Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Due to a server migration, the UniProt 'ID mapping', 'Peptide search' and 'community bibliography submission' tools will not be available on the 19th April 2021 during the morning (EST).
Entry version 210 (07 Apr 2021)
Sequence version 3 (01 Oct 1996)
Previous versions | rss
Add a publicationFeedback
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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates (PubMed:21454554, PubMed:31445887). By recruiting and promoting the degradation of ubiquitinated proteins, plays a role in the ubiquitin fusion degradation (UFD) pathway (PubMed:16428438). Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway which mediates the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:11813000, PubMed:11740563, PubMed:11847109, PubMed:21148305). Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1 (PubMed:11847109, PubMed:11733065). Has an additional role in the turnover of OLE1 where it targets ubiquitinated OLE1 and other proteins to the ERAD (PubMed:11847109). Regulates ubiquitin-mediated mitochondria protein degradation (PubMed:21070972, PubMed:27044889). Involved in spindle disassembly probably by promoting the degradation of spindle assembly factors ASE1 and CDC5 at the end of mitosis (PubMed:14636562). 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 (PubMed:23178123, PubMed:24261871). CDC48 may provide the mechanical force that dislodges the polyubiquitinated nascent peptides from the exit channel (PubMed:23178123, PubMed:24261871). Required for ribophagy, a process which relocalizes ribosomal particles into the vacuole for degradation in response to starvation (PubMed:20508643). Component of the DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions and support a role in protein quality control (PubMed:29355480). Substrate initially binds through the attached polyubiquitin chain to UDF1/NPL4 and then moves through the pore of the ATPase rings and is thereby unfolded (PubMed:31249135, PubMed:31249134). Acts on a broad range of even well-folded proteins via ubiquitin-binding and unfolding to initiate substrate processing (PubMed:31249135). Involved in degradation of mislocalized tail-anchored transmembrane proteins extracted from the mitochondrion outer membrane by MSP1 and ubiquitinated by DOA10 (PubMed:31445887).17 Publications

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The first ATP-binding region has low ATPase activity (By similarity). The second ATP-binding region is responsible for ATPase activity (By similarity). ATP binding to the first ATP-binding region induces intrinsic activity of the second ATP-binding region (PubMed:21454554). While ATP binding to the first ATP-binding region appears to prevent ATP hydrolysis by the second ATP-binding region, ADP-binding to first region promotes the coordinate and cooperative ATPase cycle of the second ATP-binding region (By similarity). ATP binding to the first ATP-binding region induces a conformational change, promoting the rotation of the first ATP-binding region relative to the second ATP-binding region in the hexamer (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei358ATP 1By similarity1
Binding sitei394ATP 1By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi257 – 263ATP 1By similarity7
Nucleotide bindingi531 – 536ATP 2By similarity6

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone, Hydrolase
Biological processCell cycle, Protein transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-3371511, HSF1 activation
R-SCE-5689896, Ovarian tumor domain proteases
R-SCE-6798695, Neutrophil degranulation
R-SCE-8876725, Protein methylation

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.16.1.2, the endoplasmic reticular retrotranslocon (er-rt) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cell division control protein 481 Publication (EC:3.6.4.61 Publication)
Alternative name(s):
Cell division cycle protein 481 Publication
Transitional endoplasmic reticulum ATPase homologCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CDC481 Publication
Ordered Locus Names:YDL126CImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002284, CDC48

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YDL126C

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi261K → A: Moderate reduction in growth rate. 1 Publication1
Mutagenesisi261K → T: Probable loss of ATP binding. Complete loss of catalytic activity. 1 Publication1
Mutagenesisi315E → A: Moderate reduction in growth rate. 1 Publication1
Mutagenesisi315E → D: Severe loss of catalytic activity without affecting cooperativity between the 2 ATP-binding regions. Slight reduction in growth rate. 1 Publication1
Mutagenesisi315E → N: Severe reduction in growth rate. 1 Publication1
Mutagenesisi315E → Q: Severe loss of catalytic activity and cooperativity between the 2 ATP-binding regions. Lethal. Restores cell growth; when associated with A-358; A-369; S-471; A-471 or H-475. 1 Publication1
Mutagenesisi358N → A: Slight reduction in growth rate. Restores cell growth; when associated with Q-315. 1 Publication1
Mutagenesisi369R → A: No effect on growth rate. Restores cell growth; when associated with Q-315. 1 Publication1
Mutagenesisi471P → A or S: Restores cell growth; when associated with Q-315. 1 Publication1
Mutagenesisi475R → H: Restores cell growth; when associated with Q-315. 1 Publication1
Mutagenesisi534K → A or T: Severe loss of catalytic activity. Lethal. 1 Publication1
Mutagenesisi588E → D: Moderate reduction in growth rate. 1 Publication1
Mutagenesisi588E → Q: Lethal. 1 Publication1
Mutagenesisi645R → A: Lethal. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000845871 – 835Cell division control protein 48Add BLAST835

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki305Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki346Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei472PhosphoserineCombined sources1
Modified residuei519PhosphoserineCombined sources1
Cross-linki522Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki673Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei735PhosphothreonineCombined sources1
Modified residuei770PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P25694

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P25694

PRoteomics IDEntifications database

More...
PRIDEi
P25694

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P25694

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P25694

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the HRD1 complex which contains HRD1, HRD3, USA1, DER1, YOS9, CDC48, NPL4, UFD1 AND UBX2/SEL1 (PubMed:16873066). 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 (PubMed:16873066).

Interacts with HRD1, HRD3, YOS9, UBX2, DER1, USA1 and UFD1 (PubMed:16873066).

Forms a complex composed of CDC48, NPL4, UFD1, UFD2 and SHP1 (PubMed:16427015).

Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and deubiquitinase OTU1; within the complex interacts with DOA1/UFD3 and OTU1 to prevent multiubiquitination of substrates (PubMed:16427015).

Interacts with UFD2, to add further ubiquitin moieties; the interaction with UFD2 is prevented by DOA1/UFD3 (PubMed:16427015).

Forms a complex composed of CDC48, DOA1, deubiquitinase UBP3 and probably BRE5; within the complex interacts with DOA1 and UBP3 (PubMed:20508643).

Interacts (via C-terminus) with DOA1 (via PUL domain); the interaction is direct (PubMed:16428438, PubMed:19805280, PubMed:27044889).

Interacts with NPL4 (PubMed:11733065, PubMed:11598205, PubMed:31249134).

Interacts with SHP1/UBX1, UBX2, UBX3, UBX4, UBX5, UBX6 and UBX7 (PubMed:15258615, PubMed:31249134).

Interacts with VMS1; the interaction recruits CDC48 to the mitochondria in response to mitochondrial stress (PubMed:21070972, PubMed:21148305).

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 (PubMed:23178123, PubMed:23479637). RQC forms a stable complex with 60S ribosomal subunits (PubMed:23178123, PubMed:23479637).

Interacts with ASE1 and CDC5; the interaction is likely to result in their degradation (PubMed:14636562).

Component of the DSCc E3 ligase complexes composed of at least TUL1, DSC2, DSC3, UBX3, CDC48 as well as VLD1 for the vacuole-localized complex or GLD1 for the Golgi/endosome-localized complex (PubMed:29355480).

16 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
31937, 891 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1323, CDC48-CDC23-UFD2 complex
CPX-2946, CDC48-NPL4-UFD1 AAA ATPase complex
CPX-3069, CDC48-NPL4-VMS1 AAA ATPase complex
CPX-3265, Ribosome quality control complex

Database of interacting proteins

More...
DIPi
DIP-2704N

Protein interaction database and analysis system

More...
IntActi
P25694, 166 interactors

Molecular INTeraction database

More...
MINTi
P25694

STRING: functional protein association networks

More...
STRINGi
4932.YDL126C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P25694, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P25694

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0730, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000165417

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000688_12_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P25694

Identification of Orthologs from Complete Genome Data

More...
OMAi
PIDDTTE

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593, AAA+_ATPase
IPR005938, AAA_ATPase_CDC48
IPR041569, AAA_lid_3
IPR009010, Asp_de-COase-like_dom_sf
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR004201, Cdc48_dom2
IPR029067, CDC48_domain_2-like_sf
IPR003338, CDC4_N-term_subdom
IPR027417, P-loop_NTPase
IPR015415, Vps4_C

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004, AAA, 2 hits
PF17862, AAA_lid_3, 2 hits
PF02933, CDC48_2, 1 hit
PF02359, CDC48_N, 1 hit
PF09336, Vps4_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382, AAA, 2 hits
SM01072, CDC48_2, 1 hit
SM01073, CDC48_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50692, SSF50692, 1 hit
SSF52540, SSF52540, 2 hits
SSF54585, SSF54585, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01243, CDC48, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00674, AAA, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i02ADDB9A227614D8
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X56956 Genomic DNA Translation: CAA40276.1
Z74174 Genomic DNA Translation: CAA98694.1
BK006938 Genomic DNA Translation: DAA11734.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S67669

NCBI Reference Sequences

More...
RefSeqi
NP_010157.1, NM_001180185.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDL126C_mRNA; YDL126C; YDL126C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851431

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDL126C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6OA9electron microscopy3.90A/B/C/D/E/F1-835[»]
6OAAelectron microscopy4.10B/C/D/E1-835[»]
6OABelectron microscopy3.60A/B/C/D/E1-835[»]
6OMBelectron microscopy3.70A/B/C/D/E1-835[»]
6OPCelectron microscopy3.70A/B/C/D/E/F1-835[»]
SMRiP25694
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi31937, 891 interactors
ComplexPortaliCPX-1323, CDC48-CDC23-UFD2 complex
CPX-2946, CDC48-NPL4-UFD1 AAA ATPase complex
CPX-3069, CDC48-NPL4-VMS1 AAA ATPase complex
CPX-3265, Ribosome quality control complex
DIPiDIP-2704N
IntActiP25694, 166 interactors
MINTiP25694
STRINGi4932.YDL126C

Protein family/group databases

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

PTM databases

CarbonylDBiP25694
iPTMnetiP25694

Proteomic databases

MaxQBiP25694
PaxDbiP25694
PRIDEiP25694

Genome annotation databases

EnsemblFungiiYDL126C_mRNA; YDL126C; YDL126C
GeneIDi851431
KEGGisce:YDL126C

Organism-specific databases

SGDiS000002284, CDC48
VEuPathDBiFungiDB:YDL126C

Phylogenomic databases

eggNOGiKOG0730, Eukaryota
GeneTreeiENSGT00940000165417
HOGENOMiCLU_000688_12_2_1
InParanoidiP25694
OMAiPIDDTTE

Enzyme and pathway databases

ReactomeiR-SCE-3371511, HSF1 activation
R-SCE-5689896, Ovarian tumor domain proteases
R-SCE-6798695, Neutrophil degranulation
R-SCE-8876725, Protein methylation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P25694
RNActiP25694, protein

Family and domain databases

InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR005938, AAA_ATPase_CDC48
IPR041569, AAA_lid_3
IPR009010, Asp_de-COase-like_dom_sf
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR004201, Cdc48_dom2
IPR029067, CDC48_domain_2-like_sf
IPR003338, CDC4_N-term_subdom
IPR027417, P-loop_NTPase
IPR015415, Vps4_C
PfamiView protein in Pfam
PF00004, AAA, 2 hits
PF17862, AAA_lid_3, 2 hits
PF02933, CDC48_2, 1 hit
PF02359, CDC48_N, 1 hit
PF09336, Vps4_C, 1 hit
SMARTiView protein in SMART
SM00382, AAA, 2 hits
SM01072, CDC48_2, 1 hit
SM01073, CDC48_N, 1 hit
SUPFAMiSSF50692, SSF50692, 1 hit
SSF52540, SSF52540, 2 hits
SSF54585, SSF54585, 1 hit
TIGRFAMsiTIGR01243, CDC48, 1 hit
PROSITEiView protein in PROSITE
PS00674, AAA, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDC48_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P25694
Secondary accession number(s): D6VRM4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 1, 1996
Last modified: April 7, 2021
This is version 210 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again