VDAC3_MOUSE - dbPTM
VDAC3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VDAC3_MOUSE
UniProt AC Q60931
Protein Name Voltage-dependent anion-selective channel protein 3
Gene Name Vdac3
Organism Mus musculus (Mouse).
Sequence Length 283
Subcellular Localization Mitochondrion outer membrane.
Protein Description Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules..
Protein Sequence MCNTPTYCDLGKAAKDVFNKGYGFGMVKIDLKTKSCSGVEFSTSGHAYTDTGKASGNLETKYKVCNYGLTFTQKWNTDNTLGTEISWENKLAEGLKLTLDTIFVPNTGKKSGKLKASYRRDCFSLGSNVDIDFSGPTIYGWAVLAFEGWLAGYQMSFDTAKSKLSQNNFALGYKAADFQLHTHVNDGTEFGGSIYQKVNERIETSINLAWTAGSNNTRFGIAAKYKLDCRTSLSAKVNNASLIGLGYTQTLRPGVKLTLSALIDGKNFNAGGHKVGLGFELEA
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
2Acetylation------MCNTPTYCD
------CCCCCCCCC		8.5823806337
4Phosphorylation----MCNTPTYCDLG
----CCCCCCCCCHH		16.4526824392
6Phosphorylation--MCNTPTYCDLGKA
--CCCCCCCCCHHHH		34.4425619855
7Phosphorylation-MCNTPTYCDLGKAA
-CCCCCCCCCHHHHH		5.7925619855
12AcetylationPTYCDLGKAAKDVFN
CCCCCHHHHHHHHHH		53.0923806337
12MalonylationPTYCDLGKAAKDVFN
CCCCCHHHHHHHHHH		53.0926320211
15SuccinylationCDLGKAAKDVFNKGY
CCHHHHHHHHHHCCC		60.3223954790
15MalonylationCDLGKAAKDVFNKGY
CCHHHHHHHHHHCCC		60.3226320211
15AcetylationCDLGKAAKDVFNKGY
CCHHHHHHHHHHCCC		60.3223576753
15UbiquitinationCDLGKAAKDVFNKGY
CCHHHHHHHHHHCCC		60.32-
20UbiquitinationAAKDVFNKGYGFGMV
HHHHHHHCCCCCEEE		41.88-
20SuccinylationAAKDVFNKGYGFGMV
HHHHHHHCCCCCEEE		41.88-
20AcetylationAAKDVFNKGYGFGMV
HHHHHHHCCCCCEEE		41.8823806337
20MalonylationAAKDVFNKGYGFGMV
HHHHHHHCCCCCEEE		41.8826320211
20SuccinylationAAKDVFNKGYGFGMV
HHHHHHHCCCCCEEE		41.8823954790
28UbiquitinationGYGFGMVKIDLKTKS
CCCCEEEEEEECCCC		22.93-
28AcetylationGYGFGMVKIDLKTKS
CCCCEEEEEEECCCC		22.9324062335
28MalonylationGYGFGMVKIDLKTKS
CCCCEEEEEEECCCC		22.9326320211
28SuccinylationGYGFGMVKIDLKTKS
CCCCEEEEEEECCCC		22.9323954790
48PhosphorylationFSTSGHAYTDTGKAS
EECCCEEEECCCCCC		10.2418034455
53UbiquitinationHAYTDTGKASGNLET
EEEECCCCCCCCCCC		41.28-
55PhosphorylationYTDTGKASGNLETKY
EECCCCCCCCCCCEE		31.5328464351
60PhosphorylationKASGNLETKYKVCNY
CCCCCCCCEEEEECC		42.72-
61MalonylationASGNLETKYKVCNYG
CCCCCCCEEEEECCC		33.4326320211
61AcetylationASGNLETKYKVCNYG
CCCCCCCEEEEECCC		33.4323864654
62PhosphorylationSGNLETKYKVCNYGL
CCCCCCEEEEECCCC		18.97-
63MalonylationGNLETKYKVCNYGLT
CCCCCEEEEECCCCE		41.7026320211
63UbiquitinationGNLETKYKVCNYGLT
CCCCCEEEEECCCCE		41.70-
63AcetylationGNLETKYKVCNYGLT
CCCCCEEEEECCCCE		41.7023864654
65GlutathionylationLETKYKVCNYGLTFT
CCCEEEEECCCCEEE		2.5824333276
65S-nitrosylationLETKYKVCNYGLTFT
CCCEEEEECCCCEEE		2.5824895380
65S-palmitoylationLETKYKVCNYGLTFT
CCCEEEEECCCCEEE		2.5828526873
65S-nitrosocysteineLETKYKVCNYGLTFT
CCCEEEEECCCCEEE		2.58-
67PhosphorylationTKYKVCNYGLTFTQK
CEEEEECCCCEEEEE		14.37-
90UbiquitinationTEISWENKLAEGLKL
CEEEECHHHHHCCEE		37.24-
90AcetylationTEISWENKLAEGLKL
CEEEECHHHHHCCEE		37.2423576753
107PhosphorylationDTIFVPNTGKKSGKL
EEEECCCCCCCCCCC		44.29-
109SuccinylationIFVPNTGKKSGKLKA
EECCCCCCCCCCCEE		41.5523954790
109AcetylationIFVPNTGKKSGKLKA
EECCCCCCCCCCCEE		41.5523576753
109UbiquitinationIFVPNTGKKSGKLKA
EECCCCCCCCCCCEE		41.55-
109MalonylationIFVPNTGKKSGKLKA
EECCCCCCCCCCCEE		41.5526320211
110UbiquitinationFVPNTGKKSGKLKAS
ECCCCCCCCCCCEEE		66.83-
110MalonylationFVPNTGKKSGKLKAS
ECCCCCCCCCCCEEE		66.8325418362
117PhosphorylationKSGKLKASYRRDCFS
CCCCCEEEEECCCCC		20.0023737553
118PhosphorylationSGKLKASYRRDCFSL
CCCCEEEEECCCCCC		17.9623737553
162PhosphorylationMSFDTAKSKLSQNNF
EEHHHHHHHHHCCCC		36.0428464351
163MalonylationSFDTAKSKLSQNNFA
EHHHHHHHHHCCCCC		51.9926320211
163AcetylationSFDTAKSKLSQNNFA
EHHHHHHHHHCCCCC		51.9923864654
163UbiquitinationSFDTAKSKLSQNNFA
EHHHHHHHHHCCCCC		51.99-
165PhosphorylationDTAKSKLSQNNFALG
HHHHHHHHCCCCCCE		34.3024899341
174MalonylationNNFALGYKAADFQLH
CCCCCEEEEEEEEEE		34.9926320211
174AcetylationNNFALGYKAADFQLH
CCCCCEEEEEEEEEE		34.9923236377
195PhosphorylationTEFGGSIYQKVNERI
CCCCCHHHHHHHHHC		12.1828464351
197AcetylationFGGSIYQKVNERIET
CCCHHHHHHHHHCCE		30.0123954790
224SuccinylationTRFGIAAKYKLDCRT
CEEEEEEEEEEECCC		33.6223806337
224AcetylationTRFGIAAKYKLDCRT
CEEEEEEEEEEECCC		33.6223864654
226MalonylationFGIAAKYKLDCRTSL
EEEEEEEEEECCCCE		36.8225418362
226AcetylationFGIAAKYKLDCRTSL
EEEEEEEEEECCCCE		36.8223864654
236MalonylationCRTSLSAKVNNASLI
CCCCEEEEECCEEEE		41.9626320211
241PhosphorylationSAKVNNASLIGLGYT
EEEECCEEEEECCCC		23.73-
247PhosphorylationASLIGLGYTQTLRPG
EEEEECCCCCCCCCC		10.7526643407
248PhosphorylationSLIGLGYTQTLRPGV
EEEECCCCCCCCCCC		17.1825521595
250PhosphorylationIGLGYTQTLRPGVKL
EECCCCCCCCCCCEE		19.5526824392
266AcetylationLSALIDGKNFNAGGH
EEEEECCCCCCCCCC		55.4023576753
266UbiquitinationLSALIDGKNFNAGGH
EEEEECCCCCCCCCC		55.40-
266MalonylationLSALIDGKNFNAGGH
EEEEECCCCCCCCCC		55.4026320211
274UbiquitinationNFNAGGHKVGLGFEL
CCCCCCCEEECCEEE		41.07-
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
-KUbiquitinationE3 ubiquitin ligasePrknQ9WVS6
PMID:30763678
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VDAC3_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 VDAC3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VDAC3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VDAC3_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-20; LYS-61 AND LYS-226, ANDMASS SPECTROMETRY.
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-48, AND MASSSPECTROMETRY.

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