Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Aldo-keto reductase family 1 member B10  

UniProtKB / Swiss-Prot ID :  AK1BA_HUMAN

Gene Name (Synonyms) : 
AKR1B10, AKR1B11  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Lysosome. Secreted. Note=Secreted through a lysosome-mediated non-classical pathway. 

Protein Function :  Acts as all-trans-retinaldehyde reductase. Can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). May be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. 

Protein Sequence MATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKR...
Predicted Secondary Structure CCCEEECCCCCEEEEEEEEECCCCHHHHHHHHHHHHHCCCCEEECHHHHCCHHHHHHHHHHHHHHCCCCC...
Protein Variant
LocationDescription
87P -> S (in dbSNP:rs2303312). VAR_020077
286M -> T (in dbSNP:rs3735042). VAR_020078
313N -> D (in dbSNP:rs4728329). VAR_013287
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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
23PhosphoserineGTWKSPLGK
EECCCCHHH
19.54HPRD
Link
23PhosphoserineGTWKSPLGK
EECCCCHHH
19.54Phosphositeplus
Link
27N6-acetyllysineSPLGKVKEA
CCHHHHHHH
58.79HPRD
Link
27N6-acetyllysineSPLGKVKEA
CCHHHHHHH
58.79Phosphositeplus
Link
27N6-acetyllysine.SPLGKVKEA
CCHHHHHHH
58.79UniProtKB
Link
47PhosphotyrosineIDCAYVYQN
EECHHHHCC
13.16Phosphositeplus
Link
69N6-acetyllysineEKAVKREDL
HCCCCCCEE
55.73HPRD
Link
69N6-acetyllysineEKAVKREDL
HCCCCCCEE
55.73Phosphositeplus
Link
69N6-acetyllysine.EKAVKREDL
HCCCCCCEE
55.73UniProtKB
Link
95N6-acetyllysineKAFEKTLKD
HHHHHHHHH
53.34HPRD
Link
95N6-acetyllysine.KAFEKTLKD
HHHHHHHHH
53.34UniProtKB
Link
125N6-acetyllysineDLFPKDDKG
CCCCCCCCC
71.83HPRD
Link
125N6-acetyllysineDLFPKDDKG
CCCCCCCCC
71.83Phosphositeplus
Link
125N6-acetyllysine.DLFPKDDKG
CCCCCCCCC
71.83UniProtKB
Link
179N6-acetyllysineGLKYKPVTN
CCCCCEEEE
31.27HPRD
Link
179N6-acetyllysine.GLKYKPVTN
CCCCCEEEE
31.27UniProtKB
Link
263N6-acetyllysineIVIPKSVTP
EEEECCCCH
46.57HPRD
Link
263N6-acetyllysineIVIPKSVTP
EEEECCCCH
46.57Phosphositeplus
Link
263N6-acetyllysine.IVIPKSVTP
EEEECCCCH
46.57UniProtKB
Link
288PhosphothreonineEEMATILSF
HHHHHHHHH
22.57HPRD
Link
291PhosphoserineATILSFNRN
HHHHHHCCC
19.34HPRD
Link
316PhosphotyrosineFNAEY
CCCCC
22.80Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ACACA_HUMANcolocalization
physical interaction
physical interaction
physical interaction
EBI-1573377
EBI-1573345
EBI-1
intact18056116
18056116
18056116
18056116
AADAT_HUMANENSP00000352584STRING
TGDS_HUMANENSP00000352584STRING
ADAS_HUMANENSP00000352584STRING
GALE_HUMANENSP00000352584STRING
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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
Acetylation
ReferencePubMed
"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-27; LYS-69; LYS-95; LYS-125;LYS-179 AND LYS-263, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures