CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005206
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proteasome subunit alpha type-3 
Protein Synonyms/Alias
 Macropain subunit Y13; Multicatalytic endopeptidase complex subunit Y13; Proteasome component Y13; Proteinase YSCE subunit 13 
Gene Name
 PRE9 
Gene Synonyms/Alias
 PRS5; YGR135W 
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
51IVLAAERKVTSTLLEubiquitination[1]
65EQDTSTEKLYKLNDKubiquitination[1]
100IHAQNYLKTYNEDIPubiquitination[1, 2]
199LALKTLSKTTDSSALubiquitination[1, 2, 3, 4, 5, 6]
231EVYQKIFKPQEIKDIubiquitination[1, 2]
236IFKPQEIKDILVKTGubiquitination[1, 2]
246LVKTGITKKDEDEEAubiquitination[1]
247VKTGITKKDEDEEADubiquitination[1]
Reference
 [1] 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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] 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]
 [3] A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.
 Hitchcock AL, Auld K, Gygi SP, Silver PA.
 Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12735-40. [PMID: 14557538]
 [4] A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking.
 Tagwerker C, Flick K, Cui M, Guerrero C, Dou Y, Auer B, Baldi P, Huang L, Kaiser P.
 Mol Cell Proteomics. 2006 Apr;5(4):737-48. [PMID: 16432255]
 [5] Computational identification of ubiquitylation sites from protein sequences.
 Tung CW, Ho SY.
 BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
 [6] 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
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. 
Sequence Annotation
 CROSSLNK 199 199 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Isopeptide bond; Nucleus; Protease; Proteasome; Reference proteome; Threonine protease; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 258 AA 
Protein Sequence
MGSRRYDSRT TIFSPEGRLY QVEYALESIS HAGTAIGIMA SDGIVLAAER KVTSTLLEQD 60
TSTEKLYKLN DKIAVAVAGL TADAEILINT ARIHAQNYLK TYNEDIPVEI LVRRLSDIKQ 120
GYTQHGGLRP FGVSFIYAGY DDRYGYQLYT SNPSGNYTGW KAISVGANTS AAQTLLQMDY 180
KDDMKVDDAI ELALKTLSKT TDSSALTYDR LEFATIRKGA NDGEVYQKIF KPQEIKDILV 240
KTGITKKDED EEADEDMK 258 
Gene Ontology
 GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IC:SGD.
 GO:0005634; C:nucleus; IC:SGD.
 GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:SGD.
 GO:0034515; C:proteasome storage granule; IDA: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.
 GO:0080129; P:proteasome core complex assembly; IMP:SGD. 
Interpro
 IPR000426; Proteasome_asu_N.
 IPR016050; Proteasome_bsu_CS.
 IPR023332; Proteasome_suA-type.
 IPR001353; Proteasome_sua/b. 
Pfam
 PF00227; Proteasome
 PF10584; Proteasome_A_N 
SMART
 SM00948; Proteasome_A_N 
PROSITE
 PS00388; PROTEASOME_A_1
 PS51475; PROTEASOME_A_2 
PRINTS