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1OQY

Structure of the DNA repair protein hHR23a

Functional Information from GO Data
ChainGOidnamespacecontents
A0000502cellular_componentproteasome complex
A0003684molecular_functiondamaged DNA binding
A0003697molecular_functionsingle-stranded DNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006289biological_processnucleotide-excision repair
A0006338biological_processchromatin remodeling
A0006974biological_processDNA damage response
A0019900molecular_functionkinase binding
A0031593molecular_functionpolyubiquitin modification-dependent protein binding
A0031648biological_processprotein destabilization
A0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032991cellular_componentprotein-containing complex
A0035575molecular_functionhistone H4K20 demethylase activity
A0043130molecular_functionubiquitin binding
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045070biological_processpositive regulation of viral genome replication
A0045787biological_processpositive regulation of cell cycle
A0070628molecular_functionproteasome binding
A0071942cellular_componentXPC complex
A1990381molecular_functionubiquitin-specific protease binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsDomain: {"description":"UBA 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00212","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsDomain: {"description":"UBA 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00212","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues103
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues44
DetailsRegion: {"description":"HIV-1 vpr binding"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues39
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues9
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P54726","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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