2MUX

SUMO2 non-covalently interacts with USP25 and downregulates its activity

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF22566	e2muxA1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF22566	ECOD (1.6)
A	PF21909	e2muxA2	A: extended segments	X: UIM domain (From Topology)	H: UIM domain (From Topology)	T: UIM domain	F: PF21909	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02809	Ubiquitin interaction motif (UIM)	Ubiquitin interaction motif	-	Motif

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Ubiquitin carboxyl-terminal hydrolase 25	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity protein binding binding ubiquitin binding ubiquitin-like protein binding cysteine-type peptidase activity ubiquitin-like protein peptidase activity cysteine-type deubiquitinase activity deubiquitinase activity SUMO binding ubiquitin protein ligase binding peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity protein binding binding ubiquitin binding ubiquitin-like protein binding cysteine-type peptidase activity ubiquitin-like protein peptidase activity cysteine-type deubiquitinase activity deubiquitinase activity SUMO binding ubiquitin protein ligase binding ubiquitin-like protein ligase binding enzyme binding ATPase binding	cellular response to stimulus response to organic substance regulation of cellular process negative regulation of proteolysis response to stimulus regulation of cellular response to stress negative regulation of biological process regulation of primary metabolic process ERAD pathway regulation of proteolysis proteolysis negative regulation of protein metabolic process response to endoplasmic reticulum stress regulation of ERAD pathway cellular response to stimulus response to organic substance regulation of cellular process negative regulation of proteolysis response to stimulus regulation of cellular response to stress negative regulation of biological process regulation of primary metabolic process ERAD pathway regulation of proteolysis proteolysis negative regulation of protein metabolic process response to endoplasmic reticulum stress regulation of ERAD pathway organonitrogen compound catabolic process regulation of biological process response to organonitrogen compound regulation of protein metabolic process negative regulation of metabolic process primary metabolic process response to nitrogen compound regulation of response to stimulus negative regulation of proteasomal protein catabolic process response to chemical regulation of proteasomal protein catabolic process metabolic process macromolecule metabolic process regulation of metabolic process catabolic process negative regulation of proteolysis involved in protein catabolic process proteolysis involved in protein catabolic process negative regulation of ERAD pathway regulation of response to endoplasmic reticulum stress macromolecule catabolic process negative regulation of protein catabolic process organic substance metabolic process cellular response to stress regulation of proteolysis involved in protein catabolic process regulation of response to stress response to stress negative regulation of cellular process protein metabolic process negative regulation of macromolecule metabolic process negative regulation of response to endoplasmic reticulum stress negative regulation of catabolic process organonitrogen compound metabolic process negative regulation of response to stimulus biological regulation proteasomal protein catabolic process regulation of macromolecule metabolic process protein catabolic process regulation of catabolic process cellular process organic substance catabolic process regulation of protein catabolic process macromolecule modification protein modification process protein deubiquitination protein K63-linked deubiquitination protein modification by small protein removal post-translational protein modification protein modification by small protein conjugation or removal proteasome-mediated ubiquitin-dependent protein catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process ubiquitin-dependent protein catabolic process regulation of protein stability regulation of biological quality protein K48-linked deubiquitination	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle endoplasmic reticulum endomembrane system

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR028889	Ubiquitin specific protease domain	Domain
A	IPR044635	Ubiquitin carboxyl-terminal hydrolase 14-like	Family
A	IPR018200	Ubiquitin specific protease, conserved site	Conserved Site
A	IPR038765	Papain-like cysteine peptidase superfamily	Homologous Superfamily
A	IPR001394	Peptidase C19, ubiquitin carboxyl-terminal hydrolase	Domain
A	IPR003903	Ubiquitin interacting motif	Conserved Site
A	IPR009060	UBA-like superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q9UHP3	astrocytic tumor large cell medulloblastoma non-small cell lung carcinoma breast cancer lung carcinoma ovarian cancer invasive ductal breast carcinoma medulloblastoma spina bifida

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.