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P40303 (PSA4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. 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:
Proteasome subunit alpha type-4

EC=3.4.25.1
Alternative name(s):
Macropain subunit PRE6
Multicatalytic endopeptidase complex subunit PRE6
Proteasome component PRE6
Proteinase YSCE subunit PRE6
Gene names
Name:PRE6
Ordered Locus Names:YOL038W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
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. Interacts with CIC1. Ref.5

Subcellular location

Cytoplasm. Nucleus Ref.6.

Miscellaneous

Present with 16800 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase T1A family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CIC1P387795EBI-13980,EBI-24538
cut8P389372EBI-13980,EBI-1152591From a different organism.
PRE1P221413EBI-13980,EBI-13988

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Proteasome subunit alpha type-4
PRO_0000124165

Amino acid modifications

Modified residue601Phosphothreonine Ref.8

Secondary structure

................................................ 254
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40303 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 73AEE63B836E618A

FASTA25428,439
        10         20         30         40         50         60 
MSGYDRALSI FSPDGHIFQV EYALEAVKRG TCAVGVKGKN CVVLGCERRS TLKLQDTRIT 

        70         80         90        100        110        120 
PSKVSKIDSH VVLSFSGLNA DSRILIEKAR VEAQSHRLTL EDPVTVEYLT RYVAGVQQRY 

       130        140        150        160        170        180 
TQSGGVRPFG VSTLIAGFDP RDDEPKLYQT EPSGIYSSWS AQTIGRNSKT VREFLEKNYD 

       190        200        210        220        230        240 
RKEPPATVEE CVKLTVRSLL EVVQTGAKNI EITVVKPDSD IVALSSEEIN QYVTQIEQEK 

       250 
QEQQEQDKKK KSNH 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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]Troendle N.
Thesis (1991), University of Stuttgart, Germany
Cited for: PROTEIN SEQUENCE OF 112-133.
[5]"Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4."
Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.
EMBO J. 20:4423-4431(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIC1.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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].
[8]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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 3-343 OF COMPLEX WITH THE 20S PROTEASOME.
[10]"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 COMPLEX WITH THE 20S PROTEASOME.
[11]"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 1-243 OF COMPLEX WITH THE 20S PROTEASOME.
[12]"Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor."
Groll M., Koguchi Y., Huber R., Kohno J.
J. Mol. Biol. 311:543-548(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
[13]"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 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
[14]"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 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
[15]"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 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
[16]"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 17-243 IN COMPLEX WITH THE PROTEASOME.
[17]"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
L34348 Genomic DNA. Translation: AAA34903.1.
Z74780 Genomic DNA. Translation: CAA99040.1.
BK006948 Genomic DNA. Translation: DAA10745.1.
PIRB55904.
RefSeqNP_014604.1. NM_001183292.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20D/R1-254[»]
1G0UX-ray2.40C/Q1-243[»]
1G65X-ray2.25C/Q3-243[»]
1JD2X-ray3.00C/X3-243[»]
1RYPX-ray1.90D/R3-243[»]
1VSYX-ray3.00D/R17-243[»]
1Z7QX-ray3.22D/R1-254[»]
2F16X-ray2.80C/Q3-243[»]
2FAKX-ray2.80C/Q3-243[»]
2GPLX-ray2.81C/Q3-243[»]
2ZCYX-ray2.90C/Q1-254[»]
3BDMX-ray2.70C/Q1-254[»]
3D29X-ray2.60C/Q3-236[»]
3DY3X-ray2.81C/Q3-243[»]
3DY4X-ray2.80C/Q3-243[»]
3E47X-ray3.00C/Q3-243[»]
3GPJX-ray2.70C/Q3-243[»]
3GPTX-ray2.41C/Q3-243[»]
3GPWX-ray2.50C/Q3-243[»]
3HYEX-ray2.50C/Q3-243[»]
3L5QX-ray3.00I/U17-243[»]
3MG0X-ray2.68C/Q3-243[»]
3MG4X-ray3.11C/Q3-243[»]
3MG6X-ray2.60C/Q1-243[»]
3MG7X-ray2.78C/Q1-243[»]
3MG8X-ray2.59C/Q1-243[»]
3NZJX-ray2.40C/Q1-254[»]
3NZWX-ray2.50C/Q1-254[»]
3NZXX-ray2.70C/Q1-254[»]
3OEUX-ray2.60C/Q3-243[»]
3OEVX-ray2.85C/Q3-243[»]
3OKJX-ray2.70C/Q3-243[»]
3SDIX-ray2.65C/Q3-243[»]
3SDKX-ray2.70C/Q3-243[»]
3SHJX-ray2.80C/Q3-243[»]
3TDDX-ray2.70C/Q3-243[»]
3UN4X-ray3.40C/Q1-254[»]
3UN8X-ray2.70C/Q1-254[»]
4B4Telectron microscopy7.40D1-254[»]
4C0Velectron microscopy9.80D1-254[»]
4EU2X-ray2.51D/R3-243[»]
4FZCX-ray2.80C/Q3-243[»]
4FZGX-ray3.00C/Q3-243[»]
4G4SX-ray2.49D1-254[»]
4GK7X-ray2.80C/Q3-243[»]
4HNPX-ray2.80C/Q3-243[»]
4HRCX-ray2.80C/Q3-243[»]
4HRDX-ray2.80C/Q3-243[»]
4INRX-ray2.70C/Q1-254[»]
4INTX-ray2.90C/Q1-254[»]
4INUX-ray3.10C/Q1-254[»]
4J70X-ray2.80C/Q1-254[»]
4JSQX-ray2.80C/Q1-254[»]
4JSUX-ray2.90C/Q1-254[»]
4JT0X-ray3.10C/Q1-254[»]
4LQIX-ray2.70C/Q3-243[»]
4NNNX-ray2.50C/Q1-254[»]
4NNWX-ray2.60C/Q1-254[»]
4NO1X-ray2.50C/Q1-254[»]
4NO6X-ray3.00C/Q1-254[»]
4NO8X-ray2.70C/Q1-254[»]
4NO9X-ray2.90C/Q1-254[»]
ProteinModelPortalP40303.
SMRP40303. Positions 3-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34364. 103 interactions.
DIPDIP-4844N.
IntActP40303. 42 interactions.
MINTMINT-478854.
STRING4932.YOL038W.

Proteomic databases

PaxDbP40303.
PeptideAtlasP40303.
PRIDEP40303.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL038W; YOL038W; YOL038W.
GeneID854119.
KEGGsce:YOL038W.

Organism-specific databases

CYGDYOL038w.
SGDS000005398. PRE6.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074753.
HOGENOMHOG000091085.
KOK02731.
OMAITRHIAG.
OrthoDBEOG7SBP0C.

Enzyme and pathway databases

BioCycYEAST:G3O-33452-MONOMER.

Gene expression databases

GenevestigatorP40303.

Family and domain databases

InterProIPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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

EvolutionaryTraceP40303.
NextBio975822.

Entry information

Entry namePSA4_YEAST
AccessionPrimary (citable) accession number: P40303
Secondary accession number(s): D6W229
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 149 of the entry and version 1 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