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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7V7B

CryoEM structure of DDB1-VprBP complex in ARM-up conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000166molecular_functionnucleotide binding
A0001650cellular_componentfibrillar center
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006351biological_processDNA-templated transcription
A0008180cellular_componentCOP9 signalosome
A0016301molecular_functionkinase activity
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0030183biological_processB cell differentiation
A0030331molecular_functionnuclear estrogen receptor binding
A0033151biological_processV(D)J recombination
A0035212biological_processcell competition in a multicellular organism
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0043687biological_processpost-translational protein modification
A0045732biological_processpositive regulation of protein catabolic process
A0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
A0106310molecular_functionprotein serine kinase activity
A1990244molecular_functionhistone H2AT120 kinase activity
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
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000166molecular_functionnucleotide binding
C0001650cellular_componentfibrillar center
C0004674molecular_functionprotein serine/threonine kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0006325biological_processchromatin organization
C0006338biological_processchromatin remodeling
C0006351biological_processDNA-templated transcription
C0008180cellular_componentCOP9 signalosome
C0016301molecular_functionkinase activity
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0030183biological_processB cell differentiation
C0030331molecular_functionnuclear estrogen receptor binding
C0033151biological_processV(D)J recombination
C0035212biological_processcell competition in a multicellular organism
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0043687biological_processpost-translational protein modification
C0045732biological_processpositive regulation of protein catabolic process
C0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
C0106310molecular_functionprotein serine kinase activity
C1990244molecular_functionhistone H2AT120 kinase activity
C1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
D0000781cellular_componentchromosome, telomeric region
D0003676molecular_functionnucleic acid binding
D0003677molecular_functionDNA binding
D0003684molecular_functiondamaged DNA binding
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0006281biological_processDNA repair
D0006289biological_processnucleotide-excision repair
D0006511biological_processubiquitin-dependent protein catabolic process
D0006974biological_processDNA damage response
D0007056biological_processspindle assembly involved in female meiosis
D0007283biological_processspermatogenesis
D0008283biological_processcell population proliferation
D0010498biological_processproteasomal protein catabolic process
D0010506biological_processregulation of autophagy
D0016567biological_processprotein ubiquitination
D0019076biological_processviral release from host cell
D0030174biological_processregulation of DNA-templated DNA replication initiation
D0030674molecular_functionprotein-macromolecule adaptor activity
D0031297biological_processreplication fork processing
D0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
D0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
D0032814biological_processregulation of natural killer cell activation
D0032991cellular_componentprotein-containing complex
D0034644biological_processcellular response to UV
D0035861cellular_componentsite of double-strand break
D0040029biological_processepigenetic regulation of gene expression
D0042127biological_processregulation of cell population proliferation
D0042752biological_processregulation of circadian rhythm
D0042981biological_processregulation of apoptotic process
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0044725biological_processepigenetic programming in the zygotic pronuclei
D0044877molecular_functionprotein-containing complex binding
D0045070biological_processpositive regulation of viral genome replication
D0045722biological_processpositive regulation of gluconeogenesis
D0045732biological_processpositive regulation of protein catabolic process
D0045995biological_processregulation of embryonic development
D0046726biological_processpositive regulation by virus of viral protein levels in host cell
D0048511biological_processrhythmic process
D0051702biological_processbiological process involved in interaction with symbiont
D0060964biological_processregulation of miRNA-mediated gene silencing
D0070062cellular_componentextracellular exosome
D0070914biological_processUV-damage excision repair
D0071987molecular_functionWD40-repeat domain binding
D0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
D0080135biological_processregulation of cellular response to stress
D0097602molecular_functioncullin family protein binding
D0160072molecular_functionubiquitin ligase complex scaffold activity
D1901987biological_processregulation of cell cycle phase transition
D1901990biological_processregulation of mitotic cell cycle phase transition
D1902412biological_processregulation of mitotic cytokinesis
D1904178biological_processnegative regulation of adipose tissue development
D2000036biological_processregulation of stem cell population maintenance
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues62
DetailsDomain: {"description":"Chromo"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues64
DetailsDomain: {"description":"LisH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00126","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues78
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues82
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues74
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues64
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues84
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues398
DetailsRegion: {"description":"WD repeat-like region"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues14
DetailsMotif: {"description":"DWD box 1"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues14
DetailsMotif: {"description":"DWD box 2"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1532
DetailsRegion: {"description":"Interaction with CDT1","evidences":[{"source":"PubMed","id":"15448697","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues686
DetailsRegion: {"description":"WD repeat beta-propeller A"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues632
DetailsRegion: {"description":"WD repeat beta-propeller B; Interaction with CUL4A"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248636

PDB entries from 2026-02-04

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