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7BUQ

mcGAS bound with 23-cGAMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0002218biological_processactivation of innate immune response
A0002221biological_processpattern recognition receptor signaling pathway
A0002230biological_processpositive regulation of defense response to virus by host
A0002637biological_processregulation of immunoglobulin production
A0002753biological_processcytoplasmic pattern recognition receptor signaling pathway
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003690molecular_functiondouble-stranded DNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0008289molecular_functionlipid binding
A0008340biological_processdetermination of adult lifespan
A0016604cellular_componentnuclear body
A0016779molecular_functionnucleotidyltransferase activity
A0019933biological_processcAMP-mediated signaling
A0019934biological_processcGMP-mediated signaling
A0031491molecular_functionnucleosome binding
A0032479biological_processregulation of type I interferon production
A0032481biological_processpositive regulation of type I interferon production
A0035861cellular_componentsite of double-strand break
A0038001biological_processparacrine signaling
A0042803molecular_functionprotein homodimerization activity
A0045087biological_processinnate immune response
A0045738biological_processnegative regulation of DNA repair
A0046872molecular_functionmetal ion binding
A0050776biological_processregulation of immune response
A0050863biological_processregulation of T cell activation
A0051607biological_processdefense response to virus
A0061501molecular_function2',3'-cyclic GMP-AMP synthase activity
A0071360biological_processcellular response to exogenous dsRNA
A0140693molecular_functionmolecular condensate scaffold activity
A0140896biological_processcGAS/STING signaling pathway
A0160004molecular_functionpoly-ADP-D-ribose modification-dependent protein binding
A0160049biological_processnegative regulation of cGAS/STING signaling pathway
A2000042biological_processnegative regulation of double-strand break repair via homologous recombination
A2000774biological_processpositive regulation of cellular senescence
B0002218biological_processactivation of innate immune response
B0002221biological_processpattern recognition receptor signaling pathway
B0002230biological_processpositive regulation of defense response to virus by host
B0002637biological_processregulation of immunoglobulin production
B0002753biological_processcytoplasmic pattern recognition receptor signaling pathway
B0003677molecular_functionDNA binding
B0003682molecular_functionchromatin binding
B0003690molecular_functiondouble-stranded DNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006281biological_processDNA repair
B0006974biological_processDNA damage response
B0008289molecular_functionlipid binding
B0008340biological_processdetermination of adult lifespan
B0016604cellular_componentnuclear body
B0016779molecular_functionnucleotidyltransferase activity
B0019933biological_processcAMP-mediated signaling
B0019934biological_processcGMP-mediated signaling
B0031491molecular_functionnucleosome binding
B0032479biological_processregulation of type I interferon production
B0032481biological_processpositive regulation of type I interferon production
B0035861cellular_componentsite of double-strand break
B0038001biological_processparacrine signaling
B0042803molecular_functionprotein homodimerization activity
B0045087biological_processinnate immune response
B0045738biological_processnegative regulation of DNA repair
B0046872molecular_functionmetal ion binding
B0050776biological_processregulation of immune response
B0050863biological_processregulation of T cell activation
B0051607biological_processdefense response to virus
B0061501molecular_function2',3'-cyclic GMP-AMP synthase activity
B0071360biological_processcellular response to exogenous dsRNA
B0140693molecular_functionmolecular condensate scaffold activity
B0140896biological_processcGAS/STING signaling pathway
B0160004molecular_functionpoly-ADP-D-ribose modification-dependent protein binding
B0160049biological_processnegative regulation of cGAS/STING signaling pathway
B2000042biological_processnegative regulation of double-strand break repair via homologous recombination
B2000774biological_processpositive regulation of cellular senescence
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 601
ChainResidue
AHIS378
ACYS384
ACYS385
ACYS392

site_idAC2
Number of Residues10
Detailsbinding site for residue 1SY A 602
ChainResidue
AARG364
ASER366
ASER368
AGLU371
AHOH701
AILE206
AMET215
AASP307
AILE309
ALYS350

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 601
ChainResidue
BHIS378
BCYS384
BCYS385
BCYS392

site_idAC4
Number of Residues13
Detailsbinding site for residue 1SY B 602
ChainResidue
BGLU211
BASP213
BMET215
BPRO292
BASP307
BILE309
BVAL348
BLYS350
BARG364
BSER366
BSER368
BCYS419
BTYR421

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:23647843
ChainResidueDetails
AGLU211
AASP213
AASP307
AGLU371
ALYS402
ASER420
BTHR197
BSER199
BGLU211
BASP213
BASP307
BGLU371
BLYS402
BSER420
ATHR197
ASER199

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:24332030, ECO:0007744|PDB:4LEZ
ChainResidueDetails
AARG364
BGLY290
BLYS350
BARG364
AGLY290
ALYS350

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23647843, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28902841, ECO:0000269|PubMed:28963528, ECO:0000269|PubMed:32814054, ECO:0000269|PubMed:32911481, ECO:0000269|PubMed:32913000, ECO:0007744|PDB:5N6I, ECO:0007744|PDB:5XZB, ECO:0007744|PDB:5XZE, ECO:0007744|PDB:5XZG, ECO:0007744|PDB:6X59, ECO:0007744|PDB:7BUJ, ECO:0007744|PDB:7BUM, ECO:0007744|PDB:7BUQ, ECO:0007744|PDB:7JO9, ECO:0007744|PDB:7JOA
ChainResidueDetails
BCYS384
AHIS378
ACYS384
BHIS378

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:23647843, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28902841, ECO:0000269|PubMed:28963528, ECO:0000269|PubMed:32814054, ECO:0000269|PubMed:32911481, ECO:0000269|PubMed:32913000, ECO:0007744|PDB:5N6I, ECO:0007744|PDB:5XZB, ECO:0007744|PDB:5XZE, ECO:0007744|PDB:5XZG, ECO:0007744|PDB:6XJD, ECO:0007744|PDB:7BUJ, ECO:0007744|PDB:7BUM, ECO:0007744|PDB:7BUQ, ECO:0007744|PDB:7JO9, ECO:0007744|PDB:7JOA
ChainResidueDetails
BCYS385
ACYS385

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:23647843, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28902841, ECO:0000269|PubMed:28963528, ECO:0000269|PubMed:32814054, ECO:0000269|PubMed:32911480, ECO:0000269|PubMed:32911481, ECO:0000269|PubMed:32913000, ECO:0007744|PDB:5N6I, ECO:0007744|PDB:5XZB, ECO:0007744|PDB:5XZE, ECO:0007744|PDB:5XZG, ECO:0007744|PDB:6X5A, ECO:0007744|PDB:7BUJ, ECO:0007744|PDB:7BUM, ECO:0007744|PDB:7BUQ, ECO:0007744|PDB:7JO9, ECO:0007744|PDB:7JOA
ChainResidueDetails
ACYS392
BCYS392

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Arginine-anchor => ECO:0000269|PubMed:31808743, ECO:0000269|PubMed:32911480, ECO:0000269|PubMed:32911481, ECO:0000269|PubMed:32913000
ChainResidueDetails
AARG241
BARG241

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Cleavage; by CASP3 => ECO:0000250|UniProtKB:Q8N884
ChainResidueDetails
AASP307
BASP307

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8N884
ChainResidueDetails
BTHR52
ATHR52

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269|PubMed:35460603
ChainResidueDetails
BGLU176
AGLU176

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8N884
ChainResidueDetails
BSER199
ASER199

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q8N884
ChainResidueDetails
ATYR201
BTYR201

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000269|PubMed:26829768
ChainResidueDetails
BGLU272
AGLU272

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 and PKB => ECO:0000269|PubMed:26440888, ECO:0000269|PubMed:32351706
ChainResidueDetails
BSER291
ASER291

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: 5-glutamyl glutamate => ECO:0000269|PubMed:26829768
ChainResidueDetails
BGLU302
AGLU302

site_idSWS_FT_FI15
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8N884
ChainResidueDetails
ALYS402
BLYS372
BLYS382
BLYS402
ALYS382
ALYS372

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:32474700
ChainResidueDetails
BSER420
ASER420

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000269|PubMed:35210392
ChainResidueDetails
ALYS491
BLYS491

site_idSWS_FT_FI18
Number of Residues6
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q8N884
ChainResidueDetails
ACYS459
BCYS392
BCYS393
BCYS459
ACYS392
ACYS393

site_idSWS_FT_FI19
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:27637147
ChainResidueDetails
BLYS217
ALYS217

site_idSWS_FT_FI20
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:27637147, ECO:0000269|PubMed:32457395
ChainResidueDetails
BLYS464
ALYS464

site_idSWS_FT_FI21
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27637147, ECO:0000269|PubMed:32457395
ChainResidueDetails
ALYS271
BLYS271

site_idSWS_FT_FI22
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:29426904
ChainResidueDetails
ALYS335
BLYS335

site_idSWS_FT_FI23
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:Q8N884
ChainResidueDetails
ALYS372
BLYS372

site_idSWS_FT_FI24
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:28095500
ChainResidueDetails
ALYS382
BLYS382

site_idSWS_FT_FI25
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q8N884
ChainResidueDetails
BLYS399
BLYS402
ALYS399
ALYS402

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PDB entries from 2024-06-12

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