Annotations: 2Y43

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2y43a_	Small proteins	RING/U-box	RING/U-box	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2y43b_	Small proteins	RING/U-box	RING/U-box	automated matches	automated matches	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	SCOP2B Superfamily	RING/U-box like	8079715	3000160	SCOP2B (2022-06-29)
B	SCOP2 Family	RING finger domain C3HC4	8079714	4000374	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	RING/U-box like	8079715	3000160	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	PF13923	e2y43A1	A: few secondary structure elements	X: RING/U-box-like	H: RING/U-box-like	T: RING/U-box	F: PF13923	ECOD (1.6)
B	PF13923	e2y43B1	A: few secondary structure elements	X: RING/U-box-like	H: RING/U-box-like	T: RING/U-box	F: PF13923	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.40.10	Alpha Beta	2-Layer Sandwich	Herpes Virus-1	Zinc/RING finger domain, C3HC4 (zinc finger)	CATH (4.3.0)
B	3.30.40.10	Alpha Beta	2-Layer Sandwich	Herpes Virus-1	Zinc/RING finger domain, C3HC4 (zinc finger)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF13923	Zinc finger, C3HC4 type (RING finger) (zf-C3HC4_2)	Zinc finger, C3HC4 type (RING finger)	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	E3 UBIQUITIN-PROTEIN LIGASE RAD18	molecular function inhibitor activity molecular function regulator activity DNA secondary structure binding DNA binding binding organic cyclic compound binding Y-form DNA binding nucleic acid binding damaged DNA binding aminoacyltransferase activity ubiquitin-like protein transferase activity catalytic activity, acting on a protein acyltransferase activity ubiquitin-like protein ligase activity molecular function inhibitor activity molecular function regulator activity DNA secondary structure binding DNA binding binding organic cyclic compound binding Y-form DNA binding nucleic acid binding damaged DNA binding aminoacyltransferase activity ubiquitin-like protein transferase activity catalytic activity, acting on a protein acyltransferase activity ubiquitin-like protein ligase activity ubiquitin protein ligase activity transferase activity catalytic activity ubiquitin-protein transferase activity protein-containing complex binding polyubiquitin modification-dependent protein binding protein binding modification-dependent protein binding ubiquitin protein ligase binding ubiquitin-like protein ligase binding enzyme binding cation binding ion binding metal ion binding small molecule binding identical protein binding single-stranded DNA binding	cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process organonitrogen compound metabolic process protein autoubiquitination primary metabolic process organic substance metabolic process protein ubiquitination macromolecule modification metabolic process protein metabolic process cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process organonitrogen compound metabolic process protein autoubiquitination primary metabolic process organic substance metabolic process protein ubiquitination macromolecule modification metabolic process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein modification by small protein conjugation protein modification by small protein conjugation or removal positive regulation of chromosome segregation regulation of chromosome segregation regulation of biological process regulation of cellular process regulation of cell cycle process biological regulation positive regulation of biological process positive regulation of cell cycle positive regulation of cell cycle process cell cycle regulation of cell cycle chromosome segregation positive regulation of cellular process cell cycle process postreplication repair DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA repair protein monoubiquitination	intracellular organelle centrosome microtubule organizing center intracellular anatomical structure cytoskeleton organelle intracellular non-membrane-bounded organelle cellular anatomical entity microtubule cytoskeleton non-membrane-bounded organelle cytoplasm membrane-bounded organelle nucleus membrane-enclosed lumen intracellular organelle centrosome microtubule organizing center intracellular anatomical structure cytoskeleton organelle intracellular non-membrane-bounded organelle cellular anatomical entity microtubule cytoskeleton non-membrane-bounded organelle cytoplasm membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen replication fork chromosome Rad6-Rad18 complex protein-containing complex ubiquitin ligase complex catalytic complex transferase complex intracellular protein-containing complex inclusion body nuclear inclusion body site of double-strand break site of DNA damage nuclear body

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036361	SAP domain superfamily	Homologous Superfamily
A, B	IPR039577	E3 ubiquitin-protein ligase Rad18	Family
A, B	IPR017907	Zinc finger, RING-type, conserved site	Conserved Site
A, B	IPR013083	Zinc finger, RING/FYVE/PHD-type	Homologous Superfamily
A, B	IPR003034	SAP domain	Domain
A, B	IPR006642	Rad18, zinc finger UBZ4-type	Domain
A, B	IPR001841	Zinc finger, RING-type	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: Q9NS91	atypical teratoid rhabdoid tumor malignant glioma pancreatic intraductal papillary-mucinous carcinoma glioblastoma medulloblastoma pancreatic intraductal papillary-mucinous neoplasm large cell medulloblastoma osteosarcoma primitive neuroectodermal tumor

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.