CGAS_HUMAN - dbPTM
CGAS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CGAS_HUMAN
UniProt AC Q8N884
Protein Name Cyclic GMP-AMP synthase {ECO:0000303|PubMed:23258413}
Gene Name CGAS {ECO:0000312|HGNC:HGNC:21367}
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Cytoplasm, cytosol . Upon transfection with dsDNA forms punctate structures that co-localize with DNA and Beclin-1 (BECN1) (PubMed:26048138).
(Microbial infection) Upon infection with virulent M.tuberculosis forms aggregates with dsDNA, non-vir
Protein Description Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (cGAMP) from ATP and GTP. [PubMed: 23258413]
Protein Sequence MQPWHGKAMQRASEAGATAPKASARNARGAPMDPTESPAAPEAALPKAGKFGPARKSGSRQKKSAPDTQERPPVRATGARAKKAPQRAQDTQPSDATSAPGAEGLEPPAAREPALSRAGSCRQRGARCSTKPRPPPGPWDVPSPGLPVSAPILVRRDAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPRIQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEKISVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTCCENKEEKCCRKDCLKLMKYLLEQLKERFKDKKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLRTEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MQPWHGKA
-------CCCCCHHH
-
7Methylation-MQPWHGKAMQRASE
-CCCCCHHHHHHHHH
19608861
7Acetylation-MQPWHGKAMQRASE
-CCCCCHHHHHHHHH
19608861
13PhosphorylationGKAMQRASEAGATAP
HHHHHHHHHHCCCCC
25159151
18PhosphorylationRASEAGATAPKASAR
HHHHHCCCCCHHHHC
20860994
37PhosphorylationAPMDPTESPAAPEAA
CCCCCCCCCCCCHHH
-
50AcetylationAALPKAGKFGPARKS
HHCCCCCCCCCCCCC
19608861
64PhosphorylationSGSRQKKSAPDTQER
CCCCCCCCCCCCCCC
24732914
68PhosphorylationQKKSAPDTQERPPVR
CCCCCCCCCCCCCCH
24732914
77PhosphorylationERPPVRATGARAKKA
CCCCCHHHCHHHHCC
28555341
82MethylationRATGARAKKAPQRAQ
HHHCHHHHCCCCCCC
-
91PhosphorylationAPQRAQDTQPSDATS
CCCCCCCCCCCCCCC
29214152
116PhosphorylationAAREPALSRAGSCRQ
HHCCCHHHCCCCHHH
20068231
120PhosphorylationPALSRAGSCRQRGAR
CHHHCCCCHHHCCCC
20068231
129PhosphorylationRQRGARCSTKPRPPP
HHCCCCCCCCCCCCC
21712546
131AcetylationRGARCSTKPRPPPGP
CCCCCCCCCCCCCCC
26051181
143PhosphorylationPGPWDVPSPGLPVSA
CCCCCCCCCCCCCCC
25159151
163PhosphorylationRDAAPGASKLRAVLE
CCCCCCHHHHHHHHH
22210691
164UbiquitinationDAAPGASKLRAVLEK
CCCCCHHHHHHHHHH
29967540
171AcetylationKLRAVLEKLKLSRDD
HHHHHHHHHCCCHHH
26051181
173UbiquitinationRAVLEKLKLSRDDIS
HHHHHHHCCCHHHHH
29967540
175PhosphorylationVLEKLKLSRDDISTA
HHHHHCCCHHHHHHH
-
181PhosphorylationLSRDDISTAAGMVKG
CCHHHHHHHHHHHHH
-
198AcetylationDHLLLRLKCDSAFRG
HHHHHHHHCCCCCCC
-
198UbiquitinationDHLLLRLKCDSAFRG
HHHHHHHHCCCCCCC
33845483
201PhosphorylationLLRLKCDSAFRGVGL
HHHHHCCCCCCCCEE
-
210DeamidationFRGVGLLNTGSYYEH
CCCCEECCCCCCEEE
30092200
215PhosphorylationLLNTGSYYEHVKISA
ECCCCCCEEEEEECC
30356214
221PhosphorylationYYEHVKISAPNEFDV
CEEEEEECCCCCEEE
-
231SumoylationNEFDVMFKLEVPRIQ
CCEEEEEEEECCCEE
-
231SumoylationNEFDVMFKLEVPRIQ
CCEEEEEEEECCCEE
-
248PhosphorylationEYSNTRAYYFVKFKR
ECCCCEEEEEEEECC
22817900
263PhosphorylationNPKENPLSQFLEGEI
CCCCCCHHHHHHHHH
-
282UbiquitinationKMLSKFRKIIKEEIN
HHHHHHHHHHHHHHH
29967540
285SumoylationSKFRKIIKEEINDIK
HHHHHHHHHHHHCCC
-
285UbiquitinationSKFRKIIKEEINDIK
HHHHHHHHHHHHCCC
29967540
285AcetylationSKFRKIIKEEINDIK
HHHHHHHHHHHHCCC
26051181
285SumoylationSKFRKIIKEEINDIK
HHHHHHHHHHHHCCC
-
286Formation of an isopeptide bondKFRKIIKEEINDIKD
HHHHHHHHHHHCCCC
-
2865-glutamyl polyglutamateKFRKIIKEEINDIKD
HHHHHHHHHHHCCCC
-
292UbiquitinationKEEINDIKDTDVIMK
HHHHHCCCCCCHHHH
29967540
292AcetylationKEEINDIKDTDVIMK
HHHHHCCCCCCHHHH
-
294PhosphorylationEINDIKDTDVIMKRK
HHHCCCCCCHHHHCC
20068231
301MethylationTDVIMKRKRGGSPAV
CCHHHHCCCCCCCCH
23644510
305PhosphorylationMKRKRGGSPAVTLLI
HHCCCCCCCCHHEEE
25159151
313PhosphorylationPAVTLLISEKISVDI
CCHHEEEECCCCEEE
24719451
314Formation of an isopeptide bondAVTLLISEKISVDIT
CHHEEEECCCCEEEE
-
347UbiquitinationIQNWLSAKVRKQLRL
HHHHHHHHHHHHHCC
22817900
347UbiquitinationIQNWLSAKVRKQLRL
HHHHHHHHHHHHHCC
21890473
347 (in isoform 2)Ubiquitination-21890473
347 (in isoform 1)Ubiquitination-21890473
350UbiquitinationWLSAKVRKQLRLKPF
HHHHHHHHHHCCCCE
22817900
355UbiquitinationVRKQLRLKPFYLVPK
HHHHHCCCCEEECCC
22817900
355 (in isoform 2)Ubiquitination-21890473
355UbiquitinationVRKQLRLKPFYLVPK
HHHHHCCCCEEECCC
21890473
355 (in isoform 1)Ubiquitination-21890473
355AcetylationVRKQLRLKPFYLVPK
HHHHHCCCCEEECCC
-
362MethylationKPFYLVPKHAKEGNG
CCEEECCCCCCCCCC
-
365UbiquitinationYLVPKHAKEGNGFQE
EECCCCCCCCCCCCC
29967540
374PhosphorylationGNGFQEETWRLSFSH
CCCCCCEEEEEEHHH
29083192
378PhosphorylationQEETWRLSFSHIEKE
CCEEEEEEHHHHHHH
28674419
384UbiquitinationLSFSHIEKEILNNHG
EEHHHHHHHHHHCCC
30799039
384SumoylationLSFSHIEKEILNNHG
EEHHHHHHHHHHCCC
30799039
384AcetylationLSFSHIEKEILNNHG
EEHHHHHHHHHHCCC
30799039
389DeamidationIEKEILNNHGKSKTC
HHHHHHHCCCCCCCC
30092200
392UbiquitinationEILNNHGKSKTCCEN
HHHHCCCCCCCCCCC
30799039
392AcetylationEILNNHGKSKTCCEN
HHHHCCCCCCCCCCC
20167786
394SumoylationLNNHGKSKTCCENKE
HHCCCCCCCCCCCCC
30799039
394AcetylationLNNHGKSKTCCENKE
HHCCCCCCCCCCCCC
20167786
411UbiquitinationCCRKDCLKLMKYLLE
HCHHHHHHHHHHHHH
23000965
411AcetylationCCRKDCLKLMKYLLE
HCHHHHHHHHHHHHH
26051181
414 (in isoform 2)Ubiquitination-21890473
414AcetylationKDCLKLMKYLLEQLK
HHHHHHHHHHHHHHH
19608861
414 (in isoform 1)Ubiquitination-21890473
414UbiquitinationKDCLKLMKYLLEQLK
HHHHHHHHHHHHHHH
21890473
414UbiquitinationKDCLKLMKYLLEQLK
HHHHHHHHHHHHHHH
23000965
415PhosphorylationDCLKLMKYLLEQLKE
HHHHHHHHHHHHHHH
19664995
421UbiquitinationKYLLEQLKERFKDKK
HHHHHHHHHHHCCHH
29967540
432AcetylationKDKKHLDKFSSYHVK
CCHHHHHHHHHHHHH
26051181
432UbiquitinationKDKKHLDKFSSYHVK
CCHHHHHHHHHHHHH
29967540
439AcetylationKFSSYHVKTAFFHVC
HHHHHHHHEEEEEHH
26051181
451DeamidationHVCTQNPQDSQWDRK
EHHHCCCCCCCCCHH
30092200
454DeamidationTQNPQDSQWDRKDLG
HCCCCCCCCCHHHHH
30092200
479SumoylationLQCLRTEKLENYFIP
HHHHHHHHHHHHCCC
-
479SumoylationLQCLRTEKLENYFIP
HHHHHHHHHHHHCCC
-
479AcetylationLQCLRTEKLENYFIP
HHHHHHHHHHHHCCC
-
501UbiquitinationNLIDKRSKEFLTKQI
CCCCHHHHHHHHHHH
22817900
506UbiquitinationRSKEFLTKQIEYERN
HHHHHHHHHHHHHHC
22817900
506UbiquitinationRSKEFLTKQIEYERN
HHHHHHHHHHHHHHC
21890473
506 (in isoform 1)Ubiquitination-21890473

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
215YPhosphorylationKinaseBLKP51451
Uniprot
305SPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
210NAmidation

30092200
384KAcetylation

30356214
394KAcetylation

30799039
414KAcetylation

19608861

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CGAS_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN593_HUMANZNF593physical
28514442
RN185_HUMANRNF185physical
28273161

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CGAS_HUMAN

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Related Literatures of Post-Translational Modification

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