CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006292
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 26S protease regulatory subunit 6B homolog 
Protein Synonyms/Alias
 Protein YNT1; Tat-binding homolog 2 
Gene Name
 RPT3 
Gene Synonyms/Alias
 YNT1; YTA2; YDR394W; D9509.14 
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
224TGKTMLVKAVANSTKubiquitination[1]
231KAVANSTKAAFIRVNubiquitination[1]
245NGSEFVHKYLGEGPRacetylation[2]
245NGSEFVHKYLGEGPRubiquitination[1]
280EVDSIATKRFDAQTGubiquitination[3]
337RPGRLDRKIEFPSLRacetylation[2]
337RPGRLDRKIEFPSLRubiquitination[1]
416EAYATQVKTDNTVDKubiquitination[1]
423KTDNTVDKFDFYK**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 213 220 ATP (Potential).
 MOD_RES 1 1 N-acetylmethionine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Nucleus; Proteasome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 428 AA 
Protein Sequence
MEELGIVTPV EKAVEEKPAV KSYASLLAQL NGTVNNNSAL SNVNSDIYFK LKKLEKEYEL 60
LTLQEDYIKD EQRHLKRELK RAQEEVKRIQ SVPLVIGQFL EPIDQNTGIV SSTTGMSYVV 120
RILSTLDREL LKPSMSVALH RHSNALVDIL PPDSDSSISV MGENEKPDVT YADVGGLDMQ 180
KQEIREAVEL PLVQADLYEQ IGIDPPRGVL LYGPPGTGKT MLVKAVANST KAAFIRVNGS 240
EFVHKYLGEG PRMVRDVFRL ARENAPSIIF IDEVDSIATK RFDAQTGSDR EVQRILIELL 300
TQMDGFDQST NVKVIMATNR ADTLDPALLR PGRLDRKIEF PSLRDRRERR LIFGTIASKM 360
SLAPEADLDS LIIRNDSLSG AVIAAIMQEA GLRAVRKNRY VILQSDLEEA YATQVKTDNT 420
VDKFDFYK 428 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 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:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IMP:SGD.
 GO:0070682; P:proteasome regulatory particle assembly; IMP:SGD.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; 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