CASP1_HUMAN - dbPTM
CASP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CASP1_HUMAN
UniProt AC P29466
Protein Name Caspase-1
Gene Name CASP1
Organism Homo sapiens (Human).
Sequence Length 404
Subcellular Localization Cytoplasm.
Protein Description Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. [PubMed: 28314590]
Protein Sequence MADKVLKEKRKLFIRSMGEGTINGLLDELLQTRVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAGTLGLSADQTSGNYLNMQDSQGVLSSFPAPQAVQDNPAMPTSSGSEGNVKLCSLEEAQRIWKQKSAEIYPIMDKSSRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFMSHGIREGICGKKHSEQVPDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDSVGVSGNLSLPTTEEFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTRCFYLFPGH
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
16PhosphorylationKRKLFIRSMGEGTIN
HHHHHHHHCCCCHHH		26.73-
21PhosphorylationIRSMGEGTINGLLDE
HHHCCCCHHHHHHHH		13.6327067055
28 (in isoform 5)Phosphorylation-51.8822210691
31 (in isoform 5)Phosphorylation-39.6322210691
32PhosphorylationLLDELLQTRVLNKEE
HHHHHHHHHCCCHHH		23.78-
36 (in isoform 4)Phosphorylation-47.0022210691
36 (in isoform 3)Phosphorylation-47.0022210691
37UbiquitinationLQTRVLNKEEMEKVK
HHHHCCCHHHHHHHH		51.39-
44UbiquitinationKEEMEKVKRENATVM
HHHHHHHHHHCCCHH		66.13-
49PhosphorylationKVKRENATVMDKTRA
HHHHHCCCHHHHHHH		28.1328348404
53UbiquitinationENATVMDKTRALIDS
HCCCHHHHHHHHHHH		23.09-
134UbiquitinationSGSEGNVKLCSLEEA
CCCCCCEEECCHHHH		48.02-
137PhosphorylationEGNVKLCSLEEAQRI
CCCEEECCHHHHHHH		49.6127067055
148UbiquitinationAQRIWKQKSAEIYPI
HHHHHHHHCCEEECC		48.16-
149PhosphorylationQRIWKQKSAEIYPIM
HHHHHHHCCEEECCC		28.7430108239
158UbiquitinationEIYPIMDKSSRTRLA
EEECCCCCCCCCEEE		32.71-
198 (in isoform 4)Phosphorylation-14.5330631047
203 (in isoform 4)Phosphorylation-31.32-
204UbiquitinationGYSVDVKKNLTASDM
CCCEEHHCCCCHHHH		57.97-
226PhosphorylationAHRPEHKTSDSTFLV
HCCCCCCCCCCEEEE		39.4130108239
227PhosphorylationHRPEHKTSDSTFLVF
CCCCCCCCCCEEEEE		34.0730108239
229PhosphorylationPEHKTSDSTFLVFMS
CCCCCCCCEEEEEEE		22.3330108239
230PhosphorylationEHKTSDSTFLVFMSH
CCCCCCCEEEEEEEC		26.4430108239
268UbiquitinationIFNMLNTKNCPSLKD
HHHHHCCCCCCCCCC		56.32-
274UbiquitinationTKNCPSLKDKPKVII
CCCCCCCCCCCEEEE		68.96-
278UbiquitinationPSLKDKPKVIIIQAC
CCCCCCCEEEEEEEC		52.38-
289PhosphorylationIQACRGDSPGVVWFK
EEECCCCCCCEEEEE		26.7821815630
302PhosphorylationFKDSVGVSGNLSLPT
EECCCCCCCCCCCCC		18.94-
306PhosphorylationVGVSGNLSLPTTEEF
CCCCCCCCCCCCHHH		35.9826657352
319UbiquitinationEFEDDAIKKAHIEKD
HHCCHHHHHHHHCCC		45.70-
320UbiquitinationFEDDAIKKAHIEKDF
HCCHHHHHHHHCCCE		38.80-
325UbiquitinationIKKAHIEKDFIAFCS
HHHHHHCCCEEEEEC		58.28-
339PhosphorylationSSTPDNVSWRHPTMG
CCCCCCCCCCCCCCC		25.33-
344PhosphorylationNVSWRHPTMGSVFIG
CCCCCCCCCCHHHHH		28.21-
362GlutathionylationEHMQEYACSCDVEEI
HHHHHHHHCCCHHHH		3.9922833525
376PhosphorylationIFRKVRFSFEQPDGR
HHHHHCEEEECCCCC		19.8015561713
388PhosphorylationDGRAQMPTTERVTLT
CCCCCCCCCCEEEEE		35.6323403867
389PhosphorylationGRAQMPTTERVTLTR
CCCCCCCCCEEEEEE		18.8723403867
397GlutathionylationERVTLTRCFYLFPGH
CEEEEEEEEECCCCC		1.9022833525
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
-KUbiquitinationE3 ubiquitin ligaseRNF31Q96EP0
PMID:32122970
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CASP1_HUMAN !!
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 CASP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NLRC4_HUMANNLRC4physical
15107016
NOD2_HUMANNOD2physical
15107016
XK_HUMANXKphysical
15107016
BAP31_HUMANBCAP31physical
9334338
RIPK2_HUMANRIPK2physical
9705938
IL37_HUMANIL37physical
12096920
IL18_HUMANIL18physical
12096920
EGFR_HUMANEGFRphysical
11226410
TIRAP_HUMANTIRAPphysical
20048342
CEBPB_HUMANCEBPBphysical
11684016
BIRC3_HUMANBIRC3physical
22195745
TRAF2_HUMANTRAF2physical
22195745
PARP1_HUMANPARP1physical
7642516
IL1B_HUMANIL1Bphysical
7642516
IL33_HUMANIL33physical
16286016
CED4_CAEELced-4physical
9027312
VAC14_HUMANVAC14physical
25416956
KIF3A_HUMANKIF3Aphysical
26186194
KIF11_HUMANKIF11physical
26186194
GAB1_HUMANGAB1physical
26186194
ARI4B_HUMANARID4Bphysical
26186194
PI4KB_HUMANPI4KBphysical
26186194
FMN2_HUMANFMN2physical
26186194
CAR16_HUMANCARD16physical
11432859
CASP1_HUMANCASP1physical
11432859
IF16_HUMANIFI16physical
26121674
BRCA1_HUMANBRCA1physical
26121674
PI4KB_HUMANPI4KBphysical
28514442
KIF3A_HUMANKIF3Aphysical
28514442
GAB1_HUMANGAB1physical
28514442
FMN2_HUMANFMN2physical
28514442
PLCL2_HUMANPLCL2physical
28514442
ARI4B_HUMANARID4Bphysical
28514442
KIF11_HUMANKIF11physical
28514442
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
DB01017Minocycline
Regulatory Network of CASP1_HUMAN

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Related Literatures of Post-Translational Modification

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