dbPTM

VDAC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VDAC1_HUMAN
UniProt AC	P21796
Protein Name	Voltage-dependent anion-selective channel protein 1
Gene Name	VDAC1
Organism	Homo sapiens (Human).
Sequence Length	283
Subcellular Localization	Mitochondrion outer membrane Multi-pass membrane protein . Cell membrane Multi-pass membrane protein . Membrane raft Multi-pass membrane protein .
Protein Description	Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. [PubMed: 11845315]
Protein Sequence	MAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTETTKVTGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKREHINLGCDMDFDIAGPSIRGALVLGYEGWLAGYQMNFETAKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVPPTYAD ------CCCCCCHHH	23.64	2559745
6	Phosphorylation	--MAVPPTYADLGKS --CCCCCCHHHCCHH	25.85	23401153
7	Phosphorylation	-MAVPPTYADLGKSA -CCCCCCHHHCCHHH	12.14	23401153
12	Acetylation	PTYADLGKSARDVFT CCHHHCCHHHHHHHH	48.52	25825284
12	Malonylation	PTYADLGKSARDVFT CCHHHCCHHHHHHHH	48.52	26320211
12	Ubiquitination	PTYADLGKSARDVFT CCHHHCCHHHHHHHH	48.52	-
13	Phosphorylation	TYADLGKSARDVFTK CHHHCCHHHHHHHHC	27.09	25159151
19	Phosphorylation	KSARDVFTKGYGFGL HHHHHHHHCCCCCEE	24.33	19764811
20	Malonylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	26320211
20	Acetylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	19608861
20	Succinylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	-
20	Succinylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	-
20	Ubiquitination	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	21890473
22	Phosphorylation	RDVFTKGYGFGLIKL HHHHHCCCCCEEEEE	15.73	28152594
28	Acetylation	GYGFGLIKLDLKTKS CCCCEEEEEECCCCC	40.78	23954790
28	Ubiquitination	GYGFGLIKLDLKTKS CCCCEEEEEECCCCC	40.78	19608861
33	Phosphorylation	LIKLDLKTKSENGLE EEEEECCCCCCCCCE	47.29	30108239
34	Ubiquitination	IKLDLKTKSENGLEF EEEECCCCCCCCCEE	54.94	21906983
34	Acetylation	IKLDLKTKSENGLEF EEEECCCCCCCCCEE	54.94	26051181
35	Phosphorylation	KLDLKTKSENGLEFT EEECCCCCCCCCEEE	41.34	30108239
42	Phosphorylation	SENGLEFTSSGSANT CCCCCEEEECCCCCC	16.77	30108239
43	Phosphorylation	ENGLEFTSSGSANTE CCCCEEEECCCCCCE	37.71	21712546
44	Phosphorylation	NGLEFTSSGSANTET CCCEEEECCCCCCEE	33.44	26437602
46	Phosphorylation	LEFTSSGSANTETTK CEEEECCCCCCEEEE	21.94	25159151
53	Acetylation	SANTETTKVTGSLET CCCCEEEEEEEEEEE	45.26	26051181
53	Ubiquitination	SANTETTKVTGSLET CCCCEEEEEEEEEEE	45.26	25621951
55	Phosphorylation	NTETTKVTGSLETKY CCEEEEEEEEEEEEE	23.70	23403867
57	Phosphorylation	ETTKVTGSLETKYRW EEEEEEEEEEEEEEE	17.42	29255136
60	Phosphorylation	KVTGSLETKYRWTEY EEEEEEEEEEEEEEE	38.37	23403867
61	Malonylation	VTGSLETKYRWTEYG EEEEEEEEEEEEEEC	24.36	26320211
61	Ubiquitination	VTGSLETKYRWTEYG EEEEEEEEEEEEEEC	24.36	19608861
61	Acetylation	VTGSLETKYRWTEYG EEEEEEEEEEEEEEC	24.36	23954790
62	Phosphorylation	TGSLETKYRWTEYGL EEEEEEEEEEEEECE	20.85	20090780
65	Phosphorylation	LETKYRWTEYGLTFT EEEEEEEEEECEEEE	15.44	30108239
67	Phosphorylation	TKYRWTEYGLTFTEK EEEEEEEECEEEEEE	15.29	21082442
70	Phosphorylation	RWTEYGLTFTEKWNT EEEEECEEEEEECCC	24.93	28152594
72	Phosphorylation	TEYGLTFTEKWNTDN EEECEEEEEECCCCC	31.27	28442448
77	Phosphorylation	TFTEKWNTDNTLGTE EEEEECCCCCCCCCE	29.52	24641631
80	Phosphorylation	EKWNTDNTLGTEITV EECCCCCCCCCEEEH	29.40	24641631
83	Phosphorylation	NTDNTLGTEITVEDQ CCCCCCCCEEEHHHH	27.59	24641631
96	Acetylation	DQLARGLKLTFDSSF HHHHHCCEEEECCCC	48.59	25953088
98	Phosphorylation	LARGLKLTFDSSFSP HHHCCEEEECCCCCC	24.65	23927012
101	Phosphorylation	GLKLTFDSSFSPNTG CCEEEECCCCCCCCC	29.14	23927012
102	Phosphorylation	LKLTFDSSFSPNTGK CEEEECCCCCCCCCC	31.43	22167270
104	Phosphorylation	LTFDSSFSPNTGKKN EEECCCCCCCCCCCC	21.13	19664994
107	Phosphorylation	DSSFSPNTGKKNAKI CCCCCCCCCCCCCEE	54.48	29255136
109	Sumoylation	SFSPNTGKKNAKIKT CCCCCCCCCCCEEEC	40.59	-
109	Malonylation	SFSPNTGKKNAKIKT CCCCCCCCCCCEEEC	40.59	26320211
109	Ubiquitination	SFSPNTGKKNAKIKT CCCCCCCCCCCEEEC	40.59	21890473
109	Acetylation	SFSPNTGKKNAKIKT CCCCCCCCCCCEEEC	40.59	25953088
110	Ubiquitination	FSPNTGKKNAKIKTG CCCCCCCCCCEEECC	64.58	25621951
119	Acetylation	AKIKTGYKREHINLG CEEECCCCHHHEECC	53.29	7627739
127	Glutathionylation	REHINLGCDMDFDIA HHHEECCCCCCCCCC	4.40	22555962
137	Phosphorylation	DFDIAGPSIRGALVL CCCCCCCCHHHEEEE	24.81	21082442
161	Ubiquitination	QMNFETAKSRVTQSN EECHHHHHHHCCCCC	46.33	21906983
162	Phosphorylation	MNFETAKSRVTQSNF ECHHHHHHHCCCCCE	29.53	23882029
163	Methylation	NFETAKSRVTQSNFA CHHHHHHHCCCCCEE	34.49	115919797
165	Phosphorylation	ETAKSRVTQSNFAVG HHHHHHCCCCCEEEE	25.77	20068231
167	Phosphorylation	AKSRVTQSNFAVGYK HHHHCCCCCEEEEEE	25.25	20068231
173	Phosphorylation	QSNFAVGYKTDEFQL CCCEEEEEECCEEEE	12.24	20068231
174	Methylation	SNFAVGYKTDEFQLH CCEEEEEECCEEEEE	43.50	30583575
174	Acetylation	SNFAVGYKTDEFQLH CCEEEEEECCEEEEE	43.50	26051181
193	Phosphorylation	DGTEFGGSIYQKVNK CCCCCCHHHHHHHHH	20.64	28152594
195	Phosphorylation	TEFGGSIYQKVNKKL CCCCHHHHHHHHHHH	12.18	28152594
197	Acetylation	FGGSIYQKVNKKLET CCHHHHHHHHHHHHH	30.70	23236377
197	Ubiquitination	FGGSIYQKVNKKLET CCHHHHHHHHHHHHH	30.70	21906983
201	Acetylation	IYQKVNKKLETAVNL HHHHHHHHHHHHHHH	46.48	26051181
204	Phosphorylation	KVNKKLETAVNLAWT HHHHHHHHHHHHHHC	46.47	23312004
211	O-linked_Glycosylation	TAVNLAWTAGNSNTR HHHHHHHCCCCCCCC	21.05	28657654
211	Phosphorylation	TAVNLAWTAGNSNTR HHHHHHHCCCCCCCC	21.05	26437602
215	Phosphorylation	LAWTAGNSNTRFGIA HHHCCCCCCCCEEEE	38.36	20833797
217	Phosphorylation	WTAGNSNTRFGIAAK HCCCCCCCCEEEEEE	27.48	22673903
224	Ubiquitination	TRFGIAAKYQIDPDA CCEEEEEEEECCCCC	28.76	19608861
224	Malonylation	TRFGIAAKYQIDPDA CCEEEEEEEECCCCC	28.76	26320211
224	Acetylation	TRFGIAAKYQIDPDA CCEEEEEEEECCCCC	28.76	23954790
225	Phosphorylation	RFGIAAKYQIDPDAC CEEEEEEEECCCCCC	13.13	28152594
232	Glutathionylation	YQIDPDACFSAKVNN EECCCCCCEEEEECC	3.45	22555962
232	S-nitrosylation	YQIDPDACFSAKVNN EECCCCCCEEEEECC	3.45	2212679
234	Phosphorylation	IDPDACFSAKVNNSS CCCCCCEEEEECCCC	27.37	21712546
236	Acetylation	PDACFSAKVNNSSLI CCCCEEEEECCCCCC	44.27	25825284
236	Malonylation	PDACFSAKVNNSSLI CCCCEEEEECCCCCC	44.27	26320211
240	Phosphorylation	FSAKVNNSSLIGLGY EEEEECCCCCCEECC	22.71	25159151
241	Phosphorylation	SAKVNNSSLIGLGYT EEEECCCCCCEECCC	26.57	21712546
247	Phosphorylation	SSLIGLGYTQTLKPG CCCCEECCCCCCCCC	10.75	28152594
248	Phosphorylation	SLIGLGYTQTLKPGI CCCEECCCCCCCCCC	17.18	28152594
250	Phosphorylation	IGLGYTQTLKPGIKL CEECCCCCCCCCCEE	29.02	25849741
252	Malonylation	LGYTQTLKPGIKLTL ECCCCCCCCCCEEEH	44.58	26320211
252	Ubiquitination	LGYTQTLKPGIKLTL ECCCCCCCCCCEEEH	44.58	21890473
252	Acetylation	LGYTQTLKPGIKLTL ECCCCCCCCCCEEEH	44.58	23954790
258	Phosphorylation	LKPGIKLTLSALLDG CCCCCEEEHHHHHCC	17.42	21712546
260	Phosphorylation	PGIKLTLSALLDGKN CCCEEEHHHHHCCCC	16.19	21712546
266	Acetylation	LSALLDGKNVNAGGH HHHHHCCCCCCCCCC	58.34	19608861
266	Malonylation	LSALLDGKNVNAGGH HHHHHCCCCCCCCCC	58.34	26320211
266	Ubiquitination	LSALLDGKNVNAGGH HHHHHCCCCCCCCCC	58.34	19608861
274	Malonylation	NVNAGGHKLGLGLEF CCCCCCCCCCCCCEE	47.74	26320211
274	Acetylation	NVNAGGHKLGLGLEF CCCCCCCCCCCCCEE	47.74	25953088
274	Ubiquitination	NVNAGGHKLGLGLEF CCCCCCCCCCCCCEE	47.74	21890473
274	Sumoylation	NVNAGGHKLGLGLEF CCCCCCCCCCCCCEE	47.74	-

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
13	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
107	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
193	S	Phosphorylation	Kinase	NEK1	Q96PY6	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
193	S	Phosphorylation	20230784
Phosphorylation at Ser-193 by NEK1 promotes the open conformational state preventing excessive mitochondrial membrane permeability and subsequent apoptotic cell death after injury.
274	K	ubiquitylation	25621951
Undergoes monoubiquitination and polyubiquitination by PRKN; monoubiquitination at Lys-274 inhibits apoptosis, whereas polyubiquitination leads to its degradation and promotes mitophagy.

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 VDAC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KINH_HUMAN	KIF5B	physical	17353931
DCD_HUMAN	DCD	physical	17353931
GELS_HUMAN	GSN	physical	11039896
CYC_HUMAN	CYCS	physical	12243190
B2CL1_HUMAN	BCL2L1	physical	10737788
B2CL1_HUMAN	BCL2L1	physical	10365962
B2L11_HUMAN	BCL2L11	physical	12118373
VDAC2_HUMAN	VDAC2	physical	22939629
VDAC3_HUMAN	VDAC3	physical	22939629
TBA1B_HUMAN	TUBA1B	physical	12087096
HXK1_HUMAN	HK1	physical	22304920
APOE_HUMAN	APOE	physical	26186194
ZG16B_HUMAN	ZG16B	physical	26186194
HUTH_HUMAN	HAL	physical	26186194
ATPA_HUMAN	ATP5A1	physical	26344197
ATPB_HUMAN	ATP5B	physical	26344197
ATPD_HUMAN	ATP5D	physical	26344197
ATP5I_HUMAN	ATP5I	physical	26344197
ATPO_HUMAN	ATP5O	physical	26344197
VA0D1_HUMAN	ATP6V0D1	physical	26344197
BAP29_HUMAN	BCAP29	physical	26344197
BAP31_HUMAN	BCAP31	physical	26344197
CISD1_HUMAN	CISD1	physical	26344197
CISD2_HUMAN	CISD2	physical	26344197
CLH1_HUMAN	CLTC	physical	26344197
OST48_HUMAN	DDOST	physical	26344197
GPX4_HUMAN	GPX4	physical	26344197
MAGT1_HUMAN	MAGT1	physical	26344197
NDUA8_HUMAN	NDUFA8	physical	26344197
NDUA9_HUMAN	NDUFA9	physical	26344197
PHB_HUMAN	PHB	physical	26344197
PHB2_HUMAN	PHB2	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
SGPL1_HUMAN	SGPL1	physical	26344197
SSRG_HUMAN	SSR3	physical	26344197
STX12_HUMAN	STX12	physical	26344197
TOM40_HUMAN	TOMM40	physical	26344197
TSPO_HUMAN	TSPO	physical	26344197
DYLT1_HUMAN	DYNLT1	physical	12009301
PRKN_HUMAN	PARK2	physical	26631732
APOE_HUMAN	APOE	physical	28514442
STOM_HUMAN	STOM	physical	27173435
DCD_HUMAN	DCD	physical	29128334
DNJC9_HUMAN	DNAJC9	physical	29128334
CHTOP_HUMAN	CHTOP	physical	29128334
PPM1B_HUMAN	PPM1B	physical	29128334
XRCC6_HUMAN	XRCC6	physical	29128334
ML12A_HUMAN	MYL12A	physical	29128334
THIO_HUMAN	TXN	physical	29128334
TOM22_HUMAN	TOMM22	physical	29128334
CHM4B_HUMAN	CHMP4B	physical	29128334
ADT1_HUMAN	SLC25A4	physical	29128334
TPM1_HUMAN	TPM1	physical	29128334
MIC19_HUMAN	CHCHD3	physical	29128334
SFXN1_HUMAN	SFXN1	physical	29128334
NDUA5_HUMAN	NDUFA5	physical	29128334
QCR2_HUMAN	UQCRC2	physical	29128334
ADT2_HUMAN	SLC25A5	physical	29128334
CX7A2_HUMAN	COX7A2	physical	29128334
BAF_HUMAN	BANF1	physical	29128334
VDAC3_HUMAN	VDAC3	physical	29128334
PPM1A_HUMAN	PPM1A	physical	29128334
PPIA_HUMAN	PPIA	physical	29128334
VDAC2_HUMAN	VDAC2	physical	29128334
H1X_HUMAN	H1FX	physical	29128334
SCYL2_HUMAN	SCYL2	physical	29128334
ARF1_HUMAN	ARF1	physical	29128334
PGRC1_HUMAN	PGRMC1	physical	29128334
SAP18_HUMAN	SAP18	physical	29128334
RL36_HUMAN	RPL36	physical	29128334
LMNB1_HUMAN	LMNB1	physical	29128334
ATP5H_HUMAN	ATP5H	physical	29128334
ERH_HUMAN	ERH	physical	29128334
MOB2_HUMAN	MOB2	physical	29128334
RL27_HUMAN	RPL27	physical	29128334
XRCC5_HUMAN	XRCC5	physical	29128334
D19L1_HUMAN	DPY19L1	physical	29128334
COX41_HUMAN	COX4I1	physical	29128334
STML2_HUMAN	STOML2	physical	29128334
ODPB_HUMAN	PDHB	physical	29128334
RL12_HUMAN	RPL12	physical	29128334
RL35_HUMAN	RPL35	physical	29128334
EMD_HUMAN	EMD	physical	29128334
H10_HUMAN	H1F0	physical	29128334
RMXL2_HUMAN	RBMXL2	physical	29128334
ILF2_HUMAN	ILF2	physical	29128334
RL28_HUMAN	RPL28	physical	29128334
COX5A_HUMAN	COX5A	physical	29128334
MPCP_HUMAN	SLC25A3	physical	29128334
RL30_HUMAN	RPL30	physical	29128334
DKC1_HUMAN	DKC1	physical	29128334
PRDX6_HUMAN	PRDX6	physical	29128334
FBRL_HUMAN	FBL	physical	29128334
ELAV1_HUMAN	ELAVL1	physical	29128334
CALX_HUMAN	CANX	physical	29128334
RNPS1_HUMAN	RNPS1	physical	29128334
SERPH_HUMAN	SERPINH1	physical	29128334
1433E_HUMAN	YWHAE	physical	29128334
RPN1_HUMAN	RPN1	physical	29128334
IMDH2_HUMAN	IMPDH2	physical	29128334
PRDX3_HUMAN	PRDX3	physical	29128334
SSRD_HUMAN	SSR4	physical	29128334
ATD3A_HUMAN	ATAD3A	physical	29128334
ATPK_HUMAN	ATP5J2	physical	29128334
NDUS1_HUMAN	NDUFS1	physical	29128334
MIC60_HUMAN	IMMT	physical	29128334
PROF1_HUMAN	PFN1	physical	29128334
PI51C_HUMAN	PIP5K1C	physical	29128334
ATPG_HUMAN	ATP5C1	physical	29128334
NOP56_HUMAN	NOP56	physical	29128334
SSBP_HUMAN	SSBP1	physical	29128334
TPM3_HUMAN	TPM3	physical	29128334
RCN2_HUMAN	RCN2	physical	29128334
ATPO_HUMAN	ATP5O	physical	29128334
QCR1_HUMAN	UQCRC1	physical	29128334
PABP1_HUMAN	PABPC1	physical	29128334
1433Z_HUMAN	YWHAZ	physical	29128334
NOP58_HUMAN	NOP58	physical	29128334
TRAP1_HUMAN	TRAP1	physical	29128334
COX2_HUMAN	COX2	physical	29128334
ECHB_HUMAN	HADHB	physical	29128334
RUVB1_HUMAN	RUVBL1	physical	29128334
SPIN1_HUMAN	SPIN1	physical	29128334
MCA3_HUMAN	EEF1E1	physical	29128334
SURF6_HUMAN	SURF6	physical	29128334
HNRDL_HUMAN	HNRNPDL	physical	29128334
ENPL_HUMAN	HSP90B1	physical	29128334
NDUV2_HUMAN	NDUFV2	physical	29128334
SF3B6_HUMAN	SF3B6	physical	29128334
H2AV_HUMAN	H2AFV	physical	29128334
NDUS3_HUMAN	NDUFS3	physical	29128334
CLCC1_HUMAN	CLCC1	physical	29128334
ADT3_HUMAN	SLC25A6	physical	29128334
SYDC_HUMAN	DARS	physical	29128334
LDHA_HUMAN	LDHA	physical	29128334
ETFA_HUMAN	ETFA	physical	29128334
ODPA_HUMAN	PDHA1	physical	29128334
H2AY_HUMAN	H2AFY	physical	29128334
AIFM1_HUMAN	AIFM1	physical	29128334
SSRP1_HUMAN	SSRP1	physical	29128334
TKT_HUMAN	TKT	physical	29128334
CBX3_HUMAN	CBX3	physical	29128334
ERLN2_HUMAN	ERLIN2	physical	29128334
4F2_HUMAN	SLC3A2	physical	29128334
KCRB_HUMAN	CKB	physical	29128334
ERLN1_HUMAN	ERLIN1	physical	29128334
BASI_HUMAN	BSG	physical	29128334
NP1L1_HUMAN	NAP1L1	physical	29128334
RL1D1_HUMAN	RSL1D1	physical	29128334
AAAT_HUMAN	SLC1A5	physical	29128334
LA_HUMAN	SSB	physical	29128334
RPN2_HUMAN	RPN2	physical	29128334
TR150_HUMAN	THRAP3	physical	29128334
CBX1_HUMAN	CBX1	physical	29128334
DDX21_HUMAN	DDX21	physical	29128334
CDK1_HUMAN	CDK1	physical	29128334
RM12_HUMAN	MRPL12	physical	29128334
SAFB1_HUMAN	SAFB	physical	29128334
SP16H_HUMAN	SUPT16H	physical	29128334
EF1G_HUMAN	EEF1G	physical	29128334
CMC2_HUMAN	SLC25A13	physical	29128334
ECHA_HUMAN	HADHA	physical	29128334
LMNB2_HUMAN	LMNB2	physical	29128334
PERI_HUMAN	PRPH	physical	29128334
AT1A1_HUMAN	ATP1A1	physical	29128334
HORN_HUMAN	HRNR	physical	29128334
TPIS_HUMAN	TPI1	physical	29128334
HP1B3_HUMAN	HP1BP3	physical	29128334
COPE_HUMAN	COPE	physical	29128334
SYEP_HUMAN	EPRS	physical	29128334
RTCB_HUMAN	RTCB	physical	29128334
EF2_HUMAN	EEF2	physical	29128334
SYIC_HUMAN	IARS	physical	29128334
TOP2A_HUMAN	TOP2A	physical	29128334
TCPQ_HUMAN	CCT8	physical	29128334
SYLC_HUMAN	LARS	physical	29128334
MYH11_HUMAN	MYH11	physical	29128334
OST48_HUMAN	DDOST	physical	29128334
IMB1_HUMAN	KPNB1	physical	29128334
SAFB2_HUMAN	SAFB2	physical	29128334
FILA2_HUMAN	FLG2	physical	29128334
TOP1_HUMAN	TOP1	physical	29128334
H2A1B_HUMAN	HIST1H2AE	physical	29128334
H2B1D_HUMAN	HIST1H2BD	physical	29128334
H2B1C_HUMAN	HIST1H2BD	physical	29128334
BOLA2_HUMAN	BOLA2	physical	29128334

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
DB01375	Dihydroxyaluminium

Regulatory Network of VDAC1_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-104, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Identification of human porins. II. Characterization and primarystructure of a 31-lDa porin from human B lymphocytes (Porin 31HL)."; Kayser H., Kratzin H.D., Thinnes F.P., Goetz H., Schmidt W.E.,Eckart K., Hilschmann N.; Biol. Chem. Hoppe-Seyler 370:1265-1278(1989). Cited for: PROTEIN SEQUENCE OF 2-283.	2559745 [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-20; LYS-28; LYS-61; LYS-224AND LYS-266, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-104, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-101 AND SER-104, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.	18088087 [Abstract]
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