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Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Protein Ke6) (Ke-6) (Really interesting new gene 2 protein) (Short chain dehydrogenase/reductase family 30C member 1) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239)

 DHB8_HUMAN              Reviewed;         261 AA.
Q92506; A6NLX7; Q5STP7; Q9UIQ1;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 2.
25-OCT-2017, entry version 175.
RecName: Full=Estradiol 17-beta-dehydrogenase 8;
EC=1.1.1.62 {ECO:0000269|PubMed:17978863};
AltName: Full=17-beta-hydroxysteroid dehydrogenase 8 {ECO:0000303|PubMed:17978863};
Short=17-beta-HSD 8;
AltName: Full=3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit {ECO:0000303|PubMed:25203508};
Short=KAR alpha subunit {ECO:0000303|PubMed:25203508};
AltName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
EC=1.1.1.- {ECO:0000269|PubMed:19571038, ECO:0000269|PubMed:25203508};
AltName: Full=Protein Ke6;
Short=Ke-6;
AltName: Full=Really interesting new gene 2 protein;
AltName: Full=Short chain dehydrogenase/reductase family 30C member 1;
AltName: Full=Testosterone 17-beta-dehydrogenase 8;
EC=1.1.1.239;
Name=HSD17B8; Synonyms=FABGL, HKE6, RING2, SDR30C1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-261.
PubMed=8812499; DOI=10.1006/geno.1996.0405;
Ando A., Kikuti Y.Y., Shigenari A., Kawata H., Okamoto N., Shiina T.,
Chen L., Ikemura T., Abe K., Kimura M., Inoko H.;
"cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes
at the centromeric end of the human MHC region.";
Genomics 35:600-602(1996).
[6]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
PubMed=17978863; DOI=10.1007/s11010-007-9637-9;
Ohno S., Nishikawa K., Honda Y., Nakajin S.;
"Expression in E. coli and tissue distribution of the human homologue
of the mouse Ke 6 gene, 17beta-hydroxysteroid dehydrogenase type 8.";
Mol. Cell. Biochem. 309:209-215(2008).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CBR4.
PubMed=19571038; DOI=10.1096/fj.09-133587;
Chen Z., Kastaniotis A.J., Miinalainen I.J., Rajaram V.,
Wierenga R.K., Hiltunen J.K.;
"17beta-Hydroxysteroid dehydrogenase type 8 and carbonyl reductase
type 4 assemble as a ketoacyl reductase of human mitochondrial FAS.";
FASEB J. 23:3682-3691(2009).
[8]
INDUCTION BY ESTRADIOL.
PubMed=18852215; DOI=10.1677/JOE-08-0134;
Rotinen M., Celay J., Alonso M.M., Arrazola A., Encio I., Villar J.;
"Estradiol induces type 8 17beta-hydroxysteroid dehydrogenase
expression: crosstalk between estrogen receptor alpha and C/EBPbeta.";
J. Endocrinol. 200:85-92(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-261 IN COMPLEX WITH NAD.
Structural genomics consortium (SGC);
"Structure of human hydroxysteroid dehydrogenase type 8, HSD17B8.";
Submitted (FEB-2009) to the PDB data bank.
[12] {ECO:0000244|PDB:4CQL, ECO:0000244|PDB:4CQM}
X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) IN COMPLEX WITH NAD AND CBR4,
SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF
ASP-42; ARG-148; TYR-169; LYS-173 AND ARG-189.
PubMed=25203508; DOI=10.1038/ncomms5805;
Venkatesan R., Sah-Teli S.K., Awoniyi L.O., Jiang G., Prus P.,
Kastaniotis A.J., Hiltunen J.K., Wierenga R.K., Chen Z.;
"Insights into mitochondrial fatty acid synthesis from the structure
of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA
dehydrogenase.";
Nat. Commun. 5:4805-4805(2014).
[13]
VARIANT [LARGE SCALE ANALYSIS] LEU-158.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: NAD-dependent 17-beta-hydroxysteroid dehydrogenase with
highest activity towards estradiol. Has very low activity towards
testosterone (PubMed:17978863). The heterotetramer with CBR4 has
NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity,
and thereby plays a role in mitochondrial fatty acid biosynthesis
(PubMed:19571038, PubMed:25203508). Within the heterotetramer,
HSD17B8 binds NADH; CBR4 binds NADPD (PubMed:25203508).
{ECO:0000269|PubMed:17978863, ECO:0000269|PubMed:19571038,
ECO:0000269|PubMed:25203508}.
-!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone +
NAD(P)H. {ECO:0000269|PubMed:17978863}.
-!- CATALYTIC ACTIVITY: Testosterone + NAD(+) = androstenedione +
NADH. {ECO:0000269|PubMed:17978863}.
-!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
{ECO:0000269|PubMed:17978863}.
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
{ECO:0000269|PubMed:25203508}.
-!- SUBUNIT: Heterotetramer with CBR4; contains two molecules of
HSD17B8 and CBR4. {ECO:0000269|PubMed:25203508,
ECO:0000269|Ref.11}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:19571038}.
-!- TISSUE SPECIFICITY: Highly expressed in placenta, liver and
pancreas, lower in the skeletal muscle and kidney. Widely
expressed. {ECO:0000269|PubMed:17978863}.
-!- INDUCTION: Up-regulated by estradiol.
{ECO:0000269|PubMed:18852215}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
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EMBL; BT007239; AAP35903.1; -; mRNA.
EMBL; AL031228; CAC38444.1; -; Genomic_DNA.
EMBL; AL662824; CAI17616.1; -; Genomic_DNA.
EMBL; AL713971; CAI17616.1; JOINED; Genomic_DNA.
EMBL; AL713971; CAI17657.1; -; Genomic_DNA.
EMBL; AL662824; CAI17657.1; JOINED; Genomic_DNA.
EMBL; AL645940; CAI18068.1; -; Genomic_DNA.
EMBL; AL844527; CAI41840.1; -; Genomic_DNA.
EMBL; CR759786; CAQ08245.1; -; Genomic_DNA.
EMBL; CR759733; CAQ10302.1; -; Genomic_DNA.
EMBL; CR847841; CAQ10313.1; -; Genomic_DNA.
EMBL; CH471081; EAX03682.1; -; Genomic_DNA.
EMBL; BC008185; AAH08185.1; -; mRNA.
EMBL; D82061; BAA11529.1; -; mRNA.
CCDS; CCDS4769.1; -.
RefSeq; NP_055049.1; NM_014234.4.
UniGene; Hs.415058; -.
PDB; 2PD6; X-ray; 2.00 A; A/B/C/D=6-261.
PDB; 4CQL; X-ray; 2.85 A; A/D/E/H/I/L/M/P=1-261.
PDB; 4CQM; X-ray; 2.34 A; A/D/E/H/I/L/M/P=1-261.
PDBsum; 2PD6; -.
PDBsum; 4CQL; -.
PDBsum; 4CQM; -.
ProteinModelPortal; Q92506; -.
SMR; Q92506; -.
BioGrid; 113653; 18.
IntAct; Q92506; 4.
STRING; 9606.ENSP00000363794; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB00157; NADH.
SwissLipids; SLP:000001271; -.
iPTMnet; Q92506; -.
PhosphoSitePlus; Q92506; -.
BioMuta; HSD17B8; -.
DMDM; 12643402; -.
EPD; Q92506; -.
MaxQB; Q92506; -.
PaxDb; Q92506; -.
PeptideAtlas; Q92506; -.
PRIDE; Q92506; -.
TopDownProteomics; Q92506; -.
DNASU; 7923; -.
Ensembl; ENST00000230236; ENSP00000230236; ENSG00000112474.
Ensembl; ENST00000374662; ENSP00000363794; ENSG00000204228.
Ensembl; ENST00000414463; ENSP00000387753; ENSG00000228357.
Ensembl; ENST00000422433; ENSP00000406488; ENSG00000232357.
Ensembl; ENST00000427295; ENSP00000403538; ENSG00000228712.
Ensembl; ENST00000454191; ENSP00000413950; ENSG00000225312.
GeneID; 7923; -.
KEGG; hsa:7923; -.
UCSC; uc003odi.3; human.
CTD; 7923; -.
DisGeNET; 7923; -.
EuPathDB; HostDB:ENSG00000204228.3; -.
GeneCards; HSD17B8; -.
HGNC; HGNC:3554; HSD17B8.
HPA; HPA042132; -.
MIM; 601417; gene.
neXtProt; NX_Q92506; -.
OpenTargets; ENSG00000204228; -.
PharmGKB; PA29484; -.
eggNOG; KOG1200; Eukaryota.
eggNOG; COG1028; LUCA.
GeneTree; ENSGT00760000118868; -.
HOVERGEN; HBG002145; -.
InParanoid; Q92506; -.
KO; K13370; -.
OMA; GQMGNPG; -.
OrthoDB; EOG09370VMU; -.
PhylomeDB; Q92506; -.
TreeFam; TF313099; -.
Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
SABIO-RK; Q92506; -.
UniPathway; UPA00094; -.
UniPathway; UPA00769; -.
ChiTaRS; HSD17B8; human.
EvolutionaryTrace; Q92506; -.
GeneWiki; HSD17B8; -.
GenomeRNAi; 7923; -.
PRO; PR:Q92506; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204228; -.
CleanEx; HS_HSD17B8; -.
Genevisible; Q92506; HS.
GO; GO:0005740; C:mitochondrial envelope; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
GO; GO:0047025; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADH) activity; IMP:UniProtKB.
GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:UniProtKB.
GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl.
GO; GO:0006703; P:estrogen biosynthetic process; IDA:UniProtKB.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:UniProtKB.
GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
Mitochondrion; NAD; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome; Steroid biosynthesis.
CHAIN 1 261 Estradiol 17-beta-dehydrogenase 8.
/FTId=PRO_0000054598.
NP_BIND 15 23 NAD. {ECO:0000244|PDB:2PD6,
ECO:0000244|PDB:4CQL,
ECO:0000269|PubMed:25203508,
ECO:0000269|Ref.11}.
NP_BIND 42 43 NAD. {ECO:0000244|PDB:2PD6,
ECO:0000244|PDB:4CQL,
ECO:0000269|PubMed:25203508,
ECO:0000269|Ref.11}.
NP_BIND 74 76 NAD. {ECO:0000244|PDB:2PD6,
ECO:0000244|PDB:4CQL,
ECO:0000269|PubMed:25203508,
ECO:0000269|Ref.11}.
NP_BIND 169 173 NAD. {ECO:0000244|PDB:2PD6,
ECO:0000244|PDB:4CQL,
ECO:0000269|PubMed:25203508,
ECO:0000269|Ref.11}.
NP_BIND 202 204 NAD. {ECO:0000244|PDB:2PD6,
ECO:0000244|PDB:4CQM,
ECO:0000269|Ref.11}.
ACT_SITE 169 169 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 156 156 Substrate. {ECO:0000250}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000250|UniProtKB:P50171}.
MOD_RES 160 160 N6-succinyllysine.
{ECO:0000250|UniProtKB:P50171}.
MOD_RES 173 173 N6-succinyllysine.
{ECO:0000250|UniProtKB:P50171}.
VARIANT 158 158 V -> L (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035844.
VARIANT 190 190 H -> R (in dbSNP:rs34491699).
/FTId=VAR_052316.
MUTAGEN 42 42 D->A: Reduced NADH-dependent reductase
activity with acetoacetyl-CoA. Reduced
NADH-dependent reductase activity with
9,10-phenanthrene quinone. Increases
NADPH-dependent reductase activities. No
effect on the ability to restore growth
of an OAR1-deficient yeast mutant.
{ECO:0000269|PubMed:25203508}.
MUTAGEN 148 148 R->E: No effect on the ability to restore
growth of an OAR1-deficient yeast mutant.
{ECO:0000269|PubMed:25203508}.
MUTAGEN 169 169 Y->A: Strongly reduced NADH-dependent
reductase activity with acetoacetyl-CoA.
Strongly reduced NADH-dependent reductase
activity with 9,10-phenanthrene quinone.
Decreases NADPH-dependent reductase
activity with acetoacetyl-CoA, but
increases NADPH-dependent reductase
activity with 9,10-phenanthrene quinone.
No effect on the ability to restore
growth of an OAR1-deficient yeast mutant.
{ECO:0000269|PubMed:25203508}.
MUTAGEN 173 173 K->A: Abolishes NADH-dependent reductase
activity with acetoacetyl-CoA. Strongly
reduced NADH-dependent reductase activity
with 9,10-phenanthrene quinone. Slightly
decreases NADPH-dependent reductase
activity with acetoacetyl-CoA, but
increases NADPH-dependent reductase
activity with 9,10-phenanthrene quinone.
No effect on the ability to restore
growth of an OAR1-deficient yeast mutant.
{ECO:0000269|PubMed:25203508}.
MUTAGEN 189 189 R->E: No effect on the ability to restore
growth of an OAR1-deficient yeast mutant.
{ECO:0000269|PubMed:25203508}.
CONFLICT 117 117 E -> R (in Ref. 5; BAA11529).
{ECO:0000305}.
CONFLICT 193 193 R -> P (in Ref. 5; BAA11529).
{ECO:0000305}.
CONFLICT 208 208 Q -> K (in Ref. 5; BAA11529).
{ECO:0000305}.
CONFLICT 212 212 Q -> K (in Ref. 5; BAA11529).
{ECO:0000305}.
TURN 8 11 {ECO:0000244|PDB:4CQM}.
STRAND 13 17 {ECO:0000244|PDB:2PD6}.
TURN 18 20 {ECO:0000244|PDB:2PD6}.
HELIX 22 33 {ECO:0000244|PDB:2PD6}.
STRAND 37 44 {ECO:0000244|PDB:2PD6}.
HELIX 45 53 {ECO:0000244|PDB:2PD6}.
STRAND 70 73 {ECO:0000244|PDB:2PD6}.
HELIX 79 93 {ECO:0000244|PDB:2PD6}.
STRAND 98 102 {ECO:0000244|PDB:2PD6}.
HELIX 112 114 {ECO:0000244|PDB:2PD6}.
HELIX 117 127 {ECO:0000244|PDB:2PD6}.
HELIX 129 145 {ECO:0000244|PDB:2PD6}.
STRAND 149 154 {ECO:0000244|PDB:2PD6}.
HELIX 158 161 {ECO:0000244|PDB:2PD6}.
HELIX 167 187 {ECO:0000244|PDB:2PD6}.
HELIX 188 190 {ECO:0000244|PDB:2PD6}.
STRAND 192 199 {ECO:0000244|PDB:2PD6}.
STRAND 201 204 {ECO:0000244|PDB:4CQM}.
TURN 207 209 {ECO:0000244|PDB:2PD6}.
HELIX 212 216 {ECO:0000244|PDB:2PD6}.
HELIX 219 221 {ECO:0000244|PDB:2PD6}.
HELIX 230 241 {ECO:0000244|PDB:2PD6}.
HELIX 243 245 {ECO:0000244|PDB:2PD6}.
STRAND 252 256 {ECO:0000244|PDB:2PD6}.
TURN 257 260 {ECO:0000244|PDB:4CQM}.
SEQUENCE 261 AA; 26974 MW; 8B8B2D7131714D71 CRC64;
MASQLQNRLR SALALVTGAG SGIGRAVSVR LAGEGATVAA CDLDRAAAQE TVRLLGGPGS
KEGPPRGNHA AFQADVSEAR AARCLLEQVQ ACFSRPPSVV VSCAGITQDE FLLHMSEDDW
DKVIAVNLKG TFLVTQAAAQ ALVSNGCRGS IINISSIVGK VGNVGQTNYA ASKAGVIGLT
QTAARELGRH GIRCNSVLPG FIATPMTQKV PQKVVDKITE MIPMGHLGDP EDVADVVAFL
ASEDSGYITG TSVEVTGGLF M


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Catalog number Product name Quantity
EIAAB11117 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,Hsd17b8,Rat,Rattus norvegicus,Testosterone 17-beta-dehydrogenase 8
EIAAB11118 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,FABGL,HKE6,HSD17B8,Ke-6,Pig,Protein Ke6,Sus scrofa,Testosterone 17-bet
EIAAB11116 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,H2-Ke6,Hke6,Hsd17b8,Ke-6,Mouse,Mus musculus,Protein Ke6,Testosterone 1
EIAAB11119 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,FABGL,HKE6,Homo sapiens,HSD17B8,Human,Ke-6,Protein Ke6,Really interest
EIAAB11120 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Canis familiaris,Canis lupus familiaris,Dog,Estradiol 17-beta-dehydrogenase 8,HSD17B8,Testosterone 17-be
EIAAB11097 17-beta-HSD 12,17-beta-hydroxysteroid dehydrogenase 12,3-ketoacyl-CoA reductase,Estradiol 17-beta-dehydrogenase 12,Homo sapiens,HSD17B12,Human,KAR
EIAAB11099 17-beta-HSD 12,17-beta-hydroxysteroid dehydrogenase 12,3-ketoacyl-CoA reductase,Estradiol 17-beta-dehydrogenase 12,Hsd17b12,KAR,Kik1,KIK-I,Mouse,Mus musculus
EIAAB11098 17-beta-HSD 12,17-beta-hydroxysteroid dehydrogenase 12,3-ketoacyl-CoA reductase,Estradiol 17-beta-dehydrogenase 12,Hsd17b12,KAR,Rat,Rattus norvegicus
EIAAB11100 17-beta-HSD 12,17-beta-hydroxysteroid dehydrogenase 12,3-ketoacyl-CoA reductase,Bos taurus,Bovine,Estradiol 17-beta-dehydrogenase 12,HSD17B12,KAR
EIAAB11114 17-beta-HSD 7,17-beta-hydroxysteroid dehydrogenase 7,3-keto-steroid reductase,Estradiol 17-beta-dehydrogenase 7,Hsd17b7,PRAP,PRL receptor-associated protein,Rat,Rattus norvegicus
EIAAB11115 17-beta-HSD 7,17-beta-hydroxysteroid dehydrogenase 7,3-keto-steroid reductase,Estradiol 17-beta-dehydrogenase 7,Homo sapiens,HSD17B7,Human,UNQ2563_PRO6243
EIAAB11113 17-beta-HSD 7,17-beta-hydroxysteroid dehydrogenase 7,3-keto-steroid reductase,Estradiol 17-beta-dehydrogenase 7,Hsd17b7,Mouse,Mus musculus
EIAAB11092 17-beta-HSD 1,17-beta-hydroxysteroid dehydrogenase type 1,20 alpha-hydroxysteroid dehydrogenase,20-alpha-HSD,E17KSR,E2DH,EDH17B1,EDH17B2,EDHB17,Estradiol 17-beta-dehydrogenase 1,Homo sapiens,HSD17B1,H
EIAAB11105 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,20 alpha-hydroxysteroid dehydrogenase,20-alpha-HSD,E2DH,EDH17B2,Estradiol 17-beta-dehydrogenase 2,Homo sapiens,HSD17B2,Human,Microsomal 17-bet
EIAAB11104 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,Edh17b2,Estradiol 17-beta-dehydrogenase 2,Hsd17b2,Mouse,Mus musculus,Testosterone 17-beta-dehydrogenase
EIAAB11103 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,Edh17b2,Estradiol 17-beta-dehydrogenase 2,Hsd17b2,Rat,Rattus norvegicus,Testosterone 17-beta-dehydrogenase
AKR1E2 AKR1C4 Gene aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol dehydrogenase 4)
AKR1C4 AKR1C2 Gene aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 2; bile acid binding protein; 3-alpha hydroxysteroid dehydrogenase, type III)
EIAAB11102 17-beta-HSD 14,17-beta-hydroxysteroid dehydrogenase 14,17-beta-hydroxysteroid dehydrogenase DHRS10,Dehydrogenase_reductase SDR family member 10,DHRS10,Homo sapiens,HSD17B14,Human,Retinal short-chain d
EIAAB11101 17-beta-HSD 14,17-beta-hydroxysteroid dehydrogenase 14,17-beta-hydroxysteroid dehydrogenase DHRS10,Bos taurus,Bovine,Dehydrogenase_reductase SDR family member 10,DHRS10,HSD17B14,Retinal short-chain de
EIAAB11146 11-beta-HSD3,11-beta-hydroxysteroid dehydrogenase type 3,11-DH3,Homo sapiens,HSD11B1L,HSD3,Human,Hydroxysteroid 11-beta-dehydrogenase 1-like protein,SCDR10,Short-chain dehydrogenase_reductase 10
EIAAB05627 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,Cbr4,Mouse,Mus musculus,Quinone reductase CBR4
EIAAB05625 3-oxoacyl-[acyl-carrier-protein] reductase,Bos taurus,Bovine,Carbonyl reductase family member 4,CBR4,Quinone reductase CBR4
EIAAB05628 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,Cbr4,Quinone reductase CBR4,Rat,Rattus norvegicus
EIAAB05626 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,CBR4,Homo sapiens,Human,Quinone reductase CBR4


 

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