ALDH6_YEAST - dbPTM
ALDH6_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALDH6_YEAST
UniProt AC P54115
Protein Name Magnesium-activated aldehyde dehydrogenase, cytosolic
Gene Name ALD6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 500
Subcellular Localization Cytoplasm.
Protein Description Cytosolic aldehyde dehydrogenase which utilizes NADP+ as the preferred coenzyme. Performs the conversion of acetaldehyde to acetate..
Protein Sequence MTKLHFDTAEPVKITLPNGLTYEQPTGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIKL
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
2Phosphorylation------MTKLHFDTA
------CCCCCCCCC		42.1725704821
3Ubiquitination-----MTKLHFDTAE
-----CCCCCCCCCC		38.3722106047
3Succinylation-----MTKLHFDTAE
-----CCCCCCCCCC		38.3723954790
8PhosphorylationMTKLHFDTAEPVKIT
CCCCCCCCCCCEEEE		31.7921440633
13UbiquitinationFDTAEPVKITLPNGL
CCCCCCEEEECCCCC		40.4624961812
15PhosphorylationTAEPVKITLPNGLTY
CCCCEEEECCCCCCE		30.3722369663
21PhosphorylationITLPNGLTYEQPTGL
EECCCCCCEECCCEE		26.8122369663
22PhosphorylationTLPNGLTYEQPTGLF
ECCCCCCEECCCEEE		20.0122369663
26PhosphorylationGLTYEQPTGLFINNK
CCCEECCCEEEECCE		46.3322369663
33UbiquitinationTGLFINNKFMKAQDG
CEEEECCEEEECCCC		42.2023749301
33AcetylationTGLFINNKFMKAQDG
CEEEECCEEEECCCC		42.2024489116
36UbiquitinationFINNKFMKAQDGKTY
EECCEEEECCCCCEE		46.1322817900
41UbiquitinationFMKAQDGKTYPVEDP
EEECCCCCEEECCCC		53.8522817900
95UbiquitinationERGRLLSKLADELES
HHHHHHHHHHHHHHH		47.8923749301
102PhosphorylationKLADELESQIDLVSS
HHHHHHHHHHCHHHH		45.0922369663
108PhosphorylationESQIDLVSSIEALDN
HHHHCHHHHHEEHHC		32.6624961812
109PhosphorylationSQIDLVSSIEALDNG
HHHCHHHHHEEHHCC		19.5724961812
117UbiquitinationIEALDNGKTLALARG
HEEHHCCCEEEEEEC		46.7724961812
127PhosphorylationALARGDVTIAINCLR
EEEECCEEEEEECHH		14.9421440633
139PhosphorylationCLRDAAAYADKVNGR
CHHHHHHHHHHHCCE		15.5921440633
142SuccinylationDAAAYADKVNGRTIN
HHHHHHHHHCCEEEE		29.4523954790
142AcetylationDAAAYADKVNGRTIN
HHHHHHHHHCCEEEE		29.4522865919
142UbiquitinationDAAAYADKVNGRTIN
HHHHHHHHHCCEEEE		29.4523749301
182UbiquitinationPIMMLAWKIAPALAM
HHHHHHHHHHHHHHC		24.3117644757
196UbiquitinationMGNVCILKPAAVTPL
CCCEEEEECCCCCHH		16.8222106047
201PhosphorylationILKPAAVTPLNALYF
EEECCCCCHHHHHHH		19.8221440633
213AcetylationLYFASLCKKVGIPAG
HHHHHHHHHHCCCCC		56.6524489116
213UbiquitinationLYFASLCKKVGIPAG
HHHHHHHHHHCCCCC		56.6522817900
214UbiquitinationYFASLCKKVGIPAGV
HHHHHHHHHCCCCCC		44.7023749301
231PhosphorylationIVPGPGRTVGAALTN
ECCCCCCCHHHHHHC		29.2521440633
237PhosphorylationRTVGAALTNDPRIRK
CCHHHHHHCCHHHHE		32.6130377154
244AcetylationTNDPRIRKLAFTGST
HCCHHHHEEEEECCC		41.6222865919
244UbiquitinationTNDPRIRKLAFTGST
HCCHHHHEEEEECCC		41.6224961812
248PhosphorylationRIRKLAFTGSTEVGK
HHHEEEEECCCCCCC		25.3122369663
250PhosphorylationRKLAFTGSTEVGKSV
HEEEEECCCCCCCEE		20.5222369663
251PhosphorylationKLAFTGSTEVGKSVA
EEEEECCCCCCCEEE		35.7122369663
255UbiquitinationTGSTEVGKSVAVDSS
ECCCCCCCEEEECCC		47.1023749301
256PhosphorylationGSTEVGKSVAVDSSE
CCCCCCCEEEECCCC		14.9122369663
261PhosphorylationGKSVAVDSSESNLKK
CCEEEECCCCCCCEE		29.4322369663
262PhosphorylationKSVAVDSSESNLKKI
CEEEECCCCCCCEEE		40.3525521595
264PhosphorylationVAVDSSESNLKKITL
EEECCCCCCCEEEEE		49.7822369663
267UbiquitinationDSSESNLKKITLELG
CCCCCCCEEEEEEEC		46.5124961812
267AcetylationDSSESNLKKITLELG
CCCCCCCEEEEEEEC		46.5122865919
267SuccinylationDSSESNLKKITLELG
CCCCCCCEEEEEEEC		46.5123954790
268UbiquitinationSSESNLKKITLELGG
CCCCCCEEEEEEECC		44.0524961812
276UbiquitinationITLELGGKSAHLVFD
EEEEECCEEEEEEEC		42.5424961812
276AcetylationITLELGGKSAHLVFD
EEEEECCEEEEEEEC		42.5422865919
277PhosphorylationTLELGGKSAHLVFDD
EEEECCEEEEEEECC		24.9721440633
288AcetylationVFDDANIKKTLPNLV
EECCCCHHHHHHHHH		39.2424489116
288UbiquitinationVFDDANIKKTLPNLV
EECCCCHHHHHHHHH		39.2417644757
288SuccinylationVFDDANIKKTLPNLV
EECCCCHHHHHHHHH		39.2423954790
289UbiquitinationFDDANIKKTLPNLVN
ECCCCHHHHHHHHHH		52.0424961812
290PhosphorylationDDANIKKTLPNLVNG
CCCCHHHHHHHHHHH		42.3119795423
300UbiquitinationNLVNGIFKNAGQICS
HHHHHHHCCCHHHCC		43.9224961812
300AcetylationNLVNGIFKNAGQICS
HHHHHHHCCCHHHCC		43.9224489116
307PhosphorylationKNAGQICSSGSRIYV
CCCHHHCCCCCEEEE		39.0928889911
308PhosphorylationNAGQICSSGSRIYVQ
CCHHHCCCCCEEEEE		36.0528889911
310PhosphorylationGQICSSGSRIYVQEG
HHHCCCCCEEEEECC		19.9028889911
327UbiquitinationDELLAAFKAYLETEI
HHHHHHHHHHHHCEE		31.2517644757
342UbiquitinationKVGNPFDKANFQGAI
CCCCCCCHHCCCCCC		45.6823749301
342AcetylationKVGNPFDKANFQGAI
CCCCCCCHHCCCCCC		45.6824489116
350PhosphorylationANFQGAITNRQQFDT
HCCCCCCCCHHHHHH		24.6628889911
366AcetylationMNYIDIGKKEGAKIL
HHHHHCCHHHCCEEE		48.2424489116
367AcetylationNYIDIGKKEGAKILT
HHHHCCHHHCCEEEC		57.0524489116
378AcetylationKILTGGEKVGDKGYF
EEECCCCEECCCCEE		55.5922865919
378UbiquitinationKILTGGEKVGDKGYF
EEECCCCEECCCCEE		55.5923749301
382UbiquitinationGGEKVGDKGYFIRPT
CCCEECCCCEEECCE		49.9717644757
382AcetylationGGEKVGDKGYFIRPT
CCCEECCCCEEECCE		49.9724489116
402UbiquitinationNEDMRIVKEEIFGPV
CCCCHHHHHHHHCCE		47.4624961812
402AcetylationNEDMRIVKEEIFGPV
CCCCHHHHHHHHCCE		47.4624489116
414AcetylationGPVVTVAKFKTLEEG
CCEEEEEEECCHHHH		42.9524489116
414UbiquitinationGPVVTVAKFKTLEEG
CCEEEEEEECCHHHH		42.9517644757
434PhosphorylationSSEFGLGSGIETESL
CCCCCCCCCCCCCCH		41.4628889911
438PhosphorylationGLGSGIETESLSTGL
CCCCCCCCCCHHHHH		29.0228889911
440PhosphorylationGSGIETESLSTGLKV
CCCCCCCCHHHHHHH		34.7328889911
442PhosphorylationGIETESLSTGLKVAK
CCCCCCHHHHHHHHH		29.7028889911
443PhosphorylationIETESLSTGLKVAKM
CCCCCHHHHHHHHHH		52.4028889911
449UbiquitinationSTGLKVAKMLKAGTV
HHHHHHHHHHHCCEE		47.9922817900
452UbiquitinationLKVAKMLKAGTVWIN
HHHHHHHHCCEEEEE		41.0723749301
455PhosphorylationAKMLKAGTVWINTYN
HHHHHCCEEEEEECC		19.9522369663
460PhosphorylationAGTVWINTYNDFDSR
CCEEEEEECCCCCCC		17.9922369663
461PhosphorylationGTVWINTYNDFDSRV
CEEEEEECCCCCCCC		14.3022369663
466PhosphorylationNTYNDFDSRVPFGGV
EECCCCCCCCCCCCC		34.8621440633
474SuccinylationRVPFGGVKQSGYGRE
CCCCCCCCCCCCCCC		41.8623954790
474AcetylationRVPFGGVKQSGYGRE
CCCCCCCCCCCCCCC		41.8624489116
474UbiquitinationRVPFGGVKQSGYGRE
CCCCCCCCCCCCCCC		41.8623749301
487PhosphorylationREMGEEVYHAYTEVK
CCCCCCHHHHHEEEE		5.5228889911
491PhosphorylationEEVYHAYTEVKAVRI
CCHHHHHEEEEEEEE		34.7817287358
494AcetylationYHAYTEVKAVRIKL-
HHHHEEEEEEEECC-		34.6324489116
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 ALDH6_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALDH6_YEAST !!
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 ALDH6_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GFA1_YEASTGFA1physical
16429126
IDH2_YEASTIDH2physical
16429126
LYS12_YEASTLYS12physical
16429126
METK1_YEASTSAM1physical
16429126
PMG1_YEASTGPM1physical
16429126
GPD1_YEASTGPD1genetic
16820460
ALDH6_YEASTALD6physical
19343713
ODPA_YEASTPDA1genetic
21623372
6PGD1_YEASTGND1genetic
21623372
ERG2_YEASTERG2genetic
21623372
RPE_YEASTRPE1genetic
21623372
ODP2_YEASTLAT1genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
ODPB_YEASTPDB1genetic
21623372
THRC_YEASTTHR4genetic
21623372
SUCB_YEASTLSC2genetic
21623372
FUMH_YEASTFUM1genetic
21623372
ACON2_YEASTACO2genetic
21623372
ADH3_YEASTADH3genetic
21623372
FPS1_YEASTFPS1genetic
23475614
TDA9_YEASTTDA9genetic
23692528
ALDH4_YEASTALD4genetic
23692528
MED20_YEASTSRB2genetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
RCY1_YEASTRCY1genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
ERG6_YEASTERG6genetic
27708008
GSF2_YEASTGSF2genetic
27708008
SIW14_YEASTSIW14genetic
27708008
ODPB_YEASTPDB1genetic
27708008
BUD31_YEASTBUD31genetic
27708008
MGMT_YEASTMGT1genetic
27708008
STP1_YEASTSTP1genetic
27708008
ODPA_YEASTPDA1genetic
27708008
DLDH_YEASTLPD1genetic
27708008
SUCB_YEASTLSC2genetic
27708008
HTD2_YEASTHTD2genetic
27708008
STB5_YEASTSTB5genetic
27708008
DAL81_YEASTDAL81genetic
27708008
LPLA_YEASTAIM22genetic
27708008
RPE_YEASTRPE1genetic
27708008
MPCP_YEASTMIR1genetic
27708008
FABG_YEASTOAR1genetic
27708008
LST4_YEASTLST4genetic
27708008
DCOR_YEASTSPE1genetic
27708008
SIC1_YEASTSIC1genetic
27708008
YL224_YEASTYLR224Wgenetic
27708008
LIPB_YEASTLIP2genetic
27708008
DIC1_YEASTDIC1genetic
27708008
TSR2_YEASTTSR2genetic
27708008
DATI_YEASTDAT1genetic
27708008
MSS1_YEASTMSS1genetic
27708008
PEX12_YEASTPEX12genetic
27708008
IMP2_YEASTIMP2genetic
27708008
DLT1_YEASTDLT1genetic
27708008
TGL3_YEASTTGL3genetic
27708008
PET8_YEASTPET8genetic
27708008
COG6_YEASTCOG6genetic
27708008
ODP2_YEASTLAT1genetic
27708008
NGL1_YEASTNGL1genetic
27708008
NTH2_YEASTNTG2genetic
27708008
PEX15_YEASTPEX15genetic
27708008
LIPA_YEASTLIP5genetic
27708008
ALDH4_YEASTALD4genetic
27708008
HSP31_YEASTHSP31genetic
27984092
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALDH6_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250; THR-251 ANDSER-262, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-491, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-3, AND MASS SPECTROMETRY.

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