ALDH2_HUMAN - dbPTM
ALDH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALDH2_HUMAN
UniProt AC P05091
Protein Name Aldehyde dehydrogenase, mitochondrial
Gene Name ALDH2
Organism Homo sapiens (Human).
Sequence Length 517
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
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
52AcetylationWHDAVSRKTFPTVNP
CHHHHHCCCCCCCCC		47.19-
73AcetylationCQVAEGDKEDVDKAV
EEEECCCHHHHHHHH		67.67-
78AcetylationGDKEDVDKAVKAARA
CCHHHHHHHHHHHHH		55.73-
81AcetylationEDVDKAVKAARAAFQ
HHHHHHHHHHHHHHH		40.98129583
91PhosphorylationRAAFQLGSPWRRMDA
HHHHHCCCCHHHCCH		29.8628857561
131PhosphorylationTLDNGKPYVISYLVD
HCCCCCCEEEEEEEH		17.5722817900
147MethylationDMVLKCLRYYAGWAD
HHHHHHHHHHHCCHH		31.70-
148PhosphorylationMVLKCLRYYAGWADK
HHHHHHHHHHCCHHH		5.687319975
149PhosphorylationVLKCLRYYAGWADKY
HHHHHHHHHCCHHHH		7.6921406692
155AcetylationYYAGWADKYHGKTIP
HHHCCHHHHCCEEEE		31.2525825284
156PhosphorylationYAGWADKYHGKTIPI
HHCCHHHHCCEEEEC		19.1521406692
159AcetylationWADKYHGKTIPIDGD
CHHHHCCEEEECCCC		29.93-
1592-HydroxyisobutyrylationWADKYHGKTIPIDGD
CHHHHCCEEEECCCC		29.93-
169PhosphorylationPIDGDFFSYTRHEPV
ECCCCCCCEECCCCC		26.1146162007
202PhosphorylationKLGPALATGNVVVMK
HHCHHHHCCCEEEEE		30.09125812005
208SulfoxidationATGNVVVMKVAEQTP
HCCCEEEEEECCCCC		1.6331801345
217PhosphorylationVAEQTPLTALYVANL
ECCCCCCHHHHHHHH		18.80110739349
220PhosphorylationQTPLTALYVANLIKE
CCCCHHHHHHHHHHH		8.61110739357
276PhosphorylationVIQVAAGSSNLKRVT
EEEHHCCCCCCCEEE		16.0121406692
277PhosphorylationIQVAAGSSNLKRVTL
EEHHCCCCCCCEEEE		45.3121406692
280UbiquitinationAAGSSNLKRVTLELG
HCCCCCCCEEEEECC		49.42-
2802-HydroxyisobutyrylationAAGSSNLKRVTLELG
HCCCCCCCEEEEECC		49.42-
283PhosphorylationSSNLKRVTLELGGKS
CCCCCEEEEECCCCC		20.6720166139
296PhosphorylationKSPNIIMSDADMDWA
CCCCEEECCCCHHHH		21.16125812001
332PhosphorylationTFVQEDIYDEFVERS
EEEEHHHHHHHHHHH		23.03110739365
354PhosphorylationVVGNPFDSKTEQGPQ
CCCCCCCCCCCCCCC		41.6828857561
355AcetylationVGNPFDSKTEQGPQV
CCCCCCCCCCCCCCC		58.9023236377
355UbiquitinationVGNPFDSKTEQGPQV
CCCCCCCCCCCCCCC		58.9021906983
3552-HydroxyisobutyrylationVGNPFDSKTEQGPQV
CCCCCCCCCCCCCCC		58.90-
356PhosphorylationGNPFDSKTEQGPQVD
CCCCCCCCCCCCCCC		37.1828857561
368AcetylationQVDETQFKKILGYIN
CCCHHHHHHHHCHHH		29.1423954790
368UbiquitinationQVDETQFKKILGYIN
CCCHHHHHHHHCHHH		29.1421906983
3682-HydroxyisobutyrylationQVDETQFKKILGYIN
CCCHHHHHHHHCHHH		29.14-
3692-HydroxyisobutyrylationVDETQFKKILGYINT
CCHHHHHHHHCHHHC		44.44-
369UbiquitinationVDETQFKKILGYINT
CCHHHHHHHHCHHHC		44.44-
369AcetylationVDETQFKKILGYINT
CCHHHHHHHHCHHHC		44.446270783
373PhosphorylationQFKKILGYINTGKQE
HHHHHHCHHHCCCHH		6.3821406692
376PhosphorylationKILGYINTGKQEGAK
HHHCHHHCCCHHCCE		35.8821406692
3782-HydroxyisobutyrylationLGYINTGKQEGAKLL
HCHHHCCCHHCCEEE		43.04-
378MalonylationLGYINTGKQEGAKLL
HCHHHCCCHHCCEEE		43.0426320211
378UbiquitinationLGYINTGKQEGAKLL
HCHHHCCCHHCCEEE		43.04-
383UbiquitinationTGKQEGAKLLCGGGI
CCCHHCCEEEECCCC		53.50-
383AcetylationTGKQEGAKLLCGGGI
CCCHHCCEEEECCCC		53.50-
396PhosphorylationGIAADRGYFIQPTVF
CCCCCCCEEECCCCE		9.82101545763
401PhosphorylationRGYFIQPTVFGDVQD
CCEEECCCCEECCCC		16.4624043423
411PhosphorylationGDVQDGMTIAKEEIF
ECCCCCCEEEHHHHH		24.2620068231
426AcetylationGPVMQILKFKTIEEV
HHHHHHHEECCHHHH		46.5827178108
428UbiquitinationVMQILKFKTIEEVVG
HHHHHEECCHHHHHC		47.18-
428MalonylationVMQILKFKTIEEVVG
HHHHHEECCHHHHHC		47.1826320211
428AcetylationVMQILKFKTIEEVVG
HHHHHEECCHHHHHC		47.18-
429PhosphorylationMQILKFKTIEEVVGR
HHHHEECCHHHHHCC		36.43125812003
440PhosphorylationVVGRANNSTYGLAAA
HHCCCCCCHHHEEEE		23.8628152594
441PhosphorylationVGRANNSTYGLAAAV
HCCCCCCHHHEEEEE		24.5928152594
442PhosphorylationGRANNSTYGLAAAVF
CCCCCCHHHEEEEEE		15.2328152594
450PhosphorylationGLAAAVFTKDLDKAN
HEEEEEECCCHHHHH		19.6346162013
451AcetylationLAAAVFTKDLDKANY
EEEEEECCCHHHHHH		44.84-
480PhosphorylationYDVFGAQSPFGGYKM
EECCCCCCCCCCEEC		22.9718452278
497PhosphorylationSGRELGEYGLQAYTE
CCCCCHHCCCCEEEE		22.7220561463
502PhosphorylationGEYGLQAYTEVKTVT
HHCCCCEEEEEEEEE		7.17110739373
503PhosphorylationEYGLQAYTEVKTVTV
HCCCCEEEEEEEEEE		37.00110739381
511UbiquitinationEVKTVTVKVPQKNS-
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
202TPhosphorylationKinasePRKCEQ02156
GPS
296SPhosphorylationKinasePRKCEQ02156
GPS
356TPhosphorylationKinaseAMPKA1Q13131
PSP
429TPhosphorylationKinasePRKCEQ02156
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALDH2_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U119A_HUMANUNC119physical
16169070
S35F6_HUMANSLC35F6physical
16169070
IGS21_HUMANIGSF21physical
16169070
DPYL1_HUMANCRMP1physical
16169070
ERG28_HUMANC14orf1physical
16169070
CH10_HUMANHSPE1physical
12387818
CH60_HUMANHSPD1physical
12387818
A4_HUMANAPPphysical
21832049
RL13A_HUMANRPL13Aphysical
21988832
AL1A2_HUMANALDH1A2physical
26186194
MMSA_HUMANALDH6A1physical
26186194
FIBB_HUMANFGBphysical
26186194
A1AT_HUMANSERPINA1physical
26186194
TRFE_HUMANTFphysical
26186194
FIBG_HUMANFGGphysical
26186194
APOA1_HUMANAPOA1physical
26186194
FIBA_HUMANFGAphysical
26186194
CALL5_HUMANCALML5physical
26186194
ESTD_HUMANESDphysical
26344197
PDC6I_HUMANPDCD6IPphysical
26344197
PGM1_HUMANPGM1physical
26344197
QCR2_HUMANUQCRC2physical
26344197
MMSA_HUMANALDH6A1physical
28514442
FIBB_HUMANFGBphysical
28514442
APOA1_HUMANAPOA1physical
28514442
FIBG_HUMANFGGphysical
28514442
FIBA_HUMANFGAphysical
28514442
A1AT_HUMANSERPINA1physical
28514442
TRFE_HUMANTFphysical
28514442
CALL5_HUMANCALML5physical
28514442
AL1A2_HUMANALDH1A2physical
28514442
RL11_HUMANRPL11genetic
27453043
ARI1A_HUMANARID1Agenetic
27453043
XRCC3_HUMANXRCC3genetic
27453043
ATAD5_HUMANATAD5genetic
27453043
APC_HUMANAPCgenetic
27453043
PHB2_HUMANPHB2genetic
27453043
RD23B_HUMANRAD23Bgenetic
27453043
SIR3_HUMANSIRT3physical
28248093
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01612Amyl Nitrite
DB06770Benzyl alcohol
DB00822Disulfiram
DB00536Guanidine
DB00435Nitric Oxide
DB00727Nitroglycerin
Regulatory Network of ALDH2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory