AKR1B1 | ENSG00000085662 | NCBI 231

Details for: AKR1B1

Gene ID: 231

Symbol: AKR1B1

Ensembl ID: ENSG00000085662

Description: aldo-keto reductase family 1 member B

Associated with

Fructose biosynthesis
(R-HSA-5652227)
Fructose metabolism
(R-HSA-5652084)
Metabolism
(R-HSA-1430728)
Metabolism of carbohydrates
(R-HSA-71387)
Metabolism of lipids
(R-HSA-556833)
Metabolism of steroid hormones
(R-HSA-196071)
Metabolism of steroids
(R-HSA-8957322)
Pregnenolone biosynthesis
(R-HSA-196108)
Alditol:nadp+ 1-oxidoreductase activity
(GO:0004032)
Allyl-alcohol dehydrogenase activity
(GO:0047655)
C21-steroid hormone biosynthetic process
(GO:0006700)
Carbohydrate metabolic process
(GO:0005975)
Cellular hyperosmotic salinity response
(GO:0071475)
Cytosol
(GO:0005829)
Daunorubicin metabolic process
(GO:0044597)
Doxorubicin metabolic process
(GO:0044598)
Electron transfer activity
(GO:0009055)
Electron transport chain
(GO:0022900)
Epithelial cell maturation
(GO:0002070)
Extracellular exosome
(GO:0070062)
Extracellular space
(GO:0005615)
Fructose biosynthetic process
(GO:0046370)
Glyceraldehyde oxidoreductase activity
(GO:0043795)
Glycerol dehydrogenase [nadp+] activity
(GO:0047956)
L-ascorbic acid biosynthetic process
(GO:0019853)
L-glucuronate reductase activity
(GO:0047939)
Metanephric collecting duct development
(GO:0072205)
Nadp-retinol dehydrogenase activity
(GO:0052650)
Negative regulation of apoptotic process
(GO:0043066)
Nucleoplasm
(GO:0005654)
Prostaglandin h2 endoperoxidase reductase activity
(GO:0036130)
Prostaglandin metabolic process
(GO:0006693)
Protein binding
(GO:0005515)
Regulation of urine volume
(GO:0035809)
Renal water homeostasis
(GO:0003091)
Retinal dehydrogenase activity
(GO:0001758)
Retinoid metabolic process
(GO:0001523)
Retinol metabolic process
(GO:0042572)

Other Information

Proteins

Aldo-keto reductase family 1 member B1

Genular Protein ID: 2630763080

Symbol: ALDR_HUMAN

Name: Aldo-keto reductase family 1 member B1

UniProtKB Accession Codes:

P15121 B2R8N3 Q5U031 Q6FGA4 Q6ICP2 Q9BS21 Q9UCI9

Database IDs:

Citations:

PubMed ID: 2498333

Title: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.

PubMed ID: 2498333

DOI: 10.1016/s0021-9258(18)60566-6

PubMed ID: 2504709

Title: Cloning and sequence determination of human placental aldose reductase gene.

PubMed ID: 2504709

DOI: 10.1016/s0021-9258(18)63766-4

PubMed ID: 2510130

Title: Nucleotide sequence of cDNA for human aldose reductase.

PubMed ID: 2510130

DOI: 10.1093/nar/17.20.8368

PubMed ID: 2111143

Title: Cloning and prokaryotic expression of a biologically active human placental aldose reductase.

PubMed ID: 2111143

DOI: 10.1089/dna.1990.9.149

PubMed ID: 2112546

Title: Cloning and expression of human aldose reductase.

PubMed ID: 2112546

DOI: 10.1016/s0021-9258(19)38740-x

PubMed ID: 1901857

Title: Structure of the human aldose reductase gene.

PubMed ID: 1901857

DOI: 10.1016/s0021-9258(20)89582-9

PubMed ID: 9195951

Title: Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene.

PubMed ID: 9195951

DOI: 10.1074/jbc.272.26.16431

PubMed ID: 14996095

Title: SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma.

PubMed ID: 14996095

DOI: 10.1111/j.1365-2133.2004.05651.x

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 12690205

Title: Human chromosome 7: DNA sequence and biology.

PubMed ID: 12690205

DOI: 10.1126/science.1083423

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8435445

Title: Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress.

PubMed ID: 8435445

DOI: 10.1016/0167-4889(93)90218-e

PubMed ID: 2492527

Title: Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine.

PubMed ID: 2492527

DOI: 10.1016/s0021-9258(19)81699-x

PubMed ID: 8343525

Title: Identification of the reactive cysteine residue in human placenta aldose reductase.

PubMed ID: 8343525

DOI: 10.1016/0167-4838(93)90258-s

PubMed ID: 8281941

Title: Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes.

PubMed ID: 8281941

DOI: 10.1111/j.1432-1033.1993.tb18445.x

PubMed ID: 1936586

Title: Crucial role of aldose reductase activity and plasma glucose level in sorbitol accumulation in erythrocytes from diabetic patients.

PubMed ID: 1936586

DOI: 10.2337/diab.40.10.1233

PubMed ID: 8245005

Title: Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110.

PubMed ID: 8245005

DOI: 10.1016/s0021-9258(19)74444-5

PubMed ID: 10510318

Title: Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members.

PubMed ID: 10510318

DOI: 10.1042/bj3430487

PubMed ID: 12732097

Title: Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism.

PubMed ID: 12732097

DOI: 10.1042/bj20021818

PubMed ID: 17381426

Title: Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes.

PubMed ID: 17381426

DOI: 10.1042/bj20061743

PubMed ID: 19010934

Title: Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1, 1B3 and 1B7.

PubMed ID: 19010934

DOI: 10.1093/jb/mvn152

PubMed ID: 21329684

Title: Human aldo-keto reductases 1B1 and 1B10: a comparative study on their enzyme activity toward electrophilic carbonyl compounds.

PubMed ID: 21329684

DOI: 10.1016/j.cbi.2011.02.004

PubMed ID: 21329680

Title: Human and rodent aldo-keto reductases from the AKR1B subfamily and their specificity with retinaldehyde.

PubMed ID: 21329680

DOI: 10.1016/j.cbi.2011.02.007

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 1621098

Title: An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.

PubMed ID: 1621098

DOI: 10.1126/science.1621098

PubMed ID: 1447221

Title: The crystal structure of the aldose reductase.NADPH binary complex.

PubMed ID: 1447221

DOI: 10.2210/pdb1abn/pdb

PubMed ID: 8234324

Title: Refined 1.8-A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.

PubMed ID: 8234324

DOI: 10.1073/pnas.90.21.9847

PubMed ID: 9405046

Title: The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant.

PubMed ID: 9405046

DOI: 10.1021/bi9717136

PubMed ID: 15272156

Title: The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48.

PubMed ID: 15272156

DOI: 10.1107/s0907444904011370

PubMed ID: 15146478

Title: Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A.

PubMed ID: 15146478

DOI: 10.1002/prot.20015

PubMed ID: 16337231

Title: High-resolution crystal structure of aldose reductase complexed with the novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site anchoring group.

PubMed ID: 16337231

DOI: 10.1016/j.jmb.2005.10.067

PubMed ID: 17505104

Title: The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop.

PubMed ID: 17505104

DOI: 10.1107/s0907444907011997

PubMed ID: 17418233

Title: Evidence for a novel binding site conformer of aldose reductase in ligand-bound state.

PubMed ID: 17418233

DOI: 10.1016/j.jmb.2007.03.021

PubMed ID: 17368668

Title: Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution.

PubMed ID: 17368668

DOI: 10.1016/j.jmb.2006.12.004

Sequence Information:

Length: 316
Mass: 35853
Checksum: 1852E8616B5DCEAE
Sequence:

MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ 
EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK 
EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP 
AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK 
HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA 
LLSCTSHKDY PFHEEF

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: AKR1B1

Associated with

Other Information

The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. PubMed ID: 2498333

Cloning and sequence determination of human placental aldose reductase gene. PubMed ID: 2504709

Nucleotide sequence of cDNA for human aldose reductase. PubMed ID: 2510130

Cloning and prokaryotic expression of a biologically active human placental aldose reductase. PubMed ID: 2111143

Cloning and expression of human aldose reductase. PubMed ID: 2112546

Structure of the human aldose reductase gene. PubMed ID: 1901857

Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene. PubMed ID: 9195951

SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma. PubMed ID: 14996095

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

Human chromosome 7: DNA sequence and biology. PubMed ID: 12690205

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress. PubMed ID: 8435445

Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine. PubMed ID: 2492527

Identification of the reactive cysteine residue in human placenta aldose reductase. PubMed ID: 8343525

Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes. PubMed ID: 8281941

Crucial role of aldose reductase activity and plasma glucose level in sorbitol accumulation in erythrocytes from diabetic patients. PubMed ID: 1936586

Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. PubMed ID: 8245005

Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. PubMed ID: 10510318

Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism. PubMed ID: 12732097

Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes. PubMed ID: 17381426

Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1, 1B3 and 1B7. PubMed ID: 19010934

Human aldo-keto reductases 1B1 and 1B10: a comparative study on their enzyme activity toward electrophilic carbonyl compounds. PubMed ID: 21329684

Human and rodent aldo-keto reductases from the AKR1B subfamily and their specificity with retinaldehyde. PubMed ID: 21329680

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Initial characterization of the human central proteome. PubMed ID: 21269460

An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. PubMed ID: 1621098

The crystal structure of the aldose reductase.NADPH binary complex. PubMed ID: 1447221

Refined 1.8-A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. PubMed ID: 8234324

The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. PubMed ID: 9405046

The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48. PubMed ID: 15272156

Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A. PubMed ID: 15146478

High-resolution crystal structure of aldose reductase complexed with the novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site anchoring group. PubMed ID: 16337231

The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop. PubMed ID: 17505104

Evidence for a novel binding site conformer of aldose reductase in ligand-bound state. PubMed ID: 17418233

Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution. PubMed ID: 17368668