Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9PLR

CryoEM reconstruction of HUWE1-USP7 complex in the closed state

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000209biological_processprotein polyubiquitination
A0003677molecular_functionDNA binding
A0003723molecular_functionRNA binding
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006284biological_processbase-excision repair
A0006338biological_processchromatin remodeling
A0006511biological_processubiquitin-dependent protein catabolic process
A0006513biological_processprotein monoubiquitination
A0007030biological_processGolgi organization
A0010637biological_processnegative regulation of mitochondrial fusion
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0031398biological_processpositive regulation of protein ubiquitination
A0031965cellular_componentnuclear membrane
A0032922biological_processcircadian regulation of gene expression
A0034450molecular_functionubiquitin-ubiquitin ligase activity
A0034774cellular_componentsecretory granule lumen
A0035359biological_processnegative regulation of peroxisome proliferator activated receptor signaling pathway
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0061025biological_processmembrane fusion
A0061630molecular_functionubiquitin protein ligase activity
A0070062cellular_componentextracellular exosome
A0070936biological_processprotein K48-linked ubiquitination
A0140852molecular_functionhistone ubiquitin ligase activity
A0141198biological_processprotein branched polyubiquitination
A1903749biological_processpositive regulation of protein localization to mitochondrion
A1904813cellular_componentficolin-1-rich granule lumen
A1905091biological_processpositive regulation of type 2 mitophagy
C0000151cellular_componentubiquitin ligase complex
C0002039molecular_functionp53 binding
C0004197molecular_functioncysteine-type endopeptidase activity
C0004843molecular_functioncysteine-type deubiquitinase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005694cellular_componentchromosome
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006283biological_processtranscription-coupled nucleotide-excision repair
C0006307biological_processDNA alkylation repair
C0010803biological_processregulation of tumor necrosis factor-mediated signaling pathway
C0016567biological_processprotein ubiquitination
C0016579biological_processprotein deubiquitination
C0016604cellular_componentnuclear body
C0016605cellular_componentPML body
C0031647biological_processregulation of protein stability
C0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
C0032991cellular_componentprotein-containing complex
C0035520biological_processmonoubiquitinated protein deubiquitination
C0042752biological_processregulation of circadian rhythm
C0044027biological_processnegative regulation of gene expression via chromosomal CpG island methylation
C0045721biological_processnegative regulation of gluconeogenesis
C0050821biological_processprotein stabilization
C0051090biological_processobsolete regulation of DNA-binding transcription factor activity
C0070203biological_processregulation of establishment of protein localization to telomere
C0070536biological_processprotein K63-linked deubiquitination
C0071108biological_processprotein K48-linked deubiquitination
C0075342biological_processsymbiont-mediated disruption of host cell PML body
C0101005molecular_functiondeubiquitinase activity
C0140374biological_processantiviral innate immune response
C0140936molecular_functionhistone H2B deubiquitinase activity
C0140950molecular_functionhistone H2A deubiquitinase activity
C1901796biological_processregulation of signal transduction by p53 class mediator
C1904262biological_processnegative regulation of TORC1 signaling
C1904353biological_processregulation of telomere capping
C1905279biological_processregulation of retrograde transport, endosome to Golgi
C1905368cellular_componentpeptidase complex
C1990380molecular_functionK48-linked deubiquitinase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues77
DetailsDomain: {"description":"WWE","evidences":[{"source":"PROSITE-ProRule","id":"PRU00248","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q7TMY8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P51593","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues127
DetailsDomain: {"description":"MATH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00129","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues135
DetailsRegion: {"description":"Necessary for nuclear localization"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25944111","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11923872","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15053880","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16964248","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18716620","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21745816","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22411829","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17651432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"17651432","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
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
Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails

260320

PDB entries from 2026-09-30

PDB statisticsPDBj update infoContact PDBjnumon