dbPTM

BAX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BAX_HUMAN
UniProt AC	Q07812
Protein Name	Apoptosis regulator BAX
Gene Name	BAX
Organism	Homo sapiens (Human).
Sequence Length	192
Subcellular Localization	Isoform Alpha: Mitochondrion membrane Single-pass membrane protein. Cytoplasm . Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a conformation change that causes release from JNK-phosphorylated 14-3-3 proteins a
Protein Description	Plays a role in the mitochondrial apoptotic process. Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM). [PubMed: 21458670 Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.]
Protein Sequence	MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDGSGEQP -------CCCCCCCC	13.70	25944712
4	Phosphorylation	----MDGSGEQPRGG ----CCCCCCCCCCC	34.59	29514088
9	Methylation	DGSGEQPRGGGPTSS CCCCCCCCCCCCCCH	56.96	-
14	Phosphorylation	QPRGGGPTSSEQIMK CCCCCCCCCHHHHHH	48.43	21406692
15	Phosphorylation	PRGGGPTSSEQIMKT CCCCCCCCHHHHHHH	34.70	28857561
16	Phosphorylation	RGGGPTSSEQIMKTG CCCCCCCHHHHHHHH	35.68	21406692
20	Sulfoxidation	PTSSEQIMKTGALLL CCCHHHHHHHHHHHH	2.96	30846556
21 (in isoform 8)	Ubiquitination	-	45.49	21890473
21 (in isoform 5)	Ubiquitination	-	45.49	21890473
21	Ubiquitination	TSSEQIMKTGALLLQ CCHHHHHHHHHHHHH	45.49	21890473
21 (in isoform 1)	Ubiquitination	-	45.49	21890473
21 (in isoform 2)	Ubiquitination	-	45.49	21890473
22	Phosphorylation	SSEQIMKTGALLLQG CHHHHHHHHHHHHHH	15.42	21712546
38 (in isoform 7)	Ubiquitination	-	8.71	21906983
38	Sulfoxidation	IQDRAGRMGGEAPEL HHHHCCCCCCCCCHH	8.71	21406390
57 (in isoform 1)	Ubiquitination	-	49.58	21890473
57 (in isoform 2)	Ubiquitination	-	49.58	21890473
57	Ubiquitination	VPQDASTKKLSECLK CCCCCCHHHHHHHHH	49.58	2190698
57 (in isoform 8)	Ubiquitination	-	49.58	21890473
57 (in isoform 5)	Ubiquitination	-	49.58	21890473
58	Ubiquitination	PQDASTKKLSECLKR CCCCCHHHHHHHHHH	58.28	-
60	Phosphorylation	DASTKKLSECLKRIG CCCHHHHHHHHHHHH	34.83	17911107
64	Ubiquitination	KKLSECLKRIGDELD HHHHHHHHHHHHHHH	54.34	-
72	Phosphorylation	RIGDELDSNMELQRM HHHHHHHHHHHHHHH	51.18	25338102
74	Sulfoxidation	GDELDSNMELQRMIA HHHHHHHHHHHHHHH	6.69	30846556
79	Sulfoxidation	SNMELQRMIAAVDTD HHHHHHHHHHHHCCC	1.25	21406390
85	Phosphorylation	RMIAAVDTDSPREVF HHHHHHCCCCHHHHH	31.60	20068231
87	Phosphorylation	IAAVDTDSPREVFFR HHHHCCCCHHHHHHH	28.13	20068231
123	Ubiquitination	FASKLVLKALCTKVP HHHHHHHHHHHCCHH	31.65	-
126	S-palmitoylation	KLVLKALCTKVPELI HHHHHHHHCCHHHHH	4.07	24525733
135	Phosphorylation	KVPELIRTIMGWTLD CHHHHHHHHHHHHHH	14.34	19194518
140	Phosphorylation	IRTIMGWTLDFLRER HHHHHHHHHHHHHHH	15.66	19194518
145 (in isoform 5)	Phosphorylation	-	27.29	22210691
148 (in isoform 5)	Phosphorylation	-	4.43	22210691
163 (in isoform 2)	Ubiquitination	-	24.37	-
163	Phosphorylation	GGWDGLLSYFGTPTW CCCCCHHHHHCCCCC	24.37	15525785
167	Phosphorylation	GLLSYFGTPTWQTVT CHHHHHCCCCCCEEH	13.98	16709574
172	Phosphorylation	FGTPTWQTVTIFVAG HCCCCCCEEHHHHHH	15.92	-
174	Phosphorylation	TPTWQTVTIFVAGVL CCCCCEEHHHHHHHH	16.46	-
184	Phosphorylation	VAGVLTASLTIWKKM HHHHHHHHHHHHHHC	22.32	16679323
186	Phosphorylation	GVLTASLTIWKKMG- HHHHHHHHHHHHCC-	23.46	-
207 (in isoform 2)	Phosphorylation	-		24719451
215 (in isoform 2)	Phosphorylation	-		24719451

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
163	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
184	S	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
184	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	RNF144B	Q7Z419	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:22460798

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
B2LA1_HUMAN	BCL2A1	physical	10753914
VDAC1_HUMAN	VDAC1	physical	15637055
B2CL1_HUMAN	BCL2L1	physical	12853473
OYE2_YEAST	OYE2	genetic	17897954
VDAC1_HUMAN	VDAC1	physical	12767928
BCL2_HUMAN	BCL2	physical	8358790
1433T_HUMAN	YWHAQ	physical	12426317
BCL2_HUMAN	BCL2	physical	10620799
SHLB1_HUMAN	SH3GLB1	physical	11161816
BAX_HUMAN	BAX	physical	11161816
SHLB1_HUMAN	SH3GLB1	physical	11259440
ADT1_HUMAN	SLC25A4	physical	9748162
MCL1_HUMAN	MCL1	physical	10837489
TOM40_HUMAN	TOMM40	physical	17635912
R144B_HUMAN	RNF144B	physical	20300062
BCL2_HUMAN	BCL2	physical	21778226
XRCC6_HUMAN	XRCC6	physical	19247369
PRS6A_HUMAN	PSMC3	physical	20431057
PRS8_HUMAN	PSMC5	physical	20431057
HDAC6_HUMAN	HDAC6	physical	21847364
XRCC5_HUMAN	XRCC5	physical	19177010
XRCC6_HUMAN	XRCC6	physical	19177010
XRCC6_HUMAN	XRCC6	physical	19118032
KCNA3_HUMAN	KCNA3	physical	20114030
BAX_HUMAN	BAX	physical	21712378
XIAP_HUMAN	XIAP	physical	21712378
BAK_HUMAN	BAK1	physical	21712378
CLUS_HUMAN	CLU	physical	16113678
HSP74_HUMAN	HSPA4	physical	15388581
XRCC6_HUMAN	XRCC6	physical	21042904
CRYAA_HUMAN	CRYAA	physical	14752512
CRYAB_HUMAN	CRYAB	physical	14752512
1433B_HUMAN	YWHAB	physical	22785534
BCL2_HUMAN	BCL2	physical	23479509
BAX_HUMAN	BAX	physical	19767770
ZBT24_HUMAN	ZBTB24	physical	19074440
BCL2_HUMAN	BCL2	physical	9111042
B2CL1_HUMAN	BCL2L1	physical	9111042
CASP9_HUMAN	CASP9	physical	15254227
CASP8_HUMAN	CASP8	physical	15254227
CASP7_HUMAN	CASP7	physical	15254227
CASP3_HUMAN	CASP3	physical	15254227
CYC_HUMAN	CYCS	physical	15254227
BCL2_HUMAN	BCL2	physical	16642033
BAX_HUMAN	BAX	physical	17074758
BCL2_HUMAN	BCL2	physical	17097560
B2CL1_HUMAN	BCL2L1	physical	21199865
MCL1_HUMAN	MCL1	physical	21199865
BCL2_HUMAN	BCL2	physical	21199865
SEPT7_HUMAN	SEPT7	genetic	24055994
1433T_HUMAN	YWHAQ	genetic	24055994
CDC10_YEAST	CDC10	genetic	24055994
PCBP1_HUMAN	PCBP1	physical	26344197
PRDX1_HUMAN	PRDX1	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
SERPH_HUMAN	SERPINH1	physical	26344197
B2CL1_HUMAN	BCL2L1	physical	26496610
ERCC6_HUMAN	ERCC6	physical	26496610
DNLI3_HUMAN	LIG3	physical	26496610
TYY1_HUMAN	YY1	physical	26496610
GEMI2_HUMAN	GEMIN2	physical	26496610
PLPL6_HUMAN	PNPLA6	physical	26496610
PRS23_HUMAN	PRSS23	physical	26496610
EDRF1_HUMAN	EDRF1	physical	26496610
NIN_HUMAN	NIN	physical	26496610
BDP1_HUMAN	BDP1	physical	26496610
NSF1C_HUMAN	NSFL1C	physical	26496610
ATAD5_HUMAN	ATAD5	physical	26496610
CR021_HUMAN	C18orf21	physical	26496610
SPB12_HUMAN	SERPINB12	physical	26496610
NU5M_HUMAN	ND5	physical	25115399
P53_HUMAN	TP53	physical	25115399
B2CL2_HUMAN	BCL2L2	physical	25115399

Drug and Disease Associations

Kegg Disease
H00020	Colorectal cancer
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 BAX_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]