CDC48/YDL126C Protein Information Help

Standard Name Cdc48p 1
Systematic Name Ydl126cp
ORF Classification Verified
Description AAA ATPase involved in multiple processes; subunit of polyubiquitin-selective segregase complex involved in ERAD, cell wall integrity during heat stress, mitotic spindle disassembly; subunit of complex involved in mitochondria-associated degradation; role in mobilizing membrane bound transcription factors by regulated ubiquitin/proteasome-dependent processing; roles in macroautophagy, PMN, RAD, ribophagy, and homotypic ER membrane fusion; functional ortholog of human p97/VCP (10, 2, 3, 4, 5, 6, 7, 8, 9)
Name Description Cell Division Cycle 1
Experimental Data
Molecules/cell 78400 11
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 835
Molecular Weight (Da) 91,995
Isoelectric Point (pI) 4.66

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Cdc48p (InterPro)
Physical Interactions There are 288 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000005307E | P25694
MIPS: YDL126C
NCBI: 1431189 | 1449400 | 1705679 | 6320077 | NP_010157.1
GenBank/EMBL/DDBJ: DAA11734.1 | X56956 | Z74174
Amino Acid Sequence (or in FASTA format)
       1  MGEEHKPLLD ASGVDPREED KTATAILRRK KKDNMLLVDD AINDDNSVIA
      51  INSNTMDKLE LFRGDTVLVK GKKRKDTVLI VLIDDELEDG ACRINRVVRN
     101  NLRIRLGDLV TIHPCPDIKY ATRISVLPIA DTIEGITGNL FDVFLKPYFV
     151  EAYRPVRKGD HFVVRGGMRQ VEFKVVDVEP EEYAVVAQDT IIHWEGEPIN
     201  REDEENNMNE VGYDDIGGCR KQMAQIREMV ELPLRHPQLF KAIGIKPPRG
     251  VLMYGPPGTG KTLMARAVAN ETGAFFFLIN GPEVMSKMAG ESESNLRKAF
     301  EEAEKNAPAI IFIDEIDSIA PKRDKTNGEV ERRVVSQLLT LMDGMKARSN
     351  VVVIAATNRP NSIDPALRRF GRFDREVDIG IPDATGRLEV LRIHTKNMKL
     401  ADDVDLEALA AETHGYVGAD IASLCSEAAM QQIREKMDLI DLDEDEIDAE
     451  VLDSLGVTMD NFRFALGNSN PSALRETVVE SVNVTWDDVG GLDEIKEELK
     501  ETVEYPVLHP DQYTKFGLSP SKGVLFYGPP GTGKTLLAKA VATEVSANFI
     551  SVKGPELLSM WYGESESNIR DIFDKARAAA PTVVFLDELD SIAKARGGSL
     601  GDAGGASDRV VNQLLTEMDG MNAKKNVFVI GATNRPDQID PAILRPGRLD
     651  QLIYVPLPDE NARLSILNAQ LRKTPLEPGL ELTAIAKATQ GFSGADLLYI
     701  VQRAAKYAIK DSIEAHRQHE AEKEVKVEGE DVEMTDEGAK AEQEPEVDPV
     751  PYITKEHFAE AMKTAKRSVS DAELRRYEAY SQQMKASRGQ FSNFNFNDAP
     801  LGTTATDNAN SNNSAPSGAG AAFGSNAEED DDLYS*               

external links for Cdc48p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) BioPIXIE MIPS YeastGFP
Candida (CGD) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Cdc48p
1) Moir D, et al.  (1982) Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies. Genetics 100(4):547-63
2) Ye Y, et al.  (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162(1):71-84
3) Rape M, et al.  (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107(5):667-77
4) Cao K, et al.  (2003) The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis. Cell 115(3):355-67
5) Shcherbik N and Haines DS  (2007) Cdc48p(Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors. Mol Cell 25(3):385-97
6) Ossareh-Nazari B, et al.  (2010) Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy. EMBO Rep 11(7):548-54
7) Heo JM, et al.  (2010) A stress-responsive system for mitochondrial protein degradation. Mol Cell 40(3):465-80
8) Hsieh MT and Chen RH  (2011) Cdc48 and Cofactors Npl4-Ufd1 Are Important for G1 Progression during Heat Stress by Maintaining Cell Wall Integrity in Saccharomyces cerevisiae. PLoS One 6(4):e18988
9) Stolz A, et al.  (2011) Cdc48: a power machine in protein degradation. Trends Biochem Sci 36(10):515-23
10) Verma R, et al.  (2013) Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome. Elife 2():e00308
11) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41