Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9WSQ

Structure of dimeric mouse NLRP14-KDM2A-SKP1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003674	molecular_function	molecular_function
A	0005575	cellular_component	cellular_component
A	0005737	cellular_component	cytoplasm
A	0007283	biological_process	spermatogenesis
A	0050727	biological_process	regulation of inflammatory response
C	0000209	biological_process	protein polyubiquitination
C	0000775	cellular_component	chromosome, centromeric region
C	0004842	molecular_function	ubiquitin-protein transferase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005813	cellular_component	centrosome
C	0005829	cellular_component	cytosol
C	0005921	cellular_component	gap junction
C	0006338	biological_process	chromatin remodeling
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0006513	biological_process	protein monoubiquitination
C	0006915	biological_process	apoptotic process
C	0007129	biological_process	homologous chromosome pairing at meiosis
C	0008013	molecular_function	beta-catenin binding
C	0016567	biological_process	protein ubiquitination
C	0019005	cellular_component	SCF ubiquitin ligase complex
C	0019904	molecular_function	protein domain specific binding
C	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
C	0031467	cellular_component	Cul7-RING ubiquitin ligase complex
C	0031519	cellular_component	PcG protein complex
C	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
C	0051457	biological_process	maintenance of protein location in nucleus
C	0070936	biological_process	protein K48-linked ubiquitination
C	0097602	molecular_function	cullin family protein binding
C	0140677	molecular_function	molecular function activator activity
C	0160072	molecular_function	ubiquitin ligase complex scaffold activity
C	1904037	biological_process	positive regulation of epithelial cell apoptotic process
C	1990444	molecular_function	F-box domain binding
C	1990756	molecular_function	ubiquitin-like ligase-substrate adaptor activity
C	1990757	molecular_function	ubiquitin ligase activator activity
D	0003674	molecular_function	molecular_function
D	0005575	cellular_component	cellular_component
D	0005737	cellular_component	cytoplasm
D	0007283	biological_process	spermatogenesis
D	0050727	biological_process	regulation of inflammatory response
F	0000209	biological_process	protein polyubiquitination
F	0000775	cellular_component	chromosome, centromeric region
F	0004842	molecular_function	ubiquitin-protein transferase activity
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005737	cellular_component	cytoplasm
F	0005813	cellular_component	centrosome
F	0005829	cellular_component	cytosol
F	0005921	cellular_component	gap junction
F	0006338	biological_process	chromatin remodeling
F	0006511	biological_process	ubiquitin-dependent protein catabolic process
F	0006513	biological_process	protein monoubiquitination
F	0006915	biological_process	apoptotic process
F	0007129	biological_process	homologous chromosome pairing at meiosis
F	0008013	molecular_function	beta-catenin binding
F	0016567	biological_process	protein ubiquitination
F	0019005	cellular_component	SCF ubiquitin ligase complex
F	0019904	molecular_function	protein domain specific binding
F	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
F	0031467	cellular_component	Cul7-RING ubiquitin ligase complex
F	0031519	cellular_component	PcG protein complex
F	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
F	0051457	biological_process	maintenance of protein location in nucleus
F	0070936	biological_process	protein K48-linked ubiquitination
F	0097602	molecular_function	cullin family protein binding
F	0140677	molecular_function	molecular function activator activity
F	0160072	molecular_function	ubiquitin ligase complex scaffold activity
F	1904037	biological_process	positive regulation of epithelial cell apoptotic process
F	1990444	molecular_function	F-box domain binding
F	1990756	molecular_function	ubiquitin-like ligase-substrate adaptor activity
F	1990757	molecular_function	ubiquitin ligase activator activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	84
Details	Repeat: {"description":"LRR 1"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	92
Details	Repeat: {"description":"LRR 2"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	90
Details	Repeat: {"description":"LRR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	100
Details	Repeat: {"description":"LRR 4"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	88
Details	Repeat: {"description":"LRR 5"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	96
Details	Repeat: {"description":"LRR 6"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosylarginine","evidences":[{"source":"PubMed","id":"32584788","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	40
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	118
Details	Region: {"description":"Interaction with the F-box domain of F-box proteins","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P63208","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	40
Details	Repeat: {"description":"LRR 7"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	42
Details	Repeat: {"description":"LRR 8"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	40
Details	Repeat: {"description":"LRR 9"}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)