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P14550

- AK1A1_HUMAN

UniProt

P14550 - AK1A1_HUMAN

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Protein

Alcohol dehydrogenase [NADP(+)]

Gene

AKR1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN).3 Publications

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Proton donor
Sitei80 – 801Lowers pKa of active site Tyr
Binding sitei113 – 1131Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi211 – 27363NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. alditol:NADP+ 1-oxidoreductase activity Source: ProtInc
  2. electron carrier activity Source: UniProtKB
  3. L-glucuronate reductase activity Source: Ensembl

GO - Biological processi

  1. aldehyde catabolic process Source: Ensembl
  2. cellular aldehyde metabolic process Source: ProtInc
  3. D-glucuronate catabolic process Source: Ensembl
  4. glucose metabolic process Source: ProtInc
  5. L-ascorbic acid biosynthetic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

SABIO-RKP14550.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase [NADP(+)] (EC:1.1.1.2)
Alternative name(s):
Aldehyde reductase
Aldo-keto reductase family 1 member A1
Gene namesi
Name:AKR1A1
Synonyms:ALDR1, ALR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:380. AKR1A1.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. cytosol Source: Ensembl
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501Y → F: Complete loss of enzymatic activity. 1 Publication
Mutagenesisi50 – 501Y → H: Complete loss of enzymatic activity. 1 Publication
Mutagenesisi80 – 801K → M: Complete loss of enzymatic activity. 1 Publication
Mutagenesisi113 – 1131H → Q: Strong decrease in enzymatic activity. 1 Publication
Mutagenesisi299 – 2991I → A: No change in enzymatic activity. 1 Publication
Mutagenesisi299 – 2991I → C: No change in enzymatic activity. 1 Publication
Mutagenesisi300 – 3001V → C: No change in enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA24674.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 325324Alcohol dehydrogenase [NADP(+)]PRO_0000124617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei127 – 1271N6-acetyllysine; alternateBy similarity
Modified residuei127 – 1271N6-succinyllysine; alternateBy similarity
Modified residuei145 – 1451N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP14550.
PaxDbiP14550.
PeptideAtlasiP14550.
PRIDEiP14550.

2D gel databases

REPRODUCTION-2DPAGEIPI00220271.
P14550.
SWISS-2DPAGEP14550.
UCD-2DPAGEP14550.

PTM databases

PhosphoSiteiP14550.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in kidney, salivary gland and liver. Detected in trachea, stomach, brain, lung, prostate, placenta, mammary gland, small intestine and lung.2 Publications

Gene expression databases

BgeeiP14550.
CleanExiHS_AKR1A1.
ExpressionAtlasiP14550. baseline and differential.
GenevestigatoriP14550.

Organism-specific databases

HPAiCAB006246.
HPA017919.
HPA019649.
HPA027734.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi115610. 5 interactions.
IntActiP14550. 2 interactions.
MINTiMINT-5001699.
STRINGi9606.ENSP00000312606.

Structurei

Secondary structure

1
325
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73
Beta strandi13 – 175
Helixi26 – 3914
Beta strandi43 – 453
Helixi48 – 503
Helixi53 – 6311
Beta strandi68 – 703
Helixi72 – 743
Beta strandi76 – 816
Helixi83 – 853
Helixi88 – 10215
Beta strandi107 – 1137
Beta strandi115 – 1184
Beta strandi120 – 1223
Helixi140 – 15314
Beta strandi155 – 1639
Helixi166 – 1738
Beta strandi182 – 1865
Helixi194 – 20310
Beta strandi206 – 2105
Helixi232 – 24110
Helixi245 – 25511
Helixi267 – 2748
Helixi283 – 2908
Beta strandi302 – 3054
Beta strandi308 – 3136
Beta strandi320 – 3234

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ALRX-ray2.48A2-325[»]
ProteinModelPortaliP14550.
SMRiP14550. Positions 2-325.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14550.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP14550.
KOiK00002.
OMAiWPYAFER.
OrthoDBiEOG70KGQF.
PhylomeDBiP14550.
TreeFamiTF106492.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14550-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAVKYALSVG YRHIDCAAIY
60 70 80 90 100
GNEPEIGEAL KEDVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA
110 120 130 140 150
DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTICYDSTHY KETWKALEAL
160 170 180 190 200
VAKGLVQALG LSNFNSRQID DILSVASVRP AVLQVECHPY LAQNELIAHC
210 220 230 240 250
QARGLEVTAY SPLGSSDRAW RDPDEPVLLE EPVVLALAEK YGRSPAQILL
260 270 280 290 300
RWQVQRKVIC IPKSITPSRI LQNIKVFDFT FSPEEMKQLN ALNKNWRYIV
310 320
PMLTVDGKRV PRDAGHPLYP FNDPY
Length:325
Mass (Da):36,573
Last modified:January 23, 2007 - v3
Checksum:iF6B27517EB754E37
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti305 – 3051V → A in BAF85772. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521N → S Reduced activity towards daunorubicin.
Corresponds to variant rs2229540 [ dbSNP | Ensembl ].
VAR_048212
Natural varianti55 – 551E → D Reduced activity towards daunorubicin.
Corresponds to variant rs6690497 [ dbSNP | Ensembl ].
VAR_058909

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04794 mRNA. Translation: AAA51711.1.
AF036683
, AF036680, AF036681, AF036682 Genomic DNA. Translation: AAB92369.1.
AF112485, AF112484 Genomic DNA. Translation: AAF01260.1.
AK293083 mRNA. Translation: BAF85772.1.
CR457010 mRNA. Translation: CAG33291.1.
BT007003 mRNA. Translation: AAP35649.1.
AL355480 Genomic DNA. Translation: CAI22459.1.
CH471059 Genomic DNA. Translation: EAX06970.1.
CH471059 Genomic DNA. Translation: EAX06971.1.
CH471059 Genomic DNA. Translation: EAX06972.1.
CH471059 Genomic DNA. Translation: EAX06974.1.
BC000670 mRNA. Translation: AAH00670.1.
BC005394 mRNA. Translation: AAH05394.1.
CCDSiCCDS523.1.
PIRiA33851.
RefSeqiNP_001189342.1. NM_001202413.1.
NP_001189343.1. NM_001202414.1.
NP_006057.1. NM_006066.3.
NP_697021.1. NM_153326.2.
UniGeneiHs.474584.
Hs.721160.

Genome annotation databases

EnsembliENST00000351829; ENSP00000312606; ENSG00000117448.
ENST00000372070; ENSP00000361140; ENSG00000117448.
ENST00000621846; ENSP00000480713; ENSG00000117448.
GeneIDi10327.
KEGGihsa:10327.
UCSCiuc001cod.3. human.

Polymorphism databases

DMDMi113600.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04794 mRNA. Translation: AAA51711.1 .
AF036683
, AF036680 , AF036681 , AF036682 Genomic DNA. Translation: AAB92369.1 .
AF112485 , AF112484 Genomic DNA. Translation: AAF01260.1 .
AK293083 mRNA. Translation: BAF85772.1 .
CR457010 mRNA. Translation: CAG33291.1 .
BT007003 mRNA. Translation: AAP35649.1 .
AL355480 Genomic DNA. Translation: CAI22459.1 .
CH471059 Genomic DNA. Translation: EAX06970.1 .
CH471059 Genomic DNA. Translation: EAX06971.1 .
CH471059 Genomic DNA. Translation: EAX06972.1 .
CH471059 Genomic DNA. Translation: EAX06974.1 .
BC000670 mRNA. Translation: AAH00670.1 .
BC005394 mRNA. Translation: AAH05394.1 .
CCDSi CCDS523.1.
PIRi A33851.
RefSeqi NP_001189342.1. NM_001202413.1.
NP_001189343.1. NM_001202414.1.
NP_006057.1. NM_006066.3.
NP_697021.1. NM_153326.2.
UniGenei Hs.474584.
Hs.721160.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ALR X-ray 2.48 A 2-325 [» ]
ProteinModelPortali P14550.
SMRi P14550. Positions 2-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115610. 5 interactions.
IntActi P14550. 2 interactions.
MINTi MINT-5001699.
STRINGi 9606.ENSP00000312606.

Chemistry

BindingDBi P14550.
ChEMBLi CHEMBL2246.
DrugBanki DB00997. Doxorubicin.

PTM databases

PhosphoSitei P14550.

Polymorphism databases

DMDMi 113600.

2D gel databases

REPRODUCTION-2DPAGE IPI00220271.
P14550.
SWISS-2DPAGE P14550.
UCD-2DPAGE P14550.

Proteomic databases

MaxQBi P14550.
PaxDbi P14550.
PeptideAtlasi P14550.
PRIDEi P14550.

Protocols and materials databases

DNASUi 10327.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000351829 ; ENSP00000312606 ; ENSG00000117448 .
ENST00000372070 ; ENSP00000361140 ; ENSG00000117448 .
ENST00000621846 ; ENSP00000480713 ; ENSG00000117448 .
GeneIDi 10327.
KEGGi hsa:10327.
UCSCi uc001cod.3. human.

Organism-specific databases

CTDi 10327.
GeneCardsi GC01P046017.
HGNCi HGNC:380. AKR1A1.
HPAi CAB006246.
HPA017919.
HPA019649.
HPA027734.
MIMi 103830. gene.
neXtProti NX_P14550.
PharmGKBi PA24674.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0656.
HOGENOMi HOG000250272.
HOVERGENi HBG000020.
InParanoidi P14550.
KOi K00002.
OMAi WPYAFER.
OrthoDBi EOG70KGQF.
PhylomeDBi P14550.
TreeFami TF106492.

Enzyme and pathway databases

SABIO-RK P14550.

Miscellaneous databases

ChiTaRSi AKR1A1. human.
EvolutionaryTracei P14550.
GeneWikii Aldo-keto_reductase_family_1,_member_A1.
GenomeRNAii 10327.
NextBioi 39151.
PROi P14550.
SOURCEi Search...

Gene expression databases

Bgeei P14550.
CleanExi HS_AKR1A1.
ExpressionAtlasi P14550. baseline and differential.
Genevestigatori P14550.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
PIRSFi PIRSF000097. AKR. 1 hit.
PRINTSi PR00069. ALDKETRDTASE.
SUPFAMi SSF51430. SSF51430. 1 hit.
PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases."
    Bohren K.M., Bullock B., Wermuth B., Gabbay K.H.
    J. Biol. Chem. 264:9547-9551(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "The structural organization of the human aldehyde reductase gene, AKR1A1, and mapping to chromosome 1p33-->p32."
    Fujii J., Hamaoka R., Matsumoto A., Fujii T., Yamaguchi Y., Egashira M., Miyoshi O., Niikawa N., Taniguchi N.
    Cytogenet. Cell Genet. 84:230-232(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Characterization of the human aldehyde reductase gene and promoter."
    Barski O.A., Gabbay K.H., Bohren K.M.
    Genomics 60:188-198(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon and Kidney.
  10. "Primary structure of aldehyde reductase from human liver."
    Wermuth B., Omar A., Forster A., di Francesco C., Wolf M., von Wartburg J.-P., Bullock B., Gabbay K.H.
    Prog. Clin. Biol. Res. 232:297-307(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-325.
    Tissue: Liver.
  11. "Mechanism of human aldehyde reductase: characterization of the active site pocket."
    Barski O.A., Gabbay K.H., Grimshaw C.E., Bohren K.M.
    Biochemistry 34:11264-11275(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-50; LYS-80; HIS-113; ILE-299 AND VAL-300.
  12. "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."
    O'Connor T., Ireland L.S., Harrison D.J., Hayes J.D.
    Biochem. J. 343:487-504(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  13. "Metabolic activation of polycyclic aromatic hydrocarbon trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1)."
    Palackal N.T., Burczynski M.E., Harvey R.G., Penning T.M.
    Chem. Biol. Interact. 130:815-824(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  14. "Two allelic variants of aldo-keto reductase 1A1 exhibit reduced in vitro metabolism of daunorubicin."
    Bains O.S., Takahashi R.H., Pfeifer T.A., Grigliatti T.A., Reid R.E., Riggs K.W.
    Drug Metab. Dispos. 36:904-910(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF VARIANTS SER-52 AND ASP-55.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications."
    El-Kabbani O., Green N.C., Lin G., Carson M., Narayana S.V.L., Moore K.M., Flynn T.G., DeLucas L.J.
    Acta Crystallogr. D 50:859-868(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS).

Entry informationi

Entry nameiAK1A1_HUMAN
AccessioniPrimary (citable) accession number: P14550
Secondary accession number(s): A8KAL8, D3DQ04, Q6IAZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3