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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8AJO

Negative-stain electron microscopy structure of DDB1-DCAF12-CCT5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000781cellular_componentchromosome, telomeric region
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003684molecular_functiondamaged DNA binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006289biological_processnucleotide-excision repair
A0006511biological_processubiquitin-dependent protein catabolic process
A0006974biological_processDNA damage response
A0007056biological_processspindle assembly involved in female meiosis
A0007283biological_processspermatogenesis
A0008283biological_processcell population proliferation
A0010498biological_processproteasomal protein catabolic process
A0010506biological_processregulation of autophagy
A0016567biological_processprotein ubiquitination
A0019076biological_processviral release from host cell
A0030174biological_processregulation of DNA-templated DNA replication initiation
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031297biological_processreplication fork processing
A0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
A0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
A0032814biological_processregulation of natural killer cell activation
A0032991cellular_componentprotein-containing complex
A0034644biological_processcellular response to UV
A0035861cellular_componentsite of double-strand break
A0040029biological_processepigenetic regulation of gene expression
A0042127biological_processregulation of cell population proliferation
A0042752biological_processregulation of circadian rhythm
A0042981biological_processregulation of apoptotic process
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0044725biological_processepigenetic programming in the zygotic pronuclei
A0044877molecular_functionprotein-containing complex binding
A0045070biological_processpositive regulation of viral genome replication
A0045722biological_processpositive regulation of gluconeogenesis
A0045732biological_processpositive regulation of protein catabolic process
A0045995biological_processregulation of embryonic development
A0046726biological_processpositive regulation by virus of viral protein levels in host cell
A0048511biological_processrhythmic process
A0051702biological_processbiological process involved in interaction with symbiont
A0060964biological_processregulation of miRNA-mediated gene silencing
A0070062cellular_componentextracellular exosome
A0070914biological_processUV-damage excision repair
A0071987molecular_functionWD40-repeat domain binding
A0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
A0080135biological_processregulation of cellular response to stress
A0097602molecular_functioncullin family protein binding
A0160072molecular_functionubiquitin ligase complex scaffold activity
A1901987biological_processregulation of cell cycle phase transition
A1901990biological_processregulation of mitotic cell cycle phase transition
A1902412biological_processregulation of mitotic cytokinesis
A1904178biological_processnegative regulation of adipose tissue development
A2000036biological_processregulation of stem cell population maintenance
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0010506biological_processregulation of autophagy
B0016567biological_processprotein ubiquitination
B0042110biological_processT cell activation
B0042127biological_processregulation of cell population proliferation
B0060964biological_processregulation of miRNA-mediated gene silencing
B0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
B1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
C0000166molecular_functionnucleotide binding
C0003730molecular_functionmRNA 3'-UTR binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005829cellular_componentcytosol
C0005832cellular_componentchaperonin-containing T-complex
C0005874cellular_componentmicrotubule
C0006457biological_processprotein folding
C0009615biological_processresponse to virus
C0016787molecular_functionhydrolase activity
C0016887molecular_functionATP hydrolysis activity
C0031681molecular_functionG-protein beta-subunit binding
C0032212biological_processpositive regulation of telomere maintenance via telomerase
C0044183molecular_functionprotein folding chaperone
C0044297cellular_componentcell body
C0048027molecular_functionmRNA 5'-UTR binding
C0048487molecular_functionbeta-tubulin binding
C0050821biological_processprotein stabilization
C0051082molecular_functionunfolded protein binding
C0070062cellular_componentextracellular exosome
C0140662molecular_functionATP-dependent protein folding chaperone
C1904871biological_processpositive regulation of protein localization to Cajal body
C1904874biological_processpositive regulation of telomerase RNA localization to Cajal body
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. AVSGsrDgSMGLWEV
ChainResidueDetails
BALA198-VAL212
site_idPS00750
Number of Residues13
DetailsTCP1_1 Chaperonins TCP-1 signature 1. RTsLGPnGldKMM
ChainResidueDetails
CARG49-MET61
site_idPS00751
Number of Residues17
DetailsTCP1_2 Chaperonins TCP-1 signature 2. VTNDGATILsmMdVdHQ
ChainResidueDetails
CVAL70-GLN86
site_idPS00995
Number of Residues9
DetailsTCP1_3 Chaperonins TCP-1 signature 3. QDdeIGDGT
ChainResidueDetails
CGLN98-THR106
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues766
DetailsRegion: {"description":"Interaction with CDT1","evidences":[{"source":"PubMed","id":"15448697","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues343
DetailsRegion: {"description":"WD repeat beta-propeller A"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues316
DetailsRegion: {"description":"WD repeat beta-propeller B; Interaction with CUL4A"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues334
DetailsRegion: {"description":"WD repeat beta-propeller C"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues369
DetailsRegion: {"description":"Interaction with CDT1 and CUL4A","evidences":[{"source":"PubMed","id":"15448697","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues9
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues41
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues66
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues43
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues44
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues34
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7X3J","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X3U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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