UniProt Accession

 PSB4_YEAST; P22141; D3DLQ9 

Genbank Protein ID

 X56812; U18778; AY557807; BK006939 

Genbank Nucleotide ID

 CAA40149.1; AAB64545.1; AAS56133.1; DAA07663.1 

Protein Name

 Proteasome subunit beta type-4 

Protein Synonyms/Alias

 Macropain subunit C11; Multicatalytic endopeptidase complex subunit C11; Proteasome component C11; Proteinase YSCE subunit 11 

Gene Name

 PRE1 

Gene Synonyms/Alias

 YER012W 

Created Date

 July 27, 2013 

Organism

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

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
19	SVILASSKAVTRGIS	ubiquitination	[1, 2]
29	TRGISVLKDSDDKTR	acetylation	[3]
29	TRGISVLKDSDDKTR	ubiquitination	[1, 2, 4]
109	VLIGGYDKKKNKPEL	acetylation	[3]
170	LCVQELEKRMPMDFK	ubiquitination	[2]
177	KRMPMDFKGVIVKIV	ubiquitination	[2]

Reference

 [1] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [4] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 

Functional Description

 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. 

Sequence Annotation

 MOD_RES 76 76 Phosphoserine.  

Keyword

 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus; Phosphoprotein; Protease; Proteasome; Reference proteome; Threonine protease. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 198 AA 

Protein Sequence

Gene Ontology

 GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:SGD.
 GO:0034515; C:proteasome storage granule; IC:SGD.
 GO:0061133; F:endopeptidase activator activity; IMP:SGD.
 GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD.
 GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:SGD. 

Interpro

 IPR016050; Proteasome_bsu_CS.
 IPR001353; Proteasome_sua/b.
 IPR023333; Proteasome_suB-type. 

Pfam

 PF00227; Proteasome 

SMART

  

PROSITE

 PS00854; PROTEASOME_B_1
 PS51476; PROTEASOME_B_2 

PRINTS