ALDH2_MOUSE - dbPTM
ALDH2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALDH2_MOUSE
UniProt AC P47738
Protein Name Aldehyde dehydrogenase, mitochondrial
Gene Name Aldh2
Organism Mus musculus (Mouse).
Sequence Length 519
Subcellular Localization Mitochondrion matrix.
Protein Description Is capable of converting retinaldehyde to retinoic acid..
Protein Sequence MLRAALTTVRRGPRLSRLLSAAATSAVPAPNHQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
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
54AcetylationWHDAVSRKTFPTVNP
CHHHHHCCCCCCCCC		47.1923576753
54UbiquitinationWHDAVSRKTFPTVNP
CHHHHHCCCCCCCCC		47.1922790023
68GlutathionylationPSTGEVICQVAEGNK
CCCCEEEEEEECCCH		3.0024333276
68S-nitrosocysteinePSTGEVICQVAEGNK
CCCCEEEEEEECCCH		3.00-
68S-nitrosylationPSTGEVICQVAEGNK
CCCCEEEEEEECCCH		3.0022178444
68S-palmitoylationPSTGEVICQVAEGNK
CCCCEEEEEEECCCH		3.0028526873
75GlutarylationCQVAEGNKEDVDKAV
EEEECCCHHHHHHHH		67.1724703693
75AcetylationCQVAEGNKEDVDKAV
EEEECCCHHHHHHHH		67.1723576753
80SuccinylationGNKEDVDKAVKAARA
CCHHHHHHHHHHHHH		55.7324315375
80AcetylationGNKEDVDKAVKAARA
CCHHHHHHHHHHHHH		55.7323576753
83AcetylationEDVDKAVKAARAAFQ
HHHHHHHHHHHHHHH		40.9823864654
93PhosphorylationRAAFQLGSPWRRMDA
HHHHHCCCCCCCCCH		29.8629472430
119PhosphorylationDLIERDRTYLAALET
HHHHHCHHHHHHHHH		27.4622006019
120PhosphorylationLIERDRTYLAALETL
HHHHCHHHHHHHHHC		8.6722006019
157AcetylationYYAGWADKYHGKTIP
HHHCCHHHHCCEEEE		31.2523864654
157UbiquitinationYYAGWADKYHGKTIP
HHHCCHHHHCCEEEE		31.2522790023
161AcetylationWADKYHGKTIPIDGD
CHHHHCCEEEECCCC		29.9323576753
161SuccinylationWADKYHGKTIPIDGD
CHHHHCCEEEECCCC		29.9324315375
161UbiquitinationWADKYHGKTIPIDGD
CHHHHCCEEEECCCC		29.93-
181S-palmitoylationRHEPVGVCGQIIPWN
CCCCCCCCCCCCCCC		2.4628526873
181S-nitrosylationRHEPVGVCGQIIPWN
CCCCCCCCCCCCCCC		2.4621278135
181S-nitrosocysteineRHEPVGVCGQIIPWN
CCCCCCCCCCCCCCC		2.46-
278PhosphorylationLIQVAAGSSNLKRVT
HHHHHCCCCCCCEEE		16.0123984901
279PhosphorylationIQVAAGSSNLKRVTL
HHHHCCCCCCCEEEE		45.3123984901
282AcetylationAAGSSNLKRVTLELG
HCCCCCCCEEEEECC		49.4223576753
282UbiquitinationAAGSSNLKRVTLELG
HCCCCCCCEEEEECC		49.4222790023
285PhosphorylationSSNLKRVTLELGGKS
CCCCCEEEEECCCCC		20.6722324799
321S-nitrosylationFFNQGQCCCAGSRTF
CCCCCCCCCCCCCEE		1.0522178444
321S-nitrosocysteineFFNQGQCCCAGSRTF
CCCCCCCCCCCCCEE		1.05-
347PhosphorylationRSVARAKSRVVGNPF
HHHHHHHHCCCCCCC		29.3529472430
356PhosphorylationVVGNPFDSRTEQGPQ
CCCCCCCCCCCCCCC		41.2925521595
358PhosphorylationGNPFDSRTEQGPQVD
CCCCCCCCCCCCCCC		36.2925521595
358O-linked_GlycosylationGNPFDSRTEQGPQVD
CCCCCCCCCCCCCCC		36.2928528544
370MalonylationQVDETQFKKILGYIK
CCCHHHHHHHHHHHH		29.1426320211
370AcetylationQVDETQFKKILGYIK
CCCHHHHHHHHHHHH		29.1423576753
370UbiquitinationQVDETQFKKILGYIK
CCCHHHHHHHHHHHH		29.14-
370GlutarylationQVDETQFKKILGYIK
CCCHHHHHHHHHHHH		29.1424703693
371MalonylationVDETQFKKILGYIKS
CCHHHHHHHHHHHHC		44.4426320211
371SuccinylationVDETQFKKILGYIKS
CCHHHHHHHHHHHHC		44.4426388266
371AcetylationVDETQFKKILGYIKS
CCHHHHHHHHHHHHC		44.4422826441
377AcetylationKKILGYIKSGQQEGA
HHHHHHHHCCCCCCC		39.8023576753
377UbiquitinationKKILGYIKSGQQEGA
HHHHHHHHCCCCCCC		39.80-
377MalonylationKKILGYIKSGQQEGA
HHHHHHHHCCCCCCC		39.8026320211
377GlutarylationKKILGYIKSGQQEGA
HHHHHHHHCCCCCCC		39.8024703693
385MalonylationSGQQEGAKLLCGGGA
CCCCCCCEEEECCCC		53.5026320211
385UbiquitinationSGQQEGAKLLCGGGA
CCCCCCCEEEECCCC		53.50-
385GlutarylationSGQQEGAKLLCGGGA
CCCCCCCEEEECCCC		53.5024703693
385AcetylationSGQQEGAKLLCGGGA
CCCCCCCEEEECCCC		53.5023576753
388S-nitrosocysteineQEGAKLLCGGGAAAD
CCCCEEEECCCCCCC		7.44-
388GlutathionylationQEGAKLLCGGGAAAD
CCCCEEEECCCCCCC		7.4424333276
388S-nitrosylationQEGAKLLCGGGAAAD
CCCCEEEECCCCCCC		7.4422178444
388S-palmitoylationQEGAKLLCGGGAAAD
CCCCEEEECCCCCCC		7.4428526873
409SuccinylationPTVFGDVKDGMTIAK
CCCEECCCCCCEEEH		53.9924315375
409UbiquitinationPTVFGDVKDGMTIAK
CCCEECCCCCCEEEH		53.99-
409AcetylationPTVFGDVKDGMTIAK
CCCEECCCCCCEEEH		53.9923576753
416AcetylationKDGMTIAKEEIFGPV
CCCCEEEHHHHHHHH		52.6222733758
428SuccinylationGPVMQILKFKTIEEV
HHHHHHHEECCHHHH		46.5823954790
428AcetylationGPVMQILKFKTIEEV
HHHHHHHEECCHHHH		46.5823576753
430AcetylationVMQILKFKTIEEVVG
HHHHHEECCHHHHHC		47.1823806337
430MalonylationVMQILKFKTIEEVVG
HHHHHEECCHHHHHC		47.1826073543
430GlutarylationVMQILKFKTIEEVVG
HHHHHEECCHHHHHC		47.1824703693
430UbiquitinationVMQILKFKTIEEVVG
HHHHHEECCHHHHHC		47.18-
443SuccinylationVGRANDSKYGLAAAV
HCCCCCCCCCEEEEE		46.3224315375
443AcetylationVGRANDSKYGLAAAV
HCCCCCCCCCEEEEE		46.3223576753
443UbiquitinationVGRANDSKYGLAAAV
HCCCCCCCCCEEEEE		46.32-
444PhosphorylationGRANDSKYGLAAAVF
CCCCCCCCCEEEEEE		22.7125195567
453SuccinylationLAAAVFTKDLDKANY
EEEEEEECCHHHHHH		44.8423954790
453UbiquitinationLAAAVFTKDLDKANY
EEEEEEECCHHHHHH		44.84-
453AcetylationLAAAVFTKDLDKANY
EEEEEEECCHHHHHH		44.8423576753
499PhosphorylationSGRELGEYGLQAYTE
CCCCCHHCCCCEEEE		22.7225159016
504PhosphorylationGEYGLQAYTEVKTVT
HHCCCCEEEEEEEEE		7.1725159016
505PhosphorylationEYGLQAYTEVKTVTV
HCCCCEEEEEEEEEE		37.0025159016
513AcetylationEVKTVTVKVPQKNS-
EEEEEEEECCCCCC-		38.5423864654
513SuccinylationEVKTVTVKVPQKNS-
EEEEEEEECCCCCC-		38.5424315375
513UbiquitinationEVKTVTVKVPQKNS-
EEEEEEEECCCCCC-		38.54-
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 ALDH2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALDH2_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 ALDH2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ALDH2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALDH2_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-370, AND MASS SPECTROMETRY.

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