dbPTM

VDAC1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VDAC1_RAT
UniProt AC	Q9Z2L0
Protein Name	Voltage-dependent anion-selective channel protein 1
Gene Name	Vdac1
Organism	Rattus norvegicus (Rat).
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: 25628567 May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (By similarity]
Protein Sequence	MAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTETTKVNGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKREHINLGCDVDFDIAGPSIRGALVLGYEGWLAGYQMNFETSKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQVDPDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVPPTYAD ------CCCCCCHHH	23.64	17478130
6	Phosphorylation	--MAVPPTYADLGKS --CCCCCCHHHCCHH	25.85	25575281
7	Phosphorylation	-MAVPPTYADLGKSA -CCCCCCHHHCCHHH	12.14	25575281
12	Acetylation	PTYADLGKSARDVFT CCHHHCCHHHHHHHH	48.52	22902405
12	Ubiquitination	PTYADLGKSARDVFT CCHHHCCHHHHHHHH	48.52	-
13	Phosphorylation	TYADLGKSARDVFTK CHHHCCHHHHHHHHC	27.09	17478130
19	Phosphorylation	KSARDVFTKGYGFGL HHHHHHHHCCCCCEE	24.33	23991683
20	Acetylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	22902405
20	Succinylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	-
20	Ubiquitination	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	-
20	Succinylation	SARDVFTKGYGFGLI HHHHHHHCCCCCEEE	38.38	-
22	Phosphorylation	RDVFTKGYGFGLIKL HHHHHCCCCCEEEEE	15.73	23991683
28	Acetylation	GYGFGLIKLDLKTKS CCCCEEEEEECCCCC	40.78	25786129
32	Acetylation	GLIKLDLKTKSENGL EEEEEECCCCCCCCC	54.28	22902405
33	Phosphorylation	LIKLDLKTKSENGLE EEEEECCCCCCCCCE	47.29	25575281
34	Ubiquitination	IKLDLKTKSENGLEF EEEECCCCCCCCCEE	54.94	-
34	Acetylation	IKLDLKTKSENGLEF EEEECCCCCCCCCEE	54.94	22902405
35	Phosphorylation	KLDLKTKSENGLEFT EEECCCCCCCCCEEE	41.34	25575281
42	Phosphorylation	SENGLEFTSSGSANT CCCCCEEEECCCCCC	16.77	30181290
43	Phosphorylation	ENGLEFTSSGSANTE CCCCEEEECCCCCCE	37.71	30181290
44	Phosphorylation	NGLEFTSSGSANTET CCCEEEECCCCCCEE	33.44	30181290
46	Phosphorylation	LEFTSSGSANTETTK CEEEECCCCCCEEEE	21.94	30181290
49	Phosphorylation	TSSGSANTETTKVNG EECCCCCCEEEEECC	34.13	30181290
51	Phosphorylation	SGSANTETTKVNGSL CCCCCCEEEEECCEE	29.85	30181290
52	Phosphorylation	GSANTETTKVNGSLE CCCCCEEEEECCEEE	27.11	30181290
53	Acetylation	SANTETTKVNGSLET CCCCEEEEECCEEEE	40.91	22902405
57	Phosphorylation	ETTKVNGSLETKYRW EEEEECCEEEEEEEE	20.16	30181290
60	Phosphorylation	KVNGSLETKYRWTEY EECCEEEEEEEEEEE	38.37	30181290
61	Acetylation	VNGSLETKYRWTEYG ECCEEEEEEEEEEEE	24.36	22902405
62	Phosphorylation	NGSLETKYRWTEYGL CCEEEEEEEEEEEEC	20.85	23991683
62	Nitration	NGSLETKYRWTEYGL CCEEEEEEEEEEEEC	20.85	-
65	Phosphorylation	LETKYRWTEYGLTFT EEEEEEEEEEECEEE	15.44	23991683
67	Nitration	TKYRWTEYGLTFTEK EEEEEEEEECEEEEE	15.29	-
67	Phosphorylation	TKYRWTEYGLTFTEK EEEEEEEEECEEEEE	15.29	23991683
70	Phosphorylation	RWTEYGLTFTEKWNT EEEEEECEEEEECCC	24.93	23991683
77	Phosphorylation	TFTEKWNTDNTLGTE EEEEECCCCCCCCCE	29.52	23991683
80	Phosphorylation	EKWNTDNTLGTEITV EECCCCCCCCCEEEH	29.40	23991683
83	Phosphorylation	NTDNTLGTEITVEDQ CCCCCCCCEEEHHHH	27.59	23991683
96	Acetylation	DQLARGLKLTFDSSF HHHHHCCEEEECCCC	48.59	22902405
98	Phosphorylation	LARGLKLTFDSSFSP HHHCCEEEECCCCCC	24.65	23991683
101	Phosphorylation	GLKLTFDSSFSPNTG CCEEEECCCCCCCCC	29.14	27097102
102	Phosphorylation	LKLTFDSSFSPNTGK CEEEECCCCCCCCCC	31.43	27097102
104	Phosphorylation	LTFDSSFSPNTGKKN EEECCCCCCCCCCCC	21.13	23991683
107	Phosphorylation	DSSFSPNTGKKNAKI CCCCCCCCCCCCCEE	54.48	27097102
109	Acetylation	SFSPNTGKKNAKIKT CCCCCCCCCCCEEEC	40.59	25786129
119	Acetylation	AKIKTGYKREHINLG CEEECCCCHHHEECC	53.29	22902405
137	Phosphorylation	DFDIAGPSIRGALVL EECCCCCCHHHEEEE	24.81	17478130
174	Acetylation	SNFAVGYKTDEFQLH CCEEEEEECCEEEEE	43.50	22902405
193	Phosphorylation	DGTEFGGSIYQKVNK CCCCCCHHHHHHHHH	20.64	-
195	Phosphorylation	TEFGGSIYQKVNKKL CCCCHHHHHHHHHHH	12.18	-
197	Acetylation	FGGSIYQKVNKKLET CCHHHHHHHHHHHHH	30.70	22902405
200	Acetylation	SIYQKVNKKLETAVN HHHHHHHHHHHHHHH	62.82	22902405
201	Acetylation	IYQKVNKKLETAVNL HHHHHHHHHHHHHHH	46.48	22902405
211	Phosphorylation	TAVNLAWTAGNSNTR HHHHHHHCCCCCCCC	21.05	23991683
215	Phosphorylation	LAWTAGNSNTRFGIA HHHCCCCCCCCEEEE	38.36	23991683
217	Phosphorylation	WTAGNSNTRFGIAAK HCCCCCCCCEEEEEE	27.48	23991683
224	Acetylation	TRFGIAAKYQVDPDA CCEEEEEEEECCCCC	27.48	25786129
236	Acetylation	PDACFSAKVNNSSLI CCCCEEEEECCCCCC	44.27	22902405
240	O-linked_Glycosylation	FSAKVNNSSLIGLGY EEEEECCCCCCEECC	22.71	27213235
240	Phosphorylation	FSAKVNNSSLIGLGY EEEEECCCCCCEECC	22.71	23991683
241	Phosphorylation	SAKVNNSSLIGLGYT EEEECCCCCCEECCC	26.57	23991683
252	Acetylation	LGYTQTLKPGIKLTL ECCCCCCCCCCEEEH	44.58	22902405
256	Acetylation	QTLKPGIKLTLSALL CCCCCCCEEEHHHHH	41.14	26302492
260	O-linked_Glycosylation	PGIKLTLSALLDGKN CCCEEEHHHHHCCCC	16.19	27213235
260	Phosphorylation	PGIKLTLSALLDGKN CCCEEEHHHHHCCCC	16.19	23984901
266	Acetylation	LSALLDGKNVNAGGH HHHHHCCCCCCCCCC	58.34	22902405
274	Ubiquitination	NVNAGGHKLGLGLEF CCCCCCCCCCCCCEE	47.74	-
274	Acetylation	NVNAGGHKLGLGLEF CCCCCCCCCCCCCEE	47.74	22902405

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
193	S	Phosphorylation	Kinase	NEK1	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
193	S	Phosphorylation	-
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	-
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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
B2L11_HUMAN	BCL2L11	physical	12118373

Drug and Disease Associations

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

Regulatory Network of VDAC1_RAT

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Post-translational modifications of rat liver mitochondrial outermembrane proteins identified by mass spectrometry."; Distler A.M., Kerner J., Hoppel C.L.; Biochim. Biophys. Acta 1774:628-636(2007). Cited for: PROTEIN SEQUENCE OF 2-14 AND 135-138, ACETYLATION AT ALA-2,PHOSPHORYLATION AT SER-13 AND SER-137, AND MASS SPECTROMETRY.	17478130 [Abstract]
Phosphorylation
Reference	PubMed
"Post-translational modifications of rat liver mitochondrial outermembrane proteins identified by mass spectrometry."; Distler A.M., Kerner J., Hoppel C.L.; Biochim. Biophys. Acta 1774:628-636(2007). Cited for: PROTEIN SEQUENCE OF 2-14 AND 135-138, ACETYLATION AT ALA-2,PHOSPHORYLATION AT SER-13 AND SER-137, AND MASS SPECTROMETRY.	17478130 [Abstract]

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