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7OAT

Structural basis for targeted p97 remodelling by ASPL as prerequisite for p97 trimethylation by METTL21D

Functional Information from GO Data
ChainGOidnamespacecontents
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006338biological_processchromatin remodeling
C0008168molecular_functionmethyltransferase activity
C0008276molecular_functionprotein methyltransferase activity
C0016279molecular_functionprotein-lysine N-methyltransferase activity
C0018022biological_processpeptidyl-lysine methylation
C0018023biological_processpeptidyl-lysine trimethylation
C0032259biological_processmethylation
C0032780biological_processnegative regulation of ATP-dependent activity
C0032991cellular_componentprotein-containing complex
C0042054molecular_functionhistone methyltransferase activity
C0051117molecular_functionATPase binding
Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. ViVMaATNrpnsIDpALr.R
ChainResidueDetails
BVAL341-ARG359

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|Ref.9
ChainResidueDetails
CTRP43
CGLY75
CASP96
CTRP126
CALA143
CTYR148

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER8

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER3

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER7
BSER13
BSER462

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BSER37

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634
ChainResidueDetails
BM3L315

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
BTHR436

site_idSWS_FT_FI8
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS8
BLYS18

227344

PDB entries from 2024-11-13

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