dbPTM

VDAC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VDAC2_HUMAN
UniProt AC	P45880
Protein Name	Voltage-dependent anion-selective channel protein 2
Gene Name	VDAC2
Organism	Homo sapiens (Human).
Sequence Length	294
Subcellular Localization	Mitochondrion outer membrane .
Protein Description	Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel 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..
Protein Sequence	MATHGQTCARPMCIPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSINAGGHKVGLALELEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATHGQTCA ------CCCCCCCCC	14.33	25944712
2 (in isoform 1)	Phosphorylation	-	14.33	27135362
7	Phosphorylation	-MATHGQTCARPMCI -CCCCCCCCCCCCCC	16.84	-
17	Phosphorylation	RPMCIPPSYADLGKA CCCCCCCCHHHHHHH	27.83	24043423
18	Phosphorylation	PMCIPPSYADLGKAA CCCCCCCHHHHHHHH	15.20	24043423
20 (in isoform 2)	Ubiquitination	-	47.96	21890473
28 (in isoform 2)	Ubiquitination	-	3.23	21890473
31	Acetylation	AARDIFNKGFGFGLV HHHHHHHCCCCCEEE	44.88	19608861
31	Succinylation	AARDIFNKGFGFGLV HHHHHHHCCCCCEEE	44.88	-
31	Ubiquitination	AARDIFNKGFGFGLV HHHHHHHCCCCCEEE	44.88	25621951
31	Succinylation	AARDIFNKGFGFGLV HHHHHHHCCCCCEEE	44.88	23954790
31 (in isoform 3)	Ubiquitination	-	44.88	21890473
39	Acetylation	GFGFGLVKLDVKTKS CCCCEEEEEEECCCC	43.97	23954790
39	Ubiquitination	GFGFGLVKLDVKTKS CCCCEEEEEEECCCC	43.97	21890473
39 (in isoform 3)	Ubiquitination	-	43.97	21890473
44	Phosphorylation	LVKLDVKTKSCSGVE EEEEEECCCCCCCCE	28.21	30108239
45	2-Hydroxyisobutyrylation	VKLDVKTKSCSGVEF EEEEECCCCCCCCEE	43.69	-
45	Acetylation	VKLDVKTKSCSGVEF EEEEECCCCCCCCEE	43.69	26051181
46	Phosphorylation	KLDVKTKSCSGVEFS EEEECCCCCCCCEEE	20.81	25159151
46 (in isoform 1)	Ubiquitination	-	20.81	21890473
46	Acetylation	KLDVKTKSCSGVEFS EEEECCCCCCCCEEE	20.81	19608861
46	Ubiquitination	KLDVKTKSCSGVEFS EEEECCCCCCCCEEE	20.81	19608861
47	S-nitrosocysteine	LDVKTKSCSGVEFST EEECCCCCCCCEEEC	4.35	-
47	S-nitrosylation	LDVKTKSCSGVEFST EEECCCCCCCCEEEC	4.35	22178444
48	Phosphorylation	DVKTKSCSGVEFSTS EECCCCCCCCEEECC	53.62	30108239
53	Phosphorylation	SCSGVEFSTSGSSNT CCCCCEEECCCCCCC	14.25	30108239
54	Phosphorylation	CSGVEFSTSGSSNTD CCCCEEECCCCCCCC	42.29	30108239
54 (in isoform 1)	Ubiquitination	-	42.29	21890473
54	Acetylation	CSGVEFSTSGSSNTD CCCCEEECCCCCCCC	42.29	19608861
54	Ubiquitination	CSGVEFSTSGSSNTD CCCCEEECCCCCCCC	42.29	19608861
55	Phosphorylation	SGVEFSTSGSSNTDT CCCEEECCCCCCCCC	35.16	30108239
57	Phosphorylation	VEFSTSGSSNTDTGK CEEECCCCCCCCCCE	21.85	30576142
58	Phosphorylation	EFSTSGSSNTDTGKV EEECCCCCCCCCCEE	47.47	30576142
60	Phosphorylation	STSGSSNTDTGKVTG ECCCCCCCCCCEEEE	36.56	30576142
61 (in isoform 1)	Phosphorylation	-	58.68	27251275
61 (in isoform 2)	Ubiquitination	-	58.68	21890473
62	Phosphorylation	SGSSNTDTGKVTGTL CCCCCCCCCEEEEEE	36.54	30576142
64	Acetylation	SSNTDTGKVTGTLET CCCCCCCEEEEEEEC	38.42	26051181
64	Ubiquitination	SSNTDTGKVTGTLET CCCCCCCEEEEEEEC	38.42	25621951
66	Phosphorylation	NTDTGKVTGTLETKY CCCCCEEEEEEECEE	28.12	26657352
68	Phosphorylation	DTGKVTGTLETKYKW CCCEEEEEEECEEEE	16.44	30576142
71	Phosphorylation	KVTGTLETKYKWCEY EEEEEEECEEEEECC	42.67	23403867
72	Acetylation	VTGTLETKYKWCEYG EEEEEECEEEEECCC	35.14	25825284
72	Ubiquitination	VTGTLETKYKWCEYG EEEEEECEEEEECCC	35.14	21906983
72	2-Hydroxyisobutyrylation	VTGTLETKYKWCEYG EEEEEECEEEEECCC	35.14	-
72 (in isoform 3)	Ubiquitination	-	35.14	21890473
73	Phosphorylation	TGTLETKYKWCEYGL EEEEECEEEEECCCC	19.69	24719451
74	Acetylation	GTLETKYKWCEYGLT EEEECEEEEECCCCE	47.10	23954790
74	Ubiquitination	GTLETKYKWCEYGLT EEEECEEEEECCCCE	47.10	-
74	2-Hydroxyisobutyrylation	GTLETKYKWCEYGLT EEEECEEEEECCCCE	47.10	-
74	Malonylation	GTLETKYKWCEYGLT EEEECEEEEECCCCE	47.10	26320211
76	S-nitrosocysteine	LETKYKWCEYGLTFT EECEEEEECCCCEEE	2.23	-
76	S-nitrosylation	LETKYKWCEYGLTFT EECEEEEECCCCEEE	2.23	22178444
78	Phosphorylation	TKYKWCEYGLTFTEK CEEEEECCCCEEEEC	17.82	20090780
81 (in isoform 1)	Phosphorylation	-	24.93	24719451
81	Phosphorylation	KWCEYGLTFTEKWNT EEECCCCEEEECCCC	24.93	28857561
83 (in isoform 1)	Phosphorylation	-	31.27	24719451
83	Phosphorylation	CEYGLTFTEKWNTDN ECCCCEEEECCCCCC	31.27	28102081
87 (in isoform 1)	Ubiquitination	-	48.93	21890473
87	Acetylation	LTFTEKWNTDNTLGT CEEEECCCCCCCCCC	48.93	19608861
87	Ubiquitination	LTFTEKWNTDNTLGT CEEEECCCCCCCCCC	48.93	19608861
88 (in isoform 1)	Phosphorylation	-	29.52	24719451
89	Acetylation	FTEKWNTDNTLGTEI EEECCCCCCCCCCEE	42.79	19608861
93 (in isoform 1)	Phosphorylation	-	21.18	25147952
109	Phosphorylation	ICQGLKLTFDTTFSP HHCCCEEEEEEEECC	20.20	26846344
109 (in isoform 2)	Ubiquitination	-	20.20	21890473
112	Phosphorylation	GLKLTFDTTFSPNTG CCEEEEEEEECCCCC	26.08	30266825
113	Phosphorylation	LKLTFDTTFSPNTGK CEEEEEEEECCCCCC	24.78	22167270
115	Phosphorylation	LTFDTTFSPNTGKKS EEEEEEECCCCCCCC	18.36	19664994
118	Phosphorylation	DTTFSPNTGKKSGKI EEEECCCCCCCCCCC	54.48	26846344
120	Acetylation	TFSPNTGKKSGKIKS EECCCCCCCCCCCCC	41.55	25953088
120	Ubiquitination	TFSPNTGKKSGKIKS EECCCCCCCCCCCCC	41.55	21906983
120	2-Hydroxyisobutyrylation	TFSPNTGKKSGKIKS EECCCCCCCCCCCCC	41.55	-
120	Malonylation	TFSPNTGKKSGKIKS EECCCCCCCCCCCCC	41.55	26320211
120 (in isoform 3)	Ubiquitination	-	41.55	21890473
121	Ubiquitination	FSPNTGKKSGKIKSS ECCCCCCCCCCCCCC	66.83	25621951
124	Ubiquitination	NTGKKSGKIKSSYKR CCCCCCCCCCCCCHH	54.79	25621951
128	Phosphorylation	KSGKIKSSYKRECIN CCCCCCCCCHHHHHC	29.67	20833797
128 (in isoform 1)	Phosphorylation	-	29.67	21406692
130 (in isoform 1)	Phosphorylation	-	43.60	24719451
133 (in isoform 1)	Phosphorylation	-	2.65	21406692
135 (in isoform 1)	Ubiquitination	-	41.88	21890473
136 (in isoform 1)	Ubiquitination	-	3.51	-
184	Phosphorylation	RNNFAVGYRTGDFQL CCCEEEEEECCCEEE	9.82	23911959
204	Phosphorylation	DGTEFGGSIYQKVCE CCCCCCCHHHHHHHC	20.64	28152594
206	Phosphorylation	TEFGGSIYQKVCEDL CCCCCHHHHHHHCCC	12.18	28152594
224 (in isoform 2)	Ubiquitination	-	17.36	21890473
235	Acetylation	TRFGIAAKYQLDPTA CEEEEEEEEECCCCC	25.22	25825284
235	Ubiquitination	TRFGIAAKYQLDPTA CEEEEEEEEECCCCC	25.22	21906983
235 (in isoform 3)	Ubiquitination	-	25.22	21890473
236	Phosphorylation	RFGIAAKYQLDPTAS EEEEEEEEECCCCCE	15.02	28152594
243	Phosphorylation	YQLDPTASISAKVNN EECCCCCEEEEEECC	21.39	25627689
245	Phosphorylation	LDPTASISAKVNNSS CCCCCEEEEEECCCC	21.39	-
247	Malonylation	PTASISAKVNNSSLI CCCEEEEEECCCCEE	38.41	26320211
247	Acetylation	PTASISAKVNNSSLI CCCEEEEEECCCCEE	38.41	26051181
250 (in isoform 1)	Ubiquitination	-	35.64	21890473
251	Phosphorylation	ISAKVNNSSLIGVGY EEEEECCCCEEEECC	22.71	25159151
251	O-linked_Glycosylation	ISAKVNNSSLIGVGY EEEEECCCCEEEECC	22.71	23301498
252	Phosphorylation	SAKVNNSSLIGVGYT EEEECCCCEEEECCC	26.57	28152594
258	Phosphorylation	SSLIGVGYTQTLRPG CCEEEECCCCCCCCC	8.02	28152594
259	Phosphorylation	SLIGVGYTQTLRPGV CEEEECCCCCCCCCC	14.78	28152594
259	O-linked_Glycosylation	SLIGVGYTQTLRPGV CEEEECCCCCCCCCC	14.78	23301498
261	Phosphorylation	IGVGYTQTLRPGVKL EEECCCCCCCCCCEE	19.55	25849741
262 (in isoform 1)	Ubiquitination	-	4.47	-
269	Phosphorylation	LRPGVKLTLSALVDG CCCCCEEEEEEEECC	16.98	21712546
271	Phosphorylation	PGVKLTLSALVDGKS CCCEEEEEEEECCEE	17.83	21712546
274 (in isoform 2)	Ubiquitination	-	10.23	21890473
277	Acetylation	LSALVDGKSINAGGH EEEEECCEEECCCCC	43.64	26051181
277	Ubiquitination	LSALVDGKSINAGGH EEEEECCEEECCCCC	43.64	25621951
278	Phosphorylation	SALVDGKSINAGGHK EEEECCEEECCCCCE	26.97	22210691
285	Ubiquitination	SINAGGHKVGLALEL EECCCCCEEEEEEEE	41.07	21890473
285	Acetylation	SINAGGHKVGLALEL EECCCCCEEEEEEEE	41.07	26051181
285 (in isoform 3)	Ubiquitination	-	41.07	21890473
300 (in isoform 1)	Ubiquitination	-		21890473

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
48	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VDAC2_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 VDAC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAK_HUMAN	BAK1	physical	12881569
A4_HUMAN	APP	physical	21832049
VDAC3_HUMAN	VDAC3	physical	22939629
ZFR_HUMAN	ZFR	physical	22939629
ZN454_HUMAN	ZNF454	physical	22939629
ARF5_HUMAN	ARF5	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
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
ILVBL_HUMAN	ILVBL	physical	26344197
MAGT1_HUMAN	MAGT1	physical	26344197
NDUAC_HUMAN	NDUFA12	physical	26344197
NDUA8_HUMAN	NDUFA8	physical	26344197
NDUA9_HUMAN	NDUFA9	physical	26344197
NDUV1_HUMAN	NDUFV1	physical	26344197
PHB_HUMAN	PHB	physical	26344197
PHB2_HUMAN	PHB2	physical	26344197
RER1_HUMAN	RER1	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
SGPL1_HUMAN	SGPL1	physical	26344197
ADT2_HUMAN	SLC25A5	physical	26344197
SSRG_HUMAN	SSR3	physical	26344197
STX12_HUMAN	STX12	physical	26344197
STX7_HUMAN	STX7	physical	26344197
TOM40_HUMAN	TOMM40	physical	26344197
TSPO_HUMAN	TSPO	physical	26344197
QCR8_HUMAN	UQCRQ	physical	26344197

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 VDAC2_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-115, 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-31; LYS-39; LYS-72 ANDLYS-74, 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-115, 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-115, AND MASSSPECTROMETRY.	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-115, 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-115, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND MASSSPECTROMETRY.	17081983 [Abstract]