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HUMAN:ADHX
Contents
Species (Taxon ID) | Homo sapiens (Human). (9606) | |
Gene Name(s) | ADH5 (ECO:0000312 with HGNC:HGNC:253) (synonyms: ADHX, FDH) | |
Protein Name(s) | Alcohol dehydrogenase class-3
Alcohol dehydrogenase 5 Alcohol dehydrogenase class chi chain Alcohol dehydrogenase class-III Glutathione-dependent formaldehyde dehydrogenase FALDH FDH GSH-FDH S-(hydroxymethyl)glutathione dehydrogenase | |
External Links | ||
UniProt | P11766 | |
EMBL | M30471 M29872 M81118 M81112 M81113 M81114 M81115 M81116 M81117 CR541689 BT019832 AY987960 BC014665 | |
CCDS | CCDS47111.1 | |
PIR | JH0789 | |
RefSeq | NP_000662.3 | |
UniGene | Hs.78989 | |
PDB | 1M6H 1M6W 1MA0 1MC5 1MP0 1TEH 2FZE 2FZW 3QJ5 | |
PDBsum | 1M6H 1M6W 1MA0 1MC5 1MP0 1TEH 2FZE 2FZW 3QJ5 | |
ProteinModelPortal | P11766 | |
SMR | P11766 | |
BioGrid | 106640 | |
IntAct | P11766 | |
MINT | MINT-1374117 | |
STRING | 9606.ENSP00000296412 | |
ChEMBL | CHEMBL2096668 | |
PhosphoSite | P11766 | |
DMDM | 113408 | |
REPRODUCTION-2DPAGE | IPI00746777 | |
MaxQB | P11766 | |
PaxDb | P11766 | |
PRIDE | P11766 | |
DNASU | 128 | |
Ensembl | ENST00000296412 | |
GeneID | 128 | |
KEGG | hsa:128 | |
UCSC | uc003hui.3 | |
CTD | 128 | |
GeneCards | GC04M099992 | |
HGNC | HGNC:253 | |
HPA | HPA044578 | |
MIM | 103710 | |
neXtProt | NX_P11766 | |
PharmGKB | PA24574 | |
eggNOG | COG1062 | |
HOGENOM | HOG000294674 | |
HOVERGEN | HBG000195 | |
InParanoid | P11766 | |
KO | K00121 | |
OMA | WKSVESI | |
OrthoDB | EOG72NRQ6 | |
PhylomeDB | P11766 | |
TreeFam | TF300429 | |
SABIO-RK | P11766 | |
ChiTaRS | ADH5 | |
EvolutionaryTrace | P11766 | |
GeneWiki | ADH5 | |
GenomeRNAi | 128 | |
NextBio | 511 | |
PRO | PR:P11766 | |
Proteomes | UP000005640 | |
Bgee | P11766 | |
CleanEx | HS_ADH5 | |
ExpressionAtlas | P11766 | |
Genevestigator | P11766 | |
GO | GO:0070062 GO:0005739 GO:0005634 GO:0004022 GO:0009055 GO:0005504 GO:0018467 GO:0051903 GO:0008270 GO:0007568 GO:0006068 GO:0006069 GO:0046294 GO:0018119 GO:0045777 GO:0003016 GO:0032496 GO:0051409 GO:0051775 GO:0001523 | |
Gene3D | 3.40.50.720 3.90.180.10 | |
InterPro | IPR014183 IPR013149 IPR013154 IPR002085 IPR002328 IPR011032 IPR016040 | |
PANTHER | PTHR11695 | |
Pfam | PF08240 PF00107 | |
SUPFAM | SSF50129 | |
TIGRFAMs | TIGR02818 | |
PROSITE | PS00059 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000266 |
|
F |
Table 3 shows a comparison of sequences of ADHs around residue 115 between species. |
complete | ||||
part_of |
GO:0070062 |
extracellular exosome |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0070062 |
extracellular exosome |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
part_of:(UBERON:0001088) |
Seeded From UniProt |
complete | ||
involved_in |
GO:0051775 |
response to redox state |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0018467 |
formaldehyde dehydrogenase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0005504 |
fatty acid binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0051903 |
S-(hydroxymethyl)glutathione dehydrogenase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG50010 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0046294 |
formaldehyde catabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG50010 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0008270 |
zinc ion binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG50010 |
F |
Seeded From UniProt |
complete | ||
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG50010 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0004024 |
alcohol dehydrogenase activity, zinc-dependent |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG50010 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0022900 |
electron transport chain |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0009055 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0051903 |
S-(hydroxymethyl)glutathione dehydrogenase activity |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0051409 |
response to nitrosative stress |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0046294 |
formaldehyde catabolic process |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0045777 |
positive regulation of blood pressure |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0042803 |
protein homodimerization activity |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0032496 |
response to lipopolysaccharide |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0018119 |
peptidyl-cysteine S-nitrosylation |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005739 |
mitochondrion |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0003016 |
respiratory system process |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0001523 |
retinoid metabolic process |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P28474 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006069 |
ethanol oxidation |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0008270 |
zinc ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0051903 |
S-(hydroxymethyl)glutathione dehydrogenase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR002328 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0051903 |
S-(hydroxymethyl)glutathione dehydrogenase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0051903 |
S-(hydroxymethyl)glutathione dehydrogenase activity |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0009055 |
electron transfer activity |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006069 |
ethanol oxidation |
Reactome:R-HSA-71384 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005829 |
cytosol |
Reactome:R-HSA-5692237 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
C |
Seeded From UniProt |
complete | ||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Engeland, K et al. (1993) Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation. Proc. Natl. Acad. Sci. U.S.A. 90 2491-4 PubMed GONUTS page
- ↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
- ↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
- ↑ Wagner, FW et al. (1984) Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: chi-ADH. Biochemistry 23 2193-9 PubMed GONUTS page
- ↑ 5.0 5.1 5.2 5.3 5.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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