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7MOP

Cryo-EM structure of human HUWE1 in complex with DDIT4

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
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006338biological_processchromatin remodeling
A0006511biological_processubiquitin-dependent protein catabolic process
A0006513biological_processprotein monoubiquitination
A0006974biological_processDNA damage response
A0007030biological_processGolgi organization
A0010637biological_processnegative regulation of mitochondrial fusion
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0030154biological_processcell differentiation
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
A0048511biological_processrhythmic 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
A1903955biological_processpositive regulation of protein targeting to mitochondrion
A1904813cellular_componentficolin-1-rich granule lumen
A1905091biological_processpositive regulation of type 2 mitophagy
B0001666biological_processresponse to hypoxia
B0001764biological_processneuron migration
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006915biological_processapoptotic process
B0007420biological_processbrain development
B0009968biological_processnegative regulation of signal transduction
B0030182biological_processneuron differentiation
B0032007biological_processnegative regulation of TOR signaling
B0035556biological_processintracellular signal transduction
B0042771biological_processintrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
B0048011biological_processneurotrophin TRK receptor signaling pathway
B0051607biological_processdefense response to virus
B0071889molecular_function14-3-3 protein binding
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

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PDB entries from 2025-12-24

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