| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2010-04-15 15:13:48 |
| Accession Number |
HMDB00077 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Dehydroepiandrosterone |
| Description |
Dehydroepiandrosterone (DHEA) is a natural steroid hormone produced from cholesterol by the adrenal glands. DHEA is also produced in the gonads, adipose tissue and the brain. DHEA is structurally similar to, and is a precursor of, androstenedione, testosterone, estradiol, estrone and estrogen. It is the most abundant hormone in the human body. Most of DHEA is sulfated (dehydroepiandrosterone sulfate- DEHAS) before secretion. DHEAS is the sulfated version of DHEA; - this conversion is reversibly catalyzed by sulfotransferase (SULT2A1) primarily in the adrenals, the liver, and small intestines. In blood, most DHEA is found as DHEAS with levels that are about 300 times higher than free DHEA. Blood measurements of DHEAS/DHEA are useful to detect excess adrenal activity as seen in adrenal cancer or hyperplasia, including certain forms of congenital adrenal hyperplasia. Women with polycystic ovary syndrome tend to have normal or mildly elevated levels of DHEAS. |
| Synonyms |
- (+)-Dehydroisoandrosterone
- (3-beta)-3-Hydroxyandrost-5-en-17-one
- (3beta)-3-hydroxy-Androst-5-en-17-one
- (3beta,16alpha)-3,16-dihydroxy-androst-5-en-17-one
- 17-Chetovis
- 17-Hormoforin
- 3-beta-Hydroxy-5-androsten-17-one
- 3-beta-Hydroxyandrost-5-en-17-one
- 3b-Hydroxy-D5-androsten-17-one
- 3b-Hydroxyandrost-5-en-17-one
- 3beta-Hydroxy-D5-androsten-17-one
- 3beta-Hydroxyandrost-5-en-17-one
- 3beta-hydroxy-5-androsten-17-one
- 3beta-hydroxy-Androst-5-en-17-one
- 5,6-Dehydroisoandrosterone
- 5,6-Didehydroisoandrosterone
- 5-Androsten-3-beta-ol-17-one
- 5-Androsten-3b-ol-17-one
- 5-Androsten-3beta-ol-17-one
- 5-Dehydroepiandrosterone
- 5-dehydro-Epiandrosterone
- Andrestenol
- Androst-5-ene-3b-ol-17-one
- Androst-5-ene-3beta-ol-17-one
- Androsten-3beta-ol-17-one
- Androstenolone
- Astenile
- D5-Androsten-3b-ol-17-one
- D5-Androsten-3beta-ol-17-one
- Deandros
- Dehydro-epi-androsterone
- Dehydroepiandrosterone
- Dehydroisoandrosterone
- Diandron
- Diandrone
- Hydroxyandrostenone
- Prasterona
- Prasterone
- Prasteronum
- Prestara
- Psicosterone
- trans-Dehydroandrosterone
|
| Chemical IUPAC Name |
(3S,8R,9S,10R,13S,14S)-3-hydroxy-10,13-dimethyl-1,2,3,4,7,8,9,11,12,14,15,16-dodecahydrocyclopenta[a]phenanthren-17-one |
| Chemical Formula |
C19H28O2 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Cholesterols and derivatives
|
| Class |
- Steroids and Steroid Derivatives
|
| Sub Class |
|
| Family |
|
| Species |
- ketone
- secondary alcohol
- alkene
|
| Biofunction |
- Component of Androgen and estrogen metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
288.424 |
| Monoisotopic Molecular Weight |
288.208923 |
| Isomeric SMILES |
C[C@]12CCC3C(CC=C4C[C@@H](O)CC[C@]34C)C1CCC2=O |
| Canonical SMILES |
CC12CCC3C(CC=C4CC(O)CCC34C)C1CCC2=O |
| KEGG Compound ID |
C01227  |
| BioCyc ID |
DEHYDRO-EPIANDROSTERONE-SULFATE  |
| BiGG ID |
37131  |
| Wikipedia Link |
Dehydroepiandrosterone  |
| NuGOwiki Link |
HMDB00077  |
| Metagene Link |
HMDB00077  |
| METLIN ID |
5133  |
| PubChem Compound |
5881  |
| PubChem Substance |
8153636  |
| ChEBI ID |
28689  |
| CAS Registry Number |
53-43-0 |
| InChI Identifier |
InChI=1/C19H28O2/c1-18-9-7-13(20)11-12(18)3-4-14-15-5-6-17(21)19(15,2)10-8-16(14)18/h3,13-16,20H,4-11H2,1-2H3/t13-,14?,15?,16?,18-,19-/m0/s1 |
| Synthesis Reference |
Nguyen Xuan Cuong; Nguyen Van Dan. Synthesis of dehydroepiandrosterone (DHA) from 16-dehydropregnenolone acetate (DPA). Tap Chi Duoc Hoc (1983), (4), 12-14. |
| Melting Point (Experimental) |
140-141 oC |
| Experimental Water Solubility |
0.0635 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)]
Source: PhysProp
|
| Predicted Water Solubility |
0.0438 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
0 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
3.23 [HANSCH,C ET AL. (1995)]
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
3 [Predicted by PubChem via XLOGP]; 3.53 [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
|
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Varian) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
|
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Membrane (Predicted from LogP)
- Cytoplasm
- endoplasmic reticulum
|
| Biofluid Location |
- Blood
- Cerebrospinal Fluid
- Saliva
- Urine
|
| Tissue Location |
| Tissue |
References |
| Adipose Tissue |
— |
| Adrenal Cortex |
— |
| Adrenal Gland |
— |
| Brain |
— |
| Epidermis |
— |
| Fibroblasts |
— |
| Gonads |
— |
| Kidney |
— |
| Liver |
— |
| Muscle |
— |
| Neuron |
— |
| Placenta |
— |
| Platelet |
— |
| Prostate |
— |
| Testes |
— |
|
| Concentrations (Normal) |
| Biofluid |
Blood |
| Value |
0.001 (0.00034-0.0017) uM |
| Age |
Children:1-13 yrs old |
| Sex |
Female |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shackleton C, Malunowicz E: Apparent pregnene hydroxylation deficiency (APHD): seeking the parentage of an orphan metabolome. Steroids. 2003 Oct;68(9):707-17. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.0087 (0.0035-0.013) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Female |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shackleton C, Malunowicz E: Apparent pregnene hydroxylation deficiency (APHD): seeking the parentage of an orphan metabolome. Steroids. 2003 Oct;68(9):707-17. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.023 (0.005-0.042) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
|
| Biofluid |
Blood |
| Value |
0.020 +/- 0.011 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Male |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Yamada Y, Sekihara H, Omura M, Yanase T, Takayanagi R, Mune T, Yasuda K, Ishizuka T, Ueshiba H, Miyachi Y, Iwasaki T, Nakajima A, Nawata H: Changes in serum sex hormone profiles after short-term low-dose administration of dehydroepiandrosterone (DHEA) to young and elderly persons. Endocr J. 2007 Feb;54(1):153-62. Epub 2006 Dec 21. [PubMed
]
|
| Biofluid |
CSF |
| Value |
0.00101 (0.00002-0.002) uM |
| Age |
Adult:>18 yrs old |
| Sex |
N/A |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Schwarz S, Pohl P: Steroid hormones and steroid hormone binding globulins in cerebrospinal fluid studied in individuals with intact and with disturbed blood-cerebrospinal fluid barrier. Neuroendocrinology. 1992 Feb;55(2):174-82. [PubMed
]
|
| Biofluid |
Saliva |
| Value |
0.0033 (0.0024-0.0090) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Finlay EM, Morton MS, Gaskell SJ: Identification and quantification of dehydroepiandrosterone sulphate in saliva. Steroids. 1982 Jan;39(1):63-71. [PubMed
]
|
| Biofluid |
Urine |
| Value |
0.13 +/- 0.057 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Poor V, Biro I, Bufa A, Gati A, Fenyvesi I, Juricskay S, Tenyi T, Kilar F: Urinary steroids in young women with eating disorders. J Biochem Biophys Methods. 2004 Oct 29;61(1-2):199-205. [PubMed
]
|
| Biofluid |
Urine |
| Value |
0.0016 +/- 0.00026 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed
]
|
| Biofluid |
Urine |
| Value |
0.10 (0.066-0.17) umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Male |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shamim W, Yousufuddin M, Bakhai A, Coats AJ, Honour JW: Gender differences in the urinary excretion rates of cortisol and androgen metabolites. Ann Clin Biochem. 2000 Nov;37 ( Pt 6):770-4. [PubMed
]
|
| Biofluid |
Urine |
| Value |
0.022 (0.017-0.041) umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Female |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shamim W, Yousufuddin M, Bakhai A, Coats AJ, Honour JW: Gender differences in the urinary excretion rates of cortisol and androgen metabolites. Ann Clin Biochem. 2000 Nov;37 ( Pt 6):770-4. [PubMed
]
|
|
| Concentrations (Abnormal) |
| Biofluid |
Urine |
| Value |
0.00032 +/- 0.000065 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Rheumatoid arthritis |
| Comments |
Rheumatoid arthritis with prednisolone treatment |
| References |
- Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed
]
|
| Biofluid |
Urine |
| Value |
0.00066 +/- 0.00021 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Rheumatoid arthritis |
| Comments |
Rheumatoid arthritis without prednisolone treatment |
| References |
- Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed
]
|
| Biofluid |
Urine |
| Value |
0.00034 +/- 0.000078 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Comments |
Systemic lupus erythematosus (SLE) with prednisolone treatment |
| References |
- Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed
]
|
| Biofluid |
Urine |
| Value |
0.0011 +/- 0.00026 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Comments |
Systemic lupus erythematosus (SLE) without prednisolone treatment |
| References |
- Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed
]
|
|
| Associated Disorders |
| Condition |
References |
| Rheumatoid arthritis |
- Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed
]
|
|
| OMIM ID |
|
| Pathways |
|
| General References |
- Robinzon B, Michael KK, Ripp SL, Winters SJ, Prough RA: Glucocorticoids inhibit interconversion of 7-hydroxy and 7-oxo metabolites of dehydroepiandrosterone: a role for 11beta-hydroxysteroid dehydrogenases? Arch Biochem Biophys. 2003 Apr 15;412(2):251-8. [PubMed
]
- Rao MS, Subbarao V, Yeldandi AV, Reddy JK: Hepatocarcinogenicity of dehydroepiandrosterone in the rat. Cancer Res. 1992 May 15;52(10):2977-9. [PubMed
]
- Saruc M, Yuceyar H, Ayhan S, Turkel N, Tuzcuoglu I, Can M: The association of dehydroepiandrosterone, obesity, waist-hip ratio and insulin resistance with fatty liver in postmenopausal women--a hyperinsulinemic euglycemic insulin clamp study. Hepatogastroenterology. 2003 May-Jun;50(51):771-4. [PubMed
]
- Bamberg E, Aichinger A, Mitteregger G: In vitro metabolism of dehydroepiandrosterone and testosterone by canine hair follicle cells. Vet Dermatol. 2004 Feb;15(1):19-24. [PubMed
]
- Gordon GB, Bush TL, Helzlsouer KJ, Miller SR, Comstock GW: Relationship of serum levels of dehydroepiandrosterone and dehydroepiandrosterone sulfate to the risk of developing postmenopausal breast cancer. Cancer Res. 1990 Jul 1;50(13):3859-62. [PubMed
]
- Schwarz S, Pohl P: Steroid hormones and steroid hormone binding globulins in cerebrospinal fluid studied in individuals with intact and with disturbed blood-cerebrospinal fluid barrier. Neuroendocrinology. 1992 Feb;55(2):174-82. [PubMed
]
- Weill-Engerer S, David JP, Sazdovitch V, Liere P, Schumacher M, Delacourte A, Baulieu EE, Akwa Y: In vitro metabolism of dehydroepiandrosterone (DHEA) to 7alpha-hydroxy-DHEA and Delta5-androstene-3beta,17beta-diol in specific regions of the aging brain from Alzheimer's and non-demented patients. Brain Res. 2003 Apr 18;969(1-2):117-25. [PubMed
]
- Finlay EM, Morton MS, Gaskell SJ: Identification and quantification of dehydroepiandrosterone sulphate in saliva. Steroids. 1982 Jan;39(1):63-71. [PubMed
]
- Uzieblo-Zyczkowska B, Sidlo E, Stelmaszuk T: [Dehydroepiandrosterone (DHEA)--slows down the aging process?] Pol Merkur Lekarski. 2005 Dec;19(114):831-4. [PubMed
]
- Prost O, Nicollier M, Laurent R, Adessi GL: Estrone- and dehydroepiandrosterone-sulfatase activities in human female epidermis. Arch Dermatol Res. 1985;277(3):195-200. [PubMed
]
- Friess E, Schiffelholz T, Steckler T, Steiger A: Dehydroepiandrosterone--a neurosteroid. Eur J Clin Invest. 2000 Dec;30 Suppl 3:46-50. [PubMed
]
- Hakkinen A, Pakarinen A, Hannonen P, Kautiainen H, Nyman K, Kraemer WJ, Hakkinen K: Effects of prolonged combined strength and endurance training on physical fitness, body composition and serum hormones in women with rheumatoid arthritis and in healthy controls. Clin Exp Rheumatol. 2005 Jul-Aug;23(4):505-12. [PubMed
]
- Shackleton C, Malunowicz E: Apparent pregnene hydroxylation deficiency (APHD): seeking the parentage of an orphan metabolome. Steroids. 2003 Oct;68(9):707-17. [PubMed
]
- Kim SB, Hill M, Kwak YT, Hampl R, Jo DH, Morfin R: Neurosteroids: Cerebrospinal fluid levels for Alzheimer's disease and vascular dementia diagnostics. J Clin Endocrinol Metab. 2003 Nov;88(11):5199-206. [PubMed
]
- Chalbot S, Morfin R: Human liver S9 fractions: metabolism of dehydroepiandrosterone, epiandrosterone, and related 7-hydroxylated derivatives. Drug Metab Dispos. 2005 Apr;33(4):563-9. Epub 2005 Jan 13. [PubMed
]
- Miller KK, Cai J, Ripp SL, Pierce WM Jr, Rushmore TH, Prough RA: Stereo- and regioselectivity account for the diversity of dehydroepiandrosterone (DHEA) metabolites produced by liver microsomal cytochromes P450. Drug Metab Dispos. 2004 Mar;32(3):305-13. [PubMed
]
- Martina V, Benso A, Gigliardi VR, Masha A, Origlia C, Granata R, Ghigo E: Short-term dehydroepiandrosterone treatment increases platelet cGMP production in elderly male subjects. Clin Endocrinol (Oxf). 2006 Mar;64(3):260-4. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Sulfotransferase family cytosolic 2B member 1
- Solute carrier organic anion transporter family member 1B3
- Solute carrier organic anion transporter family member 1B1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I
- Steryl-sulfatase precursor
- Cytochrome P450 17A1
- cDNA FLJ75712, highly similar to Homo sapiens hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
- Solute carrier family 22 member 7
- HSD3B2 protein
- cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA (Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform C
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5591 |
| Enzyme 1 Name |
Sulfotransferase family cytosolic 2B member 1 |
| Enzyme 1 Synonyms |
- Sulfotransferase 2B1
- Alcohol sulfotransferase
- Hydroxysteroid sulfotransferase 2
|
| Enzyme 1 Gene Name |
SULT2B1 |
| Enzyme 1 Protein Sequence |
>Sulfotransferase family cytosolic 2B member 1
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRD
DDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPR
LMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFL
KGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSV
VAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQ
MRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETP
HPRPS
|
| Enzyme 1 Number of Residues |
365 |
| Enzyme 1 Molecular Weight |
41308 |
| Enzyme 1 Theoretical pI |
5.05 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Catalyzes the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol |
| Enzyme 1 Pathways |
- Androgen and Estrogen Metabolism (map00150
)
- Sulfate and Sulfite Metabolism (map00920
)
|
| Enzyme 1 Reactions |
- 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
1923291  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O00204  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ST2B1_HUMAN  |
| Enzyme 1 PDB ID |
1Q1Q  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1053 bp
ATGGCGTCTCCCCCACCTTTCCACAGCCAGAAGTTGCCAGGTGAATACTTCCGGTACAAG
GGCGTCCCCTTCCCCGTCGGCCTGTACTCGCTCGAGAGCATCAGCTTGGCGGAGAACACC
CAAGATGTGCGGGACGACGACATCTTTATCATCACCTACCCCAAGTCAGGCACGACCTGG
ATGATCGAGATCATCTGCTTAATCCTGAAGGAAGGGGATCCATCCTGGATCCGCTCCGTG
CCCATCTGGGAGCGGGCACCCTGGTGTGAGACCATTGTGGGTGCTTTCAGCCTCCCGGAC
CAGTACAGCCCCCGCCTCATGAGCTCCCATCTTCCCATCCAGATCTTCACCAAGGCCTTC
TTCAGCTCCAAGGCCAAGGTGATCTACATGGGCCGCAACCCCCGGGACGTTGTGGTCTCC
CTCTATCATTACTCCAAGATCGCCGGGCAGTTAAAGGACCCGGGCACACCCGACCAGTTC
CTGAGGGACTTCCTCAAAGGCGAAGTGCAGTTTGGCTCCTGGTTCGACCACATTAAGGGC
TGGCTTCGGATGAAGGGCAAAGACAACTTCCTATTTATCACCTACGAGGAGCTGCAGCAG
GACTTACAGGGCTCCGTGGAGCGCATCTGTGGGTTCCTGGGCCGTCCGCTGGGCAAGGAG
GCACTGGGCTCCGTCGTGGCACACTCAACCTTCAGCGCCATGAAGGCCAACACCATGTCC
AACTACACGCTGCTGCCTCCCAGCCTGCTGGACCACCGTCGCGGGGCCTTCCTCCGGAAA
GGGGTCTGCGGCGACTGGAAGAACCACTTCACGGTGGCCCAGAGCGAAGCCTTCGATCGT
GCCTACCGCAAGCAGATGCGGGGGATGCCGACCTTCCCCTGGGATGAAGACCCGGAGGAG
GATGGCAGCCCAGATCCTGAGCCCAGCCCTGAGCCTGAGCCCAAGCCCAGCCTTGAGCCC
AACACCAGCCTGGAGCGTGAGCCCAGACCCAACTCCAGCCCCAACCCCAGCCCCGGCCAG
GCCTCTGAGACCCCGCACCCACGACCCTCATAA
|
| Enzyme 1 GenBank Gene ID |
U92314  |
| Enzyme 1 GeneCard ID |
SULT2B1  |
| Enzyme 1 GenAtlas ID |
SULT2B1  |
| Enzyme 1 HGNC ID |
HGNC:11459  |
| Enzyme 1 Chromosome Location |
19 |
| Enzyme 1 Locus |
19q13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Her C, Wood TC, Eichler EE, Mohrenweiser HW, Ramagli LS, Siciliano MJ, Weinshilboum RM: Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene. Genomics. 1998 Nov 1;53(3):284-95. [PubMed
]
- Fuda H, Lee YC, Shimizu C, Javitt NB, Strott CA: Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase. J Biol Chem. 2002 Sep 27;277(39):36161-6. Epub 2002 Jul 26. [PubMed
]
- Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC: Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. J Biol Chem. 2003 Nov 7;278(45):44593-9. Epub 2003 Aug 14. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5684 |
| Enzyme 2 Name |
Solute carrier organic anion transporter family member 1B3 |
| Enzyme 2 Synonyms |
- Solute carrier family 21 member 8
- Organic anion transporter 8
- Organic anion-transporting polypeptide 8
- OATP8
- Liver-specific organic anion transporter 2
- LST-2
|
| Enzyme 2 Gene Name |
SLCO1B3 |
| Enzyme 2 Protein Sequence |
>Solute carrier organic anion transporter family member 1B3
MDQHQHLNKTAESASSEKKKTRRCNGFKMFLAALSFSYIAKALGGIIMKISITQIERRFD
ISSSLAGLIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCLLMGTGSILTSLPHFFMGY
YRYSKETHINPSENSTSSLSTCLINQTLSFNGTSPEIVEKDCVKESGSHMWIYVFMGNML
RGIGETPIVPLGISYIDDFAKEGHSSLYLGSLNAIGMIGPVIGFALGSLFAKMYVDIGYV
DLSTIRITPKDSRWVGAWWLGFLVSGLFSIISSIPFFFLPKNPNKPQKERKISLSLHVLK
TNDDRNQTANLTNQGKNVTKNVTGFFQSLKSILTNPLYVIFLLLTLLQVSSFIGSFTYVF
KYMEQQYGQSASHANFLLGIITIPTVATGMFLGGFIIKKFKLSLVGIAKFSFLTSMISFL
FQLLYFPLICESKSVAGLTLTYDGNNSVASHVDVPLSYCNSECNCDESQWEPVCGNNGIT
YLSPCLAGCKSSSGIKKHTVFYNCSCVEVTGLQNRNYSAHLGECPRDNTCTRKFFIYVAI
QVINSLFSATGGTTFILLTVKIVQPELKALAMGFQSMVIRTLGGILAPIYFGALIDKTCM
KWSTNSCGAQGACRIYNSVFFGRVYLGLSIALRFPALVLYIVFIFAMKKKFQGKDTKASD
NERKVMDEANLEFLNNGEHFVPSAGTDSKTCNLDMQDNAAAN
|
| Enzyme 2 Number of Residues |
702 |
| Enzyme 2 Molecular Weight |
77404 |
| Enzyme 2 Theoretical pI |
8.95 |
| Enzyme 2 GO Classification |
| Function |
|
| Process |
- cellular physiological process
- physiological process
- transport
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Mediates the Na(+)-independent transport of organic anions such as 17-beta-glucuronosyl estradiol, taurocholate, triiodothyronine (T3), leukotriene C4, dehydroepiandrosterone sulfate (DHEAS), methotrexate and sulfobromophthalein (BSP) |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
Not Available |
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
- 30-50
65-85
97-117
171-191
207-227
259-279
336-356
377-397
410-430
538-558
575-595
626-646
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
9188300  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9NPD5  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
SO1B3_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>84 bp
ATGGACCAACATCAACATTTGAATAAAACAGCAGAGTCAGCATCTTCAGAGAAAAAGAAA
ACAAGACGCTGCAATGGATTCAAG
|
| Enzyme 2 GenBank Gene ID |
AJ400763  |
| Enzyme 2 GeneCard ID |
SLCO1B3  |
| Enzyme 2 GenAtlas ID |
SLCO1B3  |
| Enzyme 2 HGNC ID |
HGNC:10961  |
| Enzyme 2 Chromosome Location |
12 |
| Enzyme 2 Locus |
12p12 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Konig J, Cui Y, Nies AT, Keppler D: Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide. J Biol Chem. 2000 Jul 28;275(30):23161-8. [PubMed
]
- Abe T, Unno M, Onogawa T, Tokui T, Kondo TN, Nakagomi R, Adachi H, Fujiwara K, Okabe M, Suzuki T, Nunoki K, Sato E, Kakyo M, Nishio T, Sugita J, Asano N, Tanemoto M, Seki M, Date F, Ono K, Kondo Y, Shiiba K, Suzuki M, Ohtani H, Shimosegawa T, Iinuma K, Nagura H, Ito S, Matsuno S: LST-2, a human liver-specific organic anion transporter, determines methotrexate sensitivity in gastrointestinal cancers. Gastroenterology. 2001 Jun;120(7):1689-99. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5692 |
| Enzyme 3 Name |
Solute carrier organic anion transporter family member 1B1 |
| Enzyme 3 Synonyms |
- Solute carrier family 21 member 6
- Sodium-independent organic anion- transporting polypeptide 2
- OATP 2
- Liver-specific organic anion transporter 1
- LST-1
- OATP-C
|
| Enzyme 3 Gene Name |
SLCO1B1 |
| Enzyme 3 Protein Sequence |
>Solute carrier organic anion transporter family member 1B1
MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFE
ISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGY
YRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNML
RGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYV
DLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLE
TNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVF
KYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLS
FYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGIT
YISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAI
QVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCI
KWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASE
NGSVMDEANLESLNKNKHFVPSAGADSETHC
|
| Enzyme 3 Number of Residues |
691 |
| Enzyme 3 Molecular Weight |
76450 |
| Enzyme 3 Theoretical pI |
8.68 |
| Enzyme 3 GO Classification |
| Function |
|
| Process |
- cellular physiological process
- physiological process
- transport
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 3 General Function |
Carbohydrate transport and metabolism |
| Enzyme 3 Specific Function |
Mediates the Na(+)-independent transport of organic anions such as pravastatin, taurocholate, methotrexate, dehydroepiandrosterone sulfate, 17-beta-glucuronosyl estradiol, estrone sulfate, prostaglandin E2, thromboxane B2, leukotriene C3, leukotriene E4, thyroxine and triiodothyronine. May play an important role in the clearance of bile acids and organic anions from the liver |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
- 97-117
207-227
259-279
336-356
376-396
410-430
575-595
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
5051630  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9Y6L6  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
SO1B1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2076 bp
ATGGACCAAAATCAACATTTGAATAAAACAGCAGAGGCACAACCTTCAGAGAATAAGAAA
ACAAGATACTGCAATGGATTGAAGATGTTCTTGGCAGCTCTGTCACTCAGCTTTATTGCT
AAGACACTAGGTGCAATTATTATGAAAAGTTCCATCATTCATATAGAACGGAGATTTGAG
ATATCCTCTTCTCTTGTTGGTTTTATTGACGGAAGCTTTGAAATTGGAAATTTGCTTGTG
ATTGTATTTGTGAGTTACTTTGGATCCAAACTACATAGACCAAAGTTAATTGGAATCGGT
TGTTTCATTATGGGAATTGGAGGTGTTTTGACTGCTTTGCCACATTTCTTCATGGGATAT
TACAGGTATTCTAAAGAAACTAATATCAATTCATCAGAAAATTCAACATCGACCTTATCC
ACTTGTTTAATTAATCAAATTTTATCACTCAATAAAGCATCACCTGAGATAGTGGGAAAA
GGTTGTTTAAAGGAATCTGGGTCATACATGTGGATATATGTGTTCATGGGTAATATGCTT
CGTGGAATAGGGGAGACTCCCATAGTACCACTGGGGCTTTCTTACATTGATGATTTCGCT
AAAGAAGGACATTCTTCTTTGTATTTAGGTATATTGAATGCAATAGCAATGATTGGTCCA
ATCATTGGCTTTACCCTGGGATCTCTGTTTTCTAAAATGTACGTGGATATTGGATATGTT
AATCTAAGCACTATCAGGATAACTCCTACTGATTCTCGATGGGTTGGAGCTTGGTGGCTT
AATTTCCTTGTGTCTGGACTATTCTCCATTATTTCTTCCATACCATTCTTTTTCTTGCCC
CAAACTCCAAATAAACCACAAAAAGAAAGAAAAGCTTCACTGTCTTTGCATGTGCTGGAA
ACAAATGATGAAAAGGATCAAACAGCTAATTTGACCAATCAAGGAAAAAATATTACCAAA
AATGTGACTGGTTTTTTCCAGTCTTTTAAAAGCATCCTTACTAATCCCCTGTATGTTATG
TTTGTGCTTTTGACGTTGTTACAAGTAAGCAGCTATATTGGTGCTTTTACTTATGTCTTC
AAATACGTAGAGCAACAGTATGGTCAGCCTTCATCTAAGGCTAACATCTTATTGGGAGTC
ATAACCATACCTATTTTTGCAAGTGGAATGTTTTTAGGAGGATATATCATTAAAAAATTC
AAACTGAACACCGTTGGAATTGCCAAATTCTCATGTTTTACTGCTGTGATGTCATTGTCC
TTTTACCTATTATATTTTTTCATACTCTGTGAAAACAAATCAGTTGCCGGACTAACCATG
ACCTATGATGGAAATAATCCAGTGACATCTCATAGAGATGTACCACTTTCTTATTGCAAC
TCAGACTGCAATTGTGATGAAAGTCAATGGGAACCAGTCTGTGGAAACAATGGAATAACT
TACATCTCACCCTGTCTAGCAGGTTGCAAATCTTCAAGTGGCAATAAAAAGCCTATAGTG
TTTTACAACTGCAGTTGTTTGGAAGTAACTGGTCTCCAGAACAGAAATTACTCAGCCCAT
TTGGGTGAATGCCCAAGAGATGATGCTTGTACAAGGAAATTTTACTTTTTTGTTGCAATA
CAAGTCTTGAATTTATTTTTCTCTGCACTTGGAGGCACCTCACATGTCATGCTGATTGTT
AAAATTGTTCAACCTGAATTGAAATCACTTGCACTGGGTTTCCACTCAATGGTTATACGA
GCACTAGGAGGAATTCTAGCTCCTATATATTTTGGGGCTCTGATTGATACAACGTGTATA
AAGTGGTCCACCAACAACTGTGGCACACGTGGGTCATGTAGGACATATAATTCCACATCA
TTTTCAAGGGTCTACTTGGGCTTGTCTTCAATGTTAAGAGTCTCATCACTTGTTTTATAT
ATTATATTAATTTATGCCATGAAGAAAAAATATCAAGAGAAAGATATCAATGCATCAGAA
AATGGAAGTGTCATGGATGAAGCAAACTTAGAATCCTTAAATAAAAATAAACATTTTGTC
CCTTCTGCTGGGGCAGATAGTGAAACACATTGTTAA
|
| Enzyme 3 GenBank Gene ID |
AF060500  |
| Enzyme 3 GeneCard ID |
SLCO1B1  |
| Enzyme 3 GenAtlas ID |
SLCO1B1  |
| Enzyme 3 HGNC ID |
HGNC:10959  |
| Enzyme 3 Chromosome Location |
12 |
| Enzyme 3 Locus |
12p |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Abe T, Kakyo M, Tokui T, Nakagomi R, Nishio T, Nakai D, Nomura H, Unno M, Suzuki M, Naitoh T, Matsuno S, Yawo H: Identification of a novel gene family encoding human liver-specific organic anion transporter LST-1. J Biol Chem. 1999 Jun 11;274(24):17159-63. [PubMed
]
- Hsiang B, Zhu Y, Wang Z, Wu Y, Sasseville V, Yang WP, Kirchgessner TG: A novel human hepatic organic anion transporting polypeptide (OATP2). Identification of a liver-specific human organic anion transporting polypeptide and identification of rat and human hydroxymethylglutaryl-CoA reductase inhibitor transporters. J Biol Chem. 1999 Dec 24;274(52):37161-8. [PubMed
]
- Konig J, Cui Y, Nies AT, Keppler D: A novel human organic anion transporting polypeptide localized to the basolateral hepatocyte membrane. Am J Physiol Gastrointest Liver Physiol. 2000 Jan;278(1):G156-64. [PubMed
]
- Konig J, Cui Y, Nies AT, Keppler D: Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide. J Biol Chem. 2000 Jul 28;275(30):23161-8. [PubMed
]
- Tirona RG, Leake BF, Merino G, Kim RB: Polymorphisms in OATP-C: identification of multiple allelic variants associated with altered transport activity among European- and African-Americans. J Biol Chem. 2001 Sep 21;276(38):35669-75. Epub 2001 Jul 26. [PubMed
]
- Michalski C, Cui Y, Nies AT, Nuessler AK, Neuhaus P, Zanger UM, Klein K, Eichelbaum M, Keppler D, Konig J: A naturally occurring mutation in the SLC21A6 gene causing impaired membrane localization of the hepatocyte uptake transporter. J Biol Chem. 2002 Nov 8;277(45):43058-63. Epub 2002 Aug 23. [PubMed
]
- Nozawa T, Nakajima M, Tamai I, Noda K, Nezu J, Sai Y, Tsuji A, Yokoi T: Genetic polymorphisms of human organic anion transporters OATP-C (SLC21A6) and OATP-B (SLC21A9): allele frequencies in the Japanese population and functional analysis. J Pharmacol Exp Ther. 2002 Aug;302(2):804-13. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5738 |
| Enzyme 4 Name |
3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I |
| Enzyme 4 Synonyms |
- 3- beta-HSD I
- Trophoblast antigen FDO161G[Includes: 3-beta-hydroxy- Delta(5-steroid dehydrogenase
- 3-beta-hydroxy-5-ene steroid dehydrogenase
- Progesterone reductase
- Steroid Delta- isomerase
- Delta-5-3-ketosteroid isomerase]
|
| Enzyme 4 Gene Name |
HSD3B1 |
| Enzyme 4 Protein Sequence |
>4-isomerase type I
MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLE
GDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVF
IYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTL
YTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRAL
QDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEI
VSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSL
VDRHKETLKSKTQ
|
| Enzyme 4 Number of Residues |
373 |
| Enzyme 4 Molecular Weight |
42252 |
| Enzyme 4 Theoretical pI |
8.98 |
| Enzyme 4 GO Classification |
| Function |
- 3-beta-hydroxy-delta5-steroid dehydrogenase activity
- catalytic activity
- intramolecular oxidoreductase activity
- intramolecular oxidoreductase activity, transposing C=C bonds
- isomerase activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
- steroid dehydrogenase activity
- steroid delta-isomerase activity
|
| Process |
- cellular lipid metabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
- steroid biosynthesis
- steroid metabolism
|
| Component |
| — |
|
| Enzyme 4 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 4 Specific Function |
3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids |
| Enzyme 4 Pathways |
- Androgen and Estrogen Metabolism (map00150
)
- C21 Steroid Hormone Metabolism (map00140
)
|
| Enzyme 4 Reactions |
- A 3-oxo-delta5-steroid = a 3-oxo-delta4-steroid
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
306889  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P14060  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
3BHS1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1122 bp
ATGACGGGCTGGAGCTGCCTTGTGACAGGAGCAGGAGGGTTTCTGGGACAGAGGATCATC
CGCCTCTTGGTGAAGGAGAAGGAGCTGAAGGAGATCAGGGTCTTGGACAAGGCCTTCGGA
CCAGAATTGAGAGAGGAATTTTCTAAACTCCAGAACAAGACCAAGCTGACAGTGCTGGAA
GGAGACATTCTGGATGAGCCATTCCTGAAGAGAGCCTGCCAGGACGTCTCGGTCATCATC
CACACCGCCTGTATCATTGATGTCTTCGGTGTCACTCACAGAGAGTCTATCATGAATGTC
AATGTGAAAGGTACCCAGCTCCTGTTAGAGGCCTGTGTCCAAGCTAGTGTGCCAGTCTTC
ATCTACACCAGTAGCATAGAGGTAGCCGGGCCCAACTCCTACAAGGAAATCATCCAGAAT
GGCCATGAAGAAGAGCCTCTGGAAAACACATGGCCCGCTCCATACCCACACAGCAAAAAG
CTTGCTGAGAAGGCTGTACTGGCGGCTAACGGGTGGAATCTGAAAAACGGCGGCACCCTG
TACACTTGTGCCTTACGACCCATGTATATCTATGGGGAAGGAAGCCGATTCCTTTCTGCT
AGTATAAACGAGGCCCTGAACAACAATGGGATCCTGTCAAGTGTTGGAAAGTTCTCCACT
GTTAACCCAGTCTATGTTGGCAATGTGGCCTGGGCCCACATTCTGGCCTTGAGGGCCCTG
CAGGACCCCAAGAAGGCCCCAAGCATCCGAGGACAGTTCTACTATATCTCAGATGACACG
CCTCACCAAAGCTATGATAACCTTAATTACACCCTGAGCAAAGAGTTCGGCCTCCGCCTT
GATTCCAGATGGAGCTTTCCTTTATCCCTGATGTATTGGATTGGCTTCCTGCTGGAAATA
GTGAGCTTCCTACTCAGGCCAATTTACACCTATCGACCGCCCTTCAACCGCCACATAGTC
ACATTGTCAAATAGCGTATTCACCTTCTCTTATAAGAAGGCTCAGCGAGATCTGGCGTAT
AAGCCACTCTACAGCTGGGAGGAAGCCAAGCAGAAAACGGTGGAGTGGGTTGGTTCCCTT
GTGGACCGGCACAAGGAGACCCTGAAGTCCAAGACTCAGTGA
|
| Enzyme 4 GenBank Gene ID |
M27137  |
| Enzyme 4 GeneCard ID |
HSD3B1  |
| Enzyme 4 GenAtlas ID |
HSD3B1  |
| Enzyme 4 HGNC ID |
HGNC:5217  |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Luu The V, Lachance Y, Labrie C, Leblanc G, Thomas JL, Strickler RC, Labrie F: Full length cDNA structure and deduced amino acid sequence of human 3 beta-hydroxy-5-ene steroid dehydrogenase. Mol Endocrinol. 1989 Aug;3(8):1310-2. [PubMed
]
- Lorence MC, Murry BA, Trant JM, Mason JI: Human 3 beta-hydroxysteroid dehydrogenase/delta 5----4isomerase from placenta: expression in nonsteroidogenic cells of a protein that catalyzes the dehydrogenation/isomerization of C21 and C19 steroids. Endocrinology. 1990 May;126(5):2493-8. [PubMed
]
- Lorence MC, Corbin CJ, Kamimura N, Mahendroo MS, Mason JI: Structural analysis of the gene encoding human 3 beta-hydroxysteroid dehydrogenase/delta 5----4-isomerase. Mol Endocrinol. 1990 Dec;4(12):1850-5. [PubMed
]
- Lachance Y, Luu-The V, Labrie C, Simard J, Dumont M, de Launoit Y, Guerin S, Leblanc G, Labrie F: Characterization of human 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase gene and its expression in mammalian cells. J Biol Chem. 1990 Nov 25;265(33):20469-75. [PubMed
]
- Nickson DA, McBride MW, Zeinali S, Hawes CS, Petropoulos A, Mueller UW, Sutcliffe RG: Molecular cloning and expression of human trophoblast antigen FDO161G and its identification as 3 beta-hydroxy-5-ene steroid dehydrogenase. J Reprod Fertil. 1991 Sep;93(1):149-56. [PubMed
]
- Dumont M, Luu-The V, Dupont E, Pelletier G, Labrie F: Characterization, expression, and immunohistochemical localization of 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase in human skin. J Invest Dermatol. 1992 Oct;99(4):415-21. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5740 |
| Enzyme 5 Name |
Steryl-sulfatase precursor |
| Enzyme 5 Synonyms |
- Steroid sulfatase
- Steryl- sulfate sulfohydrolase
- Arylsulfatase C
- ASC
|
| Enzyme 5 Gene Name |
STS |
| Enzyme 5 Protein Sequence |
>Steryl-sulfatase precursor
MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLAS
GGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAK
LLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTT
GFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPL
NCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFA
GKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGS
NGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRI
IDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNG
CFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQT
LPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR
|
| Enzyme 5 Number of Residues |
583 |
| Enzyme 5 Molecular Weight |
65493 |
| Enzyme 5 Theoretical pI |
7.71 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- sulfuric ester hydrolase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Inorganic ion transport and metabolism |
| Enzyme 5 Specific Function |
Conversion of sulfated steroid precursors to estrogens during pregnancy |
| Enzyme 5 Pathways |
- Androgen and Estrogen Metabolism (map00150
)
|
| Enzyme 5 Reactions |
- 3beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + sulfate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
338565  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P08842  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
STS_HUMAN  |
| Enzyme 5 PDB ID |
1P49  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1752 bp
ATGCCTTTAAGGAAGATGAAGATCCCTTTCCTCCTACTGTTCTTTCTGTGGGAAGCCGAG
AGCCACGCAGCATCAAGGCCGAACATCATCCTGGTGATGGCTGACGACCTCGGCATTGGA
GATCCTGGGTGCTATGGGAACAAAACTATCAGGACTCCCAATATCGACCGGTTGGCCAGT
GGGGGAGTGAAACTCACTCAGCACCTGGCAGCATCACCGCTGTGCACACCAAGCAGGGCA
GCCTTCATGACTGGCCGGTACCCTGTCCGATCAGGAATGGCATCTTGGTCCCGCACTGGA
GTTTTCCTCTTCACAGCCTCTTCGGGAGGACTTCCCACCGATGAGATTACCTTTGCTAAG
CTTCTGAAGGATCAAGGTTATTCAACAGCACTGATAGGGAAATGGCACCTTGGGATGAGC
TGTCACAGCAAGACTGACTTCTGTCACCACCCTTTACATCACGGCTTCAATTATTTCTAT
GGGATCTCTTTGACCAATCTGAGAGACTGCAAGCCCGGAGAGGGCAGTGTCTTCACCACG
GGCTTCAAGAGGCTGGTCTTCCTCCCCCTGCAGATCGTCGGGGTCACCCTCCTTACCCTT
GCTGCACTCAATTGTCTGGGGCTACTCCACGTGCCTCTAGGCGTTTTTTTCAGCCTTCTC
TTCCTAGCAGCCCTAATCCTGACCCTTTTCTTGGGCTTCCTTCATTACTTCCGGCCCCTG
AACTGCTTCATGATGAGGAACTACGAGATCATTCAGCAGCCCATGTCCTATGACAATCTC
ACCCAGAGGCTAACGGTGGAGGCGGCCCAGTTCATACAGCGGAACACTGAGACTCCGTTC
CTGCTTGTCTTGTCCTACCTCCACGTGCACACAGCCCTGTTCTCCAGCAAAGACTTTGCT
GGCAAAAGTCAACACGGAGTCTACGGGGATGCTGTTGAGGAAATGGACTGGAGTGTGGGG
CAGATCTTGAACCTTCTGGATGAGCTGAGATTGGCTAATGATACCCTCATCTACTTCACA
TCGGACCAGGGAGCACATGTAGAGGAGGTGTCTTCCAAAGGAGAAATTCATGGCGGAAGT
AATGGGATCTATAAAGGAGGAAAAGCAAACAACTGGGAAGGAGGTATCCGGGTTCCAGGC
ATCCTTCGTTGGCCCAGGGTGATACAGGCTGGCCAGAAGATTGATGAGCCCACTAGCAAC
ATGGACATATTTCCTACAGTAGCCAAGCTGGCTGGAGCTCCCTTGCCTGAGGACAGGATC
ATTGATGGACGTGATCTGATGCCCCTGCTTGAAGGAAAAAGCCAACGCTCCGATCATGAG
TTTCTCTTCCATTACTGCAACGCCTACTTAAATGCTGTGCGCTGGCACCCTCAGAACAGC
ACATCCATCTGGAAGGCCTTTTTCTTCACCCCCAACTTCAACCCCGTGGGTTCCAACGGA
TGCTTTGCCACACACGTGTGCTTCTGTTTCGGGAGTTATGTCACCCATCACGACCCACCT
TTACTCTTTGATATTTCCAAAGATCCCAGAGAGAGAAACCCACTAACTCCAGCATCCGAG
CCCCGGTTTTATGAAATCCTCAAAGTCATGCAGGAAGCTGCGGACAGACACACCCAGACC
CTGCCAGAGGTGCCCGATCAGTTTTCATGGAACAACTTTCTTTGGAAGCCCTGGCTTCAG
CTGTGCTGTCCTTCCACCGGCCTGTCTTGCCAGTGTGATAGAGAAAAACAGGATAAGAGA
CTGAGCCGCTAG
|
| Enzyme 5 GenBank Gene ID |
J04964  |
| Enzyme 5 GeneCard ID |
STS  |
| Enzyme 5 GenAtlas ID |
STS  |
| Enzyme 5 HGNC ID |
HGNC:11425  |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Stein C, Hille A, Seidel J, Rijnbout S, Waheed A, Schmidt B, Geuze H, von Figura K: Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells. J Biol Chem. 1989 Aug 15;264(23):13865-72. [PubMed
]
- Yen PH, Allen E, Marsh B, Mohandas T, Wang N, Taggart RT, Shapiro LJ: Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange. Cell. 1987 May 22;49(4):443-54. [PubMed
]
- Yen PH, Marsh B, Allen E, Tsai SP, Ellison J, Connolly L, Neiswanger K, Shapiro LJ: The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: evidence for an inversion of the Y chromosome during primate evolution. Cell. 1988 Dec 23;55(6):1123-35. [PubMed
]
- Kawano J, Kotani T, Ohtaki S, Minamino N, Matsuo H, Oinuma T, Aikawa E: Characterization of rat and human steroid sulfatases. Biochim Biophys Acta. 1989 Aug 31;997(3):199-205. [PubMed
]
- Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D: Structure of human estrone sulfatase suggests functional roles of membrane association. J Biol Chem. 2003 Jun 20;278(25):22989-97. Epub 2003 Mar 25. [PubMed
]
- Basler E, Grompe M, Parenti G, Yates J, Ballabio A: Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis. Am J Hum Genet. 1992 Mar;50(3):483-91. [PubMed
]
- Alperin ES, Shapiro LJ: Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein. J Biol Chem. 1997 Aug 15;272(33):20756-63. [PubMed
]
- Sugawara T, Shimizu H, Hoshi N, Fujimoto Y, Nakajima A, Fujimoto S: PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene. Hum Mutat. 2000 Mar;15(3):296. [PubMed
]
- Oyama N, Satoh M, Iwatsuki K, Kaneko F: Novel point mutations in the steroid sulfatase gene in patients with X-linked ichthyosis: transfection analysis using the mutated genes. J Invest Dermatol. 2000 Jun;114(6):1195-9. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6332 |
| Enzyme 6 Name |
Cytochrome P450 17A1 |
| Enzyme 6 Synonyms |
- CYPXVII
- P450-C17
- P450c17
- Steroid 17-alpha-monooxygenase
- Steroid 17-alpha-hydroxylase/17,20 lyase
|
| Enzyme 6 Gene Name |
CYP17A1 |
| Enzyme 6 Protein Sequence |
>Cytochrome P450 17A1
MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKY
GPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAH
WQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRN
DLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIF
GAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREV
LRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNP
AGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP
KVVFLIDSFKVKIKVRQAWREAQAEGST
|
| Enzyme 6 Number of Residues |
508 |
| Enzyme 6 Molecular Weight |
57371 |
| Enzyme 6 Theoretical pI |
8.87 |
| Enzyme 6 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 6 Specific Function |
Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty |
| Enzyme 6 Pathways |
- C21 Steroid Hormone Metabolism (map00140
)
|
| Enzyme 6 Reactions |
- a steroid + AH2 + O2 = a 17alpha-hydroxysteroid + A + H2O
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
181342  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P05093  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
CP17A_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1527 bp
ATGTGGGAGCTCGTGGCTCTCTTGCTGCTTACCCTAGCTTATTTGTTTTGGCCCAAGAGA
AGGTGCCCTGGTGCCAAGTACCCCAAGAGCCTCCTGTCCCTGCCCCTGGTGGGCAGCCTG
CCATTCCTCCCCAGACATGGCCATATGCATAACAACTTCTTCAAGCTGCAGAAAAAATAT
GGCCCCATCTATTCTGTTCGTATGGGCACCAAGACTACAGTGATTGTCGGCCACCACCAG
CTGGCCAAGGAGGTGCTTATTAAGAAGGGCAAGGACTTCTCTGGGCGGCCTCAAATGGCA
ACTCTAGACATCGCGTCCAACAACCGTAAGGGTATCGCCTTCGCTGACTCTGGCGCACAC
TGGCAGCTGCATCGAAGGCTGGCGATGGCCACCTTTGCCCTGTTCAAGGATGGCGATCAG
AAGCTGGAGAAGATCATTTGTCAGGAAATCAGTACATTGTGTGATATGCTGGCCACCCAC
AACGGACAGTCCATAGACATCTCCTTTCCTGTCTTCGTGGCGGTAACCAATGTCATCTCC
TTGATCTGCTTCAATACCTCCTACAAGAATGGGGACCCTGAGTTGAATGTCATACAGAAT
TACAATGAAGGCATCATAGACAACCTGAGCAAAGACAGCCTGGTGGACCTAGTCCCCTGG
TTGAAGATTTTCCCCAACAAAACCCTGGAAAAATTAAAGAGCCATGTTAAAATACGAAAT
GATCTGCTGAATAAAATACTTGAAAATTACAAGGAGAAATTCCGGAGTGACTCTATCACC
AACATGCTGGACACACTGATGCAAGCCAAGATGAACTCAGATAATGGCAATGCTGGCCCA
GATCAAGATTCAGAGCTGCTTTCAGATAACCACATTCTCACCACCATAGGGGACATCTTT
GGGGCTGGCGTGGAGACCACCACCTCTGTGGTTAAATGGACCCTGGCCTTCCTGCTGCAC
AATCCTCAGGTGAAGAAGAAGCTCTACGAGGAGATTGACCAGAATGTGGGTTTCAGCCGC
ACACCAACTATCAGTGACCGTAACCGTCTCCTCCTGCTGGAGGCCACCATCCGAGAGGTG
CTTCGCCTCAGGCCCGTGGCCCCTATGCTCATCCCCCACAAGGCCAACGTTGACTCCAGC
ATCGGTGAGTTTGCTGTGGACAAGGGCACAGAAGTTATCATCAATCTGTGGGCGCTGCAT
CACAATGAGAAGGAGTGGCACCAGCCGGATCAGTTCATGCCTGAGCGTTTCTTGAATCCA
GCGGGGACCCAGCTCATCTCACCGTCAGTAAGCTATTTGCCCTTCGGAGCAGGACCTCGC
TCCTGTATAGGTGAGATCCTGGCCCGCCAGGAGCTCTTCCTCATCATGGCCTGGCTGCTG
CAGAGGTTCGACCTGGAGGTGCCAGATGATGGGCAGCTGCCCTCCCTGGAAGGCATCCCC
AAGGTGGTCTTTCTGATCGACTCTTTCAAAGTGAAGATCAAGGTGCGCCAGGCCTGGAGG
GAAGCCCAGGCTGAGGGTAGCACCTAA
|
| Enzyme 6 GenBank Gene ID |
M14564  |
| Enzyme 6 GeneCard ID |
CYP17A1  |
| Enzyme 6 GenAtlas ID |
CYP17A1  |
| Enzyme 6 HGNC ID |
HGNC:2593  |
| Enzyme 6 Chromosome Location |
10 |
| Enzyme 6 Locus |
10q24.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Chung BC, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, Shively JE, Miller WL: Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc Natl Acad Sci U S A. 1987 Jan;84(2):407-11. [PubMed
]
- Picado-Leonard J, Miller WL: Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21. DNA. 1987 Oct;6(5):439-48. [PubMed
]
- Bradshaw KD, Waterman MR, Couch RT, Simpson ER, Zuber MX: Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency. Mol Endocrinol. 1987 May;1(5):348-54. [PubMed
]
- Brentano ST, Picado-Leonard J, Mellon SH, Moore CC, Miller WL: Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells. Mol Endocrinol. 1990 Dec;4(12):1972-9. [PubMed
]
- Kagimoto M, Winter JS, Kagimoto K, Simpson ER, Waterman MR: Structural characterization of normal and mutant human steroid 17 alpha-hydroxylase genes: molecular basis of one example of combined 17 alpha-hydroxylase/17,20 lyase deficiency. Mol Endocrinol. 1988 Jun;2(6):564-70. [PubMed
]
- Auchus RJ, Miller WL: Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol Endocrinol. 1999 Jul;13(7):1169-82. [PubMed
]
- Yanase T, Kagimoto M, Suzuki S, Hashiba K, Simpson ER, Waterman MR: Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1989 Oct 25;264(30):18076-82. [PubMed
]
- Lin D, Harikrishna JA, Moore CC, Jones KL, Miller WL: Missense mutation serine106----proline causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1991 Aug 25;266(24):15992-8. [PubMed
]
- Yanase T, Waterman MR, Zachmann M, Winter JS, Simpson ER, Kagimoto M: Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)----Cys, Gln(461)----Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency. Biochim Biophys Acta. 1992 Aug 25;1139(4):275-9. [PubMed
]
- Ahlgren R, Yanase T, Simpson ER, Winter JS, Waterman MR: Compound heterozygous mutations (Arg 239----stop, Pro 342----Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Clin Endocrinol Metab. 1992 Mar;74(3):667-72. [PubMed
]
- Imai T, Globerman H, Gertner JM, Kagawa N, Waterman MR: Expression and purification of functional human 17 alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1993 Sep 15;268(26):19681-9. [PubMed
]
- Monno S, Ogawa H, Date T, Fujioka M, Miller WL, Kobayashi M: Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1993 Dec 5;268(34):25811-7. [PubMed
]
- Fardella CE, Zhang LH, Mahachoklertwattana P, Lin D, Miller WL: Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Aug;77(2):489-93. [PubMed
]
- Fardella CE, Hum DW, Homoki J, Miller WL: Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1994 Jul;79(1):160-4. [PubMed
]
- Laflamme N, Leblanc JF, Mailloux J, Faure N, Labrie F, Simard J: Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients. J Clin Endocrinol Metab. 1996 Jan;81(1):264-8. [PubMed
]
- Biason-Lauber A, Kempken B, Werder E, Forest MG, Einaudi S, Ranke MB, Matsuo N, Brunelli V, Schonle EJ, Zachmann M: 17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation. J Clin Endocrinol Metab. 2000 Mar;85(3):1226-31. [PubMed
]
- Gupta MK, Geller DH, Auchus RJ: Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency. J Clin Endocrinol Metab. 2001 Sep;86(9):4416-23. [PubMed
]
- Di Cerbo A, Biason-Lauber A, Savino M, Piemontese MR, Di Giorgio A, Perona M, Savoia A: Combined 17alpha-Hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene. J Clin Endocrinol Metab. 2002 Feb;87(2):898-905. [PubMed
]
- Van Den Akker EL, Koper JW, Boehmer AL, Themmen AP, Verhoef-Post M, Timmerman MA, Otten BJ, Drop SL, De Jong FH: Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency. J Clin Endocrinol Metab. 2002 Dec;87(12):5714-21. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
12986 |
| Enzyme 7 Name |
cDNA FLJ75712, highly similar to Homo sapiens hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1 |
| Enzyme 7 Synonyms |
- HSD3B1, mRNA
|
| Enzyme 7 Gene Name |
Not Available |
| Enzyme 7 Protein Sequence |
>cDNA FLJ75712, highly similar to Homo sapiens hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLE
GDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVF
IYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTL
YTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRAL
QDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEI
VSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSL
VDRHKETLKSKTQ
|
| Enzyme 7 Number of Residues |
373 |
| Enzyme 7 Molecular Weight |
42252 |
| Enzyme 7 Theoretical pI |
8.98 |
| Enzyme 7 GO Classification |
Not Available |
| Enzyme 7 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 7 Specific Function |
Not Available |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
Not Available |
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
158256544  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
A8K691  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
A8K691_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
Not Available |
| Enzyme 7 GenBank Gene ID |
AK291556  |
| Enzyme 7 GeneCard ID |
A8K691  |
| Enzyme 7 GenAtlas ID |
Not Available |
| Enzyme 7 HGNC ID |
Not Available |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
Not Available |
| Enzyme 7 General References |
Not Available |
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
14810 |
| Enzyme 8 Name |
Solute carrier family 22 member 7 |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
SLC22A7 |
| Enzyme 8 Protein Sequence |
>Solute carrier family 22 member 7
MGFEELLEQVGGFGPFQLRNVALLALPRVLLPLHFLLPIFLAAVPAHRCALPGAPANFSH
QDVWLEAHLPREPDGTLSSCLRFAYPQALPNTTLGEERQSRGELEDEPATVPCSQGWEYD
HSEFSSTIATESQWDLVCEQKGLNRAASTFFFAGVLVGAVAFGYLSDRFGRRRLLLVAYV
STLVLGLASAASVSYVMFAITRTLTGSALAGFTIIVMPLELEWLDVEHRTVAGVLSSTFW
TGGVMLLALVGYLIRDWRWLLLAVTLPCAPGILSLWWVPESARWLLTQGHVKEAHRYLLH
CARLNGRPVCEDSFSQEAVSKVAAGERVVRRPSYLDLFRTPRLRHISLCCVVVWFGVNFS
YYGLSLDVSGLGLNVYQTQLLFGAVELPSKLLVYLSVRYAGRRLTQAGTLLGTALAFGTR
LLVSSDMKSWSTVLAVMGKAFSEAAFTTAYLFTSELYPTVLRQTGMGLTALVGRLGGSLA
PLAALLDGVWLSLPKLTYGGIALLAAGTALLLPETRQAQLPETIQDVERKSAPTSLQEEE
MPMKQVQN
|
| Enzyme 8 Number of Residues |
548 |
| Enzyme 8 Molecular Weight |
60026 |
| Enzyme 8 Theoretical pI |
7.03 |
| Enzyme 8 GO Classification |
| Function |
- ion transporter activity
- transporter activity
|
| Process |
- cellular physiological process
- ion transport
- physiological process
- transport
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 8 General Function |
Carbohydrate transport and metabolism |
| Enzyme 8 Specific Function |
Not Available |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
- 22-44
- 143-165
- 175-197
- 204-221
- 231-253
- 260-279
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
5001689  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9Y694  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
Q9Y694_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1647 bp
ATGGGCTTTGAGGAGCTGCTGGAGCAGGTGGGCGGCTTTGGGCCCTTCCAACTGCGGAAT
GTGGCACTGCTGGCCCTGCCCCGAGTGCTGCTACCACTGCACTTCCTCCTGCCCATCTTC
CTGGCTGCCGTGCCTGCCCACCGATGTGCCCTGCCGGGTGCCCCTGCCAACTTCAGCCAT
CAGGATGTGTGGCTGGAGGCCCATCTTCCCCGGGAGCCTGATGGCACGCTCAGCTCCTGC
CTCCGCTTTGCCTATCCCCAGGCTCTCCCCAACACCACGTTGGGGGAAGAAAGGCAGAGC
CGTGGGGAGCTGGAGGATGAACCTGCCACAGTGCCCTGCTCTCAGGGCTGGGAGTACGAC
CACTCAGAATTCTCCTCTACCATTGCAACTGAGTCCCAGTGGGATCTGGTGTGTGAGCAG
AAAGGTCTGAACAGAGCTGCGTCCACTTTCTTCTTCGCCGGTGTGCTGGTGGGGGCTGTG
GCCTTTGGATATCTGTCCGACAGGTTTGGGCGGCGGCGTCTGCTGCTGGTAGCCTACGTG
AGTACCCTGGTGCTGGGCCTGGCATCTGCAGCCTCCGTCAGCTATGTAATGTTTGCCATC
ACCCGCACCCTTACTGGCTCAGCCCTGGCTGGTTTTACCATCATCGTGATGCCACTGGAG
CTGGAGTGGCTGGATGTGGAGCACCGCACCGTGGCTGGAGTCCTGAGCAGCACCTTCTGG
ACAGGGGGCGTGATGCTGCTGGCACTGGTTGGGTACCTGATACGGGACTGGCGATGGCTT
CTGCTAGCTGTCACCCTGCCTTGTGCCCCAGGCATCCTCAGCCTCTGGTGGGTGCCTGAG
TCTGCACGCTGGCTTCTGACCCAAGGCCATGTGAAAGAGGCCCACAGGTACTTGCTCCAC
TGTGCCAGGCTCAATGGGCGGCCAGTGTGTGAGGACAGCTTCAGCCAGGAGGCTGTGAGC
AAAGTGGCCGCCGGGGAACGGGTGGTCCGAAGACCTTCATACCTAGACCTGTTCCGCACA
CCACGGCTCCGACACATCTCACTGTGCTGCGTGGTGGTGTGGTTCGGAGTGAACTTCTCC
TATTACGGCCTGAGTCTGGATGTGTCGGGGCTGGGGCTGAACGTGTACCAGACACAGCTG
TTGTTCGGGGCTGTGGAACTGCCCTCCAAGCTGCTGGTCTACTTGTCGGTGCGCTACGCA
GGACGCCGCCTCACGCAAGCCGGGACACTGCTGGGCACGGCCCTGGCGTTCGGCACTAGA
CTGCTAGTGTCCTCCGATATGAAGTCCTGGAGCACTGTCCTGGCAGTGATGGGGAAAGCT
TTTTCTGAAGCTGCCTTCACCACTGCTTACCTGTTCACTTCAGAGTTGTACCCTACGGTG
CTCAGACAGACAGGGATGGGGCTGACTGCACTGGTGGGCCGGCTGGGGGGCTCTTTGGCC
CCACTGGCGGCCTTGCTAGATGGAGTGTGGCTGTCACTGCCCAAGCTTACTTATGGGGGG
ATCGCCCTGCTGGCTGCCGGCACCGCCCTCCTGCTGCCAGAGACGAGGCAGGCACAGCTG
CCAGAGACCATCCAGGACGTGGAGAGAAAGAGTGCCCCAACCAGTCTTCAGGAGGAAGAG
ATGCCCATGAAGCAGGTCCAGAACTAA
|
| Enzyme 8 GenBank Gene ID |
AF097518  |
| Enzyme 8 GeneCard ID |
Q9Y694  |
| Enzyme 8 GenAtlas ID |
SLC22A7  |
| Enzyme 8 HGNC ID |
HGNC:10971  |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
14860 |
| Enzyme 9 Name |
HSD3B2 protein |
| Enzyme 9 Synonyms |
- Hydroxy-delta-5-steroid dehydrogenase, 3 beta-and steroid delta-isomerase 2, isoform CRA_a
|
| Enzyme 9 Gene Name |
HSD3B2 |
| Enzyme 9 Protein Sequence |
>HSD3B2 protein
MGWSCLVTGAGGLLGQRIVRLLVEEKELKEIRALDKAFRPELREEFSKLQNRTKLTVLEG
DILDEPFLKRACQDVSVVIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFI
YTSSIEVAGPNSYKEIIQNGHEEEPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLY
TCALRPTYIYGEGGPFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALR
DPKKAPSVRGQFYYISDDTPHQSYDNLNYILSKEFGLRLDSRWSLPLTLMYWIGFLLEVV
SFLLSPIYSYQPPFNRHTVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLV
DRHKETLKSKTQ
|
| Enzyme 9 Number of Residues |
372 |
| Enzyme 9 Molecular Weight |
42053 |
| Enzyme 9 Theoretical pI |
8.17 |
| Enzyme 9 GO Classification |
| Function |
- 3-beta-hydroxy-delta5-steroid dehydrogenase activity
- catalytic activity
- intramolecular oxidoreductase activity
- intramolecular oxidoreductase activity, transposing C=C bonds
- isomerase activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
- steroid dehydrogenase activity
- steroid delta-isomerase activity
|
| Process |
- cellular lipid metabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
- steroid biosynthesis
- steroid metabolism
|
| Component |
| — |
|
| Enzyme 9 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
124297709  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
A2RRA5  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
A2RRA5_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1119 bp
ATGGGCTGGAGCTGCCTTGTGACAGGAGCAGGAGGGCTTCTGGGTCAGAGGATCGTCCGC
CTGTTGGTGGAAGAGAAGGAACTGAAGGAGATCAGGGCCTTGGACAAGGCCTTCAGACCA
GAATTGAGAGAGGAATTTTCTAAGCTCCAGAACAGGACCAAGCTGACTGTACTTGAAGGA
GACATTCTGGATGAGCCATTCCTGAAAAGAGCCTGCCAGGACGTCTCGGTCGTCATCCAC
ACCGCCTGTATCATTGATGTCTTTGGTGTCACTCACAGAGAGTCCATCATGAATGTCAAT
GTGAAAGGTACCCAGCTACTGTTGGAGGCCTGTGTCCAAGCCAGTGTGCCAGTCTTCATC
TACACCAGTAGCATAGAGGTAGCCGGGCCCAACTCCTACAAGGAAATCATCCAGAACGGC
CACGAAGAAGAGCCTCTGGAAAACACATGGCCCACTCCATACCCGTACAGCAAAAAGCTT
GCTGAGAAGGCTGTGCTGGCGGCTAATGGGTGGAATCTAAAAAATGGTGATACCTTGTAC
ACTTGTGCGTTAAGACCCACATATATCTATGGGGAAGGAGGCCCATTCCTTTCTGCCAGT
ATAAATGAGGCCCTGAACAACAATGGGATCCTGTCAAGTGTTGGAAAGTTCTCTACAGTC
AACCCAGTCTATGTTGGCAACGTGGCCTGGGCCCACATTCTGGCCTTGAGGGCTCTGCGG
GACCCCAAGAAGGCCCCAAGTGTCCGAGGTCAATTCTATTACATCTCAGATGACACGCCT
CACCAAAGCTATGATAACCTTAATTACATCCTGAGCAAAGAGTTTGGCCTCCGCCTTGAT
TCCAGATGGAGCCTTCCTTTAACCCTGATGTACTGGATTGGCTTCCTGCTGGAAGTAGTG
AGCTTCCTACTCAGCCCAATTTACTCCTATCAACCCCCCTTCAACCGCCACACAGTCACA
TTATCAAATAGTGTGTTCACCTTCTCTTACAAGAAGGCTCAGCGAGATCTGGCGTATAAG
CCACTCTACAGCTGGGAGGAAGCCAAGCAGAAAACCGTGGAGTGGGTTGGTTCCCTTGTG
GACCGGCACAAGGAGACCCTGAAGTCCAAGACTCAGTGA
|
| Enzyme 9 GenBank Gene ID |
BC131488  |
| Enzyme 9 GeneCard ID |
A2RRA5  |
| Enzyme 9 GenAtlas ID |
Not Available |
| Enzyme 9 HGNC ID |
Not Available |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
15181 |
| Enzyme 10 Name |
cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA (Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform C |
| Enzyme 10 Synonyms |
Not Available |
| Enzyme 10 Gene Name |
SULT2A1 |
| Enzyme 10 Protein Sequence |
>cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA (Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform CRA_a)
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSK
GDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLM
RNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL
LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVV
DKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
|
| Enzyme 10 Number of Residues |
285 |
| Enzyme 10 Molecular Weight |
33780 |
| Enzyme 10 Theoretical pI |
5.76 |
| Enzyme 10 GO Classification |
Not Available |
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Not Available |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
Not Available |
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
158259783  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
A8K015  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
A8K015_HUMAN  |
| Enzyme 10 PDB ID |
1OV4  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>858 bp
ATGTCGGACGATTTCTTATGGTTTGAAGGCATAGCTTTCCCTACTATGGGTTTCAGATCC
GAAACCTTAAGAAAAGTACGTGATGAGTTCGTGATAAGGGATGAAGATGTAATAATATTG
ACTTACCCCAAATCAGGAACAAACTGGTTGGCTGAGATTCTCTGCCTGATGCACTCCAAG
GGGGATGCCAAGTGGATCCAATCTGTGCCCATCTGGGAGCGATCACCCTGGGTAGAGAGT
GAGATTGGGTATACAGCACTCAGTGAAACGGAGAGTCCACGTTTATTCTCCTCCCACCTC
CCCATCCAGTTATTCCCCAAGTCTTTCTTCAGTTCCAAGGCCAAGGTGATTTATCTCATG
AGAAATCCCAGAGATGTTTTGGTGTCTGGTTATTTTTTCTGGAAAAACATGAAGTTTATT
AAGAAACCAAAGTCATGGGAAGAATATTTTGAATGGTTTTGTCAAGGAACTGTGCTATAT
GGGTCATGGTTTGACCACATTCATGGCTGGATGCCCATGAGAGAGGAGAAAAACTTCCTG
TTACTGAGTTATGAGGAGCTGAAACAGGACACAGGAAGAACCATAGAGAAGATCTGTCAA
TTCCTGGGAAAGACGTTAGAACCCGAAGAACTGAACTTAATTCTCAAGAACAGCTCCTTT
CAGAGCATGAAAGAAAACAAGATGTCCAATTATTCCCTCCTGAGTGTTGATTATGTAGTG
GACAAAGCACAACTTCTGAGAAAAGGTGTATCTGGGGACTGGAAAAATCACTTCACAGTG
GCCCAAGCTGAAGACTTTGATAAATTGTTCCAAGAGAAGATGGCAGATCTTCCTCGAGAG
CTGTTCCCATGGGAATAA
|
| Enzyme 10 GenBank Gene ID |
AK289380  |
| Enzyme 10 GeneCard ID |
A8K015  |
| Enzyme 10 GenAtlas ID |
Not Available |
| Enzyme 10 HGNC ID |
Not Available |
| Enzyme 10 Chromosome Location |
19 |
| Enzyme 10 Locus |
19q13.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
Not Available |
| Enzyme 10 Metabolite References |
Not Available |