Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Aflatoxin B1 aldehyde reductase member 2  

UniProtKB / Swiss-Prot ID :  ARK72_HUMAN

Gene Name (Synonyms) : 
AKR7A2, AFAR, AFAR1, AKR7  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Golgi apparatus (By similarity). Cytoplasm. 

Protein Function :  Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2- nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. 

Protein Sequence MLSAASRVVSRAAVHCALRSPPPEARALAMSRPPPPRVASVLGTMEMGRRMDAPASAAAVRAFLERGHTE...
Predicted Secondary Structure CCCHHHHHHHHHHHCCCCCCCCCCCEECCCCCCCCCCEEEEEECCCCCCCCCHHHHHHHHHHHHHCCCCE...
Protein Variant
LocationDescription
135V -> M (in dbSNP:rs6670759). VAR_048209
142A -> T (in dbSNP:rs1043657). VAR_017413
157Q -> H (in dbSNP:rs859208). VAR_017414
180E -> K (in dbSNP:rs859210). VAR_060222
198G -> S (in dbSNP:rs2231200). VAR_048210
214C -> Y (in dbSNP:rs2235794). VAR_017415
255S -> N (in dbSNP:rs2231203). VAR_048211
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
56PhosphoserineDAPASAAAV
CHHHHHHHH
19.85Phosphositeplus
Link
223PhosphotyrosineGLRFYAYNP
CCEEEEECC
11.18Phosphositeplus
Link
225PhosphotyrosineRFYAYNPLA
EEEEECCCC
13.11Phosphositeplus
Link
250noneQPVGRFFGN
CCCCCCCCC
24.77HPRD
Link
255PhosphoserineFFGNSWAET
CCCCCHHHH
28.21HPRD
Link
255PhosphoserineFFGNSWAET
CCCCCHHHH
28.21Phosphositeplus
Link
255Phosphoserine.FFGNSWAET
CCCCCHHHH
28.21UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ARK73_HUMANphysical interactionEBI-756850
intact16189514
ARK73_HUMANyeast 2-hybridHPRD:04567HPRD16189514
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures