dbPTM

CASP9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CASP9_HUMAN
UniProt AC	P55211
Protein Name	Caspase-9
Gene Name	CASP9
Organism	Homo sapiens (Human).
Sequence Length	416
Subcellular Localization
Protein Description	Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).; Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9..
Protein Sequence	MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMIEDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFLRTNRQAAKLSKPTLENLTPVVLRPEIRKPEVLRPETPRPVDIGSGGFGDVGALESLRGNADLAYILSMEPCGHCLIINNVNFCRESGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQQDHGALDCCVVVILSHGCQASHLQFPGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATPFQEGLRTFDQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAVSVKGIYKQMPGCFNFLRKKLFFKTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
87	Phosphorylation	TGQDMLASFLRTNRQ HCHHHHHHHHHHHHH	22.35	24719451
97	Ubiquitination	RTNRQAAKLSKPTLE HHHHHHHHCCCCCHH	57.20	-
99	Phosphorylation	NRQAAKLSKPTLENL HHHHHHCCCCCHHHC	35.56	15703181
100	Ubiquitination	RQAAKLSKPTLENLT HHHHHCCCCCHHHCC	53.08	-
107	Phosphorylation	KPTLENLTPVVLRPE CCCHHHCCCEEECCC	26.14	25159151
117	Ubiquitination	VLRPEIRKPEVLRPE EECCCCCCCCCCCCC	51.71	-
125	Phosphorylation	PEVLRPETPRPVDIG CCCCCCCCCCCEEEC	27.55	16888006
133	Phosphorylation	PRPVDIGSGGFGDVG CCCEEECCCCCCCHH	35.76	26074081
144	Phosphorylation	GDVGALESLRGNADL CCHHHHHHHCCCCCE	24.98	16287866
153	Phosphorylation	RGNADLAYILSMEPC CCCCCEEEEECCCCC	15.08	15657060
175	Phosphorylation	NVNFCRESGLRTRTG CCCCHHHCCCCCCCC	24.63	-
181	Phosphorylation	ESGLRTRTGSNIDCE HCCCCCCCCCCCCHH	44.33	23403867
183	Phosphorylation	GLRTRTGSNIDCEKL CCCCCCCCCCCHHHH	29.96	9812896
189	Ubiquitination	GSNIDCEKLRRRFSS CCCCCHHHHHHHHHH	54.33	-
195	Phosphorylation	EKLRRRFSSLHFMVE HHHHHHHHHCCEEEE	30.13	15703181
196	Phosphorylation	KLRRRFSSLHFMVEV HHHHHHHHCCEEEEE	24.13	9812896
204	Ubiquitination	LHFMVEVKGDLTAKK CCEEEEECCCCHHHH	32.95	-
208	Phosphorylation	VEVKGDLTAKKMVLA EEECCCCHHHHHHHH	40.97	21712546
210	Ubiquitination	VKGDLTAKKMVLALL ECCCCHHHHHHHHHH	35.85	-
211	Ubiquitination	KGDLTAKKMVLALLE CCCCHHHHHHHHHHH	31.60	-
251	Phosphorylation	LQFPGAVYGTDGCPV CCCCCCEECCCCCCE	17.49	-
278	Ubiquitination	SCPSLGGKPKLFFIQ CCCCCCCCCEEEEEE	36.86	-
300	Phosphorylation	DHGFEVASTSPEDES CCCEEEEECCCCCCC	34.29	23663014
301	Phosphorylation	HGFEVASTSPEDESP CCEEEEECCCCCCCC	38.27	28122231
302	Phosphorylation	GFEVASTSPEDESPG CEEEEECCCCCCCCC	24.64	21712546
307	Phosphorylation	STSPEDESPGSNPEP ECCCCCCCCCCCCCC	47.05	25159151
310	Phosphorylation	PEDESPGSNPEPDAT CCCCCCCCCCCCCCC	53.23	25159151
317	Phosphorylation	SNPEPDATPFQEGLR CCCCCCCCCHHHHCC	31.83	20873877
394	Ubiquitination	VANAVSVKGIYKQMP HHHHHCHHCHHHHCC	31.89	-
397	Phosphorylation	AVSVKGIYKQMPGCF HHCHHCHHHHCCCHH	12.11	-

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
99	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
125	T	Phosphorylation	Kinase	CDK1	P06493	PSP
125	T	Phosphorylation	Kinase	DYRK1A	Q13627	GPS
125	T	Phosphorylation	Kinase	MK01	P28482	PhosphoELM
125	T	Phosphorylation	Kinase	MAPK1	P63086	GPS
125	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
144	S	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
153	Y	Phosphorylation	Kinase	ABL	P00519	PSP
153	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
183	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
195	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
196	S	Phosphorylation	Kinase	AKT1	P31749	PSP
196	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
196	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
251	Y	Phosphorylation	Kinase	SRC	P12931	PSP
397	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	XIAP	P98170	PMID:15749826
-	K	Ubiquitination	E3 ubiquitin ligase	HECTD3	Q5T447	PMID:28716524

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
125	T	Phosphorylation	12792650
Phosphorylated at Thr-125 by MAPK1/ERK2.
125	T	Phosphorylation	12792650
Phosphorylation at Thr-125 is sufficient to block caspase-9 processing and subsequent caspase-3 activation.

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 CASP9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XIAP_HUMAN	XIAP	physical	15280366
BIRC1_HUMAN	NAIP	physical	15280366
APAF_HUMAN	APAF1	physical	9390557
DCC_HUMAN	DCC	physical	11248093
APAF_HUMAN	APAF1	physical	11113115
NLRP1_HUMAN	NLRP1	physical	11113115
BIRC7_HUMAN	BIRC7	physical	11024045
XIAP_HUMAN	XIAP	physical	11390657
BIRC8_HUMAN	BIRC8	physical	11390657
XIAP_HUMAN	XIAP	physical	14523016
RING2_HUMAN	RNF2	physical	17379327
BIRC6_HUMAN	BIRC6	physical	15507451
CASP3_HUMAN	CASP3	physical	11242052
XIAP_HUMAN	XIAP	physical	11242052
APAF_HUMAN	APAF1	physical	19698783
RB_HUMAN	RB1	physical	15735701
XIAP_HUMAN	XIAP	physical	16322207
MSTO1_HUMAN	MSTO1	physical	21988832
DHB4_HUMAN	HSD17B4	physical	21988832
JUN_HUMAN	JUN	physical	23678002
CRYAB_HUMAN	CRYAB	physical	23074197
XIAP_HUMAN	XIAP	physical	23074197
ABL1_HUMAN	ABL1	physical	15657060
BIRC7_HUMAN	BIRC7	physical	25416956
BIRC8_HUMAN	BIRC8	physical	25416956
BIRC2_HUMAN	BIRC2	physical	27197231

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 CASP9_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125; SER-302; SER-307AND SER-310, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Inhibition of caspase-9 through phosphorylation at Thr 125 by ERKMAPK."; Allan L.A., Morrice N., Brady S., Magee G., Pathak S., Clarke P.R.; Nat. Cell Biol. 5:647-654(2003). Cited for: PHOSPHORYLATION AT THR-125.	12792650 [Abstract]

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