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6SJ7

Structure of the human DDB1-DDA1-DCAF15 E3 ubiquitin ligase bound to RBM39 and Indisulam

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0002376biological_processimmune system process
A0005515molecular_functionprotein binding
A0016567biological_processprotein ubiquitination
A0032814biological_processregulation of natural killer cell activation
A0036094molecular_functionsmall molecule binding
A0046872molecular_functionmetal ion binding
A0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B0000781cellular_componentchromosome, telomeric region
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003684molecular_functiondamaged DNA binding
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0006281biological_processDNA repair
B0006289biological_processnucleotide-excision repair
B0006511biological_processubiquitin-dependent protein catabolic process
B0006915biological_processapoptotic process
B0006974biological_processDNA damage response
B0007056biological_processspindle assembly involved in female meiosis
B0010498biological_processproteasomal protein catabolic process
B0016055biological_processWnt signaling pathway
B0016567biological_processprotein ubiquitination
B0019076biological_processviral release from host cell
B0030674molecular_functionprotein-macromolecule adaptor activity
B0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
B0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
B0032991cellular_componentprotein-containing complex
B0034644biological_processcellular response to UV
B0035234biological_processectopic germ cell programmed cell death
B0035861cellular_componentsite of double-strand break
B0042752biological_processregulation of circadian rhythm
B0043066biological_processnegative regulation of apoptotic process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0044725biological_processepigenetic programming in the zygotic pronuclei
B0044877molecular_functionprotein-containing complex binding
B0045070biological_processpositive regulation of viral genome replication
B0045722biological_processpositive regulation of gluconeogenesis
B0045732biological_processpositive regulation of protein catabolic process
B0046726biological_processpositive regulation by virus of viral protein levels in host cell
B0048511biological_processrhythmic process
B0051093biological_processnegative regulation of developmental process
B0051702biological_processbiological process involved in interaction with symbiont
B0070062cellular_componentextracellular exosome
B0070914biological_processUV-damage excision repair
B0071987molecular_functionWD40-repeat domain binding
B0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B0097602molecular_functioncullin family protein binding
B0160072molecular_functionubiquitin ligase complex scaffold activity
B1901990biological_processregulation of mitotic cell cycle phase transition
B2000242biological_processnegative regulation of reproductive process
C0003676molecular_functionnucleic acid binding
C0003723molecular_functionRNA binding
C0005634cellular_componentnucleus
C0006397biological_processmRNA processing
D0000209biological_processprotein polyubiquitination
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0016567biological_processprotein ubiquitination
D0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue EF6 A 701
ChainResidue
ATHR230
APHE231
AGLN232
APRO233
AALA234
APHE235
CASN260
CASP264
CMET265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378
ChainResidueDetails
DALA2
ACYS196
ACYS211
AHIS214

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER33

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER95

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS1121
ASER310

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER314

223166

PDB entries from 2024-07-31

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