Annotations: 1WH0

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1wh0a1	All beta proteins	HSP20-like chaperones	HSP20-like chaperones	GS domain	Ubiquitin carboxyl-terminal hydrolase 19, USP19	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1wh0a3	Artifacts	Tags	Tags	Tags	C-terminal Tags	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1wh0a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	CS domain	8031157	4000815	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Hsp20 chaperone-like	8043535	3001242	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	CS	e1wh0A1	A: beta sandwiches	X: HSP20-like	H: HSP20-like chaperones (From Topology)	T: HSP20-like chaperones	F: CS	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.790	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF04969	CS domain (CS)	CS domain	The CS and CHORD (Pfam:PF04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD [1]. It has been suggested that the CS domain ...	The CS and CHORD (Pfam:PF04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD [1]. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies [2]. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19) (Swiss:O94966), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2 [3].	Domain
A	PF16602	Linker region of USP19 deubiquitinase (USP19_linker)	Linker region of USP19 deubiquitinase	-	Disordered

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Ubiquitin carboxyl-terminal hydrolase 19	cysteine-type peptidase activity ubiquitin-like protein peptidase activity peptidase activity cysteine-type deubiquitinase activity catalytic activity, acting on a protein hydrolase activity catalytic activity deubiquitinase activity Hsp90 protein binding protein binding binding heat shock protein binding cation binding ion binding cysteine-type peptidase activity ubiquitin-like protein peptidase activity peptidase activity cysteine-type deubiquitinase activity catalytic activity, acting on a protein hydrolase activity catalytic activity deubiquitinase activity Hsp90 protein binding protein binding binding heat shock protein binding cation binding ion binding metal ion binding small molecule binding	cellular response to stimulus response to decreased oxygen levels regulation of cellular response to hypoxia regulation of biological process regulation of cellular process response to stimulus cellular response to oxygen levels cellular response to hypoxia regulation of cellular response to stress biological regulation cellular response to decreased oxygen levels cellular response to chemical stimulus cellular response to stress regulation of response to stimulus response to hypoxia cellular response to stimulus response to decreased oxygen levels regulation of cellular response to hypoxia regulation of biological process regulation of cellular process response to stimulus cellular response to oxygen levels cellular response to hypoxia regulation of cellular response to stress biological regulation cellular response to decreased oxygen levels cellular response to chemical stimulus cellular response to stress regulation of response to stimulus response to hypoxia regulation of response to stress response to stress response to chemical response to oxygen levels cellular process response to abiotic stimulus regulation of protein stability regulation of biological quality protein stabilization developmental process regulation of muscle tissue development regulation of developmental process skeletal muscle tissue development negative regulation of developmental process animal organ development negative regulation of biological process tissue development negative regulation of muscle tissue development regulation of skeletal muscle tissue development muscle structure development skeletal muscle organ development anatomical structure development muscle tissue development muscle organ development negative regulation of skeletal muscle tissue development protein deubiquitination organonitrogen compound metabolic process primary metabolic process organic substance metabolic process protein modification by small protein removal macromolecule modification metabolic process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein modification by small protein conjugation or removal response to organic substance catabolic process proteolysis involved in protein catabolic process regulation of response to endoplasmic reticulum stress macromolecule catabolic process regulation of primary metabolic process ERAD pathway regulation of proteolysis involved in protein catabolic process regulation of proteolysis proteolysis regulation of ERAD pathway response to endoplasmic reticulum stress organonitrogen compound catabolic process response to organonitrogen compound regulation of protein metabolic process proteasomal protein catabolic process response to nitrogen compound regulation of macromolecule metabolic process protein catabolic process regulation of catabolic process regulation of proteasomal protein catabolic process regulation of metabolic process organic substance catabolic process regulation of protein catabolic process regulation of cell cycle process positive regulation of biological process positive regulation of cell cycle positive regulation of cell cycle process cell cycle regulation of cell cycle positive regulation of cellular process cell cycle process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle organelle subcompartment membrane intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum subcompartment intracellular organelle organelle nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle organelle subcompartment membrane intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum subcompartment intracellular organelle organelle nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR028889	Ubiquitin specific protease domain	Domain
A	IPR002893	Zinc finger, MYND-type	Domain
A	IPR018200	Ubiquitin specific protease, conserved site	Conserved Site
A	IPR007052	CS domain	Domain
A	IPR001394	Peptidase C19, ubiquitin carboxyl-terminal hydrolase	Domain
A	IPR038765	Papain-like cysteine peptidase superfamily	Homologous Superfamily
A	IPR008978	HSP20-like chaperone	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: O94966	endogenous depression myocardial infarction endometriosis osteosarcoma heart disease psoriasis

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.