dbPTM

VDAC1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VDAC1_MOUSE
UniProt AC	Q60932
Protein Name	Voltage-dependent anion-selective channel protein 1
Gene Name	Vdac1
Organism	Mus musculus (Mouse).
Sequence Length	296
Subcellular Localization	Isoform Mt-VDAC1: Mitochondrion outer membrane Multi-pass membrane protein . Isoform Pl-VDAC1: 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. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis..
Protein Sequence	MCSFFLVLLLWQNMAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTETTKVNGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKREHINLGCDVDFDIAGPSIRGALVLGYEGWLAGYQMNFETSKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQVDPDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MCSFFLVLL ------CCHHHHHHH	4.96	-
2 (in isoform 2)	Acetylation	-	4.96	-
14	Acetylation	VLLLWQNMAVPPTYA HHHHHHHCCCCCCHH	2.08	-
19	Phosphorylation	QNMAVPPTYADLGKS HHCCCCCCHHHHCHH	25.85	29895711
20	Ubiquitination	NMAVPPTYADLGKSA HCCCCCCHHHHCHHH	12.14	27667366
25	Malonylation	PTYADLGKSARDVFT CCHHHHCHHHHHHHH	48.52	26320211
25	Acetylation	PTYADLGKSARDVFT CCHHHHCHHHHHHHH	48.52	23806337
26	Phosphorylation	TYADLGKSARDVFTK CHHHHCHHHHHHHHC	27.09	23375375
32	Phosphorylation	KSARDVFTKGYGFGL HHHHHHHHCCCCCEE	24.33	22817900
33	Acetylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	23806337
33	Succinylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	-
33	Ubiquitination	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	-
33	Malonylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	25418362
33	Succinylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	23806337
34	Ubiquitination	ARDVFTKGYGFGLIK HHHHHHCCCCCEEEE	25.41	27667366
35	Phosphorylation	RDVFTKGYGFGLIKL HHHHHCCCCCEEEEE	15.73	23140645
41	Acetylation	GYGFGLIKLDLKTKS CCCCEEEEEECCCCC	40.78	23864654
41	Ubiquitination	GYGFGLIKLDLKTKS CCCCEEEEEECCCCC	40.78	-
41	Malonylation	GYGFGLIKLDLKTKS CCCCEEEEEECCCCC	40.78	26073543
45	Acetylation	GLIKLDLKTKSENGL EEEEEECCCCCCCCC	54.28	23201123
46	Phosphorylation	LIKLDLKTKSENGLE EEEEECCCCCCCCCE	47.29	22817900
47	Ubiquitination	IKLDLKTKSENGLEF EEEECCCCCCCCCEE	54.94	22790023
47	Acetylation	IKLDLKTKSENGLEF EEEECCCCCCCCCEE	54.94	23201123
48	Phosphorylation	KLDLKTKSENGLEFT EEECCCCCCCCCEEE	41.34	28464351
56	Phosphorylation	ENGLEFTSSGSANTE CCCCEEECCCCCCCE	37.71	29899451
59	Phosphorylation	LEFTSSGSANTETTK CEEECCCCCCCEEEE	21.94	25521595
61	Ubiquitination	FTSSGSANTETTKVN EECCCCCCCEEEEEC	39.90	27667366
65	Phosphorylation	GSANTETTKVNGSLE CCCCCEEEEECCEEE	27.11	28464351
66	Ubiquitination	SANTETTKVNGSLET CCCCEEEEECCEEEE	40.91	22790023
70	Phosphorylation	ETTKVNGSLETKYRW EEEEECCEEEEEEEE	20.16	22324799
73	Phosphorylation	KVNGSLETKYRWTEY EECCEEEEEEEEEEE	38.37	23737553
74	Acetylation	VNGSLETKYRWTEYG ECCEEEEEEEEEEEE	24.36	23864654
74	Ubiquitination	VNGSLETKYRWTEYG ECCEEEEEEEEEEEE	24.36	-
74	Malonylation	VNGSLETKYRWTEYG ECCEEEEEEEEEEEE	24.36	26073543
75	Phosphorylation	NGSLETKYRWTEYGL CCEEEEEEEEEEEEC	20.85	22807455
78	Phosphorylation	LETKYRWTEYGLTFT EEEEEEEEEEECEEE	15.44	26745281
80	Phosphorylation	TKYRWTEYGLTFTEK EEEEEEEEECEEEEE	15.29	29899451
83	Phosphorylation	RWTEYGLTFTEKWNT EEEEEECEEEEECCC	24.93	26745281
85	Phosphorylation	TEYGLTFTEKWNTDN EEEECEEEEECCCCC	31.27	28066266
93	Phosphorylation	EKWNTDNTLGTEITV EECCCCCCCCCEEEH	29.40	28464351
102	Ubiquitination	GTEITVEDQLARGLK CCEEEHHHHHHHCCE	44.45	27667366
109	Ubiquitination	DQLARGLKLTFDSSF HHHHHCCEEEECCCC	48.59	27667366
109	Acetylation	DQLARGLKLTFDSSF HHHHHCCEEEECCCC	48.59	23864654
109	Malonylation	DQLARGLKLTFDSSF HHHHHCCEEEECCCC	48.59	26320211
111	Phosphorylation	LARGLKLTFDSSFSP HHHCCEEEECCCCCC	24.65	25619855
114	Phosphorylation	GLKLTFDSSFSPNTG CCEEEECCCCCCCCC	29.14	24925903
115	Phosphorylation	LKLTFDSSFSPNTGK CEEEECCCCCCCCCC	31.43	24925903
115	Ubiquitination	LKLTFDSSFSPNTGK CEEEECCCCCCCCCC	31.43	27667366
116	Ubiquitination	KLTFDSSFSPNTGKK EEEECCCCCCCCCCC	19.07	27667366
117	Phosphorylation	LTFDSSFSPNTGKKN EEECCCCCCCCCCCC	21.13	24925903
120	Phosphorylation	DSSFSPNTGKKNAKI CCCCCCCCCCCCCEE	54.48	25521595
122	Acetylation	SFSPNTGKKNAKIKT CCCCCCCCCCCEEEC	40.59	23576753
122	Ubiquitination	SFSPNTGKKNAKIKT CCCCCCCCCCCEEEC	40.59	-
122	Malonylation	SFSPNTGKKNAKIKT CCCCCCCCCCCEEEC	40.59	26320211
123	Ubiquitination	FSPNTGKKNAKIKTG CCCCCCCCCCEEECC	64.58	-
123	Malonylation	FSPNTGKKNAKIKTG CCCCCCCCCCEEECC	64.58	25418362
123	Succinylation	FSPNTGKKNAKIKTG CCCCCCCCCCEEECC	64.58	26388266
132	Acetylation	AKIKTGYKREHINLG CEEECCCCHHHEECC	53.29	7627733
140	S-nitrosocysteine	REHINLGCDVDFDIA HHHEECCCCEEECCC	5.33	-
140	Glutathionylation	REHINLGCDVDFDIA HHHEECCCCEEECCC	5.33	24333276
140	S-nitrosylation	REHINLGCDVDFDIA HHHEECCCCEEECCC	5.33	24895380
143	Ubiquitination	INLGCDVDFDIAGPS EECCCCEEECCCCCC	23.42	27667366
174	Ubiquitination	QMNFETSKSRVTQSN EEECCCCCCCEEECC	50.10	-
175	Phosphorylation	MNFETSKSRVTQSNF EECCCCCCCEEECCE	31.58	25521595
180	Phosphorylation	SKSRVTQSNFAVGYK CCCCEEECCEEEEEE	25.25	28542873
187	Succinylation	SNFAVGYKTDEFQLH CCEEEEEECCEEEEE	43.50	23954790
191	Ubiquitination	VGYKTDEFQLHTNVN EEEECCEEEEEECCC	11.87	27667366
197	Ubiquitination	EFQLHTNVNDGTEFG EEEEEECCCCCCCCC	7.89	27667366
201	Phosphorylation	HTNVNDGTEFGGSIY EECCCCCCCCCHHHH	30.88	28464351
206	Phosphorylation	DGTEFGGSIYQKVNK CCCCCCHHHHHHHHH	20.64	-
208	Phosphorylation	TEFGGSIYQKVNKKL CCCCHHHHHHHHHHH	12.18	22817900
210	Ubiquitination	FGGSIYQKVNKKLET CCHHHHHHHHHHHHH	30.70	-
210	Acetylation	FGGSIYQKVNKKLET CCHHHHHHHHHHHHH	30.70	23864654
210	Malonylation	FGGSIYQKVNKKLET CCHHHHHHHHHHHHH	30.70	26320211
214	Acetylation	IYQKVNKKLETAVNL HHHHHHHHHHHHHHH	46.48	23576753
224	Phosphorylation	TAVNLAWTAGNSNTR HHHHHHHHCCCCCCC	21.05	22210690
228	Phosphorylation	LAWTAGNSNTRFGIA HHHHCCCCCCCEEEE	38.36	22210690
230	Phosphorylation	WTAGNSNTRFGIAAK HHCCCCCCCEEEEEE	27.48	22210690
237	Acetylation	TRFGIAAKYQVDPDA CCEEEEEEEECCCCC	27.48	23864654
237	Malonylation	TRFGIAAKYQVDPDA CCEEEEEEEECCCCC	27.48	26320211
238	Phosphorylation	RFGIAAKYQVDPDAC CEEEEEEEECCCCCC	14.72	28464351
245	S-nitrosocysteine	YQVDPDACFSAKVNN EECCCCCCEEEEECC	3.45	-
245	Glutathionylation	YQVDPDACFSAKVNN EECCCCCCEEEEECC	3.45	24333276
245	S-nitrosylation	YQVDPDACFSAKVNN EECCCCCCEEEEECC	3.45	24895380
245	S-palmitoylation	YQVDPDACFSAKVNN EECCCCCCEEEEECC	3.45	28526873
249	Acetylation	PDACFSAKVNNSSLI CCCCEEEEECCCCCC	44.27	23864654
249	Succinylation	PDACFSAKVNNSSLI CCCCEEEEECCCCCC	44.27	23806337
249	Malonylation	PDACFSAKVNNSSLI CCCCEEEEECCCCCC	44.27	26320211
252	Ubiquitination	CFSAKVNNSSLIGLG CEEEEECCCCCCEEC	35.64	27667366
253	Phosphorylation	FSAKVNNSSLIGLGY EEEEECCCCCCEECC	22.71	25521595
254	Phosphorylation	SAKVNNSSLIGLGYT EEEECCCCCCEECCC	26.57	23737553
260	Phosphorylation	SSLIGLGYTQTLKPG CCCCEECCCCCCCCC	10.75	27742792
261	Phosphorylation	SLIGLGYTQTLKPGI CCCEECCCCCCCCCC	17.18	27742792
263	Phosphorylation	IGLGYTQTLKPGIKL CEECCCCCCCCCCEE	29.02	29899451
265	Acetylation	LGYTQTLKPGIKLTL ECCCCCCCCCCEEEH	44.58	23576753
265	Ubiquitination	LGYTQTLKPGIKLTL ECCCCCCCCCCEEEH	44.58	-
265	Malonylation	LGYTQTLKPGIKLTL ECCCCCCCCCCEEEH	44.58	26320211
274	Ubiquitination	GIKLTLSALLDGKNV CCEEEHHHHHCCCCC	18.43	27667366
279	Acetylation	LSALLDGKNVNAGGH HHHHHCCCCCCCCCC	58.34	23864654
279	Ubiquitination	LSALLDGKNVNAGGH HHHHHCCCCCCCCCC	58.34	-
279	Malonylation	LSALLDGKNVNAGGH HHHHHCCCCCCCCCC	58.34	26320211
287	Acetylation	NVNAGGHKLGLGLEF CCCCCCCCCCCCCEE	47.74	24062335
287	Ubiquitination	NVNAGGHKLGLGLEF CCCCCCCCCCCCCEE	47.74	22790023
334	Ubiquitination	--------------------------------------------- ---------------------------------------------		27667366
356	Ubiquitination	------------------------------------------------------------------- -------------------------------------------------------------------		27667366

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
206	S	Phosphorylation	Kinase	NEK1	P51954	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
206	S	Phosphorylation	-
Phosphorylation at Ser-206 by NEK1 promotes the open conformational state preventing excessive mitochondrial membrane permeability and subsequent apoptotic cell death after injury.
287	K	ubiquitylation	32047033
Undergoes monoubiquitination and polyubiquitination by PRKN; monoubiquitination at Lys-287 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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of VDAC1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of VDAC1_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-41; LYS-74 ANDLYS-237, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASSSPECTROMETRY.	17208939 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80 AND TYR-208, AND MASSSPECTROMETRY.	18034455 [Abstract]

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