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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8QH5

CryoEM structure of UVSSA(VHS)-CSA-DDB1-DDA1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000012biological_processsingle strand break repair
A0000109cellular_componentnucleotide-excision repair complex
A0000209biological_processprotein polyubiquitination
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006281biological_processDNA repair
A0006283biological_processtranscription-coupled nucleotide-excision repair
A0006289biological_processnucleotide-excision repair
A0006974biological_processDNA damage response
A0006979biological_processresponse to oxidative stress
A0009411biological_processresponse to UV
A0010996biological_processresponse to auditory stimulus
A0016363cellular_componentnuclear matrix
A0016567biological_processprotein ubiquitination
A0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
A0032991cellular_componentprotein-containing complex
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0043204cellular_componentperikaryon
A0051865biological_processprotein autoubiquitination
A0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
A0090262biological_processregulation of transcription-coupled nucleotide-excision repair
A0090734cellular_componentsite of DNA damage
A0097680biological_processdouble-strand break repair via classical nonhomologous end joining
A1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
B0000781cellular_componentchromosome, telomeric region
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003684molecular_functiondamaged DNA binding
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0006281biological_processDNA repair
B0006289biological_processnucleotide-excision repair
B0006511biological_processubiquitin-dependent protein catabolic process
B0006974biological_processDNA damage response
B0007056biological_processspindle assembly involved in female meiosis
B0007283biological_processspermatogenesis
B0008283biological_processcell population proliferation
B0010498biological_processproteasomal protein catabolic process
B0010506biological_processregulation of autophagy
B0016567biological_processprotein ubiquitination
B0019076biological_processviral release from host cell
B0030174biological_processregulation of DNA-templated DNA replication initiation
B0030674molecular_functionprotein-macromolecule adaptor activity
B0031297biological_processreplication fork processing
B0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
B0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
B0032814biological_processregulation of natural killer cell activation
B0032991cellular_componentprotein-containing complex
B0034644biological_processcellular response to UV
B0035861cellular_componentsite of double-strand break
B0040029biological_processepigenetic regulation of gene expression
B0042127biological_processregulation of cell population proliferation
B0042752biological_processregulation of circadian rhythm
B0042981biological_processregulation of apoptotic process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0044725biological_processepigenetic programming in the zygotic pronuclei
B0044877molecular_functionprotein-containing complex binding
B0045070biological_processpositive regulation of viral genome replication
B0045722biological_processpositive regulation of gluconeogenesis
B0045732biological_processpositive regulation of protein catabolic process
B0045995biological_processregulation of embryonic development
B0046726biological_processpositive regulation by virus of viral protein levels in host cell
B0048511biological_processrhythmic process
B0051702biological_processbiological process involved in interaction with symbiont
B0060964biological_processregulation of miRNA-mediated gene silencing
B0070062cellular_componentextracellular exosome
B0070914biological_processUV-damage excision repair
B0071987molecular_functionWD40-repeat domain binding
B0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B0080135biological_processregulation of cellular response to stress
B0097602molecular_functioncullin family protein binding
B0160072molecular_functionubiquitin ligase complex scaffold activity
B1901987biological_processregulation of cell cycle phase transition
B1901990biological_processregulation of mitotic cell cycle phase transition
B1902412biological_processregulation of mitotic cytokinesis
B1904178biological_processnegative regulation of adipose tissue development
B2000036biological_processregulation of stem cell population maintenance
C0000209biological_processprotein polyubiquitination
C0005515molecular_functionprotein binding
C0005654cellular_componentnucleoplasm
C0016567biological_processprotein ubiquitination
C0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
C0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
C0032814biological_processregulation of natural killer cell activation
C0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
D0000993molecular_functionRNA polymerase II complex binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005694cellular_componentchromosome
D0006281biological_processDNA repair
D0006283biological_processtranscription-coupled nucleotide-excision repair
D0006325biological_processchromatin organization
D0006974biological_processDNA damage response
D0008270molecular_functionzinc ion binding
D0009411biological_processresponse to UV
D0016567biological_processprotein ubiquitination
D0046872molecular_functionmetal ion binding
D0090734cellular_componentsite of DNA damage
D0140463molecular_functionchromatin-protein adaptor activity
D0140870molecular_functionRNA polymerase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LATAsaDsRVKLWDV
ChainResidueDetails
ALEU202-VAL216
ALEU260-SER274
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues143
DetailsRegion: {"description":"VHS-like"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues9
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues40
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues41
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues40
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues39
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues40
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues38
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues343
DetailsRegion: {"description":"WD repeat beta-propeller A"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues316
DetailsRegion: {"description":"WD repeat beta-propeller B; Interaction with CUL4A"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
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_FI16
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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