,EBI-27189

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 250

250

Proteasome component Y7

PRO_0000124090

Amino acid modifications

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphoserine Ref.5

Secondary structure

250

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P23639-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 12D7DFB1AA10E9FE
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FASTA

250

27,162

        10         20         30         40         50         60 
MTDRYSFSLT TFSPSGKLGQ IDYALTAVKQ GVTSLGIKAT NGVVIATEKK SSSPLAMSET 

        70         80         90        100        110        120 
LSKVSLLTPD IGAVYSGMGP DYRVLVDKSR KVAHTSYKRI YGEYPPTKLL VSEVAKIMQE 

       130        140        150        160        170        180 
ATQSGGVRPF GVSLLIAGHD EFNGFSLYQV DPSGSYFPWK ATAIGKGSVA AKTFLEKRWN 

       190        200        210        220        230        240 
DELELEDAIH IALLTLKESV EGEFNGDTIE LAIIGDENPD LLGYTGIPTD KGPRFRKLTS 

       250 
QEINDRLEAL

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References

	« Hide 'large scale' referencesShow '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], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 26786 / X2180-1A.
[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]	"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-13 AND SER-53, 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 (1.9 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

EMBL
GenBank
DDBJ

X56731 Genomic DNA. Translation: CAA40055.1.
Z46660 Genomic DNA. Translation: CAA86646.1.
AY557762 Genomic DNA. Translation: AAS56088.1.

PIR

SNBYY7. S12938.

RefSeq

NP_013618.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FNT	X-ray	3.20	B/P	1-250	[»]
1G0U	X-ray	2.40	A/O	1-250	[»]
1G65	X-ray	2.25	A/O	1-250	[»]
1JD2	X-ray	3.00	A/V	1-250	[»]
1RYP	X-ray	1.90	B/P	1-250	[»]
1Z7Q	X-ray	3.22	B/P	1-250	[»]
2F16	X-ray	2.80	A/O	1-250	[»]
2FAK	X-ray	2.80	A/O	1-250	[»]
2GPL	X-ray	2.81	A/O	1-250	[»]
2ZCY	X-ray	2.90	A/O	1-250	[»]
3BDM	X-ray	2.70	A/O	1-250	[»]
3D29	X-ray	2.60	A/O	1-250	[»]
3DY3	X-ray	2.81	A/O	1-250	[»]
3DY4	X-ray	2.80	A/O	1-250	[»]
3E47	X-ray	3.00	A/O	1-250	[»]
3GPJ	X-ray	2.70	A/O	1-250	[»]
3GPT	X-ray	2.41	A/O	1-250	[»]
3GPW	X-ray	2.50	A/O	1-250	[»]
3HYE	X-ray	2.50	A/O	1-250	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2822N.

IntAct

P23639. 37 interactions.

STRING

P23639.

Protein family/group databases

MEROPS

T01.972.

Proteomic databases

PeptideAtlas

P23639.

PRIDE

P23639.

Genome annotation databases

Ensembl

YML092C; YML092C; YML092C; Saccharomyces cerevisiae. [Genome view]

GeneID

854882.

KEGG

sce:YML092C.

NMPDR

fig|4932.3.peg.4655.

Organism-specific databases

CYGD

YML092c.

SGD

S000004557. PRE8.

Phylogenomic databases

eggNOG

HOGENOM

OMA

OrthoDB

PhylomeDB

P23639.

Enzyme and pathway databases

BRENDA

3.4.25.1. 250.

Gene expression databases

ArrayExpress

P23639.

Genevestigator

P23639.

GermOnline

YML092C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000426. Proteasome_asu_CS.
IPR001353. Proteasome_sua/b.
[Graphical view]

Pfam

PF00227. Proteasome. 1 hit.
PF10584. 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 Resources

NextBio

977831.

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Entry information

Entry name

PSA2_YEAST

Accession

Primary (citable) accession number: P23639

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	February 9, 2010
This is version 111 of the entry and version 1 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 XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: 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

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