BAD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BAD_HUMAN
• UniProt AC: Q92934
• Protein Name: Bcl2-associated agonist of cell death
• Gene Name: BAD
• Organism: Homo sapiens (Human).
• Sequence Length: 168
• Subcellular Localization: Mitochondrion outer membrane. Cytoplasm . Colocalizes with HIF3A in the cytoplasm (By similarity). Upon phosphorylation, locates to the cytoplasm.
• Protein Description: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways..
• Protein Sequence: MFQIPEFEPSEQEDSSSAERGLGPSPAGDGPSGSGKHHRQAPGLLWDASHQQEQPTSSSHHGGAGAVEIRSRHSSYPAGTEDDEGMGEEPSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFVDSFKKGLPRPKSAGTATQMRQSSSWTRVFQSWWDRNLGRGSSAPSQ

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
1	Acetylation	-------MFQIPEFE -------CCCCCCCC	5.14	22814378
10	Phosphorylation	QIPEFEPSEQEDSSS CCCCCCCCCCCCCCC	44.72	24173317
15	Phosphorylation	EPSEQEDSSSAERGL CCCCCCCCCCCCCCC	25.99	28348404
16	Phosphorylation	PSEQEDSSSAERGLG CCCCCCCCCCCCCCC	45.98	24173317
17	Phosphorylation	SEQEDSSSAERGLGP CCCCCCCCCCCCCCC	37.79	24173317
25	Phosphorylation	AERGLGPSPAGDGPS CCCCCCCCCCCCCCC	26.11	30266825
32	Phosphorylation	SPAGDGPSGSGKHHR CCCCCCCCCCCCCCC	51.63	23927012
34	Phosphorylation	AGDGPSGSGKHHRQA CCCCCCCCCCCCCCC	49.35	23927012
36	Acetylation	DGPSGSGKHHRQAPG CCCCCCCCCCCCCCC	37.62	19608861
57	Phosphorylation	HQQEQPTSSSHHGGA CCCCCCCCCCCCCCC	36.20	28555341
71	Phosphorylation	AGAVEIRSRHSSYPA CCCEEEHHCCCCCCC	39.75	22322096
74	Phosphorylation	VEIRSRHSSYPAGTE EEEHHCCCCCCCCCC	30.38	22322096
75	Phosphorylation	EIRSRHSSYPAGTED EEHHCCCCCCCCCCC	29.07	11085518
75	Dephosphorylation	EIRSRHSSYPAGTED EEHHCCCCCCCCCCC	29.07	10195903
76	Phosphorylation	IRSRHSSYPAGTEDD EHHCCCCCCCCCCCC	10.50	22322096
80	Phosphorylation	HSSYPAGTEDDEGMG CCCCCCCCCCCCCCC	38.04	30266825
91	Phosphorylation	EGMGEEPSPFRGRSR CCCCCCCCCCCCCCC	39.69	30266825
94	Methylation	GEEPSPFRGRSRSAP CCCCCCCCCCCCCCC	42.89	21444773
94	Asymmetric dimethylarginine	GEEPSPFRGRSRSAP CCCCCCCCCCCCCCC	42.89	-
96	Asymmetric dimethylarginine	EPSPFRGRSRSAPPN CCCCCCCCCCCCCCC	25.33	-
96	Methylation	EPSPFRGRSRSAPPN CCCCCCCCCCCCCCC	25.33	21444773
97	Phosphorylation	PSPFRGRSRSAPPNL CCCCCCCCCCCCCCH	33.15	23401153
99	Dephosphorylation	PFRGRSRSAPPNLWA CCCCCCCCCCCCHHH	46.50	10195903
99	Phosphorylation	PFRGRSRSAPPNLWA CCCCCCCCCCCCHHH	46.50	19664994
110	Phosphorylation	NLWAAQRYGRELRRM CHHHHHHHHHHHHHH	14.41	26074081
118	Phosphorylation	GRELRRMSDEFVDSF HHHHHHHCHHHHHHH	31.98	29255136
124	Phosphorylation	MSDEFVDSFKKGLPR HCHHHHHHHHHCCCC	33.39	23927012
126	2-Hydroxyisobutyrylation	DEFVDSFKKGLPRPK HHHHHHHHHCCCCCC	50.30	-
134	Phosphorylation	KGLPRPKSAGTATQM HCCCCCCCCCHHHHH	34.31	23401153
137	Phosphorylation	PRPKSAGTATQMRQS CCCCCCCHHHHHHHC	26.67	23927012
139	Phosphorylation	PKSAGTATQMRQSSS CCCCCHHHHHHHCCH	23.80	23927012
144	Phosphorylation	TATQMRQSSSWTRVF HHHHHHHCCHHHHHH	18.90	27251275
145	Phosphorylation	ATQMRQSSSWTRVFQ HHHHHHCCHHHHHHH	22.89	25072903
146	Phosphorylation	TQMRQSSSWTRVFQS HHHHHCCHHHHHHHH	37.40	20363803
148	Phosphorylation	MRQSSSWTRVFQSWW HHHCCHHHHHHHHHH	20.92	20363803
153	Phosphorylation	SWTRVFQSWWDRNLG HHHHHHHHHHHHCCC	20.76	10949026
161	Methylation	WWDRNLGRGSSAPSQ HHHHCCCCCCCCCCC	45.01	24129315
163	Phosphorylation	DRNLGRGSSAPSQ-- HHCCCCCCCCCCC--	23.20	23403867
164	Phosphorylation	RNLGRGSSAPSQ--- HCCCCCCCCCCC---	47.20	23403867

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
74	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
75	S	Phosphorylation	Kinase	PIM3	Q86V86	PSP
75	S	Phosphorylation	Kinase	PRKCI	P41743	GPS
75	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
75	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
75	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
75	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
75	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
75	S	Phosphorylation	Kinase	PIM1	P11309	PSP
75	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
75	S	Phosphorylation	Kinase	RAF1	P04049	PSP
75	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
75	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
75	S	Phosphorylation	Kinase	RAF-FAMILY	-	GPS
75	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
75	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
75	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
75	S	Phosphorylation	Kinase	ARAF	P10398	PSP
75	S	Phosphorylation	Kinase	PRKCE	Q02156	GPS
75	S	Phosphorylation	Kinase	BRAF	P15056	PSP
75	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
75	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
91	S	Phosphorylation	Kinase	CDK1	P06493	PSP
99	S	Phosphorylation	Kinase	ARAF	P10398	PSP
99	S	Phosphorylation	Kinase	PRKCE	Q02156	GPS
99	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
99	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
99	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
99	S	Phosphorylation	Kinase	BRAF	P15056	PSP
99	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
99	S	Phosphorylation	Kinase	RAF1	P04049	PSP
99	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
99	S	Phosphorylation	Kinase	PRKCI	P41743	GPS
99	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
99	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
99	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
99	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
99	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
118	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
118	S	Phosphorylation	Kinase	PRKCE	Q02156	GPS
118	S	Phosphorylation	Kinase	PRKCI	P41743	GPS
118	S	Phosphorylation	Kinase	ARAF	P10398	PSP
118	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
118	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
118	S	Phosphorylation	Kinase	RAF-FAMILY	-	GPS
118	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
118	S	Phosphorylation	Kinase	BRAF	P15056	PSP
118	S	Phosphorylation	Kinase	RAF1	P04049	PSP
118	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
134	S	Phosphorylation	Kinase	BRAF	P15056	PSP
134	S	Phosphorylation	Kinase	PAK1	Q13153	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
75	S	Phosphorylation	Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity.	11278822
75	S	Phosphorylation	Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins.	11278822
94	R	Methylation	Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.	21444773
94	R	Phosphorylation	Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.	21444773
96	R	Methylation	Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.	21444773
96	R	Phosphorylation	Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.	21444773
99	S	Methylation	Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.	10926925
99	S	Phosphorylation	Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.	10926925
99	S	Phosphorylation	Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity.	10926925
99	S	Phosphorylation	Phosphorylation at Ser-99 by PKB/AKT1 is almost completely blocked by the apoptotic C-terminus cleavage product of PKN2 generated by caspases-3 activity during apoptosis.	10926925
99	S	Phosphorylation	Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins.	10926925
99	S	Phosphorylation	Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation.	10926925
118	S	Phosphorylation	Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity.	18669648
118	S	Phosphorylation	Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation.	18669648
118	S	Phosphorylation	This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival.	18669648
134	S	Phosphorylation	Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity.	24275569

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of BAD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433S_HUMAN	SFN	physical	16189514
EWS_HUMAN	EWSR1	physical	16189514
B2CL1_HUMAN	BCL2L1	physical	15694340
BCL2_HUMAN	BCL2	physical	15694340
1433T_HUMAN	YWHAQ	physical	15694340
B2CL1_HUMAN	BCL2L1	physical	15705582
B2CL1_HUMAN	BCL2L1	physical	9824152
1433E_HUMAN	YWHAE	physical	9369453
1433B_HUMAN	YWHAB	physical	9369453
1433T_HUMAN	YWHAQ	physical	9369453
1433F_HUMAN	YWHAH	physical	9369453
S10AA_HUMAN	S100A10	physical	9369453
B2CL2_HUMAN	BCL2L2	physical	11483855
B2LA1_HUMAN	BCL2A1	physical	11483855
MCL1_HUMAN	MCL1	physical	11483855
B2CL1_HUMAN	BCL2L1	physical	10620799
BCL2_HUMAN	BCL2	physical	7834748
B2CL1_HUMAN	BCL2L1	physical	7834748
B2CL1_HUMAN	BCL2L1	physical	11206074
B2CL1_HUMAN	BCL2L1	physical	11494146
B2CL1_HUMAN	BCL2L1	physical	11077446
1433B_HUMAN	YWHAB	physical	21900206
SUMO2_HUMAN	SUMO2	physical	21900206
PP1A_HUMAN	PPP1CA	physical	17274640
BAX_HUMAN	BAX	physical	17274640
SYUA_HUMAN	SNCA	physical	15978696
BCL2_HUMAN	BCL2	physical	15990872
B2CL1_HUMAN	BCL2L1	physical	18628207
BCL2_HUMAN	BCL2	physical	15849194
B2CL1_HUMAN	BCL2L1	physical	19667065
1433Z_HUMAN	YWHAZ	physical	19667065
B2CL1_HUMAN	BCL2L1	physical	21988832
1433F_HUMAN	YWHAH	physical	21988832
CR3L3_HUMAN	CREB3L3	physical	21988832
CDN1A_HUMAN	CDKN1A	physical	21988832
1433S_HUMAN	SFN	physical	21988832
PRDX2_HUMAN	PRDX2	physical	21988832
1433E_HUMAN	YWHAE	physical	21988832
1433Z_HUMAN	YWHAZ	physical	21988832
KEAP1_HUMAN	KEAP1	physical	21988832
1433T_HUMAN	YWHAQ	physical	21988832
STEA3_HUMAN	STEAP3	physical	21988832
B2CL1_HUMAN	BCL2L1	physical	9305851
BCL2_HUMAN	BCL2	physical	9305851
B2CL1_HUMAN	BCL2L1	physical	25416956
B2CL1_HUMAN	BCL2L1	physical	19427857
1433Z_HUMAN	YWHAZ	physical	19427857
1433S_HUMAN	SFN	physical	20005908
KPCD1_HUMAN	PRKD1	physical	20179209
KPCE_HUMAN	PRKCE	physical	20179209
B2CL1_HUMAN	BCL2L1	physical	20603619
BCL2_HUMAN	BCL2	physical	20603619
B2CL2_HUMAN	BCL2L2	physical	20603619
B2CL1_HUMAN	BCL2L1	physical	25241761
RAF1_HUMAN	RAF1	physical	25241761
BCL2_HUMAN	BCL2	physical	10611223
B2CL1_HUMAN	BCL2L1	physical	10611223
1433T_HUMAN	YWHAQ	physical	10611223

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-36, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-91; SER-99 ANDSER-118, AND MASS SPECTROMETRY.
PubMed: 19690332

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.
PubMed: 19413330

"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 SER-99 AND SER-118, AND MASSSPECTROMETRY.
PubMed: 18669648

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.
PubMed: 18220336

"Inhibition of Akt and its anti-apoptotic activities by tumor necrosisfactor-induced protein kinase C-related kinase 2 (PRK2) cleavage.";
Koh H., Lee K.H., Kim D., Kim S., Kim J.W., Chung J.;
J. Biol. Chem. 275:34451-34458(2000).
Cited for: INTERACTION WITH AKT1, AND PHOSPHORYLATION AT SER-99.
PubMed: 10926925