ID   CBR1_HUMAN              Reviewed;         277 AA.
AC   P16152; B2RBZ7; Q3LHW8;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-APR-2011, entry version 130.
DE   RecName: Full=Carbonyl reductase [NADPH] 1;
DE            EC=1.1.1.184;
DE   AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP+];
DE            EC=1.1.1.197;
DE   AltName: Full=NADPH-dependent carbonyl reductase 1;
DE   AltName: Full=Prostaglandin 9-ketoreductase;
DE   AltName: Full=Prostaglandin-E(2) 9-reductase;
DE            EC=1.1.1.189;
GN   Name=CBR1; Synonyms=CBR, CRN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Placenta;
RX   MEDLINE=89034082; PubMed=3141401;
RA   Wermuth B., Bohren K.M., Heinemann G., von Wartburg J.-P.,
RA   Gabbay K.H.;
RT   "Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and
RT   amino acid sequence of the encoded protein.";
RL   J. Biol. Chem. 263:16185-16188(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Mammary gland;
RX   MEDLINE=90212644; PubMed=2182121; DOI=10.1016/0167-4781(90)90050-C;
RA   Forrest G.L., Akman S., Krutzik S., Paxton R.J., Sparkes R.S.,
RA   Doroshow J., Felsted R.L., Mohandas T., Bachur N.R.;
RT   "Induction of a human carbonyl reductase gene located on chromosome
RT   21.";
RL   Biochim. Biophys. Acta 1048:149-155(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92017676; PubMed=1921984;
RA   Forrest G.L., Akman S., Doroshow J., Rivera H., Kaplan W.D.;
RT   "Genomic sequence and expression of a cloned human carbonyl reductase
RT   gene with daunorubicin reductase activity.";
RL   Mol. Pharmacol. 40:502-507(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98414514; PubMed=9740676; DOI=10.1006/geno.1998.5380;
RA   Watanabe K., Sugawara C., Ono A., Fukuzumi Y., Itakura S.,
RA   Yamazaki M., Tashiro H., Osoegawa K., Soeda E., Nomura T.;
RT   "Mapping of a novel human carbonyl reductase, CBR3, and ribosomal
RT   pseudogenes to human chromosome 21q22.2.";
RL   Genomics 52:95-100(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal brain;
RA   Terada T., Mizobuchi H.;
RT   "Human fetal brain carbonyl reductases.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-131.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=20289799; PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA   Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA   Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA   Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA   Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA   Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA   Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA   Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA   Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA   Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA   Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA   Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [13]
RP   PARTIAL PROTEIN SEQUENCE, AND N6-1-CARBOXYETHYLATION AT LYS-239.
RX   MEDLINE=93133816; PubMed=8421682; DOI=10.1073/pnas.90.2.502;
RA   Krook M., Ghosh D., Stroemberg R., Carlquist M., Joernvall H.;
RT   "Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-
RT   dependent prostaglandin dehydrogenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:502-506(1993).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-194, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Lung carcinoma;
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [15]
RP   ENZYME REGULATION, AND FUNCTION.
RX   PubMed=18449627; DOI=10.1007/s11095-008-9592-5;
RA   Gonzalez-Covarrubias V., Kalabus J.L., Blanco J.G.;
RT   "Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the
RT   cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER).";
RL   Pharm. Res. 25:1730-1734(2008).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 2-276 IN COMPLEX WITH THE
RP   SYNTHETIC INHIBITOR HYDROXY-PP AND NADP, MASS SPECTROMETRY, PARTIAL
RP   PROTEIN SEQUENCE, AND FUNCTION.
RX   PubMed=15799708; DOI=10.1371/journal.pbio.0030128;
RA   Tanaka M., Bateman R., Rauh D., Vaisberg E., Ramachandani S.,
RA   Zhang C., Hansen K.C., Burlingame A.L., Trautman J.K., Shokat K.M.,
RA   Adams C.L.;
RT   "An unbiased cell morphology-based screen for new, biologically active
RT   small molecules.";
RL   PLoS Biol. 3:E128-E128(2005).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP
RP   AND FORMALDEHYDE-GLUTATHIONE ADDUCT, AND FUNCTION.
RX   PubMed=17912391; DOI=10.1039/b707602a;
RA   Bateman R., Rauh D., Shokat K.M.;
RT   "Glutathione traps formaldehyde by formation of a
RT   bicyclo[4.4.1]undecane adduct.";
RL   Org. Biomol. Chem. 5:3363-3367(2007).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP,
RP   SUBSTRATE ANALOGS, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18826943; DOI=10.1074/jbc.M807125200;
RA   Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.;
RT   "Human carbonyl reductase 1 is an S-nitrosoglutathione reductase.";
RL   J. Biol. Chem. 283:35756-35762(2008).
RN   [20]
RP   VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND ENZYME REGULATION.
RX   PubMed=17344335; DOI=10.1124/dmd.107.014779;
RA   Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L.,
RA   Blanco J.G.;
RT   "A functional genetic polymorphism on human carbonyl reductase 1 (CBR1
RT   V88I) impacts on catalytic activity and NADPH binding affinity.";
RL   Drug Metab. Dispos. 35:973-980(2007).
CC   -!- FUNCTION: NADPH-dependent reductase with broad substrate
CC       specificity. Catalyzes the reduction of a wide variety of carbonyl
CC       compounds including quinones, prostaglandins, menadione, plus
CC       various xenobiotics. Catalyzes the reduction of the antitumor
CC       anthracyclines doxorubicin and daunorubicin to the cardiotoxic
CC       compounds doxorubicinol and daunorubicinol. Can convert
CC       prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione,
CC       which explains its higher affinity for glutathione-conjugated
CC       substrates. Catalyzes the reduction of S-nitrosoglutathione.
CC   -!- CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH.
CC   -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha,15-
CC       trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-11-
CC       alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH.
CC   -!- CATALYTIC ACTIVITY: (13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-
CC       13-enoate + NADP(+) = (13E)-11-alpha-hydroxy-9,15-dioxoprost-13-
CC       enoate + NADPH.
CC   -!- ENZYME REGULATION: Inhibited by quercetin, rutenin and its
CC       derivatives.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=30 uM for S-nitrosoglutathione;
CC         KM=22 uM for menadione;
CC         KM=309 uM for prostaglandin E2;
CC         KM=173 uM for daunorubicin;
CC         KM=247 uM for NADPH;
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       P23508:MCC; NbExp=1; IntAct=EBI-351348, EBI-307531;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/cbr1/";
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DR   EMBL; J04056; AAA52070.1; -; mRNA.
DR   EMBL; M62420; AAA17881.1; -; Genomic_DNA.
DR   EMBL; AB003151; BAA33498.1; -; Genomic_DNA.
DR   EMBL; AP000688; BAA89424.1; -; Genomic_DNA.
DR   EMBL; AB124848; BAE45940.1; -; mRNA.
DR   EMBL; BT019843; AAV38646.1; -; mRNA.
DR   EMBL; CR541708; CAG46509.1; -; mRNA.
DR   EMBL; AK314879; BAG37394.1; -; mRNA.
DR   EMBL; EF141836; ABK97430.1; -; Genomic_DNA.
DR   EMBL; AP001724; BAA95508.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09755.1; -; Genomic_DNA.
DR   EMBL; BC002511; AAH02511.1; -; mRNA.
DR   EMBL; BC015640; AAH15640.1; -; mRNA.
DR   IPI; IPI00295386; -.
DR   PIR; A61271; RDHUCB.
DR   RefSeq; NP_001748.1; NM_001757.2.
DR   UniGene; Hs.606200; -.
DR   UniGene; Hs.88778; -.
DR   PDB; 1WMA; X-ray; 1.24 A; A=2-276.
DR   PDB; 2PFG; X-ray; 1.54 A; A=2-277.
DR   PDB; 3BHI; X-ray; 2.27 A; A=2-277.
DR   PDB; 3BHJ; X-ray; 1.77 A; A=2-277.
DR   PDB; 3BHM; X-ray; 1.80 A; A=2-277.
DR   PDBsum; 1WMA; -.
DR   PDBsum; 2PFG; -.
DR   PDBsum; 3BHI; -.
DR   PDBsum; 3BHJ; -.
DR   PDBsum; 3BHM; -.
DR   ProteinModelPortal; P16152; -.
DR   SMR; P16152; 3-277.
DR   IntAct; P16152; 17.
DR   MINT; MINT-1418935; -.
DR   STRING; P16152; -.
DR   PhosphoSite; P16152; -.
DR   REPRODUCTION-2DPAGE; IPI00295386; -.
DR   UCD-2DPAGE; P16152; -.
DR   PeptideAtlas; P16152; -.
DR   PRIDE; P16152; -.
DR   Ensembl; ENST00000290349; ENSP00000290349; ENSG00000159228.
DR   GeneID; 873; -.
DR   KEGG; hsa:873; -.
DR   UCSC; uc002yvb.1; human.
DR   CTD; 873; -.
DR   GeneCards; GC21P022920; -.
DR   H-InvDB; HIX0016099; -.
DR   HGNC; HGNC:1548; CBR1.
DR   HPA; HPA018433; -.
DR   MIM; 114830; gene.
DR   neXtProt; NX_P16152; -.
DR   PharmGKB; PA26121; -.
DR   eggNOG; prNOG15925; -.
DR   GeneTree; ENSGT00510000046499; -.
DR   HOGENOM; HBG750976; -.
DR   HOVERGEN; HBG001909; -.
DR   InParanoid; P16152; -.
DR   OMA; NTAYGVT; -.
DR   OrthoDB; EOG4BP1CB; -.
DR   PhylomeDB; P16152; -.
DR   BRENDA; 1.1.1.184; 247.
DR   BRENDA; 1.1.1.189; 247.
DR   BRENDA; 1.1.1.197; 247.
DR   DrugBank; DB00414; Acetohexamide.
DR   DrugBank; DB01046; Lubiprostone.
DR   NextBio; 3634; -.
DR   ArrayExpress; P16152; -.
DR   Bgee; P16152; -.
DR   CleanEx; HS_CBR1; -.
DR   Genevestigator; P16152; -.
DR   GermOnline; ENSG00000159228; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047021; F:15-hydroxyprostaglandin dehydrogenase (NADP+) activity; IEA:EC.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
DR   GO; GO:0050221; F:prostaglandin-E2 9-reductase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0017144; P:drug metabolic process; IDA:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0042373; P:vitamin K metabolic process; IDA:UniProtKB.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein;
KW   Polymorphism.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    277       Carbonyl reductase [NADPH] 1.
FT                                /FTId=PRO_0000054602.
FT   NP_BIND      10     34       NADP.
FT   NP_BIND      63     64       NADP.
FT   NP_BIND     194    198       NADP.
FT   NP_BIND     231    233       NADP.
FT   REGION       95     97       Glutathione binding.
FT   REGION      193    194       Glutathione binding.
FT   ACT_SITE    194    194       Proton acceptor.
FT   BINDING      90     90       NADP; via carbonyl oxygen.
FT   BINDING     106    106       Glutathione.
FT   BINDING     140    140       Substrate.
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES     194    194       Phosphotyrosine.
FT   MOD_RES     239    239       N6-1-carboxyethyl lysine.
FT   VARIANT      88     88       V -> I (reduced affinity for NADPH and
FT                                reduced activity towards daunorubicin and
FT                                prostaglandin E2; dbSNP:rs1143663).
FT                                /FTId=VAR_059053.
FT   VARIANT     131    131       P -> S (in dbSNP:rs41557318).
FT                                /FTId=VAR_031706.
FT   STRAND        7     12
FT   HELIX        16     28
FT   STRAND       29     39
FT   HELIX        40     52
FT   STRAND       58     61
FT   HELIX        67     81
FT   STRAND       82     89
FT   HELIX       103    114
FT   HELIX       116    125
FT   HELIX       126    128
FT   STRAND      129    138
FT   HELIX       141    148
FT   HELIX       152    159
FT   HELIX       165    180
FT   TURN        184    188
FT   HELIX       193    215
FT   STRAND      222    227
FT   TURN        234    236
FT   HELIX       244    247
FT   HELIX       249    255
FT   STRAND      268    270
FT   STRAND      273    275
SQ   SEQUENCE   277 AA;  30375 MW;  51A5A495EB4F4EC3 CRC64;
     MSSGIHVALV TGGNKGIGLA IVRDLCRLFS GDVVLTARDV TRGQAAVQQL QAEGLSPRFH
     QLDIDDLQSI RALRDFLRKE YGGLDVLVNN AGIAFKVADP TPFHIQAEVT MKTNFFGTRD
     VCTELLPLIK PQGRVVNVSS IMSVRALKSC SPELQQKFRS ETITEEELVG LMNKFVEDTK
     KGVHQKEGWP SSAYGVTKIG VTVLSRIHAR KLSEQRKGDK ILLNACCPGW VRTDMAGPKA
     TKSPEEGAET PVYLALLPPD AEGPHGQFVS EKRVEQW
//
