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P22141 (PSB4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 142. 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
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 beta type-4
EC=3.4.25.1
Alternative name(s):
Macropain subunit C11
Multicatalytic endopeptidase complex subunit C11
Proteasome component C11
Proteinase YSCE subunit 11
Gene names
Name:PRE1
Ordered Locus Names:YER012W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length198 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. 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.

Sequence similarities

Belongs to the peptidase T1B family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRE10P212423EBI-13988,EBI-13963
PRE2P306563EBI-13988,EBI-14001
PRE6P403033EBI-13988,EBI-13980

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Proteasome subunit beta type-4
PRO_0000148055

Amino acid modifications

Modified residue761Phosphoserine Ref.6
Modified residue821Phosphoserine Ref.6

Experimental info

Sequence conflict1831I → T Ref.1
Sequence conflict1881G → R Ref.1

Secondary structure

1 ..................................... 198
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22141 [UniParc].

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

FASTA19822,517
        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

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [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. 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.
[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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-82, MASS SPECTROMETRY.
[7]"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 COMPLEX WITH THE 20S PROTEASOME.
[8]"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 AND A 11S REGULATORY COMPLEX.
[9]"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.
[10]"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 COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
[11]"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 COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
[12]"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 COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X56812 Genomic DNA. Translation: CAA40149.1.
U18778 Genomic DNA. Translation: AAB64545.1.
AY557807 Genomic DNA. Translation: AAS56133.1.
BK006939 Genomic DNA. Translation: DAA07663.1.
PIRS50470.
RefSeqNP_010928.1. NM_001178903.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20K/Y1-198[»]
1G0UX-ray2.40J/X1-198[»]
1G65X-ray2.25J/X1-198[»]
1JD2X-ray3.00J/Q1-198[»]
1RYPX-ray1.90K/Y1-198[»]
1VSYX-ray3.00K/Y1-198[»]
1Z7QX-ray3.22K/Y1-198[»]
2F16X-ray2.80J/X1-198[»]
2FAKX-ray2.80J/X1-198[»]
2GPLX-ray2.81J/X1-198[»]
2ZCYX-ray2.90J/X1-198[»]
3BDMX-ray2.70J/X1-198[»]
3D29X-ray2.60J/X1-198[»]
3DY3X-ray2.81J/X1-198[»]
3DY4X-ray2.80J/X1-198[»]
3E47X-ray3.00J/X1-198[»]
3GPJX-ray2.70J/X1-198[»]
3GPTX-ray2.41J/X1-198[»]
3GPWX-ray2.50J/X1-198[»]
3HYEX-ray2.50J/X1-198[»]
3L5QX-ray3.001/O1-198[»]
3MG0X-ray2.68J/X1-198[»]
3MG4X-ray3.11J/X1-198[»]
3MG6X-ray2.60J/X1-198[»]
3MG7X-ray2.78J/X1-198[»]
3MG8X-ray2.59J/X1-198[»]
3NZJX-ray2.40J/X1-198[»]
3NZWX-ray2.50J/X1-198[»]
3NZXX-ray2.70J/X1-198[»]
3OEUX-ray2.60J/X1-198[»]
3OEVX-ray2.85J/X1-198[»]
3OKJX-ray2.70J/X1-198[»]
3SDIX-ray2.65J/X1-198[»]
3SDKX-ray2.70J/X1-198[»]
3SHJX-ray2.80J/X1-198[»]
3TDDX-ray2.70J/X1-198[»]
3UN4X-ray3.40J/X1-198[»]
3UN8X-ray2.70J/X1-198[»]
4B4Telectron microscopy7.4041-198[»]
4FZCX-ray2.80J/X1-198[»]
4FZGX-ray3.00J/X1-198[»]
4G4SX-ray2.49K1-198[»]
4GK7X-ray2.80J/X1-198[»]
4INRX-ray2.70J/X1-198[»]
4INTX-ray2.90J/X1-198[»]
4INUX-ray3.10J/X1-198[»]
ProteinModelPortalP22141.
SMRP22141. Positions 1-198.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2808N.
IntActP22141. 25 interactions.
MINTMINT-592869.
STRING4932.YER012W.

Protein family/group databases

MEROPST01.984.

Proteomic databases

PaxDbP22141.
PeptideAtlasP22141.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER012W; YER012W; YER012W.
GeneID856731.
KEGGsce:YER012W.

Organism-specific databases

CYGDYER012w.
SGDS000000814. PRE1.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00640000091536.
HOGENOMHOG000188743.
KOK02734.
OMAMPIDFKG.
OrthoDBEOG4TB7MP.

Gene expression databases

GenevestigatorP22141.
GermOnlineYER012W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PROSITEPS00854. PROTEASOME_B_1. 1 hit.
PS51476. PROTEASOME_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP22141.
ChEMBLCHEMBL4206.
EvolutionaryTraceP22141.
NextBio982843.

Entry information

Entry namePSB4_YEAST
AccessionPrimary (citable) accession number: P22141
Secondary accession number(s): D3DLQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1995
Last modified: April 3, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: 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

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents