2FUN
alternative p35-caspase-8 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
A | 0006915 | biological_process | apoptotic process |
A | 0019049 | biological_process | virus-mediated perturbation of host defense response |
A | 0033668 | biological_process | symbiont-mediated suppression of host apoptosis |
A | 0043027 | molecular_function | cysteine-type endopeptidase inhibitor activity involved in apoptotic process |
A | 0043066 | biological_process | negative regulation of apoptotic process |
A | 0052150 | biological_process | symbiont-mediated perturbation of host apoptosis |
A | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
A | 0140533 | biological_process | symbiont-mediated suppression of host RNAi-mediated antiviral immune response |
B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008234 | molecular_function | cysteine-type peptidase activity |
C | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
C | 0006915 | biological_process | apoptotic process |
C | 0019049 | biological_process | virus-mediated perturbation of host defense response |
C | 0033668 | biological_process | symbiont-mediated suppression of host apoptosis |
C | 0043027 | molecular_function | cysteine-type endopeptidase inhibitor activity involved in apoptotic process |
C | 0043066 | biological_process | negative regulation of apoptotic process |
C | 0052150 | biological_process | symbiont-mediated perturbation of host apoptosis |
C | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
C | 0140533 | biological_process | symbiont-mediated suppression of host RNAi-mediated antiviral immune response |
D | 0004197 | molecular_function | cysteine-type endopeptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:10508785 |
Chain | Residue | Details |
B | HIS2317 | |
B | CYS2360 | |
D | HIS3317 | |
D | CYS3360 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by CASP6 => ECO:0000269|PubMed:22858542 |
Chain | Residue | Details |
B | ASP2374 | |
D | ASP3374 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Cleavage; by autocatalytic cleavage => ECO:0000269|PubMed:8962078, ECO:0000269|PubMed:9184224 |
Chain | Residue | Details |
B | ASP2384 | |
D | ASP3384 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O89110 |
Chain | Residue | Details |
B | LYS2224 | |
D | LYS3224 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
Chain | Residue | Details |
B | TYR2334 | |
D | TYR3334 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:16619028, ECO:0000269|PubMed:27109099 |
Chain | Residue | Details |
B | TYR2380 | |
D | TYR3380 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:20937773 |
Chain | Residue | Details |
B | SER2387 | |
D | SER3387 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120 |
Chain | Residue | Details |
B | ARG2413 | |
D | ARG3413 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1nw9 |
Chain | Residue | Details |
B | GLY2318 | |
B | CYS2360 | |
B | ARG2258 | |
B | HIS2317 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1nw9 |
Chain | Residue | Details |
D | HIS3317 | |
D | ARG3258 | |
D | GLY3318 | |
D | CYS3360 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1nw9 |
Chain | Residue | Details |
B | GLY2350 | |
B | CYS2360 | |
B | ARG2258 | |
B | HIS2317 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1nw9 |
Chain | Residue | Details |
D | GLY3350 | |
D | HIS3317 | |
D | ARG3258 | |
D | CYS3360 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1nw9 |
Chain | Residue | Details |
B | CYS2360 | |
B | GLY2318 | |
B | HIS2317 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1nw9 |
Chain | Residue | Details |
D | HIS3317 | |
D | GLY3318 | |
D | CYS3360 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 818 |
Chain | Residue | Details |
B | ARG2258 | electrostatic stabiliser |
B | HIS2317 | proton acceptor, proton donor |
B | GLY2318 | electrostatic stabiliser |
B | CYS2360 | nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 818 |
Chain | Residue | Details |
D | ARG3258 | electrostatic stabiliser |
D | HIS3317 | proton acceptor, proton donor |
D | GLY3318 | electrostatic stabiliser |
D | CYS3360 | nucleofuge, nucleophile, proton acceptor, proton donor |