CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008699
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 26S protease subunit RPT4 
Protein Synonyms/Alias
 26S protease subunit SUG2; Proteasomal cap subunit 
Gene Name
 RPT4 
Gene Synonyms/Alias
 CRL13; PCS1; SUG2; YOR259C 
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
75RRYDDQLKQRRQNIRubiquitination[1]
362AGRLEIFKIHTAKVKacetylation[2]
427RKVAEVKKLEGTIEYubiquitination[3]
436EGTIEYQKL******ubiquitination[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] 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]
 [3] 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 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). 
Sequence Annotation
 NP_BIND 222 229 ATP (Potential).
 MOD_RES 2 2 N-acetylserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; Nucleotide-binding; Proteasome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 437 AA 
Protein Sequence
MSEEQDPLLA GLGETSGDNH TQQSHEQQPE QPQETEEHHE EEPSRVDPEQ EAHNKALNQF 60
KRKLLEHRRY DDQLKQRRQN IRDLEKLYDK TENDIKALQS IGQLIGEVMK ELSEEKYIVK 120
ASSGPRYIVG VRNSVDRSKL KKGVRVTLDI TTLTIMRILP RETDPLVYNM TSFEQGEITF 180
DGIGGLTEQI RELREVIELP LKNPEIFQRV GIKPPKGVLL YGPPGTGKTL LAKAVAATIG 240
ANFIFSPASG IVDKYIGESA RIIREMFAYA KEHEPCIIFM DEVDAIGGRR FSEGTSADRE 300
IQRTLMELLT QMDGFDNLGQ TKIIMATNRP DTLDPALLRP GRLDRKVEIP LPNEAGRLEI 360
FKIHTAKVKK TGEFDFEAAV KMSDGFNGAD IRNCATEAGF FAIRDDRDHI NPDDLMKAVR 420
KVAEVKKLEG TIEYQKL 437 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; ISS:SGD.
 GO:0019904; F:protein domain specific binding; IDA:SGD.
 GO:0030433; P:ER-associated protein catabolic process; IMP:SGD.
 GO:0006289; P:nucleotide-excision repair; IGI:SGD.
 GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IMP:SGD.
 GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
 GO:0070682; P:proteasome regulatory particle assembly; IMP:SGD. 
Interpro
 IPR005937; 26S_Psome_P45.
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR003960; ATPase_AAA_CS.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00004; AAA 
SMART
 SM00382; AAA 
PROSITE
 PS00674; AAA 
PRINTS