dbPTM

CASP8_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CASP8_MOUSE
UniProt AC	O89110
Protein Name	Caspase-8
Gene Name	Casp8
Organism	Mus musculus (Mouse).
Sequence Length	480
Subcellular Localization	Cytoplasm.
Protein Description	Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-\|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein..
Protein Sequence	MDFQSCLYAIAEELGSEDLAALKFLCLDYIPHKKQETIEDAQKLFLRLREKGMLEEGNLSFLKELLFHISRWDLLVNFLDCNREEMVRELRDPDNAQISPYRVMLFKLSEEVSELELRSFKFLLNNEIPKCKLEDDLSLLEIFVEMEKRTMLAENNLETLKSICDQVNKSLLGKIEDYERSSTERRMSLEGREELPPSVLDEMSLKMAELCDSPREQDSESRTSDKVYQMKNKPRGYCLIINNHDFSKAREDITQLRKMKDRKGTDCDKEALSKTFKELHFEIVSYDDCTANEIHEILEGYQSADHKNKDCFICCILSHGDKGVVYGTDGKEASIYDLTSYFTGSKCPSLSGKPKIFFIQACQGSNFQKGVPDEAGFEQQNHTLEVDSSSHKNYIPDEADFLLGMATVKNCVSYRDPVNGTWYIQSLCQSLRERCPQGDDILSILTGVNYDVSNKDDRRNKGKQMPQPTFTLRKKLFFPP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
170	Phosphorylation	ICDQVNKSLLGKIED HHHHHHHHHHHCHHH	24.51	26239621
181	Phosphorylation	KIEDYERSSTERRMS CHHHHHCCCHHHHHC	29.67	27818261
182	Phosphorylation	IEDYERSSTERRMSL HHHHHCCCHHHHHCC	40.27	27818261
183	Phosphorylation	EDYERSSTERRMSLE HHHHCCCHHHHHCCC	34.46	27818261
187	Oxidation	RSSTERRMSLEGREE CCCHHHHHCCCCCCC	7.21	17242355
188	Phosphorylation	SSTERRMSLEGREEL CCHHHHHCCCCCCCC	22.81	26824392
198	Phosphorylation	GREELPPSVLDEMSL CCCCCCHHHHHHHHH	33.11	28833060
204	Phosphorylation	PSVLDEMSLKMAELC HHHHHHHHHHHHHHC	23.84	28833060
207	Oxidation	LDEMSLKMAELCDSP HHHHHHHHHHHCCCC	4.20	17242355
211	Glutathionylation	SLKMAELCDSPREQD HHHHHHHCCCCCCCC	3.51	24333276
213	Phosphorylation	KMAELCDSPREQDSE HHHHHCCCCCCCCCC	25.51	27087446
219	Phosphorylation	DSPREQDSESRTSDK CCCCCCCCCCCCCCH	36.85	23984901
221	Phosphorylation	PREQDSESRTSDKVY CCCCCCCCCCCCHHH	44.82	23984901
223	Phosphorylation	EQDSESRTSDKVYQM CCCCCCCCCCHHHHC	51.02	23984901
224	Phosphorylation	QDSESRTSDKVYQMK CCCCCCCCCHHHHCC	34.03	23984901
226	Acetylation	SESRTSDKVYQMKNK CCCCCCCHHHHCCCC	42.48	23806337
336	Phosphorylation	DGKEASIYDLTSYFT CCCEEEEEEHHHHHC	11.47	-
389	Phosphorylation	HTLEVDSSSHKNYIP CEEEECCCCCCCCCC	31.81	-
463	Malonylation	DDRRNKGKQMPQPTF HHCCCCCCCCCCCCE	45.06	26320211

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
389	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
389	S	Phosphorylation		-
Phosphorylation on Ser-389 during mitosis by CDK1 inhibits activation by proteolysis and prevents apoptosis.

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 CASP8_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SQSTM_MOUSE	Sqstm1	physical	21628531
SQSTM_MOUSE	Sqstm1	physical	21576355
CYLD_MOUSE	Cyld	physical	22037414

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CASP8_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.	17242355 [Abstract]

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