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P30657 (PSB7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit beta type-7

EC=3.4.25.1
Alternative name(s):
Macropain subunit PRE4
Multicatalytic endopeptidase complex subunit PRE4
Proteasome component PRE4
Proteinase YSCE subunit PRE4
Gene names
Name:PRE4
Ordered Locus Names:YFR050C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length266 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. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity. Ref.1

Catalytic activity

Cleavage of peptide bonds with very broad specificity. Ref.1

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.1 Ref.6

Subcellular location

Cytoplasm. Nucleus Ref.7.

Miscellaneous

Present with 16900 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase T1B family.

Caution

It is uncertain whether Met-1 or Met-31 is the initiator.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 3333
PRO_0000331490
Chain34 – 266233Proteasome subunit beta type-7
PRO_0000148073

Experimental info

Sequence conflict1881L → V in AAT92966. Ref.5

Secondary structure

........................................... 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30657 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: E585BB3B5D0C8E2C

FASTA26629,443
        10         20         30         40         50         60 
MNHDPFSWGR PADSTYGAYN TQIANAGASP MVNTQQPIVT GTSVISMKYD NGVIIAADNL 

        70         80         90        100        110        120 
GSYGSLLRFN GVERLIPVGD NTVVGISGDI SDMQHIERLL KDLVTENAYD NPLADAEEAL 

       130        140        150        160        170        180 
EPSYIFEYLA TVMYQRRSKM NPLWNAIIVA GVQSNGDQFL RYVNLLGVTY SSPTLATGFG 

       190        200        210        220        230        240 
AHMANPLLRK VVDRESDIPK TTVQVAEEAI VNAMRVLYYR DARSSRNFSL AIIDKNTGLT 

       250        260 
FKKNLQVENM KWDFAKDIKG YGTQKI 

« Hide

References

« Hide 'large scale' references
[1]"The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity. Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis."
Hilt W., Enenkel C., Gruhler A., Singer T., Wolf D.H.
J. Biol. Chem. 268:3479-3486(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[2]"Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae."
Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.
Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.
Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"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.
[7]"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].
[8]"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].
[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 34-266 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING.
[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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
[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 COMPLEX WITH THE 20S PROTEASOME.
[12]"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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
[13]"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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
[14]"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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
[15]"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 34-266 IN COMPLEX WITH THE PROTEASOME.
[16]"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
X68663 Genomic DNA. Translation: CAA48629.1.
D50617 Genomic DNA. Translation: BAA09289.1.
AY692947 Genomic DNA. Translation: AAT92966.1.
BK006940 Genomic DNA. Translation: DAA12493.1.
PIRA46610.
RefSeqNP_116708.1. NM_001180015.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20N/b34-265[»]
1G0UX-ray2.401/M1-266[»]
1G65X-ray2.251/M34-266[»]
1JD2X-ray3.00M/T34-266[»]
1RYPX-ray1.902/N34-266[»]
1VSYX-ray3.002/N34-266[»]
1Z7QX-ray3.22N/b34-266[»]
2F16X-ray2.801/M34-266[»]
2FAKX-ray2.801/M34-266[»]
2GPLX-ray2.811/M34-266[»]
2ZCYX-ray2.900/M1-266[»]
3BDMX-ray2.700/M1-266[»]
3D29X-ray2.601/M34-266[»]
3DY3X-ray2.811/M34-266[»]
3DY4X-ray2.801/M34-266[»]
3E47X-ray3.001/M34-266[»]
3GPJX-ray2.701/M34-266[»]
3GPTX-ray2.411/M34-266[»]
3GPWX-ray2.501/M34-266[»]
3HYEX-ray2.501/M34-266[»]
3L5QX-ray3.004/R34-266[»]
3MG0X-ray2.681/M34-266[»]
3MG4X-ray3.111/M34-266[»]
3MG6X-ray2.601/M1-266[»]
3MG7X-ray2.781/M1-266[»]
3MG8X-ray2.591/M1-266[»]
3NZJX-ray2.401/M1-266[»]
3NZWX-ray2.501/M1-266[»]
3NZXX-ray2.701/M1-266[»]
3OEUX-ray2.601/M34-266[»]
3OEVX-ray2.851/M34-266[»]
3OKJX-ray2.701/M34-266[»]
3SDIX-ray2.651/M34-253[»]
3SDKX-ray2.701/M34-266[»]
3SHJX-ray2.801/M34-266[»]
3TDDX-ray2.701/M34-266[»]
3UN4X-ray3.40M/a34-266[»]
3UN8X-ray2.70M/a34-266[»]
4CR2electron microscopy7.7071-266[»]
4CR3electron microscopy9.3071-266[»]
4CR4electron microscopy8.8071-266[»]
4EU2X-ray2.512/N34-266[»]
4FZCX-ray2.80M/a34-266[»]
4FZGX-ray3.00M/a34-266[»]
4G4SX-ray2.49N34-266[»]
4GK7X-ray2.80M/a34-266[»]
4HNPX-ray2.80M/a34-266[»]
4HRCX-ray2.80M/a34-266[»]
4HRDX-ray2.80M/a34-266[»]
4INRX-ray2.70M/a34-266[»]
4INTX-ray2.90M/a34-266[»]
4INUX-ray3.10M/a34-266[»]
4J70X-ray2.80M/a34-266[»]
4JSQX-ray2.80M/a34-266[»]
4JSUX-ray2.90M/a34-266[»]
4JT0X-ray3.10M/a34-266[»]
4LQIX-ray2.70M/a34-266[»]
4NNNX-ray2.50M/a21-266[»]
4NNWX-ray2.60M/a21-266[»]
4NO1X-ray2.50M/a21-266[»]
4NO6X-ray3.00M/a21-266[»]
4NO8X-ray2.70M/a21-266[»]
4NO9X-ray2.90M/a21-266[»]
ProteinModelPortalP30657.
SMRP30657. Positions 34-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31208. 74 interactions.
DIPDIP-2807N.
IntActP30657. 20 interactions.
MINTMINT-592513.
STRING4932.YFR050C.

Protein family/group databases

MEROPST01.987.

Proteomic databases

MaxQBP30657.
PaxDbP30657.
PeptideAtlasP30657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFR050C; YFR050C; YFR050C.
GeneID850611.
KEGGsce:YFR050C.

Organism-specific databases

CYGDYFR050c.
SGDS000001946. PRE4.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00390000000698.
HOGENOMHOG000181719.
KOK02736.
OMAYHASTIA.
OrthoDBEOG73BVQ8.

Enzyme and pathway databases

BioCycYEAST:G3O-30496-MONOMER.

Gene expression databases

GenevestigatorP30657.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30657.
NextBio966499.
PROP30657.

Entry information

Entry namePSB7_YEAST
AccessionPrimary (citable) accession number: P30657
Secondary accession number(s): D6VTT3, E9P8Z8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 151 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 VI

Yeast (Saccharomyces cerevisiae) chromosome VI: 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