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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1KPS

Structural Basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin conjugating enzyme Ubc9 and RanGAP1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000166molecular_functionnucleotide binding
A0000795cellular_componentsynaptonemal complex
A0001221molecular_functiontranscription coregulator binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0007059biological_processchromosome segregation
A0007084biological_processmitotic nuclear membrane reassembly
A0008134molecular_functiontranscription factor binding
A0016604cellular_componentnuclear body
A0016605cellular_componentPML body
A0016740molecular_functiontransferase activity
A0016925biological_processprotein sumoylation
A0019789molecular_functionSUMO transferase activity
A0019899molecular_functionenzyme binding
A0030335biological_processpositive regulation of cell migration
A0036211biological_processprotein modification process
A0043398molecular_functionHLH domain binding
A0044388molecular_functionsmall protein activating enzyme binding
A0045892biological_processnegative regulation of DNA-templated transcription
A0048471cellular_componentperinuclear region of cytoplasm
A0050804biological_processmodulation of chemical synaptic transmission
A0051168biological_processnuclear export
A0051170biological_processimport into nucleus
A0051301biological_processcell division
A0061656molecular_functionSUMO conjugating enzyme activity
A0071535molecular_functionRING-like zinc finger domain binding
A0098685cellular_componentSchaffer collateral - CA1 synapse
A0098978cellular_componentglutamatergic synapse
A0099523cellular_componentpresynaptic cytosol
A0099524cellular_componentpostsynaptic cytosol
A0106068cellular_componentSUMO ligase complex
A1990234cellular_componenttransferase complex
B0005096molecular_functionGTPase activator activity
B0007165biological_processsignal transduction
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
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
D0005096molecular_functionGTPase activator activity
D0007165biological_processsignal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 601
ChainResidue
DSER536
DLEU537
DHIS538
DHOH681
site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 602
ChainResidue
CHOH724
CGLY47
CLYS48
CLYS49
CGLN117
CHOH656
site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 603
ChainResidue
BSER536
BLEU537
BHIS538
site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 604
ChainResidue
BLYS502
BHOH660
BHOH683
DLYS502
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyps.GtVCLsiL
ChainResidueDetails
APHE82-LEU97
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues306
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues10
DetailsRegion: {"description":"Interaction with SUMO1"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Glycyl thioester intermediate"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Interaction with RANBP2"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Substrate binding"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
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_FI9
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails
site_idSWS_FT_FI10
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_FI11
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_FI12
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
site_idSWS_FT_FI13
Number of Residues50
DetailsRegion: {"description":"Important for accumulation in the nucleus","evidences":[{"source":"PubMed","id":"26506250","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues6
DetailsMotif: {"description":"SUMO conjugation","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsSite: {"description":"Hydrophobic interaction with UBE2I","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P46060","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P46060","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15037602","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19131326","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P46060","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P46060","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P46060","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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