CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005442
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell division control protein 48 
Protein Synonyms/Alias
  
Gene Name
 CDC48 
Gene Synonyms/Alias
 YDL126C 
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
21VDPREEDKTATAILRubiquitination[1]
119IHPCPDIKYATRISVacetylation[2]
119IHPCPDIKYATRISVubiquitination[1]
158EAYRPVRKGDHFVVRubiquitination[1]
221DDIGGCRKQMAQIREubiquitination[1]
241LRHPQLFKAIGIKPPubiquitination[3]
246LFKAIGIKPPRGVLMubiquitination[1]
261YGPPGTGKTLMARAVubiquitination[1]
298ESESNLRKAFEEAEKubiquitination[1]
305KAFEEAEKNAPAIIFubiquitination[3]
322EIDSIAPKRDKTNGEubiquitination[3]
346LTLMDGMKARSNVVVubiquitination[3]
522KFGLSPSKGVLFYGPubiquitination[1, 3]
534YGPPGTGKTLLAKAVubiquitination[1]
539TGKTLLAKAVATEVSubiquitination[1, 3]
594DELDSIAKARGGSLGubiquitination[1, 3, 4, 5, 6]
624EMDGMNAKKNVFVIGubiquitination[1]
673ILNAQLRKTPLEPGLubiquitination[1, 4, 5, 6]
740EMTDEGAKAEQEPEVubiquitination[1]
755DPVPYITKEHFAEAMacetylation[2]
763EHFAEAMKTAKRSVSacetylation[2]
763EHFAEAMKTAKRSVSubiquitination[1]
785EAYSQQMKASRGQFSubiquitination[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]
 [4] A proteomics approach to understanding protein ubiquitination.
 Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
 Nat Biotechnol. 2003 Aug;21(8):921-6. [PMID: 12872131]
 [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
 Involved in spindle disassembly, degradation of ubiquitinated proteins and protein export from the endoplasmic reticulum to the cytoplasm. Acts as a chaperone that collects ubiquitinated substrates. Has a role in the endoplasmic reticulum- associated degradation (ERAD) pathway. Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1. Has an additional role in the turnover of OLE1 where it targets ubiquitinated OLE1 and other proteins to the ERAD. 
Sequence Annotation
 NP_BIND 255 262 ATP (Potential).
 NP_BIND 528 535 ATP (Potential).
 MOD_RES 683 683 Phosphothreonine.
 CROSSLNK 594 594 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 673 673 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 ATP-binding; Cell cycle; Complete proteome; Endoplasmic reticulum; Isopeptide bond; Microsome; Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 835 AA 
Protein Sequence
MGEEHKPLLD ASGVDPREED KTATAILRRK KKDNMLLVDD AINDDNSVIA INSNTMDKLE 60
LFRGDTVLVK GKKRKDTVLI VLIDDELEDG ACRINRVVRN NLRIRLGDLV TIHPCPDIKY 120
ATRISVLPIA DTIEGITGNL FDVFLKPYFV EAYRPVRKGD HFVVRGGMRQ VEFKVVDVEP 180
EEYAVVAQDT IIHWEGEPIN REDEENNMNE VGYDDIGGCR KQMAQIREMV ELPLRHPQLF 240
KAIGIKPPRG VLMYGPPGTG KTLMARAVAN ETGAFFFLIN GPEVMSKMAG ESESNLRKAF 300
EEAEKNAPAI IFIDEIDSIA PKRDKTNGEV ERRVVSQLLT LMDGMKARSN VVVIAATNRP 360
NSIDPALRRF GRFDREVDIG IPDATGRLEV LRIHTKNMKL ADDVDLEALA AETHGYVGAD 420
IASLCSEAAM QQIREKMDLI DLDEDEIDAE VLDSLGVTMD NFRFALGNSN PSALRETVVE 480
SVNVTWDDVG GLDEIKEELK ETVEYPVLHP DQYTKFGLSP SKGVLFYGPP GTGKTLLAKA 540
VATEVSANFI SVKGPELLSM WYGESESNIR DIFDKARAAA PTVVFLDELD SIAKARGGSL 600
GDAGGASDRV VNQLLTEMDG MNAKKNVFVI GATNRPDQID PAILRPGRLD QLIYVPLPDE 660
NARLSILNAQ LRKTPLEPGL ELTAIAKATQ GFSGADLLYI VQRAAKYAIK DSIEAHRQHE 720
AEKEVKVEGE DVEMTDEGAK AEQEPEVDPV PYITKEHFAE AMKTAKRSVS DAELRRYEAY 780
SQQMKASRGQ FSNFNFNDAP LGTTATDNAN SNNSAPSGAG AAFGSNAEED DDLYS 835 
Gene Ontology
 GO:0034098; C:Cdc48p-Npl4p-Ufd1p AAA ATPase complex; IDA:SGD.
 GO:0036266; C:Cdc48p-Npl4p-Vms1p AAA ATPase complex; IDA:SGD.
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0000837; C:Doa10p ubiquitin ligase complex; IDA:SGD.
 GO:0043332; C:mating projection tip; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IDA:SGD.
 GO:0043130; F:ubiquitin binding; IDA:SGD.
 GO:0071629; P:cytoplasm-associated proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD.
 GO:0016320; P:endoplasmic reticulum membrane fusion; IMP:SGD.
 GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:SGD.
 GO:0016236; P:macroautophagy; IMP:SGD.
 GO:0072671; P:mitochondria-associated protein catabolic process; IMP:SGD.
 GO:0051228; P:mitotic spindle disassembly; IMP:SGD.
 GO:0071630; P:nucleus-associated proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD.
 GO:0034727; P:piecemeal microautophagy of nucleus; IMP:SGD.
 GO:1900182; P:positive regulation of protein localization to nucleus; IMP:SGD.
 GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:SGD.
 GO:0034517; P:ribophagy; IMP:SGD.
 GO:0031134; P:sister chromatid biorientation; IMP:SGD. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR009010; Asp_de-COase-like_dom.
 IPR005938; ATPase_AAA_CDC48.
 IPR003959; ATPase_AAA_core.
 IPR003960; ATPase_AAA_CS.
 IPR004201; Cdc48_dom2.
 IPR003338; CDC4_N-term_subdom.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00004; AAA
 PF02933; CDC48_2
 PF02359; CDC48_N 
SMART
 SM00382; AAA
 SM01072; CDC48_2
 SM01073; CDC48_N 
PROSITE
 PS00674; AAA 
PRINTS