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UniProtKB/Swiss-Prot entry P25694


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDC48_YEAST
Primary accession number P25694
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on October 1, 1996 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 83)
Name and origin of the protein
Protein name Cell division control protein 48
Synonyms None
Gene name
Name: CDC48
OrderedLocusNames: YDL126C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1083/jcb.114.3.443; PubMed=1860879 [NCBI, ExPASy, EBI, Israel, Japan]
Froehlich K.-U., Fries H.W., Ruediger M., Erdmann R., Botstein D., Mecke D.;
"Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression.";
J. Cell Biol. 114:443-453(1991).
[2]
SEQUENCE REVISION.
Froehlich K.-U.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
FUNCTION, INTERACTION WITH NPL4, AND SUBCELLULAR LOCATION.
DOI=10.1016/S0092-8674(01)00595-5; PubMed=11733065 [NCBI, ExPASy, EBI, Israel, Japan]
Rape M., Hoppe T., Gorr I., Kalocay M., Richly H., Jentsch S.;
"Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone.";
Cell 107:667-677(2001).
[5]
INTERACTION WITH NPL4.
PubMed=11598205 [NCBI, ExPASy, EBI, Israel, Japan]
Hitchcock A.L., Krebber H., Frietze S., Lin A., Latterich M., Silver P.A.;
"The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation.";
Mol. Biol. Cell 12:3226-3241(2001).
[6]
FUNCTION.
DOI=10.1038/ncb746; PubMed=11813000 [NCBI, ExPASy, EBI, Israel, Japan]
Jarosch E., Taxis C., Volkwein C., Bordallo J., Finley D., Wolf D.H., Sommer T.;
"Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.";
Nat. Cell Biol. 4:134-139(2002).
[7]
FUNCTION.
DOI=10.1038/414652a; PubMed=11740563 [NCBI, ExPASy, EBI, Israel, Japan]
Ye Y., Meyer H.H., Rapoport T.A.;
"The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.";
Nature 414:652-656(2001).
[8]
FUNCTION.
DOI=10.1093/emboj/21.4.615; PubMed=11847109 [NCBI, ExPASy, EBI, Israel, Japan]
Braun S., Matuschewski K., Rape M., Thoms S., Jentsch S.;
"Role of the ubiquitin-selective CDC48(UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates.";
EMBO J. 21:615-621(2002).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-683, UBIQUITINATION AT LYS-594 AND LYS-673, AND MASS SPECTROMETRY.
DOI=10.1038/nbt849; PubMed=12872131 [NCBI, ExPASy, EBI, Israel, Japan]
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.;
"A proteomics approach to understanding protein ubiquitination.";
Nat. Biotechnol. 21:921-926(2003).
[11]
INTERACTION WITH UBX PROTEINS.
DOI=10.1038/sj.embor.7400203; PubMed=15258615 [NCBI, ExPASy, EBI, Israel, Japan]
Schuberth C., Richly H., Rumpf S., Buchberger A.;
"Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation.";
EMBO Rep. 5:818-824(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[13]
INTERACTION WITH OTU1; UFD2 AND DOA1.
DOI=10.1016/j.molcel.2005.12.014; PubMed=16427015 [NCBI, ExPASy, EBI, Israel, Japan]
Rumpf S., Jentsch S.;
"Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone.";
Mol. Cell 21:261-269(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-770, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; THR-735 AND SER-770, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292; SER-318; SER-423; SER-472; SER-519; SER-599; THR-735 AND SER-770, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X56956; CAA40276.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74174; CAA98694.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S67669; S67669.
RefSeq NP_010157.1; -.
3D structure databases
HSSP Q01853; 1E32. [HSSP ENTRY / PDB]
SMR P25694; 28-466.
ModBase P25694.
Protein-protein interaction databases
DIP DIP:2704N; -.
IntAct P25694; -.
Organism-specific databases
CYGD YDL126c; -.
SGD S000002284; CDC48.
Yeast-GFP YDL126C.
Gene expression databases
ArrayExpress P25694; -.
GermOnline YDL126C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0034098; Cellular component: Cdc48p-Npl4p-Ufd1p AAA ATPase complex (inferred from direct assay from SGD).
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0000837; Cellular component: Doa10p ubiquitin ligase complex (inferred from direct assay from SGD).
GO:0005792; Cellular component: microsome (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0016887; Molecular function: ATPase activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006915; Biological process: apoptosis (traceable author statement from SGD).
GO:0030433; Biological process: ER-associated protein catabolic process (inferred from mutant phenotype from SGD).
GO:0000278; Biological process: mitotic cell cycle (inferred from mutant phenotype from SGD).
GO:0015031; Biological process: protein transport (inferred from direct assay from SGD).
GO:0006906; Biological process: vesicle fusion (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR003593; AAA+_ATPase_core.
IPR003959; AAA_ATPase_core.
IPR003960; AAA_ATPase_CS.
IPR005938; AAA_CDC48.
IPR009010; Asp_de-COase-like_fold.
IPR003338; ATPaseVAT_N.
Graphical view of domain structure.
Gene3D G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
Pfam PF00004; AAA; 2.
PF02359; CDC48_N; 1.
Pfam graphical view of domain structure.
SMART SM00382; AAA; 2.
SMART graphical view of domain structure.
TIGRFAMs TIGR01243; CDC48; 1.
PROSITE PS00674; AAA; 2.
BLOCKS P25694.
Proteomic databases
PeptideAtlas P25694; -.
Genome annotation databases
Ensembl YDL126C; Saccharomyces cerevisiae. [Contig view]
GeneID 851431; -.
GenomeReviews Z71256_GR; YDL126C.
KEGG sce:YDL126C; -.
NMPDR fig|4932.3.peg.894; -.
Phylogenomic databases
HOGENOM P25694; -.
Other
LinkHub P25694; -.
ProtoNet P25694.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell cycle; Complete proteome; Endoplasmic reticulum; Microsome; Nucleotide-binding; Phosphoprotein; Protein transport; Repeat; Transport; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   835  835     Cell division control protein 48. PRO_0000084587
NP_BIND   255   262  8     ATP (Potential). 
NP_BIND   528   535  8     ATP (Potential). 
MOD_RES   292   292        Phosphoserine. 
MOD_RES   318   318        Phosphoserine. 
MOD_RES   423   423        Phosphoserine. 
MOD_RES   472   472        Phosphoserine. 
MOD_RES   519   519        Phosphoserine. 
MOD_RES   599   599        Phosphoserine. 
MOD_RES   683   683        Phosphothreonine. 
MOD_RES   735   735        Phosphothreonine. 
MOD_RES   770   770        Phosphoserine. 
CROSSLNK   594   594        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   673   673        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
Sequence information
Length: 835 AA [This is the length of the unprocessed precursor] Molecular weight: 91996 Da [This is the MW of the unprocessed precursor] CRC64: 02ADDB9A227614D8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGEEHKPLLD ASGVDPREED KTATAILRRK KKDNMLLVDD AINDDNSVIA INSNTMDKLE 

        70         80         90        100        110        120 
LFRGDTVLVK GKKRKDTVLI VLIDDELEDG ACRINRVVRN NLRIRLGDLV TIHPCPDIKY 

       130        140        150        160        170        180 
ATRISVLPIA DTIEGITGNL FDVFLKPYFV EAYRPVRKGD HFVVRGGMRQ VEFKVVDVEP 

       190        200        210        220        230        240 
EEYAVVAQDT IIHWEGEPIN REDEENNMNE VGYDDIGGCR KQMAQIREMV ELPLRHPQLF 

       250        260        270        280        290        300 
KAIGIKPPRG VLMYGPPGTG KTLMARAVAN ETGAFFFLIN GPEVMSKMAG ESESNLRKAF 

       310        320        330        340        350        360 
EEAEKNAPAI IFIDEIDSIA PKRDKTNGEV ERRVVSQLLT LMDGMKARSN VVVIAATNRP 

       370        380        390        400        410        420 
NSIDPALRRF GRFDREVDIG IPDATGRLEV LRIHTKNMKL ADDVDLEALA AETHGYVGAD 

       430        440        450        460        470        480 
IASLCSEAAM QQIREKMDLI DLDEDEIDAE VLDSLGVTMD NFRFALGNSN PSALRETVVE 

       490        500        510        520        530        540 
SVNVTWDDVG GLDEIKEELK ETVEYPVLHP DQYTKFGLSP SKGVLFYGPP GTGKTLLAKA 

       550        560        570        580        590        600 
VATEVSANFI SVKGPELLSM WYGESESNIR DIFDKARAAA PTVVFLDELD SIAKARGGSL 

       610        620        630        640        650        660 
GDAGGASDRV VNQLLTEMDG MNAKKNVFVI GATNRPDQID PAILRPGRLD QLIYVPLPDE 

       670        680        690        700        710        720 
NARLSILNAQ LRKTPLEPGL ELTAIAKATQ GFSGADLLYI VQRAAKYAIK DSIEAHRQHE 

       730        740        750        760        770        780 
AEKEVKVEGE DVEMTDEGAK AEQEPEVDPV PYITKEHFAE AMKTAKRSVS DAELRRYEAY 

       790        800        810        820        830 
SQQMKASRGQ FSNFNFNDAP LGTTATDNAN SNNSAPSGAG AAFGSNAEED DDLYS 

P25694 in FASTA format

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