Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5IFW

Quantitative interaction mapping reveals an extended ubiquitin regulatory domain in ASPL that disrupts functional p97 hexamers and induces cell death

Functional Information from GO Data
ChainGOidnamespacecontents
B0000153cellular_componentcytoplasmic ubiquitin ligase complex
B0000166molecular_functionnucleotide binding
B0000423biological_processmitophagy
B0000502cellular_componentproteasome complex
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005811cellular_componentlipid droplet
B0005829cellular_componentcytosol
B0006281biological_processDNA repair
B0006302biological_processdouble-strand break repair
B0006511biological_processubiquitin-dependent protein catabolic process
B0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
B0006914biological_processautophagy
B0006974biological_processDNA damage response
B0008289molecular_functionlipid binding
B0010494cellular_componentcytoplasmic stress granule
B0010498biological_processproteasomal protein catabolic process
B0010918biological_processpositive regulation of mitochondrial membrane potential
B0016236biological_processmacroautophagy
B0016567biological_processprotein ubiquitination
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0019079biological_processviral genome replication
B0019674biological_processNAD+ metabolic process
B0019903molecular_functionprotein phosphatase binding
B0019904molecular_functionprotein domain specific binding
B0019985biological_processtranslesion synthesis
B0030968biological_processendoplasmic reticulum unfolded protein response
B0030970biological_processretrograde protein transport, ER to cytosol
B0031334biological_processpositive regulation of protein-containing complex assembly
B0031593molecular_functionpolyubiquitin modification-dependent protein binding
B0031625molecular_functionubiquitin protein ligase binding
B0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
B0032510biological_processendosome to lysosome transport via multivesicular body sorting pathway
B0032991cellular_componentprotein-containing complex
B0034098cellular_componentVCP-NPL4-UFD1 AAA ATPase complex
B0034605biological_processcellular response to heat
B0034774cellular_componentsecretory granule lumen
B0035331biological_processnegative regulation of hippo signaling
B0035578cellular_componentazurophil granule lumen
B0035617biological_processstress granule disassembly
B0035800molecular_functiondeubiquitinase activator activity
B0035861cellular_componentsite of double-strand break
B0036297biological_processinterstrand cross-link repair
B0036435molecular_functionK48-linked polyubiquitin modification-dependent protein binding
B0036503biological_processERAD pathway
B0036513cellular_componentDerlin-1 retrotranslocation complex
B0042288molecular_functionMHC class I protein binding
B0042802molecular_functionidentical protein binding
B0042981biological_processregulation of apoptotic process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0043231cellular_componentintracellular membrane-bounded organelle
B0043335biological_processprotein unfolding
B0043531molecular_functionADP binding
B0044389molecular_functionubiquitin-like protein ligase binding
B0044877molecular_functionprotein-containing complex binding
B0045184biological_processestablishment of protein localization
B0045202cellular_componentsynapse
B0045732biological_processpositive regulation of protein catabolic process
B0045879biological_processnegative regulation of smoothened signaling pathway
B0046034biological_processATP metabolic process
B0048471cellular_componentperinuclear region of cytoplasm
B0050807biological_processregulation of synapse organization
B0051228biological_processmitotic spindle disassembly
B0061857biological_processendoplasmic reticulum stress-induced pre-emptive quality control
B0070062cellular_componentextracellular exosome
B0071218biological_processcellular response to misfolded protein
B0072344biological_processrescue of stalled ribosome
B0072389biological_processflavin adenine dinucleotide catabolic process
B0090263biological_processpositive regulation of canonical Wnt signaling pathway
B0097352biological_processautophagosome maturation
B0098978cellular_componentglutamatergic synapse
B0106300biological_processprotein-DNA covalent cross-linking repair
B0120186biological_processnegative regulation of protein localization to chromatin
B0140036molecular_functionubiquitin-modified protein reader activity
B0140455biological_processcytoplasm protein quality control
B1901224biological_processpositive regulation of non-canonical NF-kappaB signal transduction
B1903006biological_processpositive regulation of protein K63-linked deubiquitination
B1903715biological_processregulation of aerobic respiration
B1903843biological_processcellular response to arsenite ion
B1903862biological_processpositive regulation of oxidative phosphorylation
B1904288molecular_functionBAT3 complex binding
B1904813cellular_componentficolin-1-rich granule lumen
B1904949cellular_componentATPase complex
B1905634biological_processregulation of protein localization to chromatin
B1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
B1990381molecular_functionubiquitin-specific protease binding
B1990730cellular_componentVCP-NSFL1C complex
B2000060biological_processpositive regulation of ubiquitin-dependent protein catabolic process
B2001171biological_processpositive regulation of ATP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ADP B 901
ChainResidue
BASP205
BHIS384
BGLY408
BALA409
BGLY207
BPRO247
BGLY248
BTHR249
BGLY250
BLYS251
BTHR252
BLEU253

site_idAC2
Number of Residues11
Detailsbinding site for residue ADP B 902
ChainResidue
BGLY480
BPRO520
BGLY521
BCYS522
BGLY523
BLYS524
BTHR525
BLEU526
BILE656
BGLY684
BALA685

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. ViVMaATNrpnsIDpALr.R
ChainResidueDetails
BVAL341-ARG359
BVAL617-ARG635

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues76
DetailsDomain: {"description":"UBX","evidences":[{"source":"PROSITE-ProRule","id":"PRU00215","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues63
DetailsRegion: {"description":"Interaction with GLUT4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20512113","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q01853","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q01853","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q01853","evidenceCode":"ECO:0000250"}]}
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":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon