VDAC2_MOUSE - dbPTM
VDAC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VDAC2_MOUSE
UniProt AC Q60930
Protein Name Voltage-dependent anion-selective channel protein 2
Gene Name Vdac2
Organism Mus musculus (Mouse).
Sequence Length 295
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 (By similarity)..
Protein Sequence MAECCVPVCPRPMCIPPPYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVSGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSAYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRSNFAVGYRTGDFQLHTNVNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSFNAGGHKLGLALELEA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
9S-palmitoylationAECCVPVCPRPMCIP
CCCEECCCCCCEECC		1.6128680068
14GlutathionylationPVCPRPMCIPPPYAD
CCCCCCEECCCCCCH		4.7224333276
24UbiquitinationPPYADLGKAARDIFN
CCCCHHHHHHHHHHH		46.2822790023
32AcetylationAARDIFNKGFGFGLV
HHHHHHHCCCCCEEE		44.8823576753
32MalonylationAARDIFNKGFGFGLV
HHHHHHHCCCCCEEE		44.8826073543
32SuccinylationAARDIFNKGFGFGLV
HHHHHHHCCCCCEEE		44.8823806337
32SuccinylationAARDIFNKGFGFGLV
HHHHHHHCCCCCEEE		44.88-
32UbiquitinationAARDIFNKGFGFGLV
HHHHHHHCCCCCEEE		44.8827667366
40SuccinylationGFGFGLVKLDVKTKS
CCCCEEEEEEECCCC		43.9726388266
40UbiquitinationGFGFGLVKLDVKTKS
CCCCEEEEEEECCCC		43.97-
40AcetylationGFGFGLVKLDVKTKS
CCCCEEEEEEECCCC		43.9724062335
48S-nitrosocysteineLDVKTKSCSGVEFST
EEECCCCCCCCEEEC		4.35-
48GlutathionylationLDVKTKSCSGVEFST
EEECCCCCCCCEEEC		4.3524333276
48S-palmitoylationLDVKTKSCSGVEFST
EEECCCCCCCCEEEC		4.3528526873
48S-nitrosylationLDVKTKSCSGVEFST
EEECCCCCCCCEEEC		4.3524895380
65UbiquitinationSSNTDTGKVSGTLET
CCCCCCCEEEEEEEC		35.0122790023
67PhosphorylationNTDTGKVSGTLETKY
CCCCCEEEEEEECEE		29.5529899451
69PhosphorylationDTGKVSGTLETKYKW
CCCEEEEEEECEEEE		17.5724899341
73UbiquitinationVSGTLETKYKWCEYG
EEEEEECEEEEECCC		35.1427667366
73AcetylationVSGTLETKYKWCEYG
EEEEEECEEEEECCC		35.1423236377
73MalonylationVSGTLETKYKWCEYG
EEEEEECEEEEECCC		35.1426320211
75UbiquitinationGTLETKYKWCEYGLT
EEEECEEEEECCCCE		47.10-
75AcetylationGTLETKYKWCEYGLT
EEEECEEEEECCCCE		47.1024062335
75MalonylationGTLETKYKWCEYGLT
EEEECEEEEECCCCE		47.1026320211
77GlutathionylationLETKYKWCEYGLTFT
EECEEEEECCCCEEE		2.2324333276
77S-nitrosylationLETKYKWCEYGLTFT
EECEEEEECCCCEEE		2.2324895380
77S-palmitoylationLETKYKWCEYGLTFT
EECEEEEECCCCEEE		2.2328526873
77S-nitrosocysteineLETKYKWCEYGLTFT
EECEEEEECCCCEEE		2.23-
79PhosphorylationTKYKWCEYGLTFTEK
CEEEEECCCCEEEEC		17.82-
104S-nitrosocysteineIAIEDQICQGLKLTF
EEEECHHHCCCEEEE		1.87-
104S-nitrosylationIAIEDQICQGLKLTF
EEEECHHHCCCEEEE		1.8724895380
104GlutathionylationIAIEDQICQGLKLTF
EEEECHHHCCCEEEE		1.8724333276
104S-palmitoylationIAIEDQICQGLKLTF
EEEECHHHCCCEEEE		1.8728526873
110PhosphorylationICQGLKLTFDTTFSP
HHCCCEEEEEEEECC		20.2025159016
113PhosphorylationGLKLTFDTTFSPNTG
CCEEEEEEEECCCCC		26.0822942356
114PhosphorylationLKLTFDTTFSPNTGK
CEEEEEEEECCCCCC		24.7827087446
116PhosphorylationLTFDTTFSPNTGKKS
EEEEEEECCCCCCCC		18.3627087446
119PhosphorylationDTTFSPNTGKKSGKI
EEEECCCCCCCCCCC		54.4822942356
121AcetylationTFSPNTGKKSGKIKS
EECCCCCCCCCCCCE		41.5523576753
121UbiquitinationTFSPNTGKKSGKIKS
EECCCCCCCCCCCCE		41.5522790023
122MalonylationFSPNTGKKSGKIKSA
ECCCCCCCCCCCCEE		66.8325418362
122UbiquitinationFSPNTGKKSGKIKSA
ECCCCCCCCCCCCEE		66.83-
131AcetylationGKIKSAYKRECINLG
CCCCEEHHHHHHHCC		41.246571565
200PhosphorylationHTNVNNGTEFGGSIY
EEECCCCCCCCCHHH		30.2028464351
205PhosphorylationNGTEFGGSIYQKVCE
CCCCCCCHHHHHHHC		20.6422817900
207PhosphorylationTEFGGSIYQKVCEDF
CCCCCHHHHHHHCCC		12.1822817900
236AcetylationTRFGIAAKYQLDPTA
CEEEEEEEEECCCCC		25.2223236377
237PhosphorylationRFGIAAKYQLDPTAS
EEEEEEEEECCCCCE		15.0221082442
242PhosphorylationAKYQLDPTASISAKV
EEEECCCCCEEEEEE		32.4821082442
244PhosphorylationYQLDPTASISAKVNN
EECCCCCEEEEEECC		21.3921082442
248MalonylationPTASISAKVNNSSLI
CCCEEEEEECCCCEE		38.4126073543
248SuccinylationPTASISAKVNNSSLI
CCCEEEEEECCCCEE		38.4124315375
252PhosphorylationISAKVNNSSLIGVGY
EEEEECCCCEEEECC		22.7125521595
253PhosphorylationSAKVNNSSLIGVGYT
EEEECCCCEEEECCC		26.5727742792
259PhosphorylationSSLIGVGYTQTLRPG
CCEEEECCCCCCCCC		8.0219060867
260PhosphorylationSLIGVGYTQTLRPGV
CEEEECCCCCCCCCC		14.7821183079
262PhosphorylationIGVGYTQTLRPGVKL
EEECCCCCCCCCCEE		19.5520415495
272PhosphorylationPGVKLTLSALVDGKS
CCCEEEEEEEECCCC		17.8328418008
278UbiquitinationLSALVDGKSFNAGGH
EEEEECCCCCCCCCC		47.6222790023
278AcetylationLSALVDGKSFNAGGH
EEEEECCCCCCCCCC		47.62-
279PhosphorylationSALVDGKSFNAGGHK
EEEECCCCCCCCCCE		29.3029899451
286UbiquitinationSFNAGGHKLGLALEL
CCCCCCCEEEEEEEE		47.7422790023
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

Oops, there are no upstream regulatory protein records of VDAC2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VDAC2_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VDAC2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VDAC2_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-32 AND LYS-75, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-207, AND MASSSPECTROMETRY.

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