ADHX_HUMAN - dbPTM
ADHX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADHX_HUMAN
UniProt AC P11766
Protein Name Alcohol dehydrogenase class-3
Gene Name ADH5 {ECO:0000312|HGNC:HGNC:253}
Organism Homo sapiens (Human).
Sequence Length 374
Subcellular Localization Cytoplasm.
Protein Description Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione..
Protein Sequence MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGYGAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEIATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFELMHSGKSIRTVVKI
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------MANEVIKCK
------CCCCEEEEE		22.3819413330
72-Hydroxyisobutyrylation-MANEVIKCKAAVAW
-CCCCEEEEEEEEEH		34.55-
7Acetylation-MANEVIKCKAAVAW
-CCCCEEEEEEEEEH		34.5525953088
7Ubiquitination-MANEVIKCKAAVAW
-CCCCEEEEEEEEEH		34.55-
9UbiquitinationANEVIKCKAAVAWEA
CCCEEEEEEEEEHHC		34.09-
18UbiquitinationAVAWEAGKPLSIEEI
EEEHHCCCCCEEEEE		50.24-
18AcetylationAVAWEAGKPLSIEEI
EEEHHCCCCCEEEEE		50.2426051181
21PhosphorylationWEAGKPLSIEEIEVA
HHCCCCCEEEEEEEC		36.16113305849
31UbiquitinationEIEVAPPKAHEVRIK
EEEECCCCCCEEEEE		62.41-
84UbiquitinationGEGVTKLKAGDTVIP
CCCCCEECCCCEEEE		52.45-
93PhosphorylationGDTVIPLYIPQCGEC
CCEEEEEECCCCCCC		12.7628152594
97S-palmitoylationIPLYIPQCGECKFCL
EEEECCCCCCCCEEE		4.0929575903
100S-palmitoylationYIPQCGECKFCLNPK
ECCCCCCCCEEECCC		2.1929575903
101AcetylationIPQCGECKFCLNPKT
CCCCCCCCEEECCCC		34.5125953088
101UbiquitinationIPQCGECKFCLNPKT
CCCCCCCCEEECCCC		34.51-
103S-palmitoylationQCGECKFCLNPKTNL
CCCCCCEEECCCCCC		1.8829575903
107UbiquitinationCKFCLNPKTNLCQKI
CCEEECCCCCCCCEE		49.31-
107AcetylationCKFCLNPKTNLCQKI
CCEEECCCCCCCCEE		49.3126051181
1132-HydroxyisobutyrylationPKTNLCQKIRVTQGK
CCCCCCCEEEEECCC		31.33-
113UbiquitinationPKTNLCQKIRVTQGK
CCCCCCCEEEEECCC		31.3321890473
113AcetylationPKTNLCQKIRVTQGK
CCCCCCCEEEEECCC		31.3325953088
117PhosphorylationLCQKIRVTQGKGLMP
CCCEEEEECCCCCCC		23.0420068231
120MalonylationKIRVTQGKGLMPDGT
EEEEECCCCCCCCCC		38.7726320211
120UbiquitinationKIRVTQGKGLMPDGT
EEEEECCCCCCCCCC		38.77-
123SulfoxidationVTQGKGLMPDGTSRF
EECCCCCCCCCCEEE		3.7630846556
127PhosphorylationKGLMPDGTSRFTCKG
CCCCCCCCEEEEECC		24.9020068231
128PhosphorylationGLMPDGTSRFTCKGK
CCCCCCCEEEEECCC		30.8120068231
131PhosphorylationPDGTSRFTCKGKTIL
CCCCEEEEECCCEEE		16.5220068231
177PhosphorylationCLLGCGISTGYGAAV
EEECCCCCCCCCCCH		10.8928152594
178PhosphorylationLLGCGISTGYGAAVN
EECCCCCCCCCCCHH		32.2828152594
180PhosphorylationGCGISTGYGAAVNTA
CCCCCCCCCCCHHCC		12.0428152594
186PhosphorylationGYGAAVNTAKLEPGS
CCCCCHHCCCCCCCC		20.6928152594
2262-HydroxyisobutyrylationIIGVDINKDKFARAK
EEEEECCHHHHHHHH		63.73-
226UbiquitinationIIGVDINKDKFARAK
EEEEECCHHHHHHHH		63.73-
226AcetylationIIGVDINKDKFARAK
EEEEECCHHHHHHHH		63.7323236377
228UbiquitinationGVDINKDKFARAKEF
EEECCHHHHHHHHHH		42.40-
228AcetylationGVDINKDKFARAKEF
EEECCHHHHHHHHHH		42.4023749302
233SuccinylationKDKFARAKEFGATEC
HHHHHHHHHHCCCCC		48.28-
233SuccinylationKDKFARAKEFGATEC
HHHHHHHHHHCCCCC		48.2821890473
233UbiquitinationKDKFARAKEFGATEC
HHHHHHHHHHCCCCC		48.2821890473
247PhosphorylationCINPQDFSKPIQEVL
CCCHHHCCCCHHEEE		45.9025159151
303PhosphorylationASGEEIATRPFQLVT
ECCCCCCCCCEEEEE		44.5320058876
310PhosphorylationTRPFQLVTGRTWKGT
CCCEEEEECCCCCCC		29.5524719451
315SuccinylationLVTGRTWKGTAFGGW
EEECCCCCCCCCCCC		45.85-
315SuccinylationLVTGRTWKGTAFGGW
EEECCCCCCCCCCCC		45.85-
315UbiquitinationLVTGRTWKGTAFGGW
EEECCCCCCCCCCCC		45.85-
315AcetylationLVTGRTWKGTAFGGW
EEECCCCCCCCCCCC		45.8530586761
323UbiquitinationGTAFGGWKSVESVPK
CCCCCCCCCHHHHHH		48.1521890473
324PhosphorylationTAFGGWKSVESVPKL
CCCCCCCCHHHHHHH		25.3028857561
330AcetylationKSVESVPKLVSEYMS
CCHHHHHHHHHHHHC		60.4025953088
330UbiquitinationKSVESVPKLVSEYMS
CCHHHHHHHHHHHHC		60.40-
333PhosphorylationESVPKLVSEYMSKKI
HHHHHHHHHHHCCCC		33.1826552605
335PhosphorylationVPKLVSEYMSKKIKV
HHHHHHHHHCCCCCH		10.1329496907
336SulfoxidationPKLVSEYMSKKIKVD
HHHHHHHHCCCCCHH		4.0930846556
337PhosphorylationKLVSEYMSKKIKVDE
HHHHHHHCCCCCHHH		29.8726552605
338UbiquitinationLVSEYMSKKIKVDEF
HHHHHHCCCCCHHHH		41.82-
3382-HydroxyisobutyrylationLVSEYMSKKIKVDEF
HHHHHHCCCCCHHHH		41.82-
338SuccinylationLVSEYMSKKIKVDEF
HHHHHHCCCCCHHHH		41.8223954790
338AcetylationLVSEYMSKKIKVDEF
HHHHHHCCCCCHHHH		41.8225953088
339UbiquitinationVSEYMSKKIKVDEFV
HHHHHCCCCCHHHHH		40.22-
341UbiquitinationEYMSKKIKVDEFVTH
HHHCCCCCHHHHHHC		53.14-
347PhosphorylationIKVDEFVTHNLSFDE
CCHHHHHHCCCCHHH		15.4628857561
351PhosphorylationEFVTHNLSFDEINKA
HHHHCCCCHHHHHHH		35.6522167270
357AcetylationLSFDEINKAFELMHS
CCHHHHHHHHHHHHC		61.1825038526
357UbiquitinationLSFDEINKAFELMHS
CCHHHHHHHHHHHHC		61.18-
362SulfoxidationINKAFELMHSGKSIR
HHHHHHHHHCCCCEE		1.5421406390
364PhosphorylationKAFELMHSGKSIRTV
HHHHHHHCCCCEEEE		33.6728857561
366UbiquitinationFELMHSGKSIRTVVK
HHHHHCCCCEEEEEE		45.8019608861
366MalonylationFELMHSGKSIRTVVK
HHHHHCCCCEEEEEE		45.8026320211
366AcetylationFELMHSGKSIRTVVK
HHHHHCCCCEEEEEE		45.8023954790
3662-HydroxyisobutyrylationFELMHSGKSIRTVVK
HHHHHCCCCEEEEEE		45.80-
367PhosphorylationELMHSGKSIRTVVKI
HHHHCCCCEEEEEEC		22.3428857561
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 ADHX_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADHX_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 ADHX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD3_HUMANCHD3physical
16169070
ADHX_HUMANADH5physical
12484756
A4_HUMANAPPphysical
21832049
CSK2B_HUMANCSNK2Bphysical
21988832
ADHX_HUMANADH5physical
21988832
ARNT_HUMANARNTphysical
21988832
ERR1_HUMANESRRAphysical
21988832
PRDX1_HUMANPRDX1physical
21988832
VTNC_HUMANVTNphysical
21988832
PQLC1_HUMANPQLC1physical
21988832
AL4A1_HUMANALDH4A1physical
26344197
ESTD_HUMANESDphysical
26344197
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
DB00898Ethanol
Regulatory Network of ADHX_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Class III human liver alcohol dehydrogenase: a novel structural typeequidistantly related to the class I and class II enzymes.";
Kaiser R., Holmquist B., Hempel J., Vallee B.L., Joernvall H.;
Biochemistry 27:1132-1140(1988).
Cited for: PROTEIN SEQUENCE OF 2-374.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, AND MASS SPECTROMETRY.

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