Annotations: 6U75

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PINIT	e6u75A2	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: PINIT	ECOD (1.6)
A	zf-MIZ	e6u75A1	A: few secondary structure elements	X: RING/U-box-like	H: RING/U-box-like	T: RING/U-box	F: zf-MIZ	ECOD (1.6)
B	PINIT	e6u75B1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: PINIT	ECOD (1.6)
B	zf-MIZ	e6u75B2	A: few secondary structure elements	X: RING/U-box-like	H: RING/U-box-like	T: RING/U-box	F: zf-MIZ	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02891	MIZ/SP-RING zinc finger (zf-MIZ)	MIZ/SP-RING zinc finger	This domain has SUMO (small ubiquitin-like modifier) ligase activity and is involved in DNA repair and chromosome organisation [2][3].	Domain
A, B	PF14324	PINIT domain (PINIT)	PINIT domain	The PINIT domain is a protein domain that is found in PIAS proteins [2]. The PINIT domain is about 180 amino acids in length.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	E3 SUMO-protein ligase SIZ2	aminoacyltransferase activity ubiquitin-like protein transferase activity catalytic activity, acting on a protein acyltransferase activity SUMO transferase activity transferase activity catalytic activity SUMO ligase activity ubiquitin-like protein ligase activity DNA binding double-stranded DNA binding binding organic cyclic compound binding nucleic acid binding aminoacyltransferase activity ubiquitin-like protein transferase activity catalytic activity, acting on a protein acyltransferase activity SUMO transferase activity transferase activity catalytic activity SUMO ligase activity ubiquitin-like protein ligase activity DNA binding double-stranded DNA binding binding organic cyclic compound binding nucleic acid binding cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding	localization DNA double-strand break attachment to nuclear envelope chromosome localization organelle localization chromosome attachment to the nuclear envelope cellular process cell cycle cell cycle process chromosome segregation organonitrogen compound metabolic process peptidyl-lysine modification primary metabolic process organic substance metabolic process protein sumoylation localization DNA double-strand break attachment to nuclear envelope chromosome localization organelle localization chromosome attachment to the nuclear envelope cellular process cell cycle cell cycle process chromosome segregation organonitrogen compound metabolic process peptidyl-lysine modification primary metabolic process organic substance metabolic process protein sumoylation macromolecule modification peptidyl-amino acid modification metabolic process protein metabolic process macromolecule metabolic process protein modification process post-translational protein modification protein modification by small protein conjugation protein modification by small protein conjugation or removal	intracellular anatomical structure cytoplasm cellular anatomical entity intracellular organelle protein-containing complex protein-DNA complex organelle intracellular non-membrane-bounded organelle chromatin chromosome non-membrane-bounded organelle membrane-bounded organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004181	Zinc finger, MIZ-type	Domain
A, B	IPR013083	Zinc finger, RING/FYVE/PHD-type	Homologous Superfamily
A, B	IPR003034	SAP domain	Domain
A, B	IPR036361	SAP domain superfamily	Homologous Superfamily
A, B	IPR031141	E3 SUMO-protein ligase SIZ1/2, SP-RING finger	Domain
A, B	IPR023321	PINIT domain	Domain
A, B	IPR038654	PINIT domain superfamily	Homologous Superfamily

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.