CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009437
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 26S protease regulatory subunit 8 
Protein Synonyms/Alias
 26S proteasome AAA-ATPase subunit RPT6; Proteasome 26S subunit ATPase 5; Proteasome subunit p45; Thyroid hormone receptor-interacting protein 1; TRIP1; p45/SUG 
Gene Name
 PSMC5 
Gene Synonyms/Alias
 SUG1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15QMELEEGKAGSGLRQubiquitination[1, 2, 3, 4]
27LRQYYLSKIEELQLIubiquitination[5]
38LQLIVNDKSQNLRRLubiquitination[4, 6]
55QRNELNAKVRLLREEubiquitination[4, 6]
88DKKKVLVKVHPEGKFubiquitination[2, 4]
94VKVHPEGKFVVDVDKubiquitination[1, 2, 3, 4, 5, 6, 7]
101KFVVDVDKNIDINDVubiquitination[3, 4]
125NDSYTLHKILPNKVDubiquitination[2, 4, 5, 6, 7]
130LHKILPNKVDPLVSLubiquitination[2, 4, 5, 6]
142VSLMMVEKVPDSTYEubiquitination[4, 6]
156EMIGGLDKQIKEIKEubiquitination[4, 5, 6]
162DKQIKEIKEVIELPVubiquitination[4, 6]
170EVIELPVKHPELFEAubiquitination[4, 5, 6]
184ALGIAQPKGVLLYGPubiquitination[4, 6]
196YGPPGTGKTLLARAVubiquitination[2, 4, 6, 7]
222SGSELVQKFIGEGARacetylation[8]
222SGSELVQKFIGEGARubiquitination[2, 3, 4, 5, 6, 7, 9]
287LDGFEATKNIKVIMAubiquitination[3, 4, 5, 6, 10]
290FEATKNIKVIMATNRubiquitination[4, 11]
314RPGRIDRKIEFPPPNubiquitination[6]
330EARLDILKIHSRKMNubiquitination[4, 5, 6]
346TRGINLRKIAELMPGubiquitination[4, 11]
360GASGAEVKGVCTEAGubiquitination[4, 10]
389DFEMAVAKVMQKDSEubiquitination[5, 6]
397VMQKDSEKNMSIKKLubiquitination[4, 6, 11]
402SEKNMSIKKLWK***ubiquitination[7, 11]
403EKNMSIKKLWK****ubiquitination[7, 11]
Reference
 [1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [11] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
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. 
Sequence Annotation
 NP_BIND 190 197 ATP (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 222 222 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; Nucleus; Polymorphism; Proteasome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 406 AA 
Protein Sequence
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR 60
EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS 120
YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI 180
AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE 240
HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI 300
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK 360
GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK 406 
Gene Ontology
 GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031595; C:nuclear proteasome complex; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; ISS:UniProtKB.
 GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
 GO:0006915; P:apoptotic process; TAS:Reactome.
 GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0016071; P:mRNA metabolic process; TAS:Reactome.
 GO:0043069; P:negative regulation of programmed cell death; NAS:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0000209; P:protein polyubiquitination; TAS:Reactome.
 GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
 GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0016032; P:viral reproduction; TAS:Reactome. 
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