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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4I6J

A ubiquitin ligase-substrate complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000166molecular_functionnucleotide binding
A0000976molecular_functiontranscription cis-regulatory region binding
A0003677molecular_functionDNA binding
A0003684molecular_functiondamaged DNA binding
A0003697molecular_functionsingle-stranded DNA binding
A0004864molecular_functionprotein phosphatase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006351biological_processDNA-templated transcription
A0006606biological_processprotein import into nucleus
A0007623biological_processcircadian rhythm
A0009416biological_processresponse to light stimulus
A0009881molecular_functionphotoreceptor activity
A0014823biological_processresponse to activity
A0016607cellular_componentnuclear speck
A0016922molecular_functionnuclear receptor binding
A0019900molecular_functionkinase binding
A0019901molecular_functionprotein kinase binding
A0019902molecular_functionphosphatase binding
A0019915biological_processlipid storage
A0032868biological_processresponse to insulin
A0032922biological_processcircadian regulation of gene expression
A0042593biological_processglucose homeostasis
A0042752biological_processregulation of circadian rhythm
A0042754biological_processnegative regulation of circadian rhythm
A0043153biological_processentrainment of circadian clock by photoperiod
A0045892biological_processnegative regulation of DNA-templated transcription
A0048511biological_processrhythmic process
A0071949molecular_functionFAD binding
A2000323biological_processnegative regulation of nuclear receptor-mediated glucocorticoid signaling pathway
A2000850biological_processnegative regulation of glucocorticoid secretion
B0000151cellular_componentubiquitin ligase complex
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0016567biological_processprotein ubiquitination
B0016604cellular_componentnuclear body
B0019005cellular_componentSCF ubiquitin ligase complex
B0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
B0031648biological_processprotein destabilization
B0042752biological_processregulation of circadian rhythm
B0043153biological_processentrainment of circadian clock by photoperiod
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0048511biological_processrhythmic process
C0000082biological_processG1/S transition of mitotic cell cycle
C0000209biological_processprotein polyubiquitination
C0000785cellular_componentchromatin
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005829cellular_componentcytosol
C0006338biological_processchromatin remodeling
C0006355biological_processregulation of DNA-templated transcription
C0006511biological_processubiquitin-dependent protein catabolic process
C0006879biological_processintracellular iron ion homeostasis
C0007346biological_processregulation of mitotic cell cycle
C0008013molecular_functionbeta-catenin binding
C0010564biological_processregulation of cell cycle process
C0010824biological_processregulation of centrosome duplication
C0014033biological_processneural crest cell differentiation
C0016567biological_processprotein ubiquitination
C0019005cellular_componentSCF ubiquitin ligase complex
C0019904molecular_functionprotein domain specific binding
C0030510biological_processregulation of BMP signaling pathway
C0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
C0031467cellular_componentCul7-RING ubiquitin ligase complex
C0031507biological_processheterochromatin formation
C0031519cellular_componentPcG protein complex
C0032006biological_processregulation of TOR signaling
C0042752biological_processregulation of circadian rhythm
C0042981biological_processregulation of apoptotic process
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0045892biological_processnegative regulation of DNA-templated transcription
C0050727biological_processregulation of inflammatory response
C0051124biological_processsynaptic assembly at neuromuscular junction
C0051298biological_processcentrosome duplication
C0051457biological_processmaintenance of protein location in nucleus
C0051726biological_processregulation of cell cycle
C0060173biological_processlimb development
C0060271biological_processcilium assembly
C0070936biological_processprotein K48-linked ubiquitination
C0097602molecular_functioncullin family protein binding
C0140677molecular_functionmolecular function activator activity
C0160072molecular_functionubiquitin ligase complex scaffold activity
C1901524biological_processregulation of mitophagy
C1904415biological_processregulation of xenophagy
C1990444molecular_functionF-box domain binding
C1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
C1990757molecular_functionubiquitin ligase activator activity
C2000001biological_processregulation of DNA damage checkpoint
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues129
DetailsDomain: {"description":"Photolyase/cryptochrome alpha/beta"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues99
DetailsRegion: {"description":"Required for inhibition of CLOCK-BMAL1-mediated transcription","evidences":[{"source":"UniProtKB","id":"P97784","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23503662","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P97784","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P97784","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by MAPK","evidences":[{"source":"PubMed","id":"11875063","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15298678","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P97784","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23452856","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues27
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues26
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues25
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues25
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues25
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues25
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues25
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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