Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5K1A

Crystal structure of the UAF1-USP12 complex in C2 space group

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004843	molecular_function	cysteine-type deubiquitinase activity
A	0016579	biological_process	protein deubiquitination
B	0000724	biological_process	double-strand break repair via homologous recombination
B	0003677	molecular_function	DNA binding
B	0003690	molecular_function	double-stranded DNA binding
B	0003697	molecular_function	single-stranded DNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005764	cellular_component	lysosome
B	0005770	cellular_component	late endosome
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006281	biological_process	DNA repair
B	0006974	biological_process	DNA damage response
B	0035800	molecular_function	deubiquitinase activator activity
B	0043130	molecular_function	ubiquitin binding
B	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
B	0060255	biological_process	regulation of macromolecule metabolic process
B	0080090	biological_process	regulation of primary metabolic process
B	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
B	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
B	1905368	cellular_component	peptidase complex
C	0004843	molecular_function	cysteine-type deubiquitinase activity
C	0016579	biological_process	protein deubiquitination
D	0000724	biological_process	double-strand break repair via homologous recombination
D	0003677	molecular_function	DNA binding
D	0003690	molecular_function	double-stranded DNA binding
D	0003697	molecular_function	single-stranded DNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005764	cellular_component	lysosome
D	0005770	cellular_component	late endosome
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006281	biological_process	DNA repair
D	0006974	biological_process	DNA damage response
D	0035800	molecular_function	deubiquitinase activator activity
D	0043130	molecular_function	ubiquitin binding
D	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
D	0060255	biological_process	regulation of macromolecule metabolic process
D	0080090	biological_process	regulation of primary metabolic process
D	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
D	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
D	1905368	cellular_component	peptidase complex
E	0004843	molecular_function	cysteine-type deubiquitinase activity
E	0016579	biological_process	protein deubiquitination
F	0000724	biological_process	double-strand break repair via homologous recombination
F	0003677	molecular_function	DNA binding
F	0003690	molecular_function	double-stranded DNA binding
F	0003697	molecular_function	single-stranded DNA binding
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005737	cellular_component	cytoplasm
F	0005764	cellular_component	lysosome
F	0005770	cellular_component	late endosome
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0006281	biological_process	DNA repair
F	0006974	biological_process	DNA damage response
F	0035800	molecular_function	deubiquitinase activator activity
F	0043130	molecular_function	ubiquitin binding
F	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
F	0060255	biological_process	regulation of macromolecule metabolic process
F	0080090	biological_process	regulation of primary metabolic process
F	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
F	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
F	1905368	cellular_component	peptidase complex
G	0004843	molecular_function	cysteine-type deubiquitinase activity
G	0016579	biological_process	protein deubiquitination
H	0000724	biological_process	double-strand break repair via homologous recombination
H	0003677	molecular_function	DNA binding
H	0003690	molecular_function	double-stranded DNA binding
H	0003697	molecular_function	single-stranded DNA binding
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005654	cellular_component	nucleoplasm
H	0005737	cellular_component	cytoplasm
H	0005764	cellular_component	lysosome
H	0005770	cellular_component	late endosome
H	0005829	cellular_component	cytosol
H	0005886	cellular_component	plasma membrane
H	0006281	biological_process	DNA repair
H	0006974	biological_process	DNA damage response
H	0035800	molecular_function	deubiquitinase activator activity
H	0043130	molecular_function	ubiquitin binding
H	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
H	0060255	biological_process	regulation of macromolecule metabolic process
H	0080090	biological_process	regulation of primary metabolic process
H	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
H	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
H	1905368	cellular_component	peptidase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 401

Chain	Residue
A	CYS186
A	CYS189
A	CYS233
A	CYS236

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN C 401

Chain	Residue
C	CYS186
C	CYS189
C	CYS233
C	CYS236

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN E 401

Chain	Residue
E	CYS189
E	CYS233
E	CYS236
E	CYS186

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN G 401

Chain	Residue
G	CYS186
G	CYS189
G	CYS233
G	CYS236

Functional Information from PROSITE/UniProt

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LISAssDtTVKVWNA

Chain	Residue	Details
B	LEU90-ALA104
B	VAL132-VAL146

site_id	PS00972
Number of Residues	16
Details	USP_1 Ubiquitin specific protease (USP) domain signature 1. GLvnfGNtCYCNSvLQ

Chain	Residue	Details
A	GLY40-GLN55

site_id	PS00973
Number of Residues	19
Details	USP_2 Ubiquitin specific protease (USP) domain signature 2. YdLvAVvvHcGsgpnr.GHY

Chain	Residue	Details
A	TYR300-TYR318

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01035","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27373336","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01035","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PDB","id":"5K16","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L8W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PDB","id":"5K16","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L8W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	156
Details	Repeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	156
Details	Repeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	156
Details	Repeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	156
Details	Repeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	156
Details	Repeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	156
Details	Repeat: {"description":"WD 6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	156
Details	Repeat: {"description":"WD 8","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BH57","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)