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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2O25

Ubiquitin-Conjugating Enzyme E2-25 kDa Complexed With SUMO-1-Conjugating Enzyme UBC9

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
A0010994biological_processfree ubiquitin chain polymerization
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0031625molecular_functionubiquitin protein ligase binding
A0032433cellular_componentfilopodium tip
A0034450molecular_functionubiquitin-ubiquitin ligase activity
A0035458biological_processcellular response to interferon-beta
A0060340biological_processpositive regulation of type I interferon-mediated signaling pathway
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070936biological_processprotein K48-linked ubiquitination
A1903265biological_processpositive regulation of tumor necrosis factor-mediated signaling pathway
B0000166molecular_functionnucleotide binding
B0000209biological_processprotein polyubiquitination
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006511biological_processubiquitin-dependent protein catabolic process
B0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
B0010994biological_processfree ubiquitin chain polymerization
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0031625molecular_functionubiquitin protein ligase binding
B0032433cellular_componentfilopodium tip
B0034450molecular_functionubiquitin-ubiquitin ligase activity
B0035458biological_processcellular response to interferon-beta
B0060340biological_processpositive regulation of type I interferon-mediated signaling pathway
B0061631molecular_functionubiquitin conjugating enzyme activity
B0070936biological_processprotein K48-linked ubiquitination
B1903265biological_processpositive regulation of tumor necrosis factor-mediated signaling pathway
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000166molecular_functionnucleotide binding
C0000795cellular_componentsynaptonemal complex
C0001221molecular_functiontranscription coregulator binding
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005635cellular_componentnuclear envelope
C0005643cellular_componentnuclear pore
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006511biological_processubiquitin-dependent protein catabolic process
C0007059biological_processchromosome segregation
C0007084biological_processmitotic nuclear membrane reassembly
C0008134molecular_functiontranscription factor binding
C0016604cellular_componentnuclear body
C0016605cellular_componentPML body
C0016740molecular_functiontransferase activity
C0016925biological_processprotein sumoylation
C0019789molecular_functionSUMO transferase activity
C0019899molecular_functionenzyme binding
C0030335biological_processpositive regulation of cell migration
C0036211biological_processprotein modification process
C0043398molecular_functionHLH domain binding
C0044388molecular_functionsmall protein activating enzyme binding
C0045892biological_processnegative regulation of DNA-templated transcription
C0048471cellular_componentperinuclear region of cytoplasm
C0050804biological_processmodulation of chemical synaptic transmission
C0051168biological_processnuclear export
C0051170biological_processimport into nucleus
C0051301biological_processcell division
C0061656molecular_functionSUMO conjugating enzyme activity
C0071535molecular_functionRING-like zinc finger domain binding
C0098685cellular_componentSchaffer collateral - CA1 synapse
C0098978cellular_componentglutamatergic synapse
C0099523cellular_componentpresynaptic cytosol
C0099524cellular_componentpostsynaptic cytosol
C0106068cellular_componentSUMO ligase complex
C1990234cellular_componenttransferase complex
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000166molecular_functionnucleotide binding
D0000795cellular_componentsynaptonemal complex
D0001221molecular_functiontranscription coregulator binding
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005635cellular_componentnuclear envelope
D0005643cellular_componentnuclear pore
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006511biological_processubiquitin-dependent protein catabolic process
D0007059biological_processchromosome segregation
D0007084biological_processmitotic nuclear membrane reassembly
D0008134molecular_functiontranscription factor binding
D0016604cellular_componentnuclear body
D0016605cellular_componentPML body
D0016740molecular_functiontransferase activity
D0016925biological_processprotein sumoylation
D0019789molecular_functionSUMO transferase activity
D0019899molecular_functionenzyme binding
D0030335biological_processpositive regulation of cell migration
D0036211biological_processprotein modification process
D0043398molecular_functionHLH domain binding
D0044388molecular_functionsmall protein activating enzyme binding
D0045892biological_processnegative regulation of DNA-templated transcription
D0048471cellular_componentperinuclear region of cytoplasm
D0050804biological_processmodulation of chemical synaptic transmission
D0051168biological_processnuclear export
D0051170biological_processimport into nucleus
D0051301biological_processcell division
D0061656molecular_functionSUMO conjugating enzyme activity
D0071535molecular_functionRING-like zinc finger domain binding
D0098685cellular_componentSchaffer collateral - CA1 synapse
D0098978cellular_componentglutamatergic synapse
D0099523cellular_componentpresynaptic cytosol
D0099524cellular_componentpostsynaptic cytosol
D0106068cellular_componentSUMO ligase complex
D1990234cellular_componenttransferase complex
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues17
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. WHPNIssvtGaICLdiL
ChainResidueDetails
ATRP80-LEU96
CPHE82-LEU97
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues606
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Bilsland A.E.","Keith W.N."]}},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues10
DetailsRegion: {"description":"Interaction with SUMO1"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsActive site: {"description":"Glycyl thioester intermediate"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues6
DetailsSite: {"description":"Interaction with RANBP2"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsSite: {"description":"Substrate binding"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"22509284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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