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Human Metabolome Database Version 2.5

 

Showing metabocard for Estrone sulfate (HMDB01425)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-18 21:16:21
Accession Number HMDB01425
Secondary Accession Numbers Not Available
Common Name Estrone sulfate
Description Estrone sulfate is a sulfated estrone derivative. Estrone sulfate acts as a long-lived reservoir that can be converted as needed to the more active estradiol (from estrone via 17 beta-hydroxysteroid dehydrogenase). Estrone Sulfate (E1S) is the most abundant circulating estrogen in non-pregnant women as well as normal men. Estrone is primarily synthesized from estrone sulfate. Estrone is an estrogenic hormone secreted by the ovaries and adipose tissues. Estrone is one of the three estrogens found in humans. The other two are estriol and estradiol. Estrone is the least prevalent of the three. Estradiol plays a critical role on reproductive and sexual functioning in women and it also affects other organs including the bones. Estriol is an estrogen that is prevalent primarily during pregnancy.
Synonyms
  1. Conestoral
  2. Estrogenic substances
  3. Estrone
  4. Estrone 3-sulfate
  5. Estrone hydrogen sulfate
  6. Estrone sulfate
  7. Estrone sulfate sodium
  8. Estrone sulfic acid
  9. Premarin
  10. Sodium estrone 3-monosulfate
  11. Sodium estrone 3-sulfate
  12. Estrone-3-sulfate
Chemical IUPAC Name 13-methyl-17-oxo-3-sulfooxy-7,8,9,11,12,14,15,16-octahydro-6H-cyclopenta[a]phenanthrene
Chemical Formula C18H22O5S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Ketosteroids
Family
  • Mammalian Metabolite
Species
  • ketone
  • sulfuric acid monoester
  • aromatic compound
Biofunction
  • Component of Androgen and estrogen metabolism
  • Component of Sulfur metabolism
Application
Source
  • Endogenous
Average Molecular Weight 350.429
Monoisotopic Molecular Weight 350.118805
Isomeric SMILES C[C@]12CC[C@H]3[C@@H](CCC4=CC(OS(O)(=O)=O)=CC=C34)[C@@H]1CCC2=O
Canonical SMILES CC12CCC3C(CCC4=CC(OS(O)(=O)=O)=CC=C34)C1CCC2=O
KEGG Compound ID C02538 Link Image
BioCyc ID ESTRONE-SULFATE Link Image
BiGG ID 40054 Link Image
Wikipedia Link Estrone Link Image
NuGOwiki Link HMDB01425 Link Image
Metagene Link HMDB01425 Link Image
METLIN ID 3556 Link Image
PubChem Compound 699 Link Image
PubChem Substance 5545 Link Image
ChEBI ID 17474 Link Image
CAS Registry Number 481-97-0
InChI Identifier InChI=1/C18H22O5S/c1-18-9-8-14-13-5-3-12(23-24(20,21)22)10-11(13)2-4-15(14)16(18)6-7-17(18)19/h3,5,10,14-16H,2,4,6-9H2,1H3,(H,20,21,22)/t14-,15-,16+,18+/m1/s1
Synthesis Reference Price, Wm. H. Alkali metal estrone sulfates. (1959), US 2917522 19591215 Patent language unavailable.
Melting Point (Experimental) 254.5 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 5.90e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.29 [Predicted by ALOGPS]; 2.5 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Gonads
Intestine
Kidney
Liver
Placenta
Platelet
Skin
Testes
Concentrations (Normal)
Biofluid Blood
Value 0.0004 uM
Age Adult:>18 yrs old
Sex Female
Patient information postmenopause
Comments Not Available
References
  • Geisler J, Ekse D, Helle H, Duong NK, Lonning PE: An optimised, highly sensitive radioimmunoassay for the simultaneous measurement of estrone, estradiol and estrone sulfate in the ultra-low range in human plasma samples. J Steroid Biochem Mol Biol. 2008 Mar;109(1-2):90-5. Epub 2007 Dec 15. [PubMed Link Image]
Biofluid Blood
Value 0.00197 +/- 0.00107 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Giton F, Valleix A, Boudou P, Villette JM, Belanger A, Galons H, Fiet J: Specific radioimmunoassay of estrone sulfate. Application to measurement in male plasma. J Steroid Biochem Mol Biol. 2002 May;81(1):85-94. [PubMed Link Image]
Biofluid Blood
Value 0.0051 +/- 0.00045 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Wright K, Collins DC, Musey PI, Preedy JR: A specific radioimmunoassay for estrone sulfate in plasma and urine without hydrolysis. J Clin Endocrinol Metab. 1978 Nov;47(5):1092-8. [PubMed Link Image]
Biofluid Blood
Value 0.0026 +/- 0.00017 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Wright K, Collins DC, Musey PI, Preedy JR: A specific radioimmunoassay for estrone sulfate in plasma and urine without hydrolysis. J Clin Endocrinol Metab. 1978 Nov;47(5):1092-8. [PubMed Link Image]
Biofluid Blood
Value 0.0027 +/- 0.00022 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Wright K, Collins DC, Musey PI, Preedy JR: A specific radioimmunoassay for estrone sulfate in plasma and urine without hydrolysis. J Clin Endocrinol Metab. 1978 Nov;47(5):1092-8. [PubMed Link Image]
Biofluid Urine
Value 0.0008 (0.00015-0.0014) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Wright K, Collins DC, Musey PI, Preedy JR: A specific radioimmunoassay for estrone sulfate in plasma and urine without hydrolysis. J Clin Endocrinol Metab. 1978 Nov;47(5):1092-8. [PubMed Link Image]
Biofluid Urine
Value 0.0022 (0.00095-0.0035) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Wright K, Collins DC, Musey PI, Preedy JR: A specific radioimmunoassay for estrone sulfate in plasma and urine without hydrolysis. J Clin Endocrinol Metab. 1978 Nov;47(5):1092-8. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.002 (0.0014-0.003) uM
Age Adult:>18 yrs old
Sex Male
Condition Obesity
Comments Not Available
References
  • Brind J, Strain G, Miller L, Zumoff B, Vogelman J, Orentreich N: Obese men have elevated plasma levels of estrone sulfate. Int J Obes. 1990 Jun;14(6):483-6. [PubMed Link Image]
Biofluid Blood
Value 0.0012 +/- 0.00049 uM
Age Adult:>18 yrs old
Sex Both
Condition Abnormal
Comments Not Available
References
  • Reichman ME, Judd JT, Longcope C, Schatzkin A, Clevidence BA, Nair PP, Campbell WS, Taylor PR: Effects of alcohol consumption on plasma and urinary hormone concentrations in premenopausal women. J Natl Cancer Inst. 1993 May 5;85(9):722-7. [PubMed Link Image]
Associated Disorders
Condition References
Obesity
  • Brind J, Strain G, Miller L, Zumoff B, Vogelman J, Orentreich N: Obese men have elevated plasma levels of estrone sulfate. Int J Obes. 1990 Jun;14(6):483-6. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Androgen and Estrogen Metabolism SMP00068 Link Image map00150 Link Image
Sulfate/Sulfite Metabolism SMP00041 Link Image map00920 Link Image
General References
  1. Choi HY, Hobkirk R: Chromatofocusing of mammalian estrone sulfate sulfohydrolase activity. J Steroid Biochem. 1986 Dec;25(6):985-9. [PubMed Link Image]
  2. Sherstha R, McKinley C, Russ P, Scherzinger A, Bronner T, Showalter R, Everson GT: Postmenopausal estrogen therapy selectively stimulates hepatic enlargement in women with autosomal dominant polycystic kidney disease. Hepatology. 1997 Nov;26(5):1282-6. [PubMed Link Image]
  3. Gniot-Szulzycka J, Jakubowska A: Oestrone sulphate sulphohydrolase activity in nuclear envelopes from human placenta cell nuclei. Acta Biochim Pol. 1991;38(1):7-16. [PubMed Link Image]
  4. Fredricsson B, Carlstrom K, Kjessler B, Lindstedt J, Ploen L, Ritzen M, de la Torre B: Incomplete androgen insensitivity: asymmetry in morphology and steroid profile and metabolism of the gonads. An analysis of a case. Acta Endocrinol (Copenh). 1985 Dec;110(4):564-71. [PubMed Link Image]
  5. Fuchikami H, Satoh H, Tsujimoto M, Ohdo S, Ohtani H, Sawada Y: Effects of herbal extracts on the function of human organic anion-transporting polypeptide OATP-B. Drug Metab Dispos. 2006 Apr;34(4):577-82. Epub 2006 Jan 13. [PubMed Link Image]
  6. Milewich L, Sontheimer RD, Herndon JH Jr: Steroid sulfatase activity in epidermis of acne-prone and non-acne-prone skin of patients with acne vulgaris. Arch Dermatol. 1990 Oct;126(10):1312-4. [PubMed Link Image]
  7. Stewart JD, Lou Y, Squires EJ, Coussens PM: Using human microarrays to identify differentially expressed genes associated with increased steroidogenesis in boars. Anim Biotechnol. 2005;16(2):139-51. [PubMed Link Image]
  8. Ekaratanawong S, Anzai N, Jutabha P, Miyazaki H, Noshiro R, Takeda M, Kanai Y, Sophasan S, Endou H: Human organic anion transporter 4 is a renal apical organic anion/dicarboxylate exchanger in the proximal tubules. J Pharmacol Sci. 2004 Mar;94(3):297-304. [PubMed Link Image]
  9. Creidi P, Faivre B, Agache P, Richard E, Haudiquet V, Sauvanet JP: Effect of a conjugated oestrogen (Premarin) cream on ageing facial skin. A comparative study with a placebo cream. Maturitas. 1994 Oct;19(3):211-23. [PubMed Link Image]
  10. Satoh H, Yamashita F, Tsujimoto M, Murakami H, Koyabu N, Ohtani H, Sawada Y: Citrus juices inhibit the function of human organic anion-transporting polypeptide OATP-B. Drug Metab Dispos. 2005 Apr;33(4):518-23. Epub 2005 Jan 7. [PubMed Link Image]
  11. Bomba-Opon DA, Niesluchowska-Frydrych B, Szucka-May H, Kaminski P, Marianowski L: [Effects of oral administration of estrogen replacement therapy in surgical menopause] Ginekol Pol. 2001 Dec;72(12A):1377-82. [PubMed Link Image]
  12. Craddock AL, Love MW, Daniel RW, Kirby LC, Walters HC, Wong MH, Dawson PA: Expression and transport properties of the human ileal and renal sodium-dependent bile acid transporter. Am J Physiol. 1998 Jan;274(1 Pt 1):G157-69. [PubMed Link Image]
  13. AvRuskin TW, Krishnan N, Juan CS: Congenital adrenal hypoplasia and male pseudohermaphroditism due to DAX1 mutation, SF1 mutation or neither: a patient report. J Pediatr Endocrinol Metab. 2004 Aug;17(8):1125-32. [PubMed Link Image]
  14. Matsushima S, Maeda K, Kondo C, Hirano M, Sasaki M, Suzuki H, Sugiyama Y: Identification of the hepatic efflux transporters of organic anions using double-transfected Madin-Darby canine kidney II cells expressing human organic anion-transporting polypeptide 1B1 (OATP1B1)/multidrug resistance-associated protein 2, OATP1B1/multidrug resistance 1, and OATP1B1/breast cancer resistance protein. J Pharmacol Exp Ther. 2005 Sep;314(3):1059-67. Epub 2005 May 18. [PubMed Link Image]
  15. Michaud DS, Manson JE, Spiegelman D, Barbieri RL, Sepkovic DW, Bradlow HL, Hankinson SE: Reproducibility of plasma and urinary sex hormone levels in premenopausal women over a one-year period. Cancer Epidemiol Biomarkers Prev. 1999 Dec;8(12):1059-64. [PubMed Link Image]
  16. Wikipedia Link Image
Metabolic Enzymes
  1. Arylsulfatase D precursor
  2. Arylsulfatase E precursor
  3. Estrogen sulfotransferase
  4. Solute carrier organic anion transporter family member 1C1
  5. Solute carrier organic anion transporter family member 1B1
  6. Steryl-sulfatase precursor
  7. Serum albumin precursor
  8. Solute carrier organic anion transporter family member 4A1
  9. Solute carrier family 22 member 7
Enzyme 1 [top]
Enzyme 1 ID 5551
Enzyme 1 Name Arylsulfatase D precursor
Enzyme 1 Synonyms
  1. ASD
Enzyme 1 Gene Name ARSD
Enzyme 1 Protein Sequence >Arylsulfatase D precursor
MRSAARRGRAAPAARDSLPVLLFLCLLLKTCEPKTANAFKPNILLIMADDLGTGDLGCYG
NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWNA
GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTL
TNDCDPGRPPEVDAALRAQLWGYTQFLALGILTLAAGQTCGFFSVSARAVTGMAGVGCLF
FISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLMLKEAVSYIERHKHGPFLLFLSL
LHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGH
LEARDGHSQLGGWNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPT
VVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQKDSGSVWKV
HYTTPQFHPEERGLLTAEASAHAEWGGVTHHRPPLLFDLSRDPSEARPLTPDSEPLYHAV
IARVGAAVSEHRQTLSPVPQQFSMSNILWKPWLQPCCGHFPFCSCHEDGDGTP
Enzyme 1 Number of Residues 593
Enzyme 1 Molecular Weight 65072
Enzyme 1 Theoretical pI 7.10
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 1 General Function Inorganic ion transport and metabolism
Enzyme 1 Specific Function Not Available
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-33
Enzyme 1 Transmembrane Regions
  • 206-225
  • 229-251
  • 292-314
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 791002 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P51689 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ARSD_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1782 bp
ATGCGATCCGCCGCGCGGAGGGGACGCGCCGCGCCCGCCGCCAGGGACTCTTTGCCGGTG
CTACTGTTTTTATGCTTGCTTCTGAAGACGTGTGAACCTAAAACTGCAAATGCCTTTAAA
CCAAATATCCTACTGATCATGGCGGATGATCTAGGCACTGGGGATCTCGGTTGCTACGGG
AACAATACACTGAGAACGCCGAATATTGACCAGCTTGCAGAGGAAGGTGTGAGGCTCACT
CAGCACCTGGCGGCCGCCCCGCTCTGCACCCCAAGCCGAGCTGCATTCCTCACAGGGAGA
CATTCCTTCAGATCAGGCATGGACGCCAGCAATGGATACCGGGCCCTTCAGTGGAACGCA
GGCTCAGGTGGACTCCCTGAGAACGAAACCACTTTTGCAAGAATCTTGCAGCAGCATGGC
TATGCAACCGGCCTCATAGGAAAATGGCACCAGGGTGTGAATTGTGCATCCCGCGGGGAT
CACTGCCACCACCCCCTGAACCACGGATTTGACTATTTCTACGGCATGCCCTTCACGCTC
ACAAACGACTGTGACCCAGGCAGGCCCCCCGAAGTGGACGCCGCCCTGAGGGCGCAGCTC
TGGGGTTACACCCAGTTCCTGGCGCTGGGGATTCTCACCCTGGCTGCCGGCCAGACCTGC
GGTTTCTTCTCTGTCTCCGCGAGAGCAGTCACCGGCATGGCCGGCGTGGGCTGCCTGTTT
TTCATCTCTTGGTACTCCTCCTTCGGGTTTGTGCGACGCTGGAACTGTATCCTGATGAGA
AACCATGACGTCACGGAGCAACCCATGGTTCTGGAGAAAACAGCGAGTCTTATGCTAAAG
GAAGCTGTTTCCTATATTGAAAGACACAAGCATGGGCCATTTCTCCTCTTCCTTTCTTTG
CTGCATGTGCACATTCCCCTTGTGACCACGAGTGCATTCCTGGGGAAAAGTCAGCATGGC
TTATATGGTGATAATGTGGAGGAGATGGACTGGCTCATAGGTAAGGTTCTTAATGCCATC
GAAGACAATGGTTTAAAGAACTCAACATTCACGTATTTCACCTCTGACCATGGAGGACAT
TTAGAGGCAAGAGATGGACACAGCCAGTTAGGGGGATGGAACGGAATTTACAAAGGTGGG
AAGGGCATGGGAGGATGGGAAGGTGGGATCCGAGTGCCCGGGATCTTCCACTGGCCGGGG
GTGCTCCCGGCCGGCCGAGTGATTGGAGAGCCCACGAGCCTGATGGACGTGTTCCCTACT
GTGGTCCAGCTGGTGGGTGGCGAGGTGCCCCAGGACAGGGTGATTGATGGCCACAGCCTG
GTACCCTTGCTGCAGGGAGCTGAGGCACGCTCGGCACATGAGTTCCTGTTTCATTACTGT
GGGCAGCATCTTCACGCAGCACGCTGGCACCAGAAGGACAGTGGAAGCGTCTGGAAGGTT
CATTACACGACCCCGCAGTTCCACCCCGAGGAGCGGGGCCTGCTAACGGCCGAGGCGTCT
GCCCATGCTGAATGGGGAGGCGTGACCCATCACAGACCCCCTTTGCTCTTTGACCTCTCC
AGGGACCCCTCCGAGGCACGGCCCCTGACCCCCGACTCCGAGCCCCTGTACCACGCCGTG
ATAGCAAGGGTAGGTGCCGCGGTGTCGGAGCATCGGCAGACCCTGAGTCCTGTGCCCCAG
CAGTTTTCCATGAGCAACATCCTGTGGAAGCCGTGGCTGCAGCCGTGCTGCGGACATTTC
CCGTTCTGTTCATGCCACGAGGATGGGGATGGCACCCCCTGA
Enzyme 1 GenBank Gene ID X83572 Link Image
Enzyme 1 GeneCard ID ARSD Link Image
Enzyme 1 GenAtlas ID ARSD Link Image
Enzyme 1 HGNC ID HGNC:717 Link Image
Enzyme 1 Chromosome Location X
Enzyme 1 Locus Xp22.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed Link Image]
  2. Urbitsch P, Salzer MJ, Hirschmann P, Vogt PH: Arylsulfatase D gene in Xp22.3 encodes two protein isoforms. DNA Cell Biol. 2000 Dec;19(12):765-73. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5560
Enzyme 2 Name Arylsulfatase E precursor
Enzyme 2 Synonyms
  1. ASE
Enzyme 2 Gene Name ARSE
Enzyme 2 Protein Sequence >Arylsulfatase E precursor
MLHLHHSCLCFRSWLPAMLAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNT
MRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASG
GLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGD
CARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLTHLIPVSWMPVIWSALSAVLLLAS
SYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHV
HIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN
QLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR
LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFV
TPVFQPEGAGACYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMER
VQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWCLREDDPQ
Enzyme 2 Number of Residues 589
Enzyme 2 Molecular Weight 65670
Enzyme 2 Theoretical pI 6.96
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 2 General Function Inorganic ion transport and metabolism
Enzyme 2 Specific Function May be essential for the correct composition of cartilage and bone matrix during development. Has no activity toward steroid sulfates
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-31
Enzyme 2 Transmembrane Regions
  • 200-222
  • 227-249
  • 289-311
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 791004 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P51690 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ARSE_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1770 bp
ATGTTACATCTGCACCATTCTTGTTTGTGTTTCAGGAGCTGGCTGCCAGCGATGCTCGCT
GTACTGCTAAGTTTGGCACCATCAGCTTCCAGCGACATTTCCGCCTCCCGACCGAACATC
CTTCTTCTGATGGCGGACGACCTTGGCATTGGGGACATTGGCTGCTATGGCAACAACACC
ATGAGGACTCCGAATATTGACCGCCTTGCAGAGGACGGCGTGAAGCTGACCCAACACATC
TCTGCCGCATCTTTGTGCACCCCAAGCAGAGCCGCCTTCCTCACGGGCAGATACCCTGTG
CGATCAGGGATGGTTTCCAGCATTGGTTACCGTGTTCTTCAGTGGACCGGAGCATCTGGA
GGTCTTCCAACAAATGAGACAACTTTTGCAAAAATACTGAAAGAGAAAGGCTATGCCACT
GGACTCATTGGAAAATGGCATCTGGGTCTCAACTGTGAGTCAGCCAGTGATCATTGCCAC
CACCCTCTCCATCATGGCTTTGAGCATTTCTACGGAATGCCTTTCTCCTTGATGGGTGAT
TGCGCCCGCTGGGAACTCTCAGAGAAGCGTGTCAACCTGGAACAAAAACTCAACTTCCTC
TTCCAAGTCCTGGCCTTGGTTGCCCTCACACTGGTAGCAGGGAAGCTCACACACCTGATA
CCCGTCTCGTGGATGCCGGTCATCTGGTCAGCCCTTTCGGCCGTCCTCCTCCTCGCAAGC
TCCTATTTTGTGGGTGCTCTGATTGTCCATGCCGATTGCTTTCTGATGAGAAACCACACC
ATCACGGAGCAGCCCATGTGCTTCCAAAGAACGACACCCCTTATTCTGCAGGAGGTTGCG
TCCTTTCTCAAAAGGAATAAGCATGGGCCTTTCCTCCTCTTTGTTTCCTTTCTACACGTT
CACATCCCTCTTATCACTATGGAGAACTTCCTCGGGAAGAGTCTCCACGGGCTGTATGGG
GACAACGTAGAGGAGATGGACTGGATGGTAGGACGGATCCTTGACACTTTGGACGTGGAG
GGTTTGAGCAACAGCACCCTCATTTATTTTACGTCGGATCACGGCGGTTCCCTAGAGAAT
CAACTTGGAAACACCCAGTATGGTGGCTGGAATGGAATTTATAAAGGTGGGAAGGGCATG
GGAGGATGGGAAGGTGGGATCCGCGTGCCCGGGATCTTCCGCTGGCCCGGGGTGCTCCCG
GCCGGCCGAGTGATTGGCGAGCCCACGAGTCTGATGGACGTGTTCCCCACCGTGGTCCGG
CTGGCGGGCGGCGAGGTGCCCCAGGACAGAGTGATTGACGGCCAAGACCTTCTGCCCTTG
CTCCTGGGGACAGCCCAACACTCAGACCACGAGTTCCTGATGCATTATTGTGAGAGGTTT
CTGCACGCAGCCAGGTGGCATCAACGGGACAGAGGAACAATGTGGAAAGTCCACTTTGTG
ACGCCTGTGTTCCAGCCAGAGGGAGCCGGTGCCTGCTATGGAAGAAAGGTCTGCCCGTGC
TTTGGGGAAAAAGTAGTCCACCACGATCCACCTTTGCTCTTTGACCTCTCAAGAGACCCT
TCTGAGACCCACATCCTCACACCAGCCTCAGAGCCCGTGTTCTATCAGGTGATGGAACGA
GTCCAGCAGGCGGTGTGGGAACACCAGCGGACACTCAGCCCAGTTCCTCTGCAGCTGGAC
AGGCTGGGCAACATCTGGAGACCGTGGCTGCAGCCCTGCTGTGGCCCGTTCCCCCTCTGC
TGGTGCCTTAGGGAAGATGACCCACAATAA
Enzyme 2 GenBank Gene ID X83573 Link Image
Enzyme 2 GeneCard ID ARSE Link Image
Enzyme 2 GenAtlas ID ARSE Link Image
Enzyme 2 HGNC ID HGNC:719 Link Image
Enzyme 2 Chromosome Location X
Enzyme 2 Locus Xp22.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed Link Image]
  2. Daniele A, Parenti G, d'Addio M, Andria G, Ballabio A, Meroni G: Biochemical characterization of arylsulfatase E and functional analysis of mutations found in patients with X-linked chondrodysplasia punctata. Am J Hum Genet. 1998 Mar;62(3):562-72. [PubMed Link Image]
  3. Parenti G, Buttitta P, Meroni G, Franco B, Bernard L, Rizzolo MG, Brunetti-Pierri N, Ballabio A, Andria G: X-linked recessive chondrodysplasia punctata due to a new point mutation of the ARSE gene. Am J Med Genet. 1997 Dec 12;73(2):139-43. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5582
Enzyme 3 Name Estrogen sulfotransferase
Enzyme 3 Synonyms
  1. Sulfotransferase, estrogen- preferring
  2. EST-1
Enzyme 3 Gene Name SULT1E1
Enzyme 3 Protein Sequence >Estrogen sulfotransferase
MNSELDYYEKFEEVHGILMYKDFVKYWDNVEAFQARPDDLVIATYPKSGTTWVSEIVYMI
YKEGDVEKCKEDVIFNRIPFLECRKENLMNGVKQLDEMNSPRIVKTHLPPELLPASFWEK
DCKIIYLCRNAKDVAVSFYYFFLMVAGHPNPGSFPEFVEKFMQGQVPYGSWYKHVKSWWE
KGKSPRVLFLFYEDLKEDIRKEVIKLIHFLERKPSEELVDRIIHHTSFQEMKNNPSTNYT
TLPDEIMNQKLSPFMRKGITGDWKNHFTVALNEKFDKHYEQQMKESTLKFRTEI
Enzyme 3 Number of Residues 294
Enzyme 3 Molecular Weight 35127
Enzyme 3 Theoretical pI 6.61
Enzyme 3 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function May control the level of the estrogen receptor by sulfurylating free estradiol. Maximally sulfates beta-estradiol and estrone at concentrations of 20 nM. Also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 488283 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P49888 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ST1E1_HUMAN Link Image
Enzyme 3 PDB ID 1G3M Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >885 bp
ATGAATTCTGAACTTGACTATTATGAAAAGTTTGAAGAAGTCCATGGGATTCTAATGTAT
AAAGATTTTGTCAAATATTGGGATAATGTGGAAGCGTTCCAGGCAAGACCAGATGATCTT
GTCATTGCCACCTACCCTAAATCTGGTACAACCTGGGTTAGTGAAATTGTGTATATGATC
TATAAAGAGGGTGATGTGGAAAAGTGCAAAGAAGATGTAATTTTTAATCGAATACCTTTC
CTGGAATGCAGAAAAGAAAACCTCATGAATGGAGTAAAACAATTAGATGAGATGAATTCT
CCTAGAATTGTGAAGACTCATTTGCCACCTGAACTTCTTCCTGCCTCATTTTGGGAAAAG
GATTGTAAGATAATCTATCTTTGCCGGAATGCAAAGGATGTGGCTGTTTCCTTTTATTAT
TTCTTTCTAATGGTGGCTGGTCATCCAAATCCTGGATCCTTTCCAGAGTTTGTGGAGAAA
TTCATGCAAGGACAGGTTCCTTATGGTTCCTGGTATAAACATGTAAAATCTTGGTGGGAA
AAGGGAAAGAGTCCACGTGTACTATTTCTTTTCTACGAAGACCTGAAAGAGGATATCAGA
AAAGAGGTGATAAAATTGATACATTTCCTGGAAAGGAAGCCATCAGAGGAGCTTGTGGAC
AGGATTATACATCATACTTCGTTCCAAGAGATGAAGAACAATCCATCCACAAATTACACA
ACACTGCCAGACGAAATTATGAACCAGAAATTGTCGCCCTTCATGAGAAAGGGAATTACA
GGAGACTGGAAAAATCACTTTACAGTAGCCCTGAATGAAAAATTTGATAAACATTATGAG
CAGCAAATGAAGGAATCTACACTGAAGTTTCGAACTGAGATCTAA
Enzyme 3 GenBank Gene ID U08098 Link Image
Enzyme 3 GeneCard ID SULT1E1 Link Image
Enzyme 3 GenAtlas ID SULT1E1 Link Image
Enzyme 3 HGNC ID HGNC:11377 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q13.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Aksoy IA, Wood TC, Weinshilboum R: Human liver estrogen sulfotransferase: identification by cDNA cloning and expression. Biochem Biophys Res Commun. 1994 May 16;200(3):1621-9. [PubMed Link Image]
  2. Her C, Aksoy IA, Kimura S, Brandriff BF, Wasmuth JJ, Weinshilboum RM: Human estrogen sulfotransferase gene (STE): cloning, structure, and chromosomal localization. Genomics. 1995 Sep 1;29(1):16-23. [PubMed Link Image]
  3. Falany CN, Krasnykh V, Falany JL: Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase. J Steroid Biochem Mol Biol. 1995 Jun;52(6):529-39. [PubMed Link Image]
  4. Rubin GL, Harrold AJ, Mills JA, Falany CN, Coughtrie MW: Regulation of sulphotransferase expression in the endometrium during the menstrual cycle, by oral contraceptives and during early pregnancy. Mol Hum Reprod. 1999 Nov;5(11):995-1002. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5689
Enzyme 4 Name Solute carrier organic anion transporter family member 1C1
Enzyme 4 Synonyms
  1. Solute carrier family 21 member 14
  2. Organic anion transporter F
  3. OATP-F
  4. Organic anion-transporting polypeptide 14
  5. Organic anion transporter polypeptide-related protein 5
  6. OAT-RP-5
  7. OATPRP5
Enzyme 4 Gene Name SLCO1C1
Enzyme 4 Protein Sequence >Solute carrier organic anion transporter family member 1C1
MDTSSKENIQLFCKTSVQPVGRPSFKTEYPSSEEKQPCCGELKVFLCALSFVYFAKALAE
GYLKSTITQIERRFDIPSSLVGVIDGSFEIGNLLVITFVSYFGAKLHRPKIIGAGCVIMG
VGTLLIAMPQFFMEQYKYERYSPSSNSTLSISPCLLESSSQLPVSVMEKSKSKISNECEV
DTSSSMWIYVFLGNLLRGIGETPIQPLGIAYLDDFASEDNAAFYIGCVQTVAIIGPIFGF
LLGSLCAKLYVDIGFVNLDHITITPKDPQWVGAWWLGYLIAGIISLLAAVPFWYLPKSLP
RSQSREDSNSSSEKSKFIIDDHTDYQTPQGENAKIMEMARDFLPSLKNLFGNPVYFLYLC
TSTVQFNSLFGMVTYKPKYIEQQYGQSSSRANFVIGLINIPAVALGIFSGGIVMKKFRIS
VCGAAKLYLGSSVFGYLLFLSLFALGCENSDVAGLTVSYQGTKPVSYHERALFSDCNSRC
KCSETKWEPMCGENGITYVSACLAGCQTSNRSGKNIIFYNCTCVGIAASKSGNSSGIVGR
CQKDNGCPQMFLYFLVISVITSYTLSLGGIPGYILLLRCIKPQLKSFALGIYTLAIRVLA
GIPAPVYFGVLIDTSCLKWGFKRCGSRGSCRLYDSNVFRHIYLGLTVILGTVSILLSIAV
LFILKKNYVSKHRSFITKRERTMVSTRFQKENYTTSDHLLQPNYWPGKETQL
Enzyme 4 Number of Residues 712
Enzyme 4 Molecular Weight 78697
Enzyme 4 Theoretical pI 8.59
Enzyme 4 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Mediates the Na(+)-independent high affinity transport of organic anions such as the thyroid hormones thyroxine (T4) and rT3. Other potential substrates, such as triiodothyronine (T3), 17-beta-glucuronosyl estradiol, estrone-3-sulfate and sulfobromophthalein (BSP) are transported with much lower efficiency
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 80-100 111-131 222-242 270-290 353-373 393-413 427-447 550-570 592-612 643-663
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 7839587 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NYB5 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SO1C1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2139 bp
ATGGACACTTCATCCAAAGAAAATATCCAGTTGTTCTGCAAAACTTCAGTGCAACCTGTT
GGAAGGCCTTCTTTTAAAACAGAATATCCCTCCTCAGAAGAAAAGCAACCATGCTGTGGT
GAACTAAAGGTGTTCTTGTGTGCCTTGTCTTTTGTTTACTTTGCCAAAGCATTGGCAGAA
GGCTATCTGAAGAGCACCATCACTCAGATAGAGAGAAGGTTTGATATCCCTTCTTCACTG
GTGGGAGTTATTGATGGTAGTTTTGAAATTGGGAATCTCTTAGTTATAACATTTGTTAGC
TACTTTGGAGCCAAACTTCACAGGCCAAAAATAATTGGAGCAGGGTGTGTAATCATGGGA
GTTGGAACACTGCTCATTGCAATGCCTCAGTTCTTCATGGAGCAGTACAAATATGAGAGA
TATTCTCCTTCCTCCAATTCCACTCTCAGCATCTCTCCGTGTCTCCTAGAGTCAAGCAGT
CAATTACCAGTTTCAGTTATGGAAAAATCAAAATCCAAAATAAGTAACGAATGTGAAGTG
GACACTAGCTCTTCCATGTGGATTTATGTTTTCCTGGGCAATCTTCTTCGTGGAATAGGA
GAAACTCCCATTCAGCCTTTGGGCATTGCCTACCTGGATGATTTTGCCAGTGAAGACAAT
GCAGCTTTCTATATTGGGTGTGTGCAGACGGTTGCAATTATAGGACCAATCTTTGGTTTC
CTGTTAGGCTCATTATGTGCCAAACTATATGTTGACATTGGCTTTGTAAACCTAGATCAC
ATAACCATTACCCCAAAAGATCCCCAGTGGGTAGGAGCCTGGTGGCTTGGCTATCTAATA
GCAGGAATCATAAGTCTTCTTGCAGCTGTGCCTTTCTGGTATTTACCAAAGAGTTTACCA
AGATCCCAAAGTAGAGAGGATTCTAATTCTTCCTCTGAGAAATCCAAGTTTATTATAGAT
GATCACACAGACTACCAAACACCCCAGGGAGAAAATGCAAAAATAATGGAAATGGCAAGA
GATTTTCTTCCATCACTGAAGAATCTTTTTGGAAACCCAGTATACTTCCTATATTTATGT
ACAAGCACTGTTCAGTTCAATTCTCTGTTCGGCATGGTGACGTACAAACCAAAGTACATT
GAGCAGCAGTATGGACAGTCATCCTCCAGGGCCAACTTTGTGATCGGGCTCATCAACATT
CCAGCAGTGGCCCTTGGAATATTCTCTGGGGGGATAGTTATGAAAAAATTCAGAATCAGT
GTGTGTGGAGCTGCAAAACTCTACTTGGGATCATCTGTCTTTGGTTACCTCCTATTTCTT
TCCCTGTTTGCACTGGGCTGTGAAAATTCTGATGTGGCAGGACTAACTGTCTCCTACCAA
GGAACCAAACCTGTCTCTTATCATGAACGAGCTCTCTTTTCAGATTGCAACTCAAGATGC
AAATGTTCAGAGACAAAATGGGAACCCATGTGCGGTGAAAATGGAATCACATATGTATCA
GCTTGTCTTGCTGGTTGTCAAACCTCCAACAGGAGTGGAAAAAATATTATATTTTACAAC
TGCACTTGTGTGGGAATTGCAGCTTCTAAATCCGGAAATTCCTCAGGCATAGTGGGAAGA
TGTCAGAAAGACAATGGATGTCCCCAAATGTTTCTGTATTTCCTTGTAATTTCAGTCATC
ACATCCTATACTTTATCCCTAGGTGGCATACCTGGATACATATTACTTCTGAGGTGCATT
AAGCCACAGCTTAAGTCTTTTGCCTTGGGTATCTACACATTAGCAATAAGAGTTCTTGCA
GGAATCCCAGCTCCAGTGTATTTTGGAGTTTTGATTGATACTTCATGCCTCAAATGGGGA
TTTAAAAGATGTGGAAGTAGAGGATCATGCAGATTATATGATTCAAATGTCTTCAGACAT
ATATATCTGGGACTAACTGTGATACTGGGCACAGTGTCAATTCTCCTAAGCATTGCAGTA
CTTTTCATTTTAAAGAAAAATTATGTTTCAAAACACAGAAGTTTTATAACCAAGAGAGAA
AGAACAATGGTGTCTACAAGATTCCAAAAGGAAAATTACACTACAAGTGATCATCTGCTA
CAACCCAACTACTGGCCAGGCAAGGAAACTCAACTTTAG
Enzyme 4 GenBank Gene ID AF260704 Link Image
Enzyme 4 GeneCard ID SLCO1C1 Link Image
Enzyme 4 GenAtlas ID SLCO1C1 Link Image
Enzyme 4 HGNC ID HGNC:13819 Link Image
Enzyme 4 Chromosome Location 12
Enzyme 4 Locus 12p12.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Pizzagalli F, Hagenbuch B, Stieger B, Klenk U, Folkers G, Meier PJ: Identification of a novel human organic anion transporting polypeptide as a high affinity thyroxine transporter. Mol Endocrinol. 2002 Oct;16(10):2283-96. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5692
Enzyme 5 Name Solute carrier organic anion transporter family member 1B1
Enzyme 5 Synonyms
  1. Solute carrier family 21 member 6
  2. Sodium-independent organic anion- transporting polypeptide 2
  3. OATP 2
  4. Liver-specific organic anion transporter 1
  5. LST-1
  6. OATP-C
Enzyme 5 Gene Name SLCO1B1
Enzyme 5 Protein Sequence >Solute carrier organic anion transporter family member 1B1
MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFE
ISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGY
YRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNML
RGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYV
DLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLE
TNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVF
KYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLS
FYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGIT
YISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAI
QVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCI
KWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASE
NGSVMDEANLESLNKNKHFVPSAGADSETHC
Enzyme 5 Number of Residues 691
Enzyme 5 Molecular Weight 76450
Enzyme 5 Theoretical pI 8.68
Enzyme 5 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 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 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 97-117 207-227 259-279 336-356 376-396 410-430 575-595
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 5051630 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9Y6L6 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name SO1B1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 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 5 GenBank Gene ID AF060500 Link Image
Enzyme 5 GeneCard ID SLCO1B1 Link Image
Enzyme 5 GenAtlas ID SLCO1B1 Link Image
Enzyme 5 HGNC ID HGNC:10959 Link Image
Enzyme 5 Chromosome Location 12
Enzyme 5 Locus 12p
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5740
Enzyme 6 Name Steryl-sulfatase precursor
Enzyme 6 Synonyms
  1. Steroid sulfatase
  2. Steryl- sulfate sulfohydrolase
  3. Arylsulfatase C
  4. ASC
Enzyme 6 Gene Name STS
Enzyme 6 Protein Sequence >Steryl-sulfatase precursor
MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLAS
GGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAK
LLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTT
GFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPL
NCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFA
GKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGS
NGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRI
IDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNG
CFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQT
LPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR
Enzyme 6 Number of Residues 583
Enzyme 6 Molecular Weight 65493
Enzyme 6 Theoretical pI 7.71
Enzyme 6 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Inorganic ion transport and metabolism
Enzyme 6 Specific Function Conversion of sulfated steroid precursors to estrogens during pregnancy
Enzyme 6 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 6 Reactions
  • 3beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + sulfate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-21
Enzyme 6 Transmembrane Regions
  • 185-208 213-234
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 338565 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P08842 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name STS_HUMAN Link Image
Enzyme 6 PDB ID 1P49 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 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 6 GenBank Gene ID J04964 Link Image
Enzyme 6 GeneCard ID STS Link Image
Enzyme 6 GenAtlas ID STS Link Image
Enzyme 6 HGNC ID HGNC:11425 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 7556
Enzyme 7 Name Serum albumin precursor
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name ALB
Enzyme 7 Protein Sequence >Serum albumin precursor
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPF
EDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEP
ERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLF
FAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV
ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLK
ECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYAR
RHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFE
QLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVV
LNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL
SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLV
AASQAALGL
Enzyme 7 Number of Residues 609
Enzyme 7 Molecular Weight 69367
Enzyme 7 Theoretical pI 6.21
Enzyme 7 GO Classification
Function
  • carrier activity
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • extracellular region
  • extracellular space
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-18
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 28590 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P02768 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ALBU_HUMAN Link Image
Enzyme 7 PDB ID 1HA2 Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1830 bp
ATGAAGTGGGTAACCTTTATTTCCCTTCTTTTTCTCTTTAGCTCGGCTTATTCCAGGGGT
GTGTTTCGTCGAGATGCACACAAGAGTGAGGTTGCTCATCGGTTTAAAGATTTGGGAGAA
GAAAATTTCAAAGCCTTGGTGTTGATTGCCTTTGCTCAGTATCTTCAGCAGTGTCCATTT
GAAGATCATGTAAAATTAGTGAATGAAGTAACTGAATTTGCAAAAACATGTGTTGCTGAT
GAGTCAGCTGAAAATTGTGACAAATCACTTCATACCCTTTTTGGAGACAAATTATGCACA
GTTGCAACTCTTCGTGAAACCTATGGTGAAATGGCTGACTGCTGTGCAAAACAAGAACCT
GGGAGAAATGAATGCTTCTTGCAACACAAAGATGACAACCCAAACCTCCCCCGATTGGTG
AGACCAGAGGTTGATGTGATGTGCACTGCTTTTCATGACAATGAAGAGACATTTTTGAAA
AAATACTTATATGAAATTGCCAGAAGACATCCTTACTTTTATGCCCCGGAACTCCTTTTC
TTTGCTAAAAGGTATAAAGCTGCTTTTACAGAATGTTGCCAAGCTGCTGATAAAGCTGCC
TGCCTGTTGCCAAAGCTCGATGAACTTCGGGATGAAGGGAAGGCTTCGTCTGCCAAACAG
AGACTCAAGTGTGCCAGTCTCCAAAAATTTGGAGAAAGAGCTTTCAAAGCATGGGCAGTA
GCTCGCCTGAGCCAGAGATTTCCCAAAGCTGAGTTTGCAGAAGTTTCCAAGTTAGTGACA
GATCTTACCAAAGTCCACACGGAATGCTGCCATGGAGATCTGCTTGAATGTGCTGATGAC
AGGGCGGACCTTGCCAAGTATATCTGTGAAAATCAAGATTCGATCTCCAGTAAACTGAAG
GAATGCTGTGAAAAACCTCTGTTGGAAAAATCCCACTGCATTGCCGAAGTGGAAAATGAT
GAGATGCCTGCTGACTTGCCTTCATTAGCTGCTGATTTTGTTGAAAGTAAGGATGTTTGC
AAAAACTATGCTGAGGCAAAGGATGTCTTCTTGGGCATGTTTTTGTATGAATATGCAAGA
AGGCATCCTGATTACTCTGTCGTGCTGCTGCTGAGACTTGCCAAGACATATGAAACCACT
CTAGAGAAGTGCTGTGCCGCTGCAGATCCTCATGAATGCTATGCCAAAGTGTTCGATGAA
TTTAAACCTCTTGTGGAAGAGCCTCAGAATTTAATCAAACAAAATTGTGAGCTTTTTGAG
CAGCTTGGAGAGTACAAATTCCAGAATGCGCTGTTAGTTCGTTACACCAAGAAAGTACCC
GAAGTGTCAACTCCAACTCTTGTAGAGGTCTCAAGAAACCTAGGAAAAGTGGGCAGCAAA
TGTTGTAAACATCCTGAAGCAAAAAGAATGCCCTGTGCAGAAGACTATCTATCCGTGGTC
CTGAACCAGTTATGTGTGTTGCATGAGAAAACGCCAGTAAGTGACAGAGTCACCAAATGC
TGCACAGAATCCTTGGTGAACAGGCGACCATGCTTTTCAGCTCTGGAAGTCGATGAAACA
TACGTTCCCAAAGAGTTTAATGCTGAAACATTCACCTTCCATGCAGATATATGCACACTT
TCTGAGAAGGAGAGACAAATCAAGAAACAAACTGCACTTGTTGAGCTCGTGAAACACAAG
CCCAAGGCAACAAAAGAGCAACTGAAAGCTGTTATGGATGATTTCGCTGCTTTTGTAGAG
AAGTGCTGCAAGGCTGACGATAAGGAGACCTGCTTTGCCGAGGAGGGTAAAAAACTTGTT
GCTGCAAGTCAAGCTGCCTTAGGCTTATAA
Enzyme 7 GenBank Gene ID V00494 Link Image
Enzyme 7 GeneCard ID ALB Link Image
Enzyme 7 GenAtlas ID ALB Link Image
Enzyme 7 HGNC ID HGNC:399 Link Image
Enzyme 7 Chromosome Location 4
Enzyme 7 Locus 4q11-q13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Lawn RM, Adelman J, Bock SC, Franke AE, Houck CM, Najarian RC, Seeburg PH, Wion KL: The sequence of human serum albumin cDNA and its expression in E. coli. Nucleic Acids Res. 1981 Nov 25;9(22):6103-114. [PubMed Link Image]
  2. Dugaiczyk A, Law SW, Dennison OE: Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sci U S A. 1982 Jan;79(1):71-5. [PubMed Link Image]
  3. Minghetti PP, Ruffner DE, Kuang WJ, Dennison OE, Hawkins JW, Beattie WG, Dugaiczyk A: Molecular structure of the human albumin gene is revealed by nucleotide sequence within q11-22 of chromosome 4. J Biol Chem. 1986 May 25;261(15):6747-57. [PubMed Link Image]
  4. Yu Y, Zhang C, Zhou G, Wu S, Qu X, Wei H, Xing G, Dong C, Zhai Y, Wan J, Ouyang S, Li L, Zhang S, Zhou K, Zhang Y, Wu C, He F: Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs. Genome Res. 2001 Aug;11(8):1392-403. [PubMed Link Image]
  5. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  6. Urano Y, Watanabe K, Sakai M, Tamaoki T: The human albumin gene. Characterization of the 5' and 3' flanking regions and the polymorphic gene transcripts. J Biol Chem. 1986 Mar 5;261(7):3244-51. [PubMed Link Image]
  7. Meloun B, Moravek L, Kostka V: Complete amino acid sequence of human serum albumin. FEBS Lett. 1975 Oct 15;58(1):134-7. [PubMed Link Image]
  8. Corbett JM, Wheeler CH, Baker CS, Yacoub MH, Dunn MJ: The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 1994 Nov;15(11):1459-65. [PubMed Link Image]
  9. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  10. Mogard MH, Kobayashi R, Chen CF, Lee TD, Reeve JR Jr, Shively JE, Walsh JH: The amino acid sequence of kinetensin, a novel peptide isolated from pepsin-treated human plasma: homology with human serum albumin, neurotensin and angiotensin. Biochem Biophys Res Commun. 1986 May 14;136(3):983-8. [PubMed Link Image]
  11. Carraway RE, Mitra SP, Cochrane DE: Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s). J Biol Chem. 1987 May 5;262(13):5968-73. [PubMed Link Image]
  12. Walker JE: Lysine residue 199 of human serum albumin is modified by acetylsalicyclic acid. FEBS Lett. 1976 Jul 15;66(2):173-5. [PubMed Link Image]
  13. Jacobsen C: Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin. Biochem J. 1978 May 1;171(2):453-9. [PubMed Link Image]
  14. Carter DC, He XM, Munson SH, Twigg PD, Gernert KM, Broom MB, Miller TY: Three-dimensional structure of human serum albumin. Science. 1989 Jun 9;244(4909):1195-8. [PubMed Link Image]
  15. Carter DC, He XM: Structure of human serum albumin. Science. 1990 Jul 20;249(4966):302-3. [PubMed Link Image]
  16. He XM, Carter DC: Atomic structure and chemistry of human serum albumin. Nature. 1992 Jul 16;358(6383):209-15. [PubMed Link Image]
  17. Curry S, Mandelkow H, Brick P, Franks N: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat Struct Biol. 1998 Sep;5(9):827-35. [PubMed Link Image]
  18. Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K: Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 1999 Jun;12(6):439-46. [PubMed Link Image]
  19. Bhattacharya AA, Curry S, Franks NP: Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J Biol Chem. 2000 Dec 8;275(49):38731-8. [PubMed Link Image]
  20. Petitpas I, Grune T, Bhattacharya AA, Curry S: Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J Mol Biol. 2001 Dec 14;314(5):955-60. [PubMed Link Image]
  21. Brennan SO, Herbert P: Albumin Canterbury (313 Lys----Asn). A point mutation in the second domain of serum albumin. Biochim Biophys Acta. 1987 Apr 8;912(2):191-7. [PubMed Link Image]
  22. Takahashi N, Takahashi Y, Blumberg BS, Putnam FW: Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4413-7. [PubMed Link Image]
  23. Takahashi N, Takahashi Y, Isobe T, Putnam FW, Fujita M, Satoh C, Neel JV: Amino acid substitutions in inherited albumin variants from Amerindian and Japanese populations. Proc Natl Acad Sci U S A. 1987 Nov;84(22):8001-5. [PubMed Link Image]
  24. Arai K, Ishioka N, Huss K, Madison J, Putnam FW: Identical structural changes in inherited albumin variants from different populations. Proc Natl Acad Sci U S A. 1989 Jan;86(2):434-8. [PubMed Link Image]
  25. Arai K, Madison J, Huss K, Ishioka N, Satoh C, Fujita M, Neel JV, Sakurabayashi I, Putnam FW: Point substitutions in Japanese alloalbumins. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6092-6. [PubMed Link Image]
  26. Arai K, Madison J, Shimizu A, Putnam FW: Point substitutions in albumin genetic variants from Asia. Proc Natl Acad Sci U S A. 1990 Jan;87(1):497-501. [PubMed Link Image]
  27. Brennan SO, Myles T, Peach RJ, Donaldson D, George PM: Albumin Redhill (-1 Arg, 320 Ala----Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site. Proc Natl Acad Sci U S A. 1990 Jan;87(1):26-30. [PubMed Link Image]
  28. Galliano M, Minchiotti L, Porta F, Rossi A, Ferri G, Madison J, Watkins S, Putnam FW: Mutations in genetic variants of human serum albumin found in Italy. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8721-5. [PubMed Link Image]
  29. Watkins S, Madison J, Davis E, Sakamoto Y, Galliano M, Minchiotti L, Putnam FW: A donor splice mutation and a single-base deletion produce two carboxyl-terminal variants of human serum albumin. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):5959-63. [PubMed Link Image]
  30. Madison J, Arai K, Sakamoto Y, Feld RD, Kyle RA, Watkins S, Davis E, Matsuda Y, Amaki I, Putnam FW: Genetic variants of serum albumin in Americans and Japanese. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9853-7. [PubMed Link Image]
  31. Peach RJ, Brennan SO: Structural characterization of a glycoprotein variant of human serum albumin: albumin Casebrook (494 Asp----Asn). Biochim Biophys Acta. 1991 Jul 26;1097(1):49-54. [PubMed Link Image]
  32. Minchiotti L, Galliano M, Stoppini M, Ferri G, Crespeau H, Rochu D, Porta F: Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions. Biochim Biophys Acta. 1992 Mar 12;1119(3):232-8. [PubMed Link Image]
  33. Carlson J, Sakamoto Y, Laurell CB, Madison J, Watkins S, Putnam FW: Alloalbuminemia in Sweden: structural study and phenotypic distribution of nine albumin variants. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8225-9. [PubMed Link Image]
  34. Minchiotti L, Galliano M, Zapponi MC, Tenni R: The structural characterization and bilirubin-binding properties of albumin Herborn, a [Lys240-->Glu] albumin mutant. Eur J Biochem. 1993 Jun 1;214(2):437-44. [PubMed Link Image]
  35. Brennan SO, Fellowes AP: Albumin Hawkes Bay; a low level variant caused by loss of a sulphydryl group at position 177. Biochim Biophys Acta. 1993 Aug 4;1182(1):46-50. [PubMed Link Image]
  36. Galliano M, Minchiotti L, Iadarola P, Stoppini M, Giagnoni P, Watkins S, Madison J, Putnam FW: Protein and DNA sequence analysis of a 'private' genetic variant: albumin Ortonovo (Glu-505-->Lys). Biochim Biophys Acta. 1993 Nov 25;1225(1):27-32. [PubMed Link Image]
  37. Madison J, Galliano M, Watkins S, Minchiotti L, Porta F, Rossi A, Putnam FW: Genetic variants of human serum albumin in Italy: point mutants and a carboxyl-terminal variant. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6476-80. [PubMed Link Image]
  38. Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S: An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7. [PubMed Link Image]
  39. Rushbrook JI, Becker E, Schussler GC, Divino CM: Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7. [PubMed Link Image]
  40. Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T: A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50. [PubMed Link Image]
  41. Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S: Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54. [PubMed Link Image]
  42. Spahr CS, Davis MT, McGinley MD, Robinson JH, Bures EJ, Beierle J, Mort J, Courchesne PL, Chen K, Wahl RC, Yu W, Luethy R, Patterson SD: Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest. Proteomics. 2001 Jan;1(1):93-107. [PubMed Link Image]
  43. Minchiotti L, Campagnoli M, Rossi A, Cosulich ME, Monti M, Pucci P, Kragh-Hansen U, Granel B, Disdier P, Weiller PJ, Galliano M: A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges. Eur J Biochem. 2001 Jan;268(2):344-52. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 8766
Enzyme 8 Name Solute carrier organic anion transporter family member 4A1
Enzyme 8 Synonyms
  1. Solute carrier family 21 member 12
  2. Sodium-independent organic anion transporter E
  3. Organic anion-transporting polypeptide E
  4. OATP-E
  5. Colon organic anion transporter
  6. Organic anion transporter polypeptide-related protein 1
  7. OATP-RP1
  8. OATPRP1
  9. POAT
Enzyme 8 Gene Name SLCO4A1
Enzyme 8 Protein Sequence >Solute carrier organic anion transporter family member 4A1
MPLHQLGDKPLTFPSPNSAMENGLDHTPPSRRASPGTPLSPGSLRSAAHSPLDTSKQPLC
QLWAEKHGARGTHEVRYVSAGQSVACGWWAFAPPCLQVLNTPKGILFFLCAAAFLQGMTV
NGFINTVITSLERRYDLHSYQSGLIASSYDIAACLCLTFVSYFGGSGHKPRWLGWGVLLM
GTGSLVFALPHFTAGRYEVELDAGVRTCPANPGAVCADSTSGLSRYQLVFMLGQFLHGVG
ATPLYTLGVTYLDENVKSSCSPVYIAIFYTAAILGPAAGYLIGGALLNIYTEMGRRTELT
TESPLWVGAWWVGFLGSGAAAFFTAVPILGYPRQLPGSQRYAVMRAAEMHQLKDSSRGEA
SNPDFGKTIRDLPLSIWLLLKNPTFILLCLAGATEATLITGMSTFSPKFLESQFSLSASE
AATLFGYLVVPAGGGGTFLGGFFVNKLRLRGSAVIKFCLFCTVVSLLGILVFSLHCPSVP
MAGVTASYGGSLLPEGHLNLTAPCNAACSCQPEHYSPVCGSDGLMYFSLCHAGCPAATET
NVDGQKVYRDCSCIPQNLSSGFGHATAGKCTSTCQRKPLLLVFIFVVIFFTFLSSIPALT
ATLRCVRDPQRSFALGIQWIVVRILGGIPGPIAFGWVIDKACLLWQDQCGQQGSCLVYQN
SAMSRYILIMGLLYKVLGVLFFAIACFLYKPLSESSDGLETCLPSQSSAPDSATDSQLQS
SV
Enzyme 8 Number of Residues 722
Enzyme 8 Molecular Weight 77194
Enzyme 8 Theoretical pI 7.85
Enzyme 8 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Mediates the Na(+)-independent transport of organic anions such as the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and of estrone-3-sulfate and taurocholate
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-188
Enzyme 8 Transmembrane Regions
  • 104-124 144-164 172-192 229-249 263-283 309-329 372-392 424-444 454-474 579-599 617-637 667-687
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 6683743 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q96BD0 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name SO4A1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2169 bp
ATGCCCCTGCATCAGCTGGGGGACAAGCCGCTCACCTTCCCCAGCCCCAACTCAGCCATG
GAAAACGGGCTTGACCACACCCCACCCAGCAGGAGGGCATCCCCGGGCACACCCCTGAGC
CCCGGCTCCCTCCGCTCCGCTGCCCATAGCCCCCTGGACACCAGCAAGCAGCCCCTCTGC
CAGCTCTGGGCCGAGAAGCATGGCGCCCGGGGGACCCATGAGGTGCGGTACGTCTCGGCC
GGGCAGAGCGTGGCGTGCGGCTGGTGGGCCTTCGCACCGCCGTGCCTGCAGGTCCTCAAC
ACGCCCAAGGGCATCCTGTTCTTCCTGTGTGCGGCCGCATTCCTGCAGGGGATGACTGTG
AATGGCTTCATCAACACAGTCATCACCTCCCTGGAGCGCCGCTATGACCTGCACAGCTAC
CAGAGCGGGCTCATCGCCAGCTCCTACGACATTGCCGCCTGCCTCTGCCTCACCTTCGTC
AGCTACTTCGGGGGCTCAGGGCACAAGCCGCGCTGGCTGGGCTGGGGCGTGCTGCTTATG
GGCACGGGGTCGCTGGTGTTCGCGCTGCCCCACTTCACGGCTGGCCGCTATGAGGTGGAG
TTGGACGCGGGTGTCAGGACGTGCCCTGCCAACCCCGGCGCGGTGTGTGCGGACAGCACC
TCGGGCCTGTCCCGCTACCAGCTGGTCTTCATGCTGGGCCAGTTCCTGCATGGCGTGGGT
GCCACACCCCTCTACACGCTGGGCGTCACCTACCTGGATGAGAACGTCAAGTCCAGCTGC
TCGCCCGTCTACATTGCCATCTTCTACACAGCGGCCATCCTGGGCCCAGCTGCCGGCTAC
CTGATTGGAGGTGCCCTGCTGAATATCTACACGGAAATGGGCCGACGGACGGAGCTGACC
ACCGAGAGCCCACTGTGGGTCGGCGCCTGGTGGGTCGGCTTCCTGGGCTCTGGGGCCGCT
GCTTTCTTCACCGCCGTTCCCATCCTTGGTTACCCTCGGCAGCTGCCAGGCTCCCAGCGC
TACGCGGTCATGAGAGCGGCGGAAATGCACCAGTTGAAGGACAGCAGCCGTGGGGAGGCG
AGCAACCCGGACTTTGGGAAAACCATCAGAGACCTGCCTCTCTCCATCTGGCTCCTGCTG
AAGAACCCCACGTTCATCCTGCTCTGCCTGGCCGGGGCCACCGAGGCCACTCTCATCACC
GGCATGTCCACGTTCAGCCCCAAGTTCTTGGAGTCCCAGTTCAGCCTGAGTGCCTCAGAA
GCTGCCACCTTGTTTGGGTACCTGGTGGTGCCAGCGGGTGGTGGCGGCACCTTCCTGGGC
GGCTTCTTTGTGAACAAGCTCAGGCTCCGGGGCTCCGCGGTCATCAAGTTCTGCCTGTTC
TGCACCGTTGTCAGCCTGCTGGGCATCCTCGTCTTCTCACTGCACTGCCCCAGTGTGCCC
ATGGCGGGCGTCACAGCCAGCTACGGCGGGAGCCTCCTGCCCGAAGGCCACCTGAACCTA
ACGGCTCCCTGCAACGCTGCCTGCAGCTGCCAGCCAGAACACTACAGCCCTGTGTGCGGC
TCGGACGGCCTCATGTACTTCTCACTGTGCCACGCAGGGTGCCCTGCAGCCACGGAGACG
AATGTGGACGGCCAGAAGGTGTACCGAGACTGTAGCTGTATCCCTCAGAATCTTTCCTCT
GGTTTTGGCCATGCCACTGCAGGGAAATGCACTTCAACTTGTCAGAGAAAGCCCCTCCTT
CTGGTTTTCATATTCGTTGTAATTTTCTTTACATTCCTCAGCAGCATTCCTGCACTAACG
GCAACTCTACGATGTGTCCGTGACCCTCAGAGATCCTTTGCCCTGGGAATCCAGTGGATT
GTAGTTAGAATACTAGGGGGCATCCCGGGGCCCATCGCCTTCGGCTGGGTGATCGACAAG
GCCTGTCTGCTGTGGCAGGACCAGTGTGGCCAGCAGGGCTCCTGCTTGGTGTACCAGAAT
TCGGCCATGAGCCGCTACATACTCATCATGGGGCTCCTGTACAAGGTGCTGGGCGTCCTC
TTCTTTGCCATAGCCTGCTTCTTATACAAGCCCCTGTCGGAGTCTTCAGATGGCCTGGAA
ACTTGTCTGCCCAGCCAGTCCTCAGCCCCTGACAGTGCCACAGATAGCCAGCTCCAGAGC
AGCGTCTGA
Enzyme 8 GenBank Gene ID AB031051 Link Image
Enzyme 8 GeneCard ID SLCO4A1 Link Image
Enzyme 8 GenAtlas ID SLCO4A1 Link Image
Enzyme 8 HGNC ID HGNC:10953 Link Image
Enzyme 8 Chromosome Location 20
Enzyme 8 Locus 20q13.33
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Tamai I, Nezu J, Uchino H, Sai Y, Oku A, Shimane M, Tsuji A: Molecular identification and characterization of novel members of the human organic anion transporter (OATP) family. Biochem Biophys Res Commun. 2000 Jun 24;273(1):251-60. [PubMed Link Image]
  2. Fujiwara K, Adachi H, Nishio T, Unno M, Tokui T, Okabe M, Onogawa T, Suzuki T, Asano N, Tanemoto M, Seki M, Shiiba K, Suzuki M, Kondo Y, Nunoki K, Shimosegawa T, Iinuma K, Ito S, Matsuno S, Abe T: Identification of thyroid hormone transporters in humans: different molecules are involved in a tissue-specific manner. Endocrinology. 2001 May;142(5):2005-12. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 14810
Enzyme 9 Name Solute carrier family 22 member 7
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name SLC22A7
Enzyme 9 Protein Sequence >Solute carrier family 22 member 7
MGFEELLEQVGGFGPFQLRNVALLALPRVLLPLHFLLPIFLAAVPAHRCALPGAPANFSH
QDVWLEAHLPREPDGTLSSCLRFAYPQALPNTTLGEERQSRGELEDEPATVPCSQGWEYD
HSEFSSTIATESQWDLVCEQKGLNRAASTFFFAGVLVGAVAFGYLSDRFGRRRLLLVAYV
STLVLGLASAASVSYVMFAITRTLTGSALAGFTIIVMPLELEWLDVEHRTVAGVLSSTFW
TGGVMLLALVGYLIRDWRWLLLAVTLPCAPGILSLWWVPESARWLLTQGHVKEAHRYLLH
CARLNGRPVCEDSFSQEAVSKVAAGERVVRRPSYLDLFRTPRLRHISLCCVVVWFGVNFS
YYGLSLDVSGLGLNVYQTQLLFGAVELPSKLLVYLSVRYAGRRLTQAGTLLGTALAFGTR
LLVSSDMKSWSTVLAVMGKAFSEAAFTTAYLFTSELYPTVLRQTGMGLTALVGRLGGSLA
PLAALLDGVWLSLPKLTYGGIALLAAGTALLLPETRQAQLPETIQDVERKSAPTSLQEEE
MPMKQVQN
Enzyme 9 Number of Residues 548
Enzyme 9 Molecular Weight 60026
Enzyme 9 Theoretical pI 7.03
Enzyme 9 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 9 General Function Carbohydrate transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-190
Enzyme 9 Transmembrane Regions
  • 22-44
  • 143-165
  • 175-197
  • 204-221
  • 231-253
  • 260-279
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 5001689 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9Y694 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q9Y694_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 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 9 GenBank Gene ID AF097518 Link Image
Enzyme 9 GeneCard ID Q9Y694 Link Image
Enzyme 9 GenAtlas ID SLC22A7 Link Image
Enzyme 9 HGNC ID HGNC:10971 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. 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 Link Image]
Enzyme 9 Metabolite References Not Available