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Protein

Cell division control protein 48

Gene

CDC48

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (PubMed:11733065, PubMed:11740563, PubMed:11813000, PubMed:11847109, PubMed:21070972, PubMed:21148305). Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. CDC48 may provide the mechanical force that dislodges the polyubiquitinated nascent peptides from the exit channel (PubMed:23178123, PubMed:24261871).8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei358 – 3581ATPBy similarity
Binding sitei394 – 3941ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi257 – 2637ATPBy similarity

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • protein phosphatase type 1 regulator activity Source: SGD
  • ubiquitin binding Source: SGD

GO - Biological processi

  • ATP metabolic process Source: ParkinsonsUK-UCL
  • cytoplasm-associated proteasomal ubiquitin-dependent protein catabolic process Source: SGD
  • endoplasmic reticulum membrane fusion Source: SGD
  • ER-associated misfolded protein catabolic process Source: SGD
  • ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  • macroautophagy Source: SGD
  • mitochondria-associated ubiquitin-dependent protein catabolic process Source: SGD
  • mitotic spindle disassembly Source: SGD
  • negative regulation of telomerase activity Source: SGD
  • nonfunctional rRNA decay Source: SGD
  • nucleus-associated proteasomal ubiquitin-dependent protein catabolic process Source: SGD
  • piecemeal microautophagy of nucleus Source: SGD
  • positive regulation of histone H2B ubiquitination Source: SGD
  • positive regulation of protein localization to nucleus Source: SGD
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
  • retrograde protein transport, ER to cytosol Source: SGD
  • ribophagy Source: SGD
  • ribosome-associated ubiquitin-dependent protein catabolic process Source: SGD
  • SCF complex disassembly in response to cadmium stress Source: SGD
  • sister chromatid biorientation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Protein transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29525-MONOMER.
ReactomeiR-SCE-110320. Translesion Synthesis by POLH.
R-SCE-3371511. HSF1 activation.

Protein family/group databases

TCDBi3.A.16.1.2. the endoplasmic reticular retrotranslocon (er-rt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 481 Publication
Alternative name(s):
Cell division cycle protein 481 Publication
Gene namesi
Name:CDC481 Publication
Ordered Locus Names:YDL126CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL126C.
SGDiS000002284. CDC48.

Subcellular locationi

  • Microsome 1 Publication
  • Endoplasmic reticulum 1 Publication
  • Cytoplasm 1 Publication

  • Note: Bound loosely to components of the microsomal fraction.1 Publication

GO - Cellular componenti

  • Cdc48p-Npl4p-Vms1p AAA ATPase complex Source: SGD
  • cytosol Source: SGD
  • Doa10p ubiquitin ligase complex Source: SGD
  • endoplasmic reticulum membrane Source: SGD
  • Hrd1p ubiquitin ligase ERAD-L complex Source: SGD
  • nucleus Source: SGD
  • RQC complex Source: SGD
  • VCP-NPL4-UFD1 AAA ATPase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 835835Cell division control protein 48PRO_0000084587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei472 – 4721PhosphoserineCombined sources
Modified residuei519 – 5191PhosphoserineCombined sources
Cross-linki594 – 594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki673 – 673Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei735 – 7351PhosphothreonineCombined sources
Modified residuei770 – 7701PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP25694.
PeptideAtlasiP25694.
PRIDEiP25694.

PTM databases

iPTMnetiP25694.

Interactioni

Subunit structurei

Component of the HRD1 complex which contains HRD1, HRD3, USA1, DER1, YOS9, CDC48, NPL4, UFD1 AND UBX2/SEL1. The complex is composed of the core membrane complex, consisting of the E3 ligase HRD1 and its cofactors HRD3, DER1 and USA1, the substrate recruiting factor YOS9, and the heterotrimeric UFD1-NPL4-CDC48/p97 (UNC) ATPase complex recruited by UBX2/SEL1. Interacts with HRD1, HRD3, YOS9, UBX2, DER1, USA1 and UFD1. Interacts with OTU1 and DOA1/UFD3, to prevent multiubiquitination of substrates. Interacts with UFD2, to add further ubiquitin moieties; the interaction with UFD2 is prevented by DOA1/UFD3. Interacts with NPL4 and VMS1. Component of the ribosome quality control complex (RQC), composed of the E3 ubiquitin ligase RKR1/LTN1, RQC1 and RQC2, as well as CDC48 and its ubiquitin-binding cofactors. RQC forms a stable complex with 60S ribosomal subunits (PubMed:23178123, PubMed:23479637).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-4308,EBI-4308
BRE5P537414EBI-4308,EBI-28528
DER1P383075EBI-4308,EBI-5761
DOA1P360375EBI-4308,EBI-6017
HRD1Q081098EBI-4308,EBI-37613
HRD3Q057876EBI-4308,EBI-31647
NPL4P3375511EBI-4308,EBI-12193
SHP1P342239EBI-4308,EBI-17093
SSM4P403184EBI-4308,EBI-18208
UBP3Q014774EBI-4308,EBI-19834
UBX2Q0422815EBI-4308,EBI-27730
UBX3Q122293EBI-4308,EBI-35335
UBX4P547305EBI-4308,EBI-28127
UBX5Q066823EBI-4308,EBI-32041
UBX6P470493EBI-4308,EBI-25866
UBX7P383494EBI-4308,EBI-21157
VMS1Q043115EBI-4308,EBI-784329

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • ubiquitin binding Source: SGD

Protein-protein interaction databases

BioGridi31937. 283 interactions.
DIPiDIP-2704N.
IntActiP25694. 81 interactions.
MINTiMINT-547129.

Structurei

3D structure databases

ProteinModelPortaliP25694.
SMRiP25694. Positions 27-785.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00810000125456.
HOGENOMiHOG000223224.
InParanoidiP25694.
KOiK13525.
OMAiFRFPGGQ.
OrthoDBiEOG79CZ6Z.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR005938. AAA_ATPase_CDC48.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR029067. CDC48_domain_2-like.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
TIGRFAMsiTIGR01243. CDC48. 1 hit.
PROSITEiPS00674. AAA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25694-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEEHKPLLD ASGVDPREED KTATAILRRK KKDNMLLVDD AINDDNSVIA
60 70 80 90 100
INSNTMDKLE LFRGDTVLVK GKKRKDTVLI VLIDDELEDG ACRINRVVRN
110 120 130 140 150
NLRIRLGDLV TIHPCPDIKY ATRISVLPIA DTIEGITGNL FDVFLKPYFV
160 170 180 190 200
EAYRPVRKGD HFVVRGGMRQ VEFKVVDVEP EEYAVVAQDT IIHWEGEPIN
210 220 230 240 250
REDEENNMNE VGYDDIGGCR KQMAQIREMV ELPLRHPQLF KAIGIKPPRG
260 270 280 290 300
VLMYGPPGTG KTLMARAVAN ETGAFFFLIN GPEVMSKMAG ESESNLRKAF
310 320 330 340 350
EEAEKNAPAI IFIDEIDSIA PKRDKTNGEV ERRVVSQLLT LMDGMKARSN
360 370 380 390 400
VVVIAATNRP NSIDPALRRF GRFDREVDIG IPDATGRLEV LRIHTKNMKL
410 420 430 440 450
ADDVDLEALA AETHGYVGAD IASLCSEAAM QQIREKMDLI DLDEDEIDAE
460 470 480 490 500
VLDSLGVTMD NFRFALGNSN PSALRETVVE SVNVTWDDVG GLDEIKEELK
510 520 530 540 550
ETVEYPVLHP DQYTKFGLSP SKGVLFYGPP GTGKTLLAKA VATEVSANFI
560 570 580 590 600
SVKGPELLSM WYGESESNIR DIFDKARAAA PTVVFLDELD SIAKARGGSL
610 620 630 640 650
GDAGGASDRV VNQLLTEMDG MNAKKNVFVI GATNRPDQID PAILRPGRLD
660 670 680 690 700
QLIYVPLPDE NARLSILNAQ LRKTPLEPGL ELTAIAKATQ GFSGADLLYI
710 720 730 740 750
VQRAAKYAIK DSIEAHRQHE AEKEVKVEGE DVEMTDEGAK AEQEPEVDPV
760 770 780 790 800
PYITKEHFAE AMKTAKRSVS DAELRRYEAY SQQMKASRGQ FSNFNFNDAP
810 820 830
LGTTATDNAN SNNSAPSGAG AAFGSNAEED DDLYS
Length:835
Mass (Da):91,996
Last modified:October 1, 1996 - v3
Checksum:i02ADDB9A227614D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56956 Genomic DNA. Translation: CAA40276.1.
Z74174 Genomic DNA. Translation: CAA98694.1.
BK006938 Genomic DNA. Translation: DAA11734.1.
PIRiS67669.
RefSeqiNP_010157.1. NM_001180185.1.

Genome annotation databases

EnsemblFungiiYDL126C; YDL126C; YDL126C.
GeneIDi851431.
KEGGisce:YDL126C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56956 Genomic DNA. Translation: CAA40276.1.
Z74174 Genomic DNA. Translation: CAA98694.1.
BK006938 Genomic DNA. Translation: DAA11734.1.
PIRiS67669.
RefSeqiNP_010157.1. NM_001180185.1.

3D structure databases

ProteinModelPortaliP25694.
SMRiP25694. Positions 27-785.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31937. 283 interactions.
DIPiDIP-2704N.
IntActiP25694. 81 interactions.
MINTiMINT-547129.

Protein family/group databases

TCDBi3.A.16.1.2. the endoplasmic reticular retrotranslocon (er-rt) family.

PTM databases

iPTMnetiP25694.

Proteomic databases

MaxQBiP25694.
PeptideAtlasiP25694.
PRIDEiP25694.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL126C; YDL126C; YDL126C.
GeneIDi851431.
KEGGisce:YDL126C.

Organism-specific databases

EuPathDBiFungiDB:YDL126C.
SGDiS000002284. CDC48.

Phylogenomic databases

GeneTreeiENSGT00810000125456.
HOGENOMiHOG000223224.
InParanoidiP25694.
KOiK13525.
OMAiFRFPGGQ.
OrthoDBiEOG79CZ6Z.

Enzyme and pathway databases

BioCyciYEAST:G3O-29525-MONOMER.
ReactomeiR-SCE-110320. Translesion Synthesis by POLH.
R-SCE-3371511. HSF1 activation.

Miscellaneous databases

PROiP25694.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR005938. AAA_ATPase_CDC48.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR029067. CDC48_domain_2-like.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
TIGRFAMsiTIGR01243. CDC48. 1 hit.
PROSITEiPS00674. AAA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Froehlich K.-U., Fries H.W., Ruediger M., Erdmann R., Botstein D., Mecke D.
    J. Cell Biol. 114:443-453(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Froehlich K.-U.
    Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    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.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies."
    Moir D., Stewart S.E., Osmond B.C., Botstein D.
    Genetics 100:547-563(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME.
  6. "Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone."
    Rape M., Hoppe T., Gorr I., Kalocay M., Richly H., Jentsch S.
    Cell 107:667-677(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NPL4, SUBCELLULAR LOCATION.
  7. "The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation."
    Hitchcock A.L., Krebber H., Frietze S., Lin A., Latterich M., Silver P.A.
    Mol. Biol. Cell 12:3226-3241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NPL4.
  8. "Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48."
    Jarosch E., Taxis C., Volkwein C., Bordallo J., Finley D., Wolf D.H., Sommer T.
    Nat. Cell Biol. 4:134-139(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol."
    Ye Y., Meyer H.H., Rapoport T.A.
    Nature 414:652-656(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Role of the ubiquitin-selective CDC48(UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates."
    Braun S., Matuschewski K., Rape M., Thoms S., Jentsch S.
    EMBO J. 21:615-621(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-594 AND LYS-673.
    Strain: SUB592.
  13. "Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation."
    Schuberth C., Richly H., Rumpf S., Buchberger A.
    EMBO Rep. 5:818-824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBX PROTEINS.
  14. "Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins."
    Carvalho P., Goder V., Rapoport T.A.
    Cell 126:361-373(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE HRD1 COMPLEX, INTERACTION WITH HRD1; HRD3; YOS9; UBX2; DER1; USA1; NPL4 AND UFD1.
  15. "Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone."
    Rumpf S., Jentsch S.
    Mol. Cell 21:261-269(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OTU1; UFD2 AND DOA1.
  16. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-770, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  17. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472 AND THR-735, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND THR-735, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: FUNCTION, INTERACTION WITH VMS1.
  21. "A Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasis."
    Tran J.R., Tomsic L.R., Brodsky J.L.
    J. Biol. Chem. 286:5744-5755(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH CDC48.
  22. "A ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stress."
    Brandman O., Stewart-Ornstein J., Wong D., Larson A., Williams C.C., Li G.W., Zhou S., King D., Shen P.S., Weibezahn J., Dunn J.G., Rouskin S., Inada T., Frost A., Weissman J.S.
    Cell 151:1042-1054(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Cdc48-associated complex bound to 60S particles is required for the clearance of aberrant translation products."
    Defenouillere Q., Yao Y., Mouaikel J., Namane A., Galopier A., Decourty L., Doyen A., Malabat C., Saveanu C., Jacquier A., Fromont-Racine M.
    Proc. Natl. Acad. Sci. U.S.A. 110:5046-5051(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  26. "Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast."
    Matsuda R., Ikeuchi K., Nomura S., Inada T.
    Genes Cells 19:1-12(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCDC48_YEAST
AccessioniPrimary (citable) accession number: P25694
Secondary accession number(s): D6VRM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 78400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.