Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7LUP

Human TRiC/CCT complex with reovirus outer capsid protein sigma-3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005832	cellular_component	chaperonin-containing T-complex
A	0005874	cellular_component	microtubule
A	0006457	biological_process	protein folding
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0032212	biological_process	positive regulation of telomere maintenance via telomerase
A	0044183	molecular_function	protein folding chaperone
A	0050821	biological_process	protein stabilization
A	0051082	molecular_function	unfolded protein binding
A	0070062	cellular_component	extracellular exosome
A	0071987	molecular_function	WD40-repeat domain binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
A	1904851	biological_process	positive regulation of establishment of protein localization to telomere
A	1904871	biological_process	positive regulation of protein localization to Cajal body
A	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
B	0000166	molecular_function	nucleotide binding
B	0002199	cellular_component	zona pellucida receptor complex
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005813	cellular_component	centrosome
B	0005829	cellular_component	cytosol
B	0005832	cellular_component	chaperonin-containing T-complex
B	0005856	cellular_component	cytoskeleton
B	0005874	cellular_component	microtubule
B	0005929	cellular_component	cilium
B	0006457	biological_process	protein folding
B	0007339	biological_process	binding of sperm to zona pellucida
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0032212	biological_process	positive regulation of telomere maintenance via telomerase
B	0034774	cellular_component	secretory granule lumen
B	0035578	cellular_component	azurophil granule lumen
B	0042995	cellular_component	cell projection
B	0044183	molecular_function	protein folding chaperone
B	0044297	cellular_component	cell body
B	0045296	molecular_function	cadherin binding
B	0050821	biological_process	protein stabilization
B	0051082	molecular_function	unfolded protein binding
B	0070062	cellular_component	extracellular exosome
B	0140662	molecular_function	ATP-dependent protein folding chaperone
B	1904813	cellular_component	ficolin-1-rich granule lumen
B	1904871	biological_process	positive regulation of protein localization to Cajal body
B	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
C	0000166	molecular_function	nucleotide binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005832	cellular_component	chaperonin-containing T-complex
C	0005874	cellular_component	microtubule
C	0006457	biological_process	protein folding
C	0007339	biological_process	binding of sperm to zona pellucida
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0032212	biological_process	positive regulation of telomere maintenance via telomerase
C	0042802	molecular_function	identical protein binding
C	0044183	molecular_function	protein folding chaperone
C	0044297	cellular_component	cell body
C	0050821	biological_process	protein stabilization
C	0051082	molecular_function	unfolded protein binding
C	0070062	cellular_component	extracellular exosome
C	0140662	molecular_function	ATP-dependent protein folding chaperone
C	1904871	biological_process	positive regulation of protein localization to Cajal body
C	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
D	0000166	molecular_function	nucleotide binding
D	0003730	molecular_function	mRNA 3'-UTR binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005813	cellular_component	centrosome
D	0005829	cellular_component	cytosol
D	0005832	cellular_component	chaperonin-containing T-complex
D	0005856	cellular_component	cytoskeleton
D	0005874	cellular_component	microtubule
D	0006457	biological_process	protein folding
D	0007339	biological_process	binding of sperm to zona pellucida
D	0009615	biological_process	response to virus
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0031681	molecular_function	G-protein beta-subunit binding
D	0032212	biological_process	positive regulation of telomere maintenance via telomerase
D	0044183	molecular_function	protein folding chaperone
D	0044297	cellular_component	cell body
D	0048027	molecular_function	mRNA 5'-UTR binding
D	0048487	molecular_function	beta-tubulin binding
D	0050821	biological_process	protein stabilization
D	0051082	molecular_function	unfolded protein binding
D	0070062	cellular_component	extracellular exosome
D	0140662	molecular_function	ATP-dependent protein folding chaperone
D	1904871	biological_process	positive regulation of protein localization to Cajal body
D	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
E	0000166	molecular_function	nucleotide binding
E	0002199	cellular_component	zona pellucida receptor complex
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005576	cellular_component	extracellular region
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005832	cellular_component	chaperonin-containing T-complex
E	0005874	cellular_component	microtubule
E	0006457	biological_process	protein folding
E	0007339	biological_process	binding of sperm to zona pellucida
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0031625	molecular_function	ubiquitin protein ligase binding
E	0032212	biological_process	positive regulation of telomere maintenance via telomerase
E	0035578	cellular_component	azurophil granule lumen
E	0044183	molecular_function	protein folding chaperone
E	0044297	cellular_component	cell body
E	0050821	biological_process	protein stabilization
E	0051082	molecular_function	unfolded protein binding
E	0051131	biological_process	chaperone-mediated protein complex assembly
E	0070062	cellular_component	extracellular exosome
E	0090666	biological_process	scaRNA localization to Cajal body
E	0140662	molecular_function	ATP-dependent protein folding chaperone
E	1904871	biological_process	positive regulation of protein localization to Cajal body
E	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
F	0000166	molecular_function	nucleotide binding
F	0002199	cellular_component	zona pellucida receptor complex
F	0003723	molecular_function	RNA binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005654	cellular_component	nucleoplasm
F	0005737	cellular_component	cytoplasm
F	0005813	cellular_component	centrosome
F	0005829	cellular_component	cytosol
F	0005832	cellular_component	chaperonin-containing T-complex
F	0005856	cellular_component	cytoskeleton
F	0005874	cellular_component	microtubule
F	0006457	biological_process	protein folding
F	0007339	biological_process	binding of sperm to zona pellucida
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0032212	biological_process	positive regulation of telomere maintenance via telomerase
F	0042470	cellular_component	melanosome
F	0042995	cellular_component	cell projection
F	0044183	molecular_function	protein folding chaperone
F	0044297	cellular_component	cell body
F	0050821	biological_process	protein stabilization
F	0051082	molecular_function	unfolded protein binding
F	0070062	cellular_component	extracellular exosome
F	0090666	biological_process	scaRNA localization to Cajal body
F	0140662	molecular_function	ATP-dependent protein folding chaperone
F	1904871	biological_process	positive regulation of protein localization to Cajal body
F	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
G	0000166	molecular_function	nucleotide binding
G	0000242	cellular_component	pericentriolar material
G	0000792	cellular_component	heterochromatin
G	0001669	cellular_component	acrosomal vesicle
G	0002199	cellular_component	zona pellucida receptor complex
G	0003723	molecular_function	RNA binding
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005794	cellular_component	Golgi apparatus
G	0005813	cellular_component	centrosome
G	0005815	cellular_component	microtubule organizing center
G	0005829	cellular_component	cytosol
G	0005832	cellular_component	chaperonin-containing T-complex
G	0005856	cellular_component	cytoskeleton
G	0005874	cellular_component	microtubule
G	0006457	biological_process	protein folding
G	0007021	biological_process	tubulin complex assembly
G	0007339	biological_process	binding of sperm to zona pellucida
G	0016787	molecular_function	hydrolase activity
G	0016887	molecular_function	ATP hydrolysis activity
G	0031625	molecular_function	ubiquitin protein ligase binding
G	0032212	biological_process	positive regulation of telomere maintenance via telomerase
G	0044183	molecular_function	protein folding chaperone
G	0044297	cellular_component	cell body
G	0050821	biological_process	protein stabilization
G	0051082	molecular_function	unfolded protein binding
G	0070062	cellular_component	extracellular exosome
G	0090666	biological_process	scaRNA localization to Cajal body
G	0140535	cellular_component	intracellular protein-containing complex
G	0140662	molecular_function	ATP-dependent protein folding chaperone
G	1904851	biological_process	positive regulation of establishment of protein localization to telomere
G	1904871	biological_process	positive regulation of protein localization to Cajal body
G	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
H	0000166	molecular_function	nucleotide binding
H	0002199	cellular_component	zona pellucida receptor complex
H	0003723	molecular_function	RNA binding
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005832	cellular_component	chaperonin-containing T-complex
H	0005856	cellular_component	cytoskeleton
H	0005874	cellular_component	microtubule
H	0006457	biological_process	protein folding
H	0007339	biological_process	binding of sperm to zona pellucida
H	0016787	molecular_function	hydrolase activity
H	0016887	molecular_function	ATP hydrolysis activity
H	0032212	biological_process	positive regulation of telomere maintenance via telomerase
H	0044183	molecular_function	protein folding chaperone
H	0044297	cellular_component	cell body
H	0050821	biological_process	protein stabilization
H	0051082	molecular_function	unfolded protein binding
H	0070062	cellular_component	extracellular exosome
H	0140662	molecular_function	ATP-dependent protein folding chaperone
H	1904871	biological_process	positive regulation of protein localization to Cajal body
H	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
I	0000166	molecular_function	nucleotide binding
I	0003723	molecular_function	RNA binding
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0005832	cellular_component	chaperonin-containing T-complex
I	0005874	cellular_component	microtubule
I	0006457	biological_process	protein folding
I	0016787	molecular_function	hydrolase activity
I	0016887	molecular_function	ATP hydrolysis activity
I	0032212	biological_process	positive regulation of telomere maintenance via telomerase
I	0044183	molecular_function	protein folding chaperone
I	0050821	biological_process	protein stabilization
I	0051082	molecular_function	unfolded protein binding
I	0070062	cellular_component	extracellular exosome
I	0071987	molecular_function	WD40-repeat domain binding
I	0140662	molecular_function	ATP-dependent protein folding chaperone
I	1904851	biological_process	positive regulation of establishment of protein localization to telomere
I	1904871	biological_process	positive regulation of protein localization to Cajal body
I	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
J	0000166	molecular_function	nucleotide binding
J	0002199	cellular_component	zona pellucida receptor complex
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005576	cellular_component	extracellular region
J	0005737	cellular_component	cytoplasm
J	0005813	cellular_component	centrosome
J	0005829	cellular_component	cytosol
J	0005832	cellular_component	chaperonin-containing T-complex
J	0005856	cellular_component	cytoskeleton
J	0005874	cellular_component	microtubule
J	0005929	cellular_component	cilium
J	0006457	biological_process	protein folding
J	0007339	biological_process	binding of sperm to zona pellucida
J	0016787	molecular_function	hydrolase activity
J	0016887	molecular_function	ATP hydrolysis activity
J	0032212	biological_process	positive regulation of telomere maintenance via telomerase
J	0034774	cellular_component	secretory granule lumen
J	0035578	cellular_component	azurophil granule lumen
J	0042995	cellular_component	cell projection
J	0044183	molecular_function	protein folding chaperone
J	0044297	cellular_component	cell body
J	0045296	molecular_function	cadherin binding
J	0050821	biological_process	protein stabilization
J	0051082	molecular_function	unfolded protein binding
J	0070062	cellular_component	extracellular exosome
J	0140662	molecular_function	ATP-dependent protein folding chaperone
J	1904813	cellular_component	ficolin-1-rich granule lumen
J	1904871	biological_process	positive regulation of protein localization to Cajal body
J	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
K	0000166	molecular_function	nucleotide binding
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0005832	cellular_component	chaperonin-containing T-complex
K	0005874	cellular_component	microtubule
K	0006457	biological_process	protein folding
K	0007339	biological_process	binding of sperm to zona pellucida
K	0016787	molecular_function	hydrolase activity
K	0016887	molecular_function	ATP hydrolysis activity
K	0032212	biological_process	positive regulation of telomere maintenance via telomerase
K	0042802	molecular_function	identical protein binding
K	0044183	molecular_function	protein folding chaperone
K	0044297	cellular_component	cell body
K	0050821	biological_process	protein stabilization
K	0051082	molecular_function	unfolded protein binding
K	0070062	cellular_component	extracellular exosome
K	0140662	molecular_function	ATP-dependent protein folding chaperone
K	1904871	biological_process	positive regulation of protein localization to Cajal body
K	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
L	0000166	molecular_function	nucleotide binding
L	0003730	molecular_function	mRNA 3'-UTR binding
L	0005515	molecular_function	protein binding
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0005813	cellular_component	centrosome
L	0005829	cellular_component	cytosol
L	0005832	cellular_component	chaperonin-containing T-complex
L	0005856	cellular_component	cytoskeleton
L	0005874	cellular_component	microtubule
L	0006457	biological_process	protein folding
L	0007339	biological_process	binding of sperm to zona pellucida
L	0009615	biological_process	response to virus
L	0016787	molecular_function	hydrolase activity
L	0016887	molecular_function	ATP hydrolysis activity
L	0031681	molecular_function	G-protein beta-subunit binding
L	0032212	biological_process	positive regulation of telomere maintenance via telomerase
L	0044183	molecular_function	protein folding chaperone
L	0044297	cellular_component	cell body
L	0048027	molecular_function	mRNA 5'-UTR binding
L	0048487	molecular_function	beta-tubulin binding
L	0050821	biological_process	protein stabilization
L	0051082	molecular_function	unfolded protein binding
L	0070062	cellular_component	extracellular exosome
L	0140662	molecular_function	ATP-dependent protein folding chaperone
L	1904871	biological_process	positive regulation of protein localization to Cajal body
L	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
M	0000166	molecular_function	nucleotide binding
M	0002199	cellular_component	zona pellucida receptor complex
M	0005515	molecular_function	protein binding
M	0005524	molecular_function	ATP binding
M	0005576	cellular_component	extracellular region
M	0005737	cellular_component	cytoplasm
M	0005829	cellular_component	cytosol
M	0005832	cellular_component	chaperonin-containing T-complex
M	0005874	cellular_component	microtubule
M	0006457	biological_process	protein folding
M	0007339	biological_process	binding of sperm to zona pellucida
M	0016787	molecular_function	hydrolase activity
M	0016887	molecular_function	ATP hydrolysis activity
M	0031625	molecular_function	ubiquitin protein ligase binding
M	0032212	biological_process	positive regulation of telomere maintenance via telomerase
M	0035578	cellular_component	azurophil granule lumen
M	0044183	molecular_function	protein folding chaperone
M	0044297	cellular_component	cell body
M	0050821	biological_process	protein stabilization
M	0051082	molecular_function	unfolded protein binding
M	0051131	biological_process	chaperone-mediated protein complex assembly
M	0070062	cellular_component	extracellular exosome
M	0090666	biological_process	scaRNA localization to Cajal body
M	0140662	molecular_function	ATP-dependent protein folding chaperone
M	1904871	biological_process	positive regulation of protein localization to Cajal body
M	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
N	0000166	molecular_function	nucleotide binding
N	0002199	cellular_component	zona pellucida receptor complex
N	0003723	molecular_function	RNA binding
N	0005515	molecular_function	protein binding
N	0005524	molecular_function	ATP binding
N	0005654	cellular_component	nucleoplasm
N	0005737	cellular_component	cytoplasm
N	0005813	cellular_component	centrosome
N	0005829	cellular_component	cytosol
N	0005832	cellular_component	chaperonin-containing T-complex
N	0005856	cellular_component	cytoskeleton
N	0005874	cellular_component	microtubule
N	0006457	biological_process	protein folding
N	0007339	biological_process	binding of sperm to zona pellucida
N	0016787	molecular_function	hydrolase activity
N	0016887	molecular_function	ATP hydrolysis activity
N	0032212	biological_process	positive regulation of telomere maintenance via telomerase
N	0042470	cellular_component	melanosome
N	0042995	cellular_component	cell projection
N	0044183	molecular_function	protein folding chaperone
N	0044297	cellular_component	cell body
N	0050821	biological_process	protein stabilization
N	0051082	molecular_function	unfolded protein binding
N	0070062	cellular_component	extracellular exosome
N	0090666	biological_process	scaRNA localization to Cajal body
N	0140662	molecular_function	ATP-dependent protein folding chaperone
N	1904871	biological_process	positive regulation of protein localization to Cajal body
N	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
O	0000166	molecular_function	nucleotide binding
O	0000242	cellular_component	pericentriolar material
O	0000792	cellular_component	heterochromatin
O	0001669	cellular_component	acrosomal vesicle
O	0002199	cellular_component	zona pellucida receptor complex
O	0003723	molecular_function	RNA binding
O	0005515	molecular_function	protein binding
O	0005524	molecular_function	ATP binding
O	0005737	cellular_component	cytoplasm
O	0005794	cellular_component	Golgi apparatus
O	0005813	cellular_component	centrosome
O	0005815	cellular_component	microtubule organizing center
O	0005829	cellular_component	cytosol
O	0005832	cellular_component	chaperonin-containing T-complex
O	0005856	cellular_component	cytoskeleton
O	0005874	cellular_component	microtubule
O	0006457	biological_process	protein folding
O	0007021	biological_process	tubulin complex assembly
O	0007339	biological_process	binding of sperm to zona pellucida
O	0016787	molecular_function	hydrolase activity
O	0016887	molecular_function	ATP hydrolysis activity
O	0031625	molecular_function	ubiquitin protein ligase binding
O	0032212	biological_process	positive regulation of telomere maintenance via telomerase
O	0044183	molecular_function	protein folding chaperone
O	0044297	cellular_component	cell body
O	0050821	biological_process	protein stabilization
O	0051082	molecular_function	unfolded protein binding
O	0070062	cellular_component	extracellular exosome
O	0090666	biological_process	scaRNA localization to Cajal body
O	0140535	cellular_component	intracellular protein-containing complex
O	0140662	molecular_function	ATP-dependent protein folding chaperone
O	1904851	biological_process	positive regulation of establishment of protein localization to telomere
O	1904871	biological_process	positive regulation of protein localization to Cajal body
O	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
P	0000166	molecular_function	nucleotide binding
P	0002199	cellular_component	zona pellucida receptor complex
P	0003723	molecular_function	RNA binding
P	0005515	molecular_function	protein binding
P	0005524	molecular_function	ATP binding
P	0005737	cellular_component	cytoplasm
P	0005829	cellular_component	cytosol
P	0005832	cellular_component	chaperonin-containing T-complex
P	0005856	cellular_component	cytoskeleton
P	0005874	cellular_component	microtubule
P	0006457	biological_process	protein folding
P	0007339	biological_process	binding of sperm to zona pellucida
P	0016787	molecular_function	hydrolase activity
P	0016887	molecular_function	ATP hydrolysis activity
P	0032212	biological_process	positive regulation of telomere maintenance via telomerase
P	0044183	molecular_function	protein folding chaperone
P	0044297	cellular_component	cell body
P	0050821	biological_process	protein stabilization
P	0051082	molecular_function	unfolded protein binding
P	0070062	cellular_component	extracellular exosome
P	0140662	molecular_function	ATP-dependent protein folding chaperone
P	1904871	biological_process	positive regulation of protein localization to Cajal body
P	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
Q	0003723	molecular_function	RNA binding
Q	0005198	molecular_function	structural molecule activity
Q	0008270	molecular_function	zinc ion binding
Q	0019028	cellular_component	viral capsid
Q	0019058	biological_process	viral life cycle
Q	0030291	molecular_function	protein serine/threonine kinase inhibitor activity
Q	0030430	cellular_component	host cell cytoplasm
Q	0039502	biological_process	symbiont-mediated suppression of host type I interferon-mediated signaling pathway
Q	0039580	biological_process	symbiont-mediated suppression of host PKR/eIFalpha signaling
Q	0039624	cellular_component	viral outer capsid
Q	0042025	cellular_component	host cell nucleus
Q	0044423	cellular_component	virion component
Q	0046872	molecular_function	metal ion binding
Q	0052170	biological_process	symbiont-mediated suppression of host innate immune response

Functional Information from PROSITE/UniProt

site_id	PS00028
Number of Residues	21
Details	ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cmh..ClgvVgslqrklkHlph..H

Chain	Residue	Details
Q	CYS51-HIS71

site_id	PS00107
Number of Residues	26
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGDGTTSVTVlAaellreaesl........IAKK

Chain	Residue	Details
M	VAL95-LYS120

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIADTGANVVVT

Chain	Residue	Details
J	ALA282-THR293

site_id	PS00750
Number of Residues	13
Details	TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML

Chain	Residue	Details
I	ARG35-LEU47
H	ARG38-LEU50
O	LYS33-LEU45
J	ARG44-VAL56
M	LYS40-LEU52
L	ARG49-MET61
K	ARG37-ILE49
N	ARG49-ILE61

site_id	PS00751
Number of Residues	17
Details	TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP

Chain	Residue	Details
I	LEU56-PRO72
H	MET59-PRO75
O	ILE54-PRO70
J	VAL65-PRO81
M	VAL63-PRO79
L	VAL70-GLN86
K	ILE58-PRO74
N	ILE70-PRO86

site_id	PS00995
Number of Residues	9
Details	TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT

Chain	Residue	Details
I	GLN84-THR92
H	GLN87-THR95
O	GLN82-THR90
J	GLN93-THR101
M	GLN91-THR99
L	GLN98-THR106
K	GLN86-THR94
N	GLN98-THR106

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	94
Details	Binding site: {"evidences":[{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7X3J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X3U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	30
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	40
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	38
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X3U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X3U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7WZ3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P80318","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X3U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P80313","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X3U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X3U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X3U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P80317","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI48
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI49
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI50
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI51
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI52
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11983","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI53
Number of Residues	22
Details	Zinc finger: {"description":"CCHC-type","evidences":[{"source":"PubMed","id":"11230122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)