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8S7D

Cryo-EM structure of SKP1-FBXO22 in complex with a BACH1 BTB dimer at 3.2A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
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
D0000209biological_processprotein polyubiquitination
D0004842molecular_functionubiquitin-protein transferase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006511biological_processubiquitin-dependent protein catabolic process
D0030018cellular_componentZ disc
D0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0036211biological_processprotein modification process
D0048742biological_processregulation of skeletal muscle fiber development
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues59
DetailsRegion: {"description":"Interaction with the F-box domain of F-box proteins","evidences":[{"source":"PubMed","id":"35982156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
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_FI3
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

site_idSWS_FT_FI4
Number of Residues46
DetailsDomain: {"description":"F-box"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248636

PDB entries from 2026-02-04

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