dbPTM

CASP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CASP3_HUMAN
UniProt AC	P42574
Protein Name	Caspase-3
Gene Name	CASP3
Organism	Homo sapiens (Human).
Sequence Length	277
Subcellular Localization	Cytoplasm.
Protein Description	Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-\|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage..
Protein Sequence	MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MENTENSV -------CCCCCCCC	8.93	22223895
4	Phosphorylation	----MENTENSVDSK ----CCCCCCCCCHH	24.20	29978859
7	Phosphorylation	-MENTENSVDSKSIK -CCCCCCCCCHHHHH	22.52	29978859
10	Phosphorylation	NTENSVDSKSIKNLE CCCCCCCHHHHHCCC	26.58	29978859
11	Acetylation	TENSVDSKSIKNLEP CCCCCCHHHHHCCCC	52.30	23749302
11	Ubiquitination	TENSVDSKSIKNLEP CCCCCCHHHHHCCCC	52.30	-
11	Sumoylation	TENSVDSKSIKNLEP CCCCCCHHHHHCCCC	52.30	-
12	Phosphorylation	ENSVDSKSIKNLEPK CCCCCHHHHHCCCCE	42.63	29978859
14	Acetylation	SVDSKSIKNLEPKII CCCHHHHHCCCCEEE	63.67	25953088
14	Ubiquitination	SVDSKSIKNLEPKII CCCHHHHHCCCCEEE	63.67	32142685
19	Acetylation	SIKNLEPKIIHGSES HHHCCCCEEECCCCC	44.94	26051181
19	Ubiquitination	SIKNLEPKIIHGSES HHHCCCCEEECCCCC	44.94	29967540
23	Ubiquitination	LEPKIIHGSESMDSG CCCEEECCCCCCCCC	23.77	32142685
24	Phosphorylation	EPKIIHGSESMDSGI CCEEECCCCCCCCCC	16.61	23401153
26	Phosphorylation	KIIHGSESMDSGISL EEECCCCCCCCCCCC	29.59	23401153
29	Phosphorylation	HGSESMDSGISLDNS CCCCCCCCCCCCCCC	29.41	28450419
31	Ubiquitination	SESMDSGISLDNSYK CCCCCCCCCCCCCCC	4.24	32015554
35	Phosphorylation	DSGISLDNSYKMDYP CCCCCCCCCCCCCCC	53.16	32142685
41	Phosphorylation	DNSYKMDYPEMGLCI CCCCCCCCCCCEEEE	9.52	-
47	Glutathionylation	DYPEMGLCIIINNKN CCCCCEEEEEECCCC	1.41	22833525
57	Ubiquitination	INNKNFHKSTGMTSR ECCCCCCCCCCCCCC	45.64	32015554
65	Phosphorylation	STGMTSRSGTDVDAA CCCCCCCCCCCCCHH	45.90	-
66	Ubiquitination	TGMTSRSGTDVDAAN CCCCCCCCCCCCHHH	25.48	32015554
67	Phosphorylation	GMTSRSGTDVDAANL CCCCCCCCCCCHHHH	33.81	-
77	Phosphorylation	DAANLRETFRNLKYE CHHHHHHHHHHHHHH	22.82	28857561
82	Ubiquitination	RETFRNLKYEVRNKN HHHHHHHHHHHCCCC	42.80	27667366
82	Acetylation	RETFRNLKYEVRNKN HHHHHHHHHHHCCCC	42.80	19608861
88	Ubiquitination	LKYEVRNKNDLTREE HHHHHCCCCCCCHHH	41.07	29967540
105	Ubiquitination	ELMRDVSKEDHSKRS HHHHHCCHHHHHCCC	67.99	24816145
138	Ubiquitination	NGPVDLKKITNFFRG CCCCCHHHHHHCCCC	63.16	29967540
138	Malonylation	NGPVDLKKITNFFRG CCCCCHHHHHHCCCC	63.16	26320211
150	Phosphorylation	FRGDRCRSLTGKPKL CCCCCHHHCCCCCEE	33.63	22817900
152	Phosphorylation	GDRCRSLTGKPKLFI CCCHHHCCCCCEEEE	44.39	-
154	Ubiquitination	RCRSLTGKPKLFIIQ CHHHCCCCCEEEEEE	33.47	27667366
163	Glutathionylation	KLFIIQACRGTELDC EEEEEEECCCCCCCC	2.06	22833525
163	S-nitrosylation	KLFIIQACRGTELDC EEEEEEECCCCCCCC	2.06	10213689
163	S-nitrosocysteine	KLFIIQACRGTELDC EEEEEEECCCCCCCC	2.06	-
174	Phosphorylation	ELDCGIETDSGVDDD CCCCCCCCCCCCCCC	33.28	28348404
176	Phosphorylation	DCGIETDSGVDDDMA CCCCCCCCCCCCCCC	48.40	26657352
182	Sulfoxidation	DSGVDDDMACHKIPV CCCCCCCCCCCCCCC	5.72	30846556
184	Glutathionylation	GVDDDMACHKIPVEA CCCCCCCCCCCCCCC	2.42	22833525
210	Ubiquitination	YYSWRNSKDGSWFIQ EECCCCCCCCCHHHH	70.43	-
220	Glutathionylation	SWFIQSLCAMLKQYA CHHHHHHHHHHHHHH	2.24	22833525
224	Ubiquitination	QSLCAMLKQYADKLE HHHHHHHHHHHHHHH	28.33	23000965
229	Acetylation	MLKQYADKLEFMHIL HHHHHHHHHHHHHHH	41.57	25953088
229	Ubiquitination	MLKQYADKLEFMHIL HHHHHHHHHHHHHHH	41.57	23000965
249	Phosphorylation	KVATEFESFSFDATF HHHHCCCCCCCCEEE	31.35	-
260	Ubiquitination	DATFHAKKQIPCIVS CEEECHHHHHHHHHH	55.00	29967540
267	Phosphorylation	KQIPCIVSMLTKELY HHHHHHHHHHHCCHH	6.53	21406692
270	Phosphorylation	PCIVSMLTKELYFYH HHHHHHHHCCHHCCC	17.52	21406692

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
150	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	BIRC2	Q13490	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	XIAP	P98170	PMID:11447297
-	K	Ubiquitination	E3 ubiquitin ligase	BIRC3	Q13489	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CASP3_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 CASP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BCL2_HUMAN	BCL2	physical	11752215
BLM_HUMAN	BLM	physical	11470874
MCL1_HUMAN	MCL1	physical	15637055
TRAF3_HUMAN	TRAF3	physical	11261798
HCLS1_HUMAN	HCLS1	physical	11988074
DCC_HUMAN	DCC	physical	11248093
TRAF3_HUMAN	TRAF3	physical	11098060
CASP2_HUMAN	CASP2	physical	11399776
BID_HUMAN	BID	physical	11399776
PARG_HUMAN	PARG	physical	11053413
GORS1_HUMAN	GORASP1	physical	11815631
CASP6_HUMAN	CASP6	physical	8900201
SRC8_HUMAN	CTTN	physical	11689006
HCLS1_HUMAN	HCLS1	physical	11689006
DBNL_HUMAN	DBNL	physical	11689006
BMX_HUMAN	BMX	physical	11278797
CH60_HUMAN	HSPD1	physical	10205158
CH10_HUMAN	HSPE1	physical	10205158
CASP3_HUMAN	CASP3	physical	11257232
XIAP_HUMAN	XIAP	physical	11257232
USO1_HUMAN	USO1	physical	12438416
SRP72_CANLF	SRP72	physical	9857079
XIAP_HUMAN	XIAP	physical	9230442
GRAP1_HUMAN	GRIPAP1	physical	10896157
CH60_HUMAN	HSPD1	physical	10205159
NDUS1_HUMAN	NDUFS1	physical	15186778
RING2_HUMAN	RNF2	physical	17379327
GEMI_HUMAN	GMNN	physical	17261582
HEY2_HUMAN	HEY2	physical	17217622
RBX1_HUMAN	RBX1	physical	17217622
FBW1B_HUMAN	FBXW11	physical	17217622
FBW1A_HUMAN	BTRC	physical	17217622
THA11_HUMAN	THAP11	physical	18585351
MDC1_HUMAN	MDC1	physical	21148072
CSN6_HUMAN	COPS6	physical	17337451
CASP9_HUMAN	CASP9	physical	15507451
BIRC6_HUMAN	BIRC6	physical	15507451
CASP9_HUMAN	CASP9	physical	17437405
BIRC2_HUMAN	BIRC2	physical	11106668
XIAP_HUMAN	XIAP	physical	16869888
MDM2_HUMAN	MDM2	physical	9278461
XIAP_HUMAN	XIAP	physical	9525868
CRYAB_HUMAN	CRYAB	physical	18669646
PKN1_HUMAN	PKN1	physical	9751706
SP1_HUMAN	SP1	physical	10103059
GATA1_HUMAN	GATA1	physical	17167422
MK08_HUMAN	MAPK8	physical	12821118
MK09_HUMAN	MAPK9	physical	12821118
CDN1A_HUMAN	CDKN1A	physical	9660939
PARP1_HUMAN	PARP1	physical	7596430
RB_HUMAN	RB1	physical	15735701
PRKDC_HUMAN	PRKDC	physical	8804412
RB_HUMAN	RB1	physical	11420704
CDN1A_HUMAN	CDKN1A	physical	9799125
CDN1A_HUMAN	CDKN1A	physical	10022118
PARP1_HUMAN	PARP1	physical	9875225
MDM2_HUMAN	MDM2	physical	9840926
GLRX1_HUMAN	GLRX	physical	21988832
1433G_HUMAN	YWHAG	physical	21988832
SOCS5_HUMAN	SOCS5	physical	21988832
XIAP_HUMAN	XIAP	physical	18723680
GELS_HUMAN	GSN	physical	18723680
GDIR1_HUMAN	ARHGDIA	physical	18723680
PARP1_HUMAN	PARP1	physical	18723680
VIME_HUMAN	VIM	physical	18723680
SPTN1_HUMAN	SPTAN1	physical	18723680
STAT1_HUMAN	STAT1	physical	18723680
DFFA_HUMAN	DFFA	physical	18723680
ROCK1_HUMAN	ROCK1	physical	18723680
CASP6_HUMAN	CASP6	physical	18723680
CASP7_HUMAN	CASP7	physical	18723680
CASP9_HUMAN	CASP9	physical	18723680
CASP2_HUMAN	CASP2	physical	18723680
BID_HUMAN	BID	physical	18723680
MDM2_HUMAN	MDM2	physical	24842904
CRYAB_HUMAN	CRYAB	physical	23074197
XIAP_HUMAN	XIAP	physical	23074197
CRYAB_HUMAN	CRYAB	physical	23049853
PARP1_HUMAN	PARP1	physical	22451931
TEBP_HUMAN	PTGES3	physical	22451931
BECN1_HUMAN	BECN1	physical	19713971
PARP1_HUMAN	PARP1	physical	19713971
ATG4D_HUMAN	ATG4D	physical	19549685
PARP1_HUMAN	PARP1	physical	19549685
XIAP_HUMAN	XIAP	physical	26186194
ARMT1_HUMAN	C6orf211	physical	26344197
EF2_HUMAN	EEF2	physical	26344197
LCMT1_HUMAN	LCMT1	physical	26344197
SPB8_HUMAN	SERPINB8	physical	26344197
MDM2_HUMAN	MDM2	physical	25241761
SRC8_HUMAN	CTTN	physical	25241761
MET_HUMAN	MET	physical	25241761
TRAF1_HUMAN	TRAF1	physical	25241761
CADH1_HUMAN	CDH1	physical	25241761
A4_HUMAN	APP	physical	25241761
CTNB1_HUMAN	CTNNB1	physical	25241761
STK4_HUMAN	STK4	physical	25241761
AKT3_HUMAN	AKT3	physical	25241761
MLH1_HUMAN	MLH1	physical	25241761
HCLS1_HUMAN	HCLS1	physical	25241761
CDN1A_HUMAN	CDKN1A	physical	25241761
DFFA_HUMAN	DFFA	physical	25241761
PAK2_HUMAN	PAK2	physical	25241761
CASP9_HUMAN	CASP9	physical	25241761
XIAP_HUMAN	XIAP	physical	28514442
ERP44_HUMAN	ERP44	physical	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
DB01017	Minocycline

Regulatory Network of CASP3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82, AND MASS SPECTROMETRY.	19608861 [Abstract]