Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Aldose reductase  

UniProtKB / Swiss-Prot ID :  ALDR_HUMAN

Gene Name (Synonyms) : 
AKR1B1, ALDR1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. 

Protein Sequence MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKR...
Predicted Secondary Structure CCCEEECCCCCEEEEEEEEEECCCCHHHHHHHHHHHHCCCCEEECHHHHCCHHHHHHHHHHHHHHCCCCC...
Protein Variant
LocationDescription
15I -> F (in dbSNP:rs5054). VAR_014743
42H -> L (in dbSNP:rs5056). VAR_014744
73L -> V (in dbSNP:rs5057). VAR_014745
90K -> E (in dbSNP:rs2229542). VAR_048213
204G -> S (in dbSNP:rs5061). VAR_014746
288T -> I (in dbSNP:rs5062). VAR_014747
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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
2N-acetylalanine.---MASRLL
---CCCEEE
11.89UniProtKB
Link
12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NNGAKMPIL
CCCCEEEEE
46.75Phosphositeplus
Link
20PhosphothreonineLGLGTWKSP
EEEEEECCC
34.46Phosphositeplus
Link
23PhosphoserineGTWKSPPGQ
EEECCCCHH
28.08Phosphositeplus
Link
23Phosphoserine.GTWKSPPGQ
EEECCCCHH
28.08UniProtKB
Link
40PhosphotyrosineIDVGYRHID
HHCCCCEEE
10.00Phosphositeplus
Link
40Phosphotyrosine.IDVGYRHID
HHCCCCEEE
10.00UniProtKB
Link
86Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TYHEKGLVK
CCCCHHHHH
44.21Phosphositeplus
Link
86N6-acetyllysineTYHEKGLVK
CCCCHHHHH
44.21HPRD
Link
95N6-acetyllysineGACQKTLSD
HHHHHHHHH
51.85HPRD
Link
95N6-acetyllysineGACQKTLSD
HHHHHHHHH
51.85Phosphositeplus
Link
95N6-acetyllysine.GACQKTLSD
HHHHHHHHH
51.85UniProtKB
Link
190PhosphotyrosineECHPYLTQE
ECCCCCCCH
9.94Phosphositeplus
Link
222N6-acetyllysineRPWAKPEDP
CCCCCCCCC
45.10HPRD
Link-
222N6-acetyllysineRPWAKPEDP
CCCCCCCCC
45.10Phosphositeplus
Link-
222N6-acetyllysine.RPWAKPEDP
CCCCCCCCC
45.10UniProtKB
Link-
263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VVIPKSVTP
EEEECCCCH
46.57Phosphositeplus
Link
263N6-acetyllysineVVIPKSVTP
EEEECCCCH
46.57HPRD
Link
263N6-acetyllysineVVIPKSVTP
EEEECCCCH
46.57Phosphositeplus
Link
263N6-acetyllysine.VVIPKSVTP
EEEECCCCH
46.57UniProtKB
Link
299S-nitrosocysteineNWRVCALLS
CCCCCCCHH
1.33dbSNO
Link
304S-nitrosocysteineALLSCTSHK
CCHHHHCCC
4.58dbSNO
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SMAD1_HUMANphysical interactionMINT-62012MINT15231748
DESP_HUMANphysical interactionEBI-1061483
intact17353931
CRCM_HUMANphysical interactionEBI-1065692
intact17353931
BPA1_HUMANphysical interactionEBI-1067054
intact17353931
PAX7_HUMANphysical interactionEBI-1071439
intact17353931
CSMD1_HUMANphysical interactionEBI-1069809
intact17353931
Q8NCA3_HUMANphysical interactionEBI-1067155
intact17353931
AGAL_HUMANENSP00000285930STRING
AGAL_HUMANENSP00000285930STRING
GALK1_HUMANENSP00000285930STRING
GALK1_HUMANENSP00000285930STRING
ALDH2_HUMANENSP00000285930STRING
ALDH2_HUMANENSP00000285930STRING
LPH_HUMANENSP00000285930STRING
LPH_HUMANENSP00000285930STRING
DHSO_HUMANENSP00000285930STRING
DHSO_HUMANENSP00000285930STRING
AL9A1_HUMANENSP00000285930STRING
AL9A1_HUMANENSP00000285930STRING
AL7A1_HUMANENSP00000285930STRING
AL7A1_HUMANENSP00000285930STRING
DCXR_HUMANENSP00000285930STRING
DCXR_HUMANENSP00000285930STRING
BGAL_HUMANENSP00000285930STRING
BGAL_HUMANENSP00000285930STRING
GRHPR_HUMANENSP00000285930STRING
GRHPR_HUMANENSP00000285930STRING
AL1A3_HUMANENSP00000285930STRING
AL1A3_HUMANENSP00000285930STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00605Sulindac
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Sequence of pig lens aldose reductase and electrospray massspectrometry of non-covalent and covalent complexes.";
Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O.,Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F.,van Dorsselaer A.;
Eur. J. Biochem. 218:893-903(1993).
Cited for: PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2.
"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.
"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-95; LYS-222 AND LYS-263, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-40, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures