6Y5D

Structure of human cGAS (K394E) bound to the nucleosome

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0030527	molecular_function	structural constituent of chromatin
A	0046982	molecular_function	protein heterodimerization activity
B	0000781	cellular_component	chromosome, telomeric region
B	0000786	cellular_component	nucleosome
B	0003677	molecular_function	DNA binding
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005694	cellular_component	chromosome
B	0006325	biological_process	chromatin organization
B	0006334	biological_process	nucleosome assembly
B	0016020	cellular_component	membrane
B	0030527	molecular_function	structural constituent of chromatin
B	0032200	biological_process	telomere organization
B	0032991	cellular_component	protein-containing complex
B	0043505	cellular_component	CENP-A containing nucleosome
B	0045653	biological_process	negative regulation of megakaryocyte differentiation
B	0046982	molecular_function	protein heterodimerization activity
B	0061644	biological_process	protein localization to CENP-A containing chromatin
B	0070062	cellular_component	extracellular exosome
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0030527	molecular_function	structural constituent of chromatin
C	0031507	biological_process	heterochromatin formation
C	0046982	molecular_function	protein heterodimerization activity
C	0070062	cellular_component	extracellular exosome
D	0000786	cellular_component	nucleosome
D	0002227	biological_process	innate immune response in mucosa
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005615	cellular_component	extracellular space
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005694	cellular_component	chromosome
D	0005829	cellular_component	cytosol
D	0019731	biological_process	antibacterial humoral response
D	0030527	molecular_function	structural constituent of chromatin
D	0031640	biological_process	killing of cells of another organism
D	0042742	biological_process	defense response to bacterium
D	0046982	molecular_function	protein heterodimerization activity
D	0050829	biological_process	defense response to Gram-negative bacterium
D	0050830	biological_process	defense response to Gram-positive bacterium
D	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0030527	molecular_function	structural constituent of chromatin
E	0046982	molecular_function	protein heterodimerization activity
F	0000781	cellular_component	chromosome, telomeric region
F	0000786	cellular_component	nucleosome
F	0003677	molecular_function	DNA binding
F	0003723	molecular_function	RNA binding
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005694	cellular_component	chromosome
F	0006325	biological_process	chromatin organization
F	0006334	biological_process	nucleosome assembly
F	0016020	cellular_component	membrane
F	0030527	molecular_function	structural constituent of chromatin
F	0032200	biological_process	telomere organization
F	0032991	cellular_component	protein-containing complex
F	0043505	cellular_component	CENP-A containing nucleosome
F	0045653	biological_process	negative regulation of megakaryocyte differentiation
F	0046982	molecular_function	protein heterodimerization activity
F	0061644	biological_process	protein localization to CENP-A containing chromatin
F	0070062	cellular_component	extracellular exosome
G	0000786	cellular_component	nucleosome
G	0003677	molecular_function	DNA binding
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005694	cellular_component	chromosome
G	0030527	molecular_function	structural constituent of chromatin
G	0031507	biological_process	heterochromatin formation
G	0046982	molecular_function	protein heterodimerization activity
G	0070062	cellular_component	extracellular exosome
H	0000786	cellular_component	nucleosome
H	0002227	biological_process	innate immune response in mucosa
H	0003677	molecular_function	DNA binding
H	0005515	molecular_function	protein binding
H	0005615	cellular_component	extracellular space
H	0005634	cellular_component	nucleus
H	0005654	cellular_component	nucleoplasm
H	0005694	cellular_component	chromosome
H	0005829	cellular_component	cytosol
H	0019731	biological_process	antibacterial humoral response
H	0030527	molecular_function	structural constituent of chromatin
H	0031640	biological_process	killing of cells of another organism
H	0042742	biological_process	defense response to bacterium
H	0046982	molecular_function	protein heterodimerization activity
H	0050829	biological_process	defense response to Gram-negative bacterium
H	0050830	biological_process	defense response to Gram-positive bacterium
H	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
M	0000786	cellular_component	nucleosome
M	0003677	molecular_function	DNA binding
M	0030527	molecular_function	structural constituent of chromatin
M	0046982	molecular_function	protein heterodimerization activity
N	0000781	cellular_component	chromosome, telomeric region
N	0000786	cellular_component	nucleosome
N	0003677	molecular_function	DNA binding
N	0003723	molecular_function	RNA binding
N	0005515	molecular_function	protein binding
N	0005576	cellular_component	extracellular region
N	0005634	cellular_component	nucleus
N	0005654	cellular_component	nucleoplasm
N	0005694	cellular_component	chromosome
N	0006325	biological_process	chromatin organization
N	0006334	biological_process	nucleosome assembly
N	0016020	cellular_component	membrane
N	0030527	molecular_function	structural constituent of chromatin
N	0032200	biological_process	telomere organization
N	0032991	cellular_component	protein-containing complex
N	0043505	cellular_component	CENP-A containing nucleosome
N	0045653	biological_process	negative regulation of megakaryocyte differentiation
N	0046982	molecular_function	protein heterodimerization activity
N	0061644	biological_process	protein localization to CENP-A containing chromatin
N	0070062	cellular_component	extracellular exosome
O	0000786	cellular_component	nucleosome
O	0003677	molecular_function	DNA binding
O	0005515	molecular_function	protein binding
O	0005634	cellular_component	nucleus
O	0005694	cellular_component	chromosome
O	0030527	molecular_function	structural constituent of chromatin
O	0031507	biological_process	heterochromatin formation
O	0046982	molecular_function	protein heterodimerization activity
O	0070062	cellular_component	extracellular exosome
P	0000786	cellular_component	nucleosome
P	0002227	biological_process	innate immune response in mucosa
P	0003677	molecular_function	DNA binding
P	0005515	molecular_function	protein binding
P	0005615	cellular_component	extracellular space
P	0005634	cellular_component	nucleus
P	0005654	cellular_component	nucleoplasm
P	0005694	cellular_component	chromosome
P	0005829	cellular_component	cytosol
P	0019731	biological_process	antibacterial humoral response
P	0030527	molecular_function	structural constituent of chromatin
P	0031640	biological_process	killing of cells of another organism
P	0042742	biological_process	defense response to bacterium
P	0046982	molecular_function	protein heterodimerization activity
P	0050829	biological_process	defense response to Gram-negative bacterium
P	0050830	biological_process	defense response to Gram-positive bacterium
P	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
Q	0000786	cellular_component	nucleosome
Q	0003677	molecular_function	DNA binding
Q	0030527	molecular_function	structural constituent of chromatin
Q	0046982	molecular_function	protein heterodimerization activity
R	0000781	cellular_component	chromosome, telomeric region
R	0000786	cellular_component	nucleosome
R	0003677	molecular_function	DNA binding
R	0003723	molecular_function	RNA binding
R	0005515	molecular_function	protein binding
R	0005576	cellular_component	extracellular region
R	0005634	cellular_component	nucleus
R	0005654	cellular_component	nucleoplasm
R	0005694	cellular_component	chromosome
R	0006325	biological_process	chromatin organization
R	0006334	biological_process	nucleosome assembly
R	0016020	cellular_component	membrane
R	0030527	molecular_function	structural constituent of chromatin
R	0032200	biological_process	telomere organization
R	0032991	cellular_component	protein-containing complex
R	0043505	cellular_component	CENP-A containing nucleosome
R	0045653	biological_process	negative regulation of megakaryocyte differentiation
R	0046982	molecular_function	protein heterodimerization activity
R	0061644	biological_process	protein localization to CENP-A containing chromatin
R	0070062	cellular_component	extracellular exosome
S	0000786	cellular_component	nucleosome
S	0003677	molecular_function	DNA binding
S	0005515	molecular_function	protein binding
S	0005634	cellular_component	nucleus
S	0005694	cellular_component	chromosome
S	0030527	molecular_function	structural constituent of chromatin
S	0031507	biological_process	heterochromatin formation
S	0046982	molecular_function	protein heterodimerization activity
S	0070062	cellular_component	extracellular exosome
T	0000786	cellular_component	nucleosome
T	0002227	biological_process	innate immune response in mucosa
T	0003677	molecular_function	DNA binding
T	0005515	molecular_function	protein binding
T	0005615	cellular_component	extracellular space
T	0005634	cellular_component	nucleus
T	0005654	cellular_component	nucleoplasm
T	0005694	cellular_component	chromosome
T	0005829	cellular_component	cytosol
T	0019731	biological_process	antibacterial humoral response
T	0030527	molecular_function	structural constituent of chromatin
T	0031640	biological_process	killing of cells of another organism
T	0042742	biological_process	defense response to bacterium
T	0046982	molecular_function	protein heterodimerization activity
T	0050829	biological_process	defense response to Gram-negative bacterium
T	0050830	biological_process	defense response to Gram-positive bacterium
T	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue PTD A 201

Chain	Residue
A	LYS80
B	LYS80

---

site_id	AC2
Number of Residues	2
Details	binding site for residue PTD C 201

Chain	Residue
C	LYS100
G	LYS100

---

site_id	AC3
Number of Residues	1
Details	binding site for residue ZN K 601

Chain	Residue
K	CYS396

---

site_id	AC4
Number of Residues	1
Details	binding site for residue ZN L 601

Chain	Residue
L	CYS396

---

site_id	AC5
Number of Residues	7
Details	binding site for Di-peptide PTD G 701 and LYS K 355

Chain	Residue
K	LEU352
K	ARG353
K	LEU354
K	PRO356
G	ARG72
G	LYS75
K	TRP330

---

site_id	AC6
Number of Residues	5
Details	binding site for Di-peptide PTD H 301 and LYS H 35

Chain	Residue
D	LYS86
H	ARG34
H	GLU36
I	DC126
I	DA127

---

site_id	AC7
Number of Residues	6
Details	binding site for Di-peptide PTD H 302 and LYS H 86

Chain	Residue
C	LYS37
H	ALA82
H	HIS83
H	TYR84
H	ASN85
H	ARG87

---

site_id	AC8
Number of Residues	5
Details	binding site for Di-peptide PTD M 201 and LYS M 80

Chain	Residue
M	ALA76
M	GLN77
M	PHE79
M	THR81
N	LYS80

---

site_id	AC9
Number of Residues	9
Details	binding site for Di-peptide PTD M 201 and LYS N 80

Chain	Residue
M	ALA76
M	GLN77
M	PHE79
M	THR81
M	ASP82
M	LEU83
M	ARG84
N	ARG79
N	THR81

---

site_id	AD1
Number of Residues	5
Details	binding site for Di-peptide PTD O 201 and LYS O 100

Chain	Residue
O	LEU98
O	GLY99
O	VAL101
O	THR102
S	LYS100

---

site_id	AD2
Number of Residues	9
Details	binding site for Di-peptide PTD O 201 and LYS S 100

Chain	Residue
N	GLY95
O	LEU98
O	GLY99
O	VAL101
O	THR102
S	LEU98
S	GLY99
S	VAL101
S	THR102

---

site_id	AD3
Number of Residues	6
Details	binding site for Di-peptide PTD S 701 and LYS S 75

Chain	Residue
L	LYS355
S	ALA71
S	ARG72
S	ASP73
S	ASN74
S	LYS76

---

site_id	AD4
Number of Residues	5
Details	binding site for Di-peptide PTD S 701 and LYS L 355

Chain	Residue
L	LEU352
L	ARG353
L	LEU354
L	PRO356
S	LYS75

---

site_id	AD5
Number of Residues	8
Details	binding site for Di-peptide PTD S 702 and LYS S 37

Chain	Residue
P	LYS86
S	ARG33
S	LEU34
S	LEU35
S	ARG36
S	GLY38
S	ASN39
S	TYR40

---

site_id	AD6
Number of Residues	14
Details	binding site for Di-peptide PTD S 702 and LYS P 86

Chain	Residue
P	ALA82
P	HIS83
P	TYR84
P	ASN85
P	ARG87
S	LYS37
S	ARG82
S	HIS83
S	LEU84
S	GLN85
S	ALA87
S	ILE88
S	ARG89
S	ASN90

---

Functional Information from PROSITE/UniProt

site_id	PS00046
Number of Residues	7
Details	HISTONE_H2A Histone H2A signature. AGLqFPV

Chain	Residue	Details
C	ALA22-VAL28

---

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
B	GLY15-HIS19

---

site_id	PS00357
Number of Residues	23
Details	HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG

Chain	Residue	Details
D	ARG93-GLY115

---

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
A	PRO67-ILE75

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q8C6L5

Chain	Residue	Details
K	THR211
L	THR211
P	PRO2
T	PRO2

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0007744|PDB:6CTA

Chain	Residue	Details
K	SER213
K	SER380
K	LYS414
L	SER213
L	SER380
L	LYS414

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0000305|PubMed:23722159, ECO:0000305|PubMed:26229115, ECO:0007744|PDB:6CT9, ECO:0007744|PDB:6CTA

Chain	Residue	Details
K	GLU225
H	LYS12
H	LYS16
H	LYS17
H	LYS21
H	LYS24
H	LYS44
H	LYS86
P	LYS6
P	LYS12
P	LYS16
K	ASP227
P	LYS17
P	LYS21
P	LYS24
P	LYS44
P	LYS86
T	LYS6
T	LYS12
T	LYS16
T	LYS17
T	LYS21
L	GLU225
T	LYS24
T	LYS44
T	LYS86
L	ASP227
D	LYS21
D	LYS24
D	LYS44
D	LYS86
H	LYS6

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0007744|PDB:6CT9, ECO:0007744|PDB:6CTA

Chain	Residue	Details
K	ASP319
L	ASP319
P	SER7
T	SER7
O	LYS10
O	LYS96
S	LYS10
S	LYS96

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:31113940, ECO:0007744|PDB:4O67, ECO:0007744|PDB:6MJX

Chain	Residue	Details
K	LYS362
R	LYS9
R	LYS17
R	LYS45
K	ARG376
L	LYS362
L	ARG376
F	LYS17
F	LYS45
N	LYS9
N	LYS17
N	LYS45

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:23707061, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28934246, ECO:0000269|PubMed:28940468, ECO:0000269|PubMed:30007416, ECO:0000269|PubMed:31113940, ECO:0000269|PubMed:31142647, ECO:0000269|PubMed:32911482, ECO:0000269|PubMed:32912999, ECO:0007744|PDB:5V8O, ECO:0007744|PDB:5VDO, ECO:0007744|PDB:5VDP, ECO:0007744|PDB:5VDQ, ECO:0007744|PDB:5VDR, ECO:0007744|PDB:5VDS, ECO:0007744|PDB:5VDT, ECO:0007744|PDB:5VDU, ECO:0007744|PDB:5VDV, ECO:0007744|PDB:5VDW, ECO:0007744|PDB:6CT9, ECO:0007744|PDB:6CTA, ECO:0007744|PDB:6EDB, ECO:0007744|PDB:6EDC, ECO:0007744|PDB:6MJU, ECO:0007744|PDB:6MJW, ECO:0007744|PDB:6MJX, ECO:0007744|PDB:6NAO, ECO:0007744|PDB:6NFG, ECO:0007744|PDB:6NFO, ECO:0007744|PDB:6Y5D, ECO:0007744|PDB:6Y5E, ECO:0007744|PDB:7C0M

Chain	Residue	Details
K	HIS390
N	LYS32
N	LYS78
N	LYS92
R	LYS13
R	LYS32
R	LYS78
R	LYS92
L	HIS390
P	SER15
T	SER15
F	LYS13
F	LYS32
F	LYS78
F	LYS92
N	LYS13

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:23707061, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28934246, ECO:0000269|PubMed:28940468, ECO:0000269|PubMed:30007416, ECO:0000269|PubMed:31113940, ECO:0000269|PubMed:31142647, ECO:0000269|PubMed:32459092, ECO:0000269|PubMed:32911482, ECO:0000269|PubMed:32912999, ECO:0007744|PDB:5V8O, ECO:0007744|PDB:5VDO, ECO:0007744|PDB:5VDP, ECO:0007744|PDB:5VDQ, ECO:0007744|PDB:5VDR, ECO:0007744|PDB:5VDS, ECO:0007744|PDB:5VDT, ECO:0007744|PDB:5VDU, ECO:0007744|PDB:5VDV, ECO:0007744|PDB:5VDW, ECO:0007744|PDB:6CT9, ECO:0007744|PDB:6CTA, ECO:0007744|PDB:6EDB, ECO:0007744|PDB:6EDC, ECO:0007744|PDB:6LRC, ECO:0007744|PDB:6MJU, ECO:0007744|PDB:6MJW, ECO:0007744|PDB:6MJX, ECO:0007744|PDB:6NAO, ECO:0007744|PDB:6NFG, ECO:0007744|PDB:6NFO, ECO:0007744|PDB:6O47, ECO:0007744|PDB:6Y5D, ECO:0007744|PDB:6Y5E, ECO:0007744|PDB:7C0M

Chain	Residue	Details
K	CYS396
K	CYS397
K	CYS404
L	CYS396
L	CYS397
L	CYS404
S	LYS75
S	LYS76

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0000305|PubMed:24462292, ECO:0007744|PDB:6CTA

Chain	Residue	Details
K	SER435
T	LYS35
T	LYS117
T	LYS121
L	SER435
D	LYS121
H	LYS35
H	LYS117
H	LYS121
P	LYS35
P	LYS117
P	LYS121

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	SITE: Important for preferential detection of curved long DNA => ECO:0000269|PubMed:30007416

Chain	Residue	Details
K	LYS187
K	LEU195
L	LYS187
L	LEU195

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	SITE: Arginine-anchor => ECO:0000269|PubMed:32911482, ECO:0000269|PubMed:32912999, ECO:0000269|PubMed:33051594

Chain	Residue	Details
K	ARG255
S	LYS119
S	LYS120
S	LYS126
L	ARG255
P	SER37
T	SER37
G	LYS120
G	LYS126
O	LYS119
O	LYS120
O	LYS126

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	SITE: Cleavage; by CASP3 => ECO:0000269|PubMed:30878284

Chain	Residue	Details
K	ASP319
L	ASP319
H	LYS47
H	LYS109
P	LYS47
P	LYS109
T	LYS47
T	LYS109

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269|PubMed:35460603

Chain	Residue	Details
K	ASP191
L	ASP191
P	LYS58
T	LYS58

---

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:30092200

Chain	Residue	Details
K	ASN210
K	ASN389
L	ASN210
L	ASN389
O	LYS120
S	LYS120

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:33273464

Chain	Residue	Details
K	SER213
L	SER213
H	ARG87
H	ARG93
P	ARG87
P	ARG93
T	ARG87
T	ARG93

---

site_id	SWS_FT_FI15
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by BLK => ECO:0000269|PubMed:30356214

Chain	Residue	Details
K	TYR215
L	TYR215
P	THR116
T	THR116
N	LYS92
R	LYS92

---

site_id	SWS_FT_FI16
Number of Residues	2
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q8C6L5

Chain	Residue	Details
K	GLU286
R	LYS21
R	LYS60
R	LYS80
L	GLU286
P	SER113
T	SER113
F	LYS60
F	LYS80
N	LYS21
N	LYS60
N	LYS80

---

site_id	SWS_FT_FI17
Number of Residues	2
Details	MOD_RES: Phosphoserine; by CDK1 and PKB => ECO:0000269|PubMed:26440888, ECO:0000269|PubMed:32351706, ECO:0000269|PubMed:33542149

Chain	Residue	Details
K	SER305
L	SER305
P	LYS6
T	LYS6

---

site_id	SWS_FT_FI18
Number of Residues	2
Details	MOD_RES: 5-glutamyl glutamate => ECO:0000250|UniProtKB:Q8C6L5

Chain	Residue	Details
K	GLU314
L	GLU314
H	LYS121
P	LYS121
T	LYS121

---

site_id	SWS_FT_FI19
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039

Chain	Residue	Details
K	LYS384
K	LYS392
K	GLU394
L	LYS384
L	LYS392
L	GLU394

---

site_id	SWS_FT_FI20
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039, ECO:0007744|PubMed:19608861

Chain	Residue	Details
K	LYS414
L	LYS414
P	LYS35
T	LYS35

---

site_id	SWS_FT_FI21
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:32474700

Chain	Residue	Details
K	SER434
K	SER435
L	SER434
L	SER435

---

site_id	SWS_FT_FI22
Number of Residues	4
Details	MOD_RES: (Microbial infection) Deamidated glutamine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:30092200

Chain	Residue	Details
K	GLN451
K	GLN454
L	GLN451
L	GLN454

---

site_id	SWS_FT_FI23
Number of Residues	2
Details	MOD_RES: N6-methyllysine => ECO:0000269|PubMed:35210392

Chain	Residue	Details
K	LYS506
L	LYS506

---

site_id	SWS_FT_FI24
Number of Residues	4
Details	LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:37802025

Chain	Residue	Details
K	CYS404
K	CYS405
L	CYS404
L	CYS405

---

site_id	SWS_FT_FI25
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:35438208

Chain	Residue	Details
K	CYS474
L	CYS474

---

site_id	SWS_FT_FI26
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:28273161

Chain	Residue	Details
K	LYS173
L	LYS173

---

site_id	SWS_FT_FI27
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:27637147

Chain	Residue	Details
K	LYS479
L	LYS479

---

site_id	SWS_FT_FI28
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:27637147

Chain	Residue	Details
K	LYS231
L	LYS231

---

site_id	SWS_FT_FI29
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27637147

Chain	Residue	Details
K	LYS285
L	LYS285

---

site_id	SWS_FT_FI30
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:Q8C6L5

Chain	Residue	Details
K	LYS347
L	LYS347

---

site_id	SWS_FT_FI31
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:28273161

Chain	Residue	Details
K	LYS384
L	LYS384

---

site_id	SWS_FT_FI32
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250|UniProtKB:Q8C6L5

Chain	Residue	Details
K	GLU394
L	GLU394

---

site_id	SWS_FT_FI33
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:35503863

Chain	Residue	Details
K	LYS411
L	LYS411

---

site_id	SWS_FT_FI34
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27666593

Chain	Residue	Details
K	LYS414
L	LYS414

---

site_id	SWS_FT_FI35
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:38418882

Chain	Residue	Details
K	LYS427
K	LYS428
L	LYS427
L	LYS428

---