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Human Metabolome Database Version 2.5

 

Showing metabocard for Ascorbic acid (HMDB00044)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:39
Accession Number HMDB00044
Secondary Accession Numbers Not Available
Common Name Ascorbic acid
Description Ascorbic acid is an essential nutrient in human diets, and is necessary to maintain connective tissue and bone. The biologically active form of ascorbic acid is vitamin C. Vitamin C is a water soluble vitamin. Primates (including humans) and a few other species in all divisions of the animal kingdom, notably the guinea pig, have lost the ability to synthesize ascorbic acid and must obtain it in their food. Ascorbic acid is an electron donor for enzymes involved in collagen hydroxylation, biosynthesis of carnitine and norepinephrine, tyrosine metabolism, and amidation of peptide hormones. Ascrobic acid (vitamin C) deficiency causes scurvy. The amount of vitamin C necessary to prevent scurvy may not be adequate to maintain optimal health. The ability of vitamin C to donate electrons also makes it a potent water-soluble antioxidant that readily scavenges free radicals such as molecular oxygen, superoxide, hydroxyl radical, and hypochlorous acid. In this setting, several mechanisms could account for a link between vitamin C and heart disease. One is the relation between LDL oxidation and vitamins C and E. Vitamin C in vitro can recycle vitamin E, which can donate electrons to prevent LDL oxidation in vitro. As the lipid-phase vitamin E is oxidized, it can be regenerated by aqueous vitamin C. Other possibilities are that vitamin C could decrease cholesterol by mechanisms not well characterized, or could improve vasodilatation and vascular reactivity, perhaps by decreasing the interactions of nitric oxide with oxidants. (PMID: 10799361)
Synonyms
  1. (+)-ascorbate
  2. (+)-ascorbic acid
  3. 3-Keto-L-gulofuranolactone
  4. 3-Oxo-L-gulofuranolactone
  5. Adenex
  6. Allercorb
  7. Antiscorbic vitamin
  8. Antiscorbutic vitamin
  9. Arco-cee
  10. Ascoltin
  11. Ascor-B.I.D.
  12. Ascorb
  13. Ascorbajen
  14. Ascorbate
  15. Ascorbic acid
  16. Ascorbicab
  17. Ascorbicap
  18. Ascorbicin
  19. Ascorbin
  20. Ascorbutina
  21. Ascorin
  22. Ascorteal
  23. Ascorvit
  24. C-level
  25. C-long
  26. C-quin
  27. C-span
  28. C-vimin
  29. Cantan
  30. Cantaxin
  31. Catavin C
  32. Ce lent
  33. Ce-mi-lin
  34. Ce-vi-sol
  35. Cebicure
  36. Cebid
  37. Cebion
  38. Cebione
  39. Cecon
  40. Cee-caps TD
  41. Cee-vite
  42. Cegiolan
  43. Ceglion
  44. Ceklin
  45. Celaskon
  46. Celin
  47. Cell C
  48. Cemagyl
  49. Cemill
  50. Cenetone
  51. Cenolate
  52. Cereon
  53. Cergona
  54. Cescorbat
  55. Cetamid
  56. Cetane
  57. Cetane-caps TC
  58. Cetane-caps TD
  59. Cetebe
  60. Cetemican
  61. Cevalin
  62. Cevatine
  63. Cevex
  64. Cevi-bid
  65. Cevimin
  66. Cevital
  67. Cevitamate
  68. Cevitamic acid
  69. Cevitamin
  70. Cevitan
  71. Cevitex
  72. Cewin
  73. Chewcee
  74. Ciamin
  75. Cipca
  76. Citriscorb
  77. Citrovit
  78. Colascor
  79. Concemin
  80. Davitamon C
  81. Dora-C-500
  82. Duoscorb
  83. Ferrous ascorbate
  84. HiCee
  85. Hybrin
  86. Ido-C
  87. Juvamine
  88. Kangbingfeng
  89. Kyselina askorbova
  90. L(+)-ascorbate
  91. L(+)-ascorbic acid
  92. L-(+)-ascorbate
  93. L-(+)-ascorbic acid
  94. L-3-Ketothreohexuronic acid lactone
  95. L-Ascorbic acid
  96. L-ascorbate
  97. L-lyxoascorbate
  98. L-lyxoascorbic acid
  99. L-threo-ascorbic acid
  100. L-xyloascorbate
  101. L-xyloascorbic acid
  102. Laroscorbine
  103. Lemascorb
  104. Liqui-cee
  105. Meri-c
  106. Natrascorb
  107. Natrascorb injectable
  108. Planavit C
  109. Proscorbin
  110. Redoxon
  111. Ribena
  112. Ronotec 100
  113. Rontex 100
  114. Roscorbic
  115. Rovimix C
  116. Scorbacid
  117. Scorbu C
  118. Scorbu-C
  119. Secorbate
  120. Sodascorbate
  121. Suncoat VC 40
  122. Testascorbic
  123. VASC
  124. Vicelat
  125. Vicin
  126. Vicomin C
  127. Viforcit
  128. Viscorin
  129. Viscorin 100M
  130. Vitace
  131. Vitacee
  132. Vitacimin
  133. Vitacin
  134. Vitamin C
  135. Vitamisin
  136. Vitascorbol
  137. Xitix
  138. gamma-lactone L-threo-Hex-2-enonate
  139. gamma-lactone L-threo-Hex-2-enonic acid
  140. (+)-Sodium L-ascorbate
Chemical IUPAC Name (2S)-2-[(1R)-1,2-dihydroxyethyl]-4,5-dihydroxy-furan-3-one
Chemical Formula C6H8O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Hydroxy Acids
Sub Class
  • Short chain hydroxy acids
Family
  • Food Additive
Species
  • ketone
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • heterocyclic compound
Biofunction
  • Essential vitamins
  • Anti-oxidant
  • Enzyme co-factor
  • Component of Tyrosine metabolism
Application
—
Source
  • Exogenous
Average Molecular Weight 176.124
Monoisotopic Molecular Weight 176.032089
Isomeric SMILES OC[C@@H](O)[C@@H]1OC(O)=C(O)C1=O
Canonical SMILES OCC(O)C1OC(O)=C(O)C1=O
KEGG Compound ID C00072 Link Image
BioCyc ID ASCORBATE Link Image
BiGG ID 33747 Link Image
Wikipedia Link Ascorbic acid Link Image
NuGOwiki Link HMDB00044 Link Image
Metagene Link HMDB00044 Link Image
METLIN ID 3753 Link Image
PubChem Compound 644104 Link Image
PubChem Substance 15971359 Link Image
ChEBI ID 29073 Link Image
CAS Registry Number 50-81-7
InChI Identifier InChI=1/C6H8O6/c7-1-2(8)5-3(9)4(10)6(11)12-5/h2,5,7-8,10-11H,1H2/t2-,5+/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) 191 oC
Experimental Water Solubility 400 mg/mL at 40 oC [MERCK INDEX (1996)] Source: PhysProp
Predicted Water Solubility 257.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity -1.85 [AVDEEF,A (1997)] Source: PhysProp
Predicted LogP/Hydrophobicity -0.5 [Predicted by PubChem via XLOGP]; -1.87 [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 1E71 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Amniotic Fluid
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adipose Tissue —
Adrenal Cortex —
Adrenal Medulla —
Bladder —
Brain —
Epidermis —
Erythrocyte —
Eye Lens —
Fibroblasts —
Gonads —
Heart —
Intestine —
Liver —
Lung —
Lymphocyte —
Most Tissues —
Muscle —
Myelin —
Neuron —
Placenta —
Platelet —
Prostate —
Skeletal Muscle —
Spleen —
Concentrations (Normal)
Biofluid Amniotic Fluid
Value 20.4 +/- 12.21 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Blood
Value 36.0 +/- 18.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Atanasova BD, Li AC, Bjarnason I, Tzatchev KN, Simpson RJ: Duodenal ascorbate and ferric reductase in human iron deficiency. Am J Clin Nutr. 2005 Jan;81(1):130-3. [PubMed Link Image]
Biofluid Blood
Value 63.0 (11.0-114.0) 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 22.2 (14.0-40.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wannamethee SG, Lowe GD, Rumley A, Bruckdorfer KR, Whincup PH: Associations of vitamin C status, fruit and vegetable intakes, and markers of inflammation and hemostasis. Am J Clin Nutr. 2006 Mar;83(3):567-74; quiz 726-7. [PubMed Link Image]
Biofluid Blood
Value 88.6 (21.0 - 171.0) uM
Age Children:1-13 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 132. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 60.8 +/- 15.9 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 132. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 51.0 (11.0 - 125.0) uM
Age Newborn:0-30 days old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 132. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 27.0 (11.1-49.7) uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 50.9 (35.4-80.1) uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 62.57 +/- 4.71 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Cellular Cytoplasm
Value 68.0 +/- 43.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 132. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid CSF
Value 133 +/- 58.8 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Tallaksen CM, Bohmer T, Bell H: Concentrations of the water-soluble vitamins thiamin, ascorbic acid, and folic acid in serum and cerebrospinal fluid of healthy individuals. Am J Clin Nutr. 1992 Sep;56(3):559-64. [PubMed Link Image]
Biofluid CSF
Value 68.0 (17.0-119.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 164.0 (143.0-185.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. [PubMed Link Image]
Biofluid CSF
Value 144.0 (36.2-251.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Kastenbauer S, Koedel U, Becker BF, Pfister HW: Oxidative stress in bacterial meningitis in humans. Neurology. 2002 Jan 22;58(2):186-91. [PubMed Link Image]
Biofluid CSF
Value 163.8 +/- 21 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. [PubMed Link Image]
Biofluid Urine
Value 63.6 +/-142.9 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 17.0 +/- 2.5 umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal)
Biofluid Blood
Value 39.0 +/- 92.7 uM
Age Adult:>18 yrs old
Sex Both
Condition Hyperoxalemia
Comments Patients with long-term hyperoxalemia (before hemodialysis)
References
  • Ogawa Y, Machida N, Jahana M, Gakiya M, Chinen Y, Oda M, Morozumi M, Sugaya K: Major factors modulating the serum oxalic acid level in hemodialysis patients. Front Biosci. 2004 Sep 1;9:2901-8. [PubMed Link Image]
Biofluid Blood
Value 6.5 +/- 18.6 uM
Age Adult:>18 yrs old
Sex Both
Condition Hyperoxalemia
Comments Patients with long-term hyperoxalemia (after 4-hour hemodialysis session)
References
  • Ogawa Y, Machida N, Jahana M, Gakiya M, Chinen Y, Oda M, Morozumi M, Sugaya K: Major factors modulating the serum oxalic acid level in hemodialysis patients. Front Biosci. 2004 Sep 1;9:2901-8. [PubMed Link Image]
Biofluid Blood
Value 82.57 +/- 36.71 uM
Age Adult:>18 yrs old
Sex Both
Condition Canavan disease
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid CSF
Value 53.8 (45.8-61.8) uM
Age Children:1-13 yrs old
Sex Both
Condition Traumatic brain injury
Comments Pediatric traumatic brain injury
References
  • Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. [PubMed Link Image]
Biofluid CSF
Value 11.9 (0.0-24) uM
Age Adult:>18 yrs old
Sex Both
Condition Meningitis
Comments Bacterial
References
  • Kastenbauer S, Koedel U, Becker BF, Pfister HW: Oxidative stress in bacterial meningitis in humans. Neurology. 2002 Jan 22;58(2):186-91. [PubMed Link Image]
Associated Disorders
Condition References
Canavan disease
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Hyperoxalemia
  • Ogawa Y, Machida N, Jahana M, Gakiya M, Chinen Y, Oda M, Morozumi M, Sugaya K: Major factors modulating the serum oxalic acid level in hemodialysis patients. Front Biosci. 2004 Sep 1;9:2901-8. [PubMed Link Image]
Meningitis
  • Kastenbauer S, Koedel U, Becker BF, Pfister HW: Oxidative stress in bacterial meningitis in humans. Neurology. 2002 Jan 22;58(2):186-91. [PubMed Link Image]
Traumatic brain injury
  • Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Catecholamine Biosynthesis SMP00012 Link Image map00350 Link Image
General References
  1. Jacobsson L, Lindgarde F, Manthorpe R, Akesson B: Fatty acid composition of adipose tissue and serum micronutrients in relation to common rheumatic complaints in Swedish adults 50-70 years old. Scand J Rheumatol. 1992;21(4):171-7. [PubMed Link Image]
  2. Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. [PubMed Link Image]
  3. Luck MR, Jeyaseelan I, Scholes RA: Ascorbic acid and fertility. Biol Reprod. 1995 Feb;52(2):262-6. [PubMed Link Image]
  4. Sotiriou S, Gispert S, Cheng J, Wang Y, Chen A, Hoogstraten-Miller S, Miller GF, Kwon O, Levine M, Guttentag SH, Nussbaum RL: Ascorbic-acid transporter Slc23a1 is essential for vitamin C transport into the brain and for perinatal survival. Nat Med. 2002 May;8(5):514-7. [PubMed Link Image]
  5. Wolters M, Hickstein M, Flintermann A, Tewes U, Hahn A: Cognitive performance in relation to vitamin status in healthy elderly German women-the effect of 6-month multivitamin supplementation. Prev Med. 2005 Jul;41(1):253-9. Epub 2005 Jan 6. [PubMed Link Image]
  6. Chiplonkar SA, Agte VV, Tarwadi KV, Paknikar KM, Diwate UP: Micronutrient deficiencies as predisposing factors for hypertension in lacto-vegetarian Indian adults. J Am Coll Nutr. 2004 Jun;23(3):239-47. [PubMed Link Image]
  7. Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
  8. Dudek H, Farbiszewski R, Rydzewska M, Michno T, Kozlowski A: [Concentration of glutathione (GSH), ascorbic acid (vitamin C) and substances reacting with thiobarbituric acid (TBA-rs) in single human brain metastases] Wiad Lek. 2005;58(7-8):379-81. [PubMed Link Image]
  9. Berndt SI, Carter HB, Landis PK, Hallfrisch J, Rohrmann S, Metter EJ, Platz EA: Prediagnostic plasma vitamin C levels and the subsequent risk of prostate cancer. Nutrition. 2005 Jun;21(6):686-90. [PubMed Link Image]
  10. Atanasova BD, Li AC, Bjarnason I, Tzatchev KN, Simpson RJ: Duodenal ascorbate and ferric reductase in human iron deficiency. Am J Clin Nutr. 2005 Jan;81(1):130-3. [PubMed Link Image]
  11. Huang J, May JM: Ascorbic acid protects SH-SY5Y neuroblastoma cells from apoptosis and death induced by beta-amyloid. Brain Res. 2006 Jun 30;1097(1):52-8. Epub 2006 May 24. [PubMed Link Image]
  12. Kastenbauer S, Koedel U, Becker BF, Pfister HW: Oxidative stress in bacterial meningitis in humans. Neurology. 2002 Jan 22;58(2):186-91. [PubMed Link Image]
  13. Hino K, Murakami Y, Nagai A, Kitase A, Hara Y, Furutani T, Ren F, Yamaguchi Y, Yutoku K, Yamashita S, Okuda M, Okita M, Okita K: Alpha-tocopherol [corrected] and ascorbic acid attenuates the ribavirin [corrected] induced decrease of eicosapentaenoic acid in erythrocyte membrane in chronic hepatitis C patients. J Gastroenterol Hepatol. 2006 Aug;21(8):1269-75. [PubMed Link Image]
  14. Kodama M, Inoue F, Kodama T, Kodama M: Intraperitoneal administration of ascorbic acid delays the turnover of 3H-labelled cortisol in the plasma of an ODS rat, but not in the Wistar rat. Evidence in support of the cardinal role of vitamin C in the progression of glucocorticoid synthesis. In Vivo. 1996 Jan-Feb;10(1):97-102. [PubMed Link Image]
  15. Trommer H, Bottcher R, Poppl A, Hoentsch J, Wartewig S, Neubert RH: Role of ascorbic acid in stratum corneum lipid models exposed to UV irradiation. Pharm Res. 2002 Jul;19(7):982-90. [PubMed Link Image]
  16. Grunewald RA: Ascorbic acid in the brain. Brain Res Brain Res Rev. 1993 Jan-Apr;18(1):123-33. [PubMed Link Image]
  17. Close GL, Ashton T, Cable T, Doran D, Holloway C, McArdle F, MacLaren DP: Ascorbic acid supplementation does not attenuate post-exercise muscle soreness following muscle-damaging exercise but may delay the recovery process. Br J Nutr. 2006 May;95(5):976-81. [PubMed Link Image]
  18. Li C, Chen Y, Wang Q: [Whole bladder wall laser irradiation to prevent bladder cancer recurrence with intravesical HpD and ascorbic acid] Zhonghua Zhong Liu Za Zhi. 1997 Nov;19(6):463-5. [PubMed Link Image]
  19. Wannamethee SG, Lowe GD, Rumley A, Bruckdorfer KR, Whincup PH: Associations of vitamin C status, fruit and vegetable intakes, and markers of inflammation and hemostasis. Am J Clin Nutr. 2006 Mar;83(3):567-74; quiz 726-7. [PubMed Link Image]
  20. Wikipedia Link Image
Metabolic Enzymes
  1. Peptidyl-glycine alpha-amidating monooxygenase precursor
  2. Dopamine beta-hydroxylase precursor
  3. Phytanoyl-CoA dioxygenase, peroxisomal precursor
  4. Prolyl 4-hydroxylase subunit alpha-2 precursor
  5. Prolyl 4-hydroxylase subunit alpha-1 precursor
  6. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 precursor
  7. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 precursor
  8. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 precursor
  9. Protein disulfide-isomerase precursor
  10. Solute carrier family 23 member 1
  11. Solute carrier family 23 member 2
  12. Trimethyllysine dioxygenase, mitochondrial precursor
  13. CDNA PSEC0259 fis, clone NT2RP3003789, weakly similar to CYTOCHROME B561
  14. Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3
  15. Prolyl 3-hydroxylase 1 precursor
  16. Prolyl 3-hydroxylase 2 precursor
  17. Prolyl 3-hydroxylase 3 precursor
  18. Solute carrier family 23 member 3
  19. Prolyl 4-hydroxylase subunit alpha-3
  20. Egl nine homolog 1
  21. Egl nine homolog 2
  22. Egl nine homolog 3
  23. Putative HIF-prolyl hydroxylase PH-4
  24. Uncharacterized protein PAM
  25. Putative uncharacterized protein
  26. cDNA, FLJ93151, Homo sapiens procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3 (PLOD3), mRNA (Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3)
  27. 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1
  28. 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2
Enzyme 1 [top]
Enzyme 1 ID 5484
Enzyme 1 Name Peptidyl-glycine alpha-amidating monooxygenase precursor
Enzyme 1 Synonyms
  1. PAM[Includes: Peptidylglycine alpha-hydroxylating monooxygenase
  2. PHM
  3. Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
  4. Peptidylamidoglycolate lyase
  5. PAL]
Enzyme 1 Gene Name PAM
Enzyme 1 Protein Sequence >Peptidyl-glycine alpha-amidating monooxygenase precursor 
MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALD
IRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWF
CDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKD
CSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHH
LGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATH
IGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHE
HHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESES
DLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQ
PPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSF
DSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALH
QVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFS
PSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVR
EIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFD
MPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMEN
KPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGDSEH
KLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEE
YSAPLPALAPSSS
Enzyme 1 Number of Residues 973
Enzyme 1 Molecular Weight 108333
Enzyme 1 Theoretical pI 6.39
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • copper ion binding
  • ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
  • peptidylglycine monooxygenase activity
  • transition metal ion binding
Process
  • cellular metabolism
  • metabolism
  • peptide metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Bifunctional enzyme that catalyzes 2 sequencial steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • peptidylamidoglycolate = peptidyl amide + glyoxylate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-20
Enzyme 1 Transmembrane Regions
  • 864-887
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 189595 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P19021 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AMD_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2925 bp 
ATGGCTGGCCGCGTCCCTAGCCTGCTAGTTCTCCTTGTTTTTCCAAGCAGCTGTTTGGCT
TTCCGAAGCCCACTTTCTGTCTTTAAGAGGTTTAAAGAAACTACCAGACCATTTTCCAAT
GAATGTCTTGGTACCACCAGACCCGTAGTTCCTATTGATTCATCAGATTTTGCATTGGAT
ATTCGCATGCCTGGGGTTACACCTAAACAGTCCGATACATACTTCTGCATGTCTATGCGA
ATACCAGTGGATGAGGAAGCCTTCGTGATTGACTTCAAGCCTCGAGCCAGCATGGATACT
GTCCATCACATGTTACTTTTTGGATGCAATATGCCTTCATCCACTGGAAGTTACTGGTTT
TGTGATGAAGGAACCTGTACAGATAAAGCCAATATTCTGTATGCCTGGGCGAGAAATGCT
CCCCCTACCCGGCTCCCCAAAGGTGTTGGATTCAGAGTTGGAGGAGAGACTGGAAGTAAA
TACTTTGTACTACAGGTACACTATGGGGATATTAGTGCTTTTAGAGATAATAACAAGGAC
TGTTCTGGTGTGTCCTTACACCTCACACGTCTGCCACAGCCTTTAATTGCTGGCATGTAC
CTTATGATGTCTGTTGACACTGTTATCCCAGCAGGAGAAAAAGTGGTGAATTCTGACATT
TCATGCCATTATAAAAATTATCCAATGCATGTCTTTGCCTATAGAGTTCACACTCACCAT
TTAGGTAAGGTAGTAAGTGGATACAGAGTAAGAAATGGACAGTGGACACTGATTGGACGG
CAGAGCCCTCAGCTGCCACAGGCTTTCTACCCTGTGGGGCATCCAGTTGATGTAAGTTTT
GGTGACCTACTGGCTGCAAGATGTGTATTCACTGGTGAAGGAAGGACAGAAGCCACACAC
ATTGGTGGCACGTCTAGTGATGAAATGTGCAACTTATACATTATGTATTACATGGAAGCC
AAGCATGCAGTTTCTTTCATGACCTGTACCCAGAATGTAGCTCCAGATATGTTCAGAACC
ATACCACCAGAGGCCAACATTCCAATTCCCGTGAAGTCTGATATGGTTATGATGCATGAA
CATCATAAAGAAACAGAATATAAAGATAAGATTCCTTTACTACAGCAGCCAAAACGAGAA
GAAGAAGAAGTGTTAGACCAGGGTGATTTCTATTCACTACTTTCCAAGCTGCTAGGAGAA
AGGGAAGATGTTGTTCATGTGCACAAATATAATCCTACAGAAAAGGCAGAATCAGAGTCA
GACCTGGTAGCTGAGATTGCAAATGTAGTCCAAAAAAAGGATCTTGGTCGATCTGATGCC
AGAGAGGGTGCAGAACATGAGAGGGGTAATGCTATTCTTGTCAGAGACAGAATTCACAAA
TTCCACAGACTAGTATCTACCTTGAGGCCACCAGAGAGCAGAGTTTTCTCATTACAGCAG
CCCCCACCTGGTGAAGGCACCTGGGAACCAGAACACACAGGAGATTTCCACATGGAAGAG
GCACTGGATTGGCCTGGAGTATACTTGTTACCAGGCCAGGTTTCTGGGGTGGCTCTAGAC
CCTAAGAATAACCTGGTGATTTTCCACAGAGGTGACCATGTCTGGGATGGAAACTCGTTT
GACAGCAAGTTTGTTTACCAGCAAATAGGACTCGGACCAATTGAAGAAGACACTATTCTT
GTCATAGATCCAAATAATGCTGCAGTACTCCAGTCCAGTGAAAAAAATCTGTTTTACTTG
CCACATGGCTTGAGTATAGATAAAGATGGGAATTATTGGGTCACAGACGTGGCTCTCCAT
CAGGTGTTCAAACTGGATCCAAACAATAAAGAAGGCCCTGTATTAATCCTGGGAAGGAGC
ATGCAACCAGGCAGTGACCAGAATCACTTCTGTCAACCCACTGATGTGGCTGTGGATCCA
GGCACTGGAGCCATTTATGTATCAGATGGTTACTGCAACAGCAGGATTGTGCAGTTTTCA
CCAAGTGGAAAGTTCATCACACAGTGGGGAGAAGAGTCTTCAGGGAGCAGTCCTCTGCCA
GGCCAGTTCACTGTTCCTCACAGCTTGGCTCTTGTGCCTCTTTTGGGCCAATTATGTGTG
GCAGACCGGGAAAATGGTCGGATCCAGTGTTTTAAAACTGACACCAAAGAATTTGTGAGA
GAGATTAAGCATTCATCATTTGGAAGAAATGTATTTGCAATTTCATATATACCAGGCTTG
CTCTTTGCAGTGAATGGGAAGCCTCATTTTGGGGACCAAGAACCTGTACAAGGATTTGTG
ATGAACTTTTCCAATGGGGAAATTATAGACATCTTCAAGCCAGTGCGCAAGCACTTTGAT
ATGCCTCATGATATTGTTGCATCTGAAGATGGGACCGTGTACATTGGAGATGCTCATACC
AACACCGTGTGGAAGTTCACCTTGACTGAGAAATTGGAACATCGATCAGTTAAAAAGGCT
GGCATTGAGGTCCAGGAAATCAAAGAAGCCGAGGCAGTTGTTGAAACCAAAATGGAGAAC
AAACCCACCTCCTCAGAATTGCAGAAGATGCAAGAGAAACAGAAGCTGATCAAAGAGCCA
GGCTCGGGAGTGCCTGTTGTTCTCATTACAACCCTTCTGGTTATTCCGGTGGTTGTCCTG
CTGGCCATTGCCATATTTATTCGGTGGAAAAAATCAAGGGCCTTTGGAGCAGATTCTGAA
CACAAACTCGAGACGAGTTCAGGAAGAGTACTGGGAAGATTTAGAGGAAAGGGAAGTGGA
GGCTTAAACCTTGGTAATTTCTTTGCAAGCCGTAAGGGCTACAGTCGAAAAGGGTTTGAC
CGGCTTAGCACTGAGGGCAGTGACCAAGAGAAAGAGGATGATGGAAGTGAATCAGAAGAG
GAGTATTCAGCACCTCTGCCTGCGCTCGCACCTTCCTCCTCCTGA
Enzyme 1 GenBank Gene ID M37721 Link Image
Enzyme 1 GeneCard ID PAM Link Image
Enzyme 1 GenAtlas ID PAM Link Image
Enzyme 1 HGNC ID HGNC:8596 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Glauder J, Ragg H, Rauch J, Engels JW: Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells. Biochem Biophys Res Commun. 1990 Jun 15;169(2):551-8. [PubMed Link Image]
  2. Tateishi K, Arakawa F, Misumi Y, Treston AM, Vos M, Matsuoka Y: Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):282-90. [PubMed Link Image]
  3. Husten EJ, Tausk FA, Keutmann HT, Eipper BA: Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine alpha-amidating monooxygenase. J Biol Chem. 1993 May 5;268(13):9709-17. [PubMed Link Image]
  4. Yun HY, Keutmann HT, Eipper BA: Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase. J Biol Chem. 1994 Apr 8;269(14):10946-55. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5485
Enzyme 2 Name Dopamine beta-hydroxylase precursor
Enzyme 2 Synonyms
  1. Dopamine beta- monooxygenase
Enzyme 2 Gene Name DBH
Enzyme 2 Protein Sequence >Dopamine beta-hydroxylase precursor 
MREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLELSWNVSYTQEAIHF
QLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQDYQLL
QVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQR
VQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVT
KGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEE
AGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPV
MAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIV
NQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHY
YPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKA
LYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQGRSPAGPTVVSIGG
GKG
Enzyme 2 Number of Residues 603
Enzyme 2 Molecular Weight 67614
Enzyme 2 Theoretical pI 6.31
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • copper ion binding
  • dopamine beta-monooxygenase activity
  • ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • amino acid metabolism
  • biogenic amine metabolism
  • catecholamine metabolism
  • cellular metabolism
  • histidine catabolism
  • histidine family amino acid metabolism
  • histidine metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Conversion of dopamine to noradrenaline
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-25
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 30474 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P09172 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name DOPO_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1812 bp 
ATGCGGGAGGCAGCCTTCATGTACAGCACAGCAGTGGCCATCTTCCTGGTCATCCTGGTG
GCCGCACTGCAGGGCTCGGCTCCCCGTGAGAGCCCCCTCCCCTATCACATCCCCCTGGAC
CCGGAGGGGTCCCTGGAGCTCTCATGGAATGTCAGCTACACCCAGGAGGCCATCCATTTC
CAGCTCCTGGTGCGGAGGCTCAAGGCTGGCGTCCTGTTTGGGATGTCCGACCGTGGCGAG
CTTGAGAACGCAGATCTCGTGGTGCTCTGGACCGATGGGGACACTGCCTATTTTGCGGAC
GCCTGGAGTGACCAGAAGGGGCAGATCCACCTGGATCCCCAGCAGGACTACCAGCTGCTG
CAGGTGCAGAGGACCCCAGAAGGCCTGACCCTGCTTTTCAAGAGGCCCTTTGGCACCTGC
GACCCCAAGGATTACCTCATTGAAGACGGCACTGTCCACTTGGTCTACGGGATCCTGGAG
GAGCCGTTCCGGTCACTGGAGGCCATCAACGGCTCGGGCCTGCAGATGGGGCTGCAGAGG
GTGCAGCTCCTGAAGCCCAATATCCCCGAACCGGAGTTGCCCTCAGACGCGTGCACCATG
GAGGTCCAAGCTCCCAATATCCAGATCCCCAGCCAGGAGACCACGTACTGGTGCTACATT
AAGGAGCTTCCAAAGGGCTTCTCTCGGCACCACATTATCAAGTACGAGCCCATCGTCACC
AAGGGCAATGAGGCCCTTGTCCACCACATGGAAGTCTTCCAGTGCGCCCCCGAGATGGAC
AGCGTCCCCCACTTCAGCGGGCCCTGCGACTCCAAGATGAAACCCGACCGCCTCAACTAC
TGCCGCCACGTGCTGGCCGCCTGGGCCCTGGGTGCCAAGGCATTTTACTACCCAGAGGAA
GCCGGCCTTGCCTTCGGGGGTCCAGGGTCCTCCAGATATCTCCGCCTGGAAGTTCACTAC
CACAACCCACTGGTGATAGAAGGACGAAACGACTCCTCAGGCATCCGCTTGTACTACACA
GCCAAGCTGCGGCGCTTCAACGCGGGGATCATGGAGCTGGGACTGGTGTACACGCCAGTG
ATGGCCATTCCACCACGGGAGACCGCCTTCATCCTCACTGGCTACTGCACGGACAAGTGC
ACCCAGCTGGCACTGCCTCCCTCCGGGATCCACATCTTCGCCTCTCAGCTCCACACACAC
CTGACTGGGAGAAAGGTGGTCACAGTGCTGGTCCGGGACGGCCGGGAGTGGGAGATCGTG
AACCAGGACAATCACTACAGCCCTCACTTCCAGGAGATCCGCATGTTGAAGAAGGTCGTG
TCGGTCCATCCGGGAGATGTGCTCATCACCTCCTGCACGTACAACACGGAAGACCGGGAG
CTGGCCACAGTGGGGGGCTTCGGGATCCTGGAGGAGATGTGTGTCAACTACGTGCACTAC
TACCCCCAGACGCAGCTGGAGCTCTGCAAGACGGCTGTGGACGCCGGCTTCCTGCAGAAG
TACTTCCACCTCATCAACAGGTTCAACAACGAGGATGTCTGCACCTGCCCTCAGGCGTCC
GTGTCTCAGCAGTTCACCTCTGTTCCCTGGAACTCCTTCAACCGCGACGTACTGAAGGCC
CTGTACAGCTTCGCGCCCATCTCCATGCACTGCAACAAGTCCTCAGCCGTCCGCTTCCAG
GGTGAATGGAACCTGCAGCCCCTGCCCAAGGTCATCTCCACACTGGAAGAGCCCACCCCA
CAGTGCCCCACCAGCCAGGGCCGAAGCCCTGCTGGCCCCACCGTTGTCAGCATTGGTGGG
GGCAAAGGCTGA
Enzyme 2 GenBank Gene ID X13255 Link Image
Enzyme 2 GeneCard ID DBH Link Image
Enzyme 2 GenAtlas ID DBH Link Image
Enzyme 2 HGNC ID HGNC:2689 Link Image
Enzyme 2 Chromosome Location 9
Enzyme 2 Locus 9q34
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Kobayashi K, Kurosawa Y, Fujita K, Nagatsu T: Human dopamine beta-hydroxylase gene: two mRNA types having different 3'-terminal regions are produced through alternative polyadenylation. Nucleic Acids Res. 1989 Feb 11;17(3):1089-102. [PubMed Link Image]
  2. Lamouroux A, Vigny A, Faucon Biguet N, Darmon MC, Franck R, Henry JP, Mallet J: The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme. EMBO J. 1987 Dec 20;6(13):3931-7. [PubMed Link Image]
  3. Li B, Tsing S, Kosaka AH, Nguyen B, Osen EG, Bach C, Chan H, Barnett J: Expression of human dopamine beta-hydroxylase in Drosophila Schneider 2 cells. Biochem J. 1996 Jan 1;313 ( Pt 1):57-64. [PubMed Link Image]
  4. Williams HJ, Bray N, Murphy KC, Cardno AG, Jones LA, Owen MJ: No evidence for allelic association between schizophrenia and a functional variant of the human dopamine beta-hydroxylase gene (DBH). Am J Med Genet. 1999 Oct 15;88(5):557-9. [PubMed Link Image]
  5. 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 Link Image]
  6. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  7. Kim CH, Zabetian CP, Cubells JF, Cho S, Biaggioni I, Cohen BM, Robertson D, Kim KS: Mutations in the dopamine beta-hydroxylase gene are associated with human norepinephrine deficiency. Am J Med Genet. 2002 Mar 1;108(2):140-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5502
Enzyme 3 Name Phytanoyl-CoA dioxygenase, peroxisomal precursor
Enzyme 3 Synonyms
  1. Phytanoyl-CoA alpha-hydroxylase
  2. PhyH
  3. Phytanic acid oxidase
Enzyme 3 Gene Name PHYH
Enzyme 3 Protein Sequence >Phytanoyl-CoA dioxygenase, peroxisomal precursor 
MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKF
YEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITK
VQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHY
FPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYE
ENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENI
EKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
Enzyme 3 Number of Residues 338
Enzyme 3 Molecular Weight 38539
Enzyme 3 Theoretical pI 8.65
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2564671 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O14832 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PAHX_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1017 bp 
ATGGAGCAGCTTCGCGCCGCCGCCCGTCTGCAGATTGTTCTGGGCCACCTCGGCCGCCCC
TCGGCCGGGGCTGTCGTAGCTCATCCCACTTCAGGGACTATTTCCTCTGCCAGTTTCCAT
CCTCAACAATTCCAGTATACTCTGGATAATAATGTTCTAACCCTGGAACAGAGAAAATTT
TATGAAGAAAATGGGTTTCTAGTAATCAAAAATCTTGTACCTGATGCCGATATTCAACGC
TTTCGGAATGAGTTTGAAAAAATCTGCAGAAAGGAGGTGAAACCATTAGGATTAACAGTA
ATGAGAGATGTGACCATTTCGAAATCCGAATATGCTCCAAGTGAGAAGATGATCACGAAG
GTCCAGGATTTCCAGGAAGATAAGGAGCTCTTCAGATACTGCACTCTCCCCGAGATTCTG
AAATATGTGGAGTGCTTCACTGGACCTAATATTATGGCCATGCACACAATGTTGATAAAC
AAACCTCCAGATTCTGGCAAGAAGACGTCCCGTCACCCCCTGCACCAGGACCTGCACTAT
TTCCCCTTCAGGCCCAGCGATCTCATCGTTTGCGCCTGGACGGCGATGGAGCACATCAGC
CGGAACAACGGCTGTCTGGTTGTGCTCCCAGGCACGCACAAGGGCTCCCTGAAGCCCCAC
GATTACCCCAAGTGGGAGGGGGGAGTTAACAAAATGTTCCACGGGATCCAGGACTACGAG
GAAAACAAGGCCCGGGTGCACCTGGTGATGGAGAAGGGCGACACTGTTTTCTTCCATCCT
TTGCTCATCCACGGATCTGGTCAGAATAAAACCCAGGGATTCCGGAAGGCAATTTCCTGC
CATTTCGCCAGTGCCGATTGCCACTACATTGACGTGAAGGGCACCAGTCAAGAAAACATC
GAGAAGGAAGTTGTAGGAATAGCACATAAATTCTTTGGAGCTGAAAATAGCGTGAACTTG
AAGGATATTTGGATGTTTCGAGCTCGACTTGTGAAAGGAGAAAGAACCAATCTTTGA
Enzyme 3 GenBank Gene ID AF023462 Link Image
Enzyme 3 GeneCard ID PHYH Link Image
Enzyme 3 GenAtlas ID PHYH Link Image
Enzyme 3 HGNC ID HGNC:8940 Link Image
Enzyme 3 Chromosome Location 10
Enzyme 3 Locus 10pter-p11.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Mihalik SJ, Morrell JC, Kim D, Sacksteder KA, Watkins PA, Gould SJ: Identification of PAHX, a Refsum disease gene. Nat Genet. 1997 Oct;17(2):185-9. [PubMed Link Image]
  2. Jansen GA, Ofman R, Ferdinandusse S, Ijlst L, Muijsers AO, Skjeldal OH, Stokke O, Jakobs C, Besley GT, Wraith JE, Wanders RJ: Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nat Genet. 1997 Oct;17(2):190-3. [PubMed Link Image]
  3. Chambraud B, Radanyi C, Camonis JH, Rajkowski K, Schumacher M, Baulieu EE: Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2104-9. [PubMed Link Image]
  4. Jansen GA, Hogenhout EM, Ferdinandusse S, Waterham HR, Ofman R, Jakobs C, Skjeldal OH, Wanders RJ: Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease. Hum Mol Genet. 2000 May 1;9(8):1195-200. [PubMed Link Image]
  5. Lee ZH, Kim H, Ahn KY, Seo KH, Kim JK, Bae CS, Kim KK: Identification of a brain specific protein that associates with a refsum disease gene product, phytanoyl-CoA alpha-hydroxylase. Brain Res Mol Brain Res. 2000 Feb 22;75(2):237-47. [PubMed Link Image]
  6. Jansen GA, Ferdinandusse S, Hogenhout EM, Verhoeven NM, Jakobs C, Wanders RJ: Phytanoyl-CoA hydroxylase deficiency. Enzymological and molecular basis of classical Refsum disease. Adv Exp Med Biol. 1999;466:371-6. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5537
Enzyme 4 Name Prolyl 4-hydroxylase subunit alpha-2 precursor
Enzyme 4 Synonyms
  1. 4-PH alpha-2
  2. Procollagen-proline,2-oxoglutarate-4-dioxygenase alpha-2 subunit
Enzyme 4 Gene Name P4HA2
Enzyme 4 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-2 precursor 
MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKS
WANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQR
QFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEG
DYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSH
ERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVK
LTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPK
LARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVAN
YGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKK
GTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD
Enzyme 4 Number of Residues 535
Enzyme 4 Molecular Weight 60903
Enzyme 4 Theoretical pI 5.43
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Catalyzes the posttranslational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Enzyme 4 Pathways
Enzyme 4 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-21
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 2439985 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O15460 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name P4HA2_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1608 bp 
ATGAAACTCTGGGTGTCTGCATTGCTGATGGCCTGGTTTGGTGTCCTGAGCTGTGTGCAG
GCCGAATTCTTCACCTCTATTGGGCACATGACTGACCTGATTTATGCAGAGAAAGAGCTG
GTGCAGTCTCTGAAAGAGTACATCCTTGTGGAGGAAGCCAAGCTTTCCAAGATTAAGAGC
TGGGCCAACAAAATGGAAGCCTTGACTAGCAAGTCAGCTGCTGATGCTGAGGGCTACCTG
GCTCACCCTGTGAATGCCTACAAACTGGTGAAGCGGCTAAACACAGACTGGCCTGCGCTG
GAGGACCTTGTCCTGCAGGACTCAGCTGCAGGTTTTATCGCCAACCTCTCTGTGCAGCGG
CAGTTCTTCCCCACTGATGAGGACGAGATAGGAGCTGCCAAAGCCCTGATGAGACTTCAG
GACACATACAGGCTGGACCCAGGCACAATTTCCAGAGGGGAACTTCCAGGAACCAAGTAC
CAGGCAATGCTGAGTGTGGATGACTGCTTTGGGATGGGCCGCTCGGCCTACAATGAAGGG
GACTATTATCATACGGTGTTGTGGATGGAGCAGGTGCTAAAGCAGCTTGATGCCGGGGAG
GAGGCCACCACAACCAAGTCACAGGTGCTGGACTACCTCAGCTATGCTGTCTTCCAGTTG
GGTGATCTGCACCGTGCCCTGGAGCTCACCCGCCGCCTGCTCTCCCTTGACCCAAGCCAC
GAACGAGCTGGAGGGAATCTGCGGTACTTTGAGCAGTTATTGGAGGAAGAGAGAGAAAAA
ACGTTAACAAATCAGACAGAAGCTGAGCTAGCAACCCCAGAAGGCATCTATGAGAGGCCT
GTGGACTACCTGCCTGAGAGGGATGTTTACGAGAGCCTCTGTCGTGGGGAGGGTGTCAAA
CTGACACCCCGTAGACAGAAGAGGCTTTTCTGTAGGTACCACCATGGCAACAGGGCCCCA
CAGCTGCTCATTGCCCCCTTCAAAGAGGAGGACGAGTGGGACAGCCCGCACATCGTCAGG
TACTACGATGTCATGTCTGATGAGGAAATCGAGAGGATCAAGGAGATCGCAAAACCTAAA
CTTGCACGAGCCACCGTTCGTGATCCCAAGACAGGAGTCCTCACTGTCGCCAGCTACCGG
GTTTCCAAAAGCTCCTGGCTAGAGGAAGATGATGACCCTGTTGTGGCCCGAGTAAATCGT
CGGATGCAGCATATCACAGGGTTAACAGTAAAGACTGCAGAATTGTTACAGGTTGCAAAT
TATGGAGTGGGAGGACAGTATGAACCGCACTTCGACTTCTCTAGGAATGATGAGCGAGAT
ACTTTCAAGCATTTAGGGACGGGGAATCGTGTGGCTACTTTCTTAAACTACATGAGTGAT
GTAGAAGCTGGTGGTGCCACCGTCTTCCCTGATCTGGGGGCTGCAATTTGGCCTAAGAAG
GGTACAGCTGTGTTCTGGTACAACCTCTTGCGGAGCGGGGAAGGTGACTACCGAACAAGA
CATGCTGCCTGCCCTGTGCTTGTGGGCTGCAAGTGGGTCTCCAATAAGTGGTTCCATGAA
CGAGGACAGGAGTTCTTGAGACCTTGTGGATCAACAGAAGTTGACTGA
Enzyme 4 GenBank Gene ID U90441 Link Image
Enzyme 4 GeneCard ID P4HA2 Link Image
Enzyme 4 GenAtlas ID P4HA2 Link Image
Enzyme 4 HGNC ID HGNC:8547 Link Image
Enzyme 4 Chromosome Location 5
Enzyme 4 Locus 5q31
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI: Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. J Biol Chem. 1997 Jul 11;272(28):17342-8. [PubMed Link Image]
  2. Nokelainen M, Nissi R, Kukkola L, Helaakoski T, Myllyharju J: Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues. Eur J Biochem. 2001 Oct;268(20):5300-9. [PubMed Link Image]
  3. 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]
Enzyme 4 Metabolite References
  1. 8198555;6325436
Enzyme 5 [top]
Enzyme 5 ID 5539
Enzyme 5 Name Prolyl 4-hydroxylase subunit alpha-1 precursor
Enzyme 5 Synonyms
  1. 4-PH alpha-1
  2. Procollagen-proline,2-oxoglutarate-4-dioxygenase alpha-1 subunit
Enzyme 5 Gene Name P4HA1
Enzyme 5 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-1 precursor 
MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWA
EKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQY
FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADY
YHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQR
ANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKM
TPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRL
RRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANY
GVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKG
TAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE
Enzyme 5 Number of Residues 534
Enzyme 5 Molecular Weight 61050
Enzyme 5 Theoretical pI 5.84
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Catalyzes the posttranslational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Enzyme 5 Pathways
Enzyme 5 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-17
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 190786 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P13674 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name P4HA1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1605 bp 
ATGATCTGGTATATATTAATTATAGGAATTCTGCTTCCCCAGTCTTTGGCTCATCCAGGC
TTTTTTACTTCAATTGGTCAGATGACTGATTTGATCCATACTGAGAAAGATCTGGTGACT
TCTCTGAAAGATTATATTAAGGCAGAAGAGGACAAGTTAGAACAAATAAAAAAATGGGCA
GAGAAGTTAGATCGGCTAACTAGTACAGCGACAAAAGATCCAGAAGGATTTGTTGGGCAT
CCAGTAAATGCATTCAAATTAATGAAACGTCTGAATACTGAGTGGAGTGAGTTGGAGAAT
CTGGTCCTTAAGGATATGTCAGATGGCTTTATCTCTAACCTAACCATTCAGAGACCAGTA
CTTTCTAATGATGAAGATCAGGTTGGGGCAGCCAAAGCTCTGTTACGTCTCCAGGATACC
TACAATTTGGATACAGATACCATCTCAAAGGGTAATCTTCCAGGAGTGAAACACAAATCT
TTTCTAACGGCTGAGGACTGCTTTGAGTTGGGCAAAGTGGCCTATACAGAAGCAGATTAT
TACCATACGGAACTGTGGATGGAACAAGCCCTAAGGCAACTGGATGAAGGCGAGATTTCT
ACCATAGATAAAGTCTCTGTTCTAGATTATTTGAGCTATGCGGTATATCAGCAGGGAGAC
CTGGATAAGGCACTTTTGCTCACAAAGAAGCTTCTTGAACTAGATCCTGAACATCAGAGA
GCTAATGGTAACTTAAAATATTTTGAGTATATAATGGCTAAAGAAAAAGATGTCAATAAG
TCTGCTTCAGATGACCAATCTGATCAGAAAACTACACCAAAGAAAAAAGGGGTTGCTGTG
GATTACCTGCCAGAGAGACAGAAGTACGAAATGCTGTGCCGTGGGGAGGGTATCAAAATG
ACCCCTCGGAGACAGAAAAAACTCTTTTGCCGCTACCATGATGGAAACCGTAATCCTAAA
TTTATTCTGGCTCCAGCTAAACAGGAGGATGAATGGGACAAGCCTCGTATTATTCGCTTC
CATGATATTATTTCTGATGCAGAAATTGAAATCGTCAAAGACCTAGCAAAACCAAGGCTG
AGCCGAGCTACAGTACATGACCCTGAGACTGGAAAATTGACCACAGCACAGTACAGAGTA
TCTAAGAGTGCCTGGCTCTCTGGCTATGAAAATCCTGTGGTGTCTCGAATTAATATGAGA
ATACAAGATCTAACAGGACTAGATGTTTCCACAGCAGAGGAATTACAGGTAGCAAATTAT
GGAGTTGGAGGACAGTATGAACCCCATTTTGACTTTGCACGGAAAGATGAGCCAGATGCT
TTCAAAGAGCTGGGGACAGGAAATAGAATTGCTACATGGCTGTTTTATATGAGTGATGTG
TCTGCAGGAGGAGCCACTGTTTTTCCTGAAGTTGGAGCTAGTGTTTGGCCCAAAAAAGGA
ACTGCTGTTTTCTGGTATAATCTGTTTGCCAGTGGAGAAGGAGATTATAGTACACGGCAT
GCAGCCTGTCCAGTGCTAGTTGGCAACAAATGGGTATCCAATAAATGGCTCCATGAACGT
GGACAAGAATTTCGAAGACCTTGTACGTTGTCAGAATTGGAATGA
Enzyme 5 GenBank Gene ID M24486 Link Image
Enzyme 5 GeneCard ID P4HA1 Link Image
Enzyme 5 GenAtlas ID P4HA1 Link Image
Enzyme 5 HGNC ID HGNC:8546 Link Image
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10q21.3-q23.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Helaakoski T, Vuori K, Myllyla R, Kivirikko KI, Pihlajaniemi T: Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4392-6. [PubMed Link Image]
  2. Helaakoski T, Veijola J, Vuori K, Rehn M, Chow LT, Taillon-Miller P, Kivirikko KI, Pihlajaniemi T: Structure and expression of the human gene for the alpha subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues. J Biol Chem. 1994 Nov 11;269(45):27847-54. [PubMed Link Image]
Enzyme 5 Metabolite References
  1. 8198555;6325436
Enzyme 6 [top]
Enzyme 6 ID 5699
Enzyme 6 Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 precursor
Enzyme 6 Synonyms
  1. Lysyl hydroxylase 1
  2. LH1
Enzyme 6 Gene Name PLOD1
Enzyme 6 Protein Sequence >Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 precursor 
MRPLLLLALLGWLLLAEAKGDAKPEDNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGL
GEDWNVEKGTSAGGGQKVRLLKKALEKHADKEDLVILFADSYDVLFASGPRELLKKFRQA
RSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQ
LFYTKIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLI
HGNGPTKLQLNYLGNYIPRFWTFETGCTVCDEGLRSLKGIGDEALPTVLVGVFIEQPTPF
VSLFFQRLLRLHYPQKHMRLFIHNHEQHHKAQVEEFLAQHGSEYQSVKLVGPEVRMANAD
ARNMGADLCRQDRSCTYYFSVDADVALTEPNSLRLLIQQNKNVIAPLMTRHGRLWSNFWG
ALSADGYYARSEDYVDIVQGRRVGVWNVPYISNIYLIKGSALRGELQSSDLFHHSKLDPD
MAFCANIRQQDVFMFLTNRHTLGHLLSLDSYRTTHLHNDLWEVFSNPEDWKEKYIHQNYT
KALAGKLVETPCPDVYWFPIFTEVACDELVEEMEHFGQWSLGNNKDNRIQGGYENVPTID
IHMNQIGFEREWHKFLLEYIAPMTEKLYPGYYTRAQFDLAFVVRYKPDEQPSLMPHHDAS
TFTINIALNRVGVDYEGGGCRFLRYNCSIRAPRKGWTLMHPGRLTHYHEGLPTTRGTRYI
AVSFVDP
Enzyme 6 Number of Residues 727
Enzyme 6 Molecular Weight 83551
Enzyme 6 Theoretical pI 6.94
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
  • procollagen-lysine 5-dioxygenase activity
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
  • endoplasmic reticulum
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • organelle
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links
Enzyme 6 Pathways
Enzyme 6 Reactions
  • procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-18
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 190074 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q02809 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PLOD1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2184 bp 
ATGCGGCCCCTGCTGCTACTGGCCCTGCTGGGCTGGCTGCTGCTGGCCGAAGCGAAGGGC
GACGCCAAGCCGGAGGACAACCTTTTAGTCCTCACGGTGGCCACTAAGGAGACCGAGGGA
TTCCGTCGCTTCAAGCGCTCAGCTCAGTTCTTCAACTACAAGATCCAGGCGCTTGGCCTA
GGGGAGGACTGGAATGTGGAGAAGGGGACGTCGGCAGGTGGAGGGCAGAAGGTCCGGCTG
CTGAAGAAAGCTCTGGAGAAGCACGCAGACAAGGAGGATCTGGTCATTCTCTTCACAGAC
AGCTATGACGTGCTGTTTGCATCGGGGCCCCGGGAGCTCCTGAAGAAGTTCCGGCAGGCC
AGGAGCCAGGTGGTCTTCTCTGCTGAGGAGCTCATCTACCCAGACCGCAGGCTGGAGACC
AAGTATCCGGTGGTGTCCGATGGCAAGAGGTTCCTGGGCTCTGGAGGCTTCATCGGTTAT
GCCCCCAACCTCAGCAAACTGGTGGCCGAGTGGGAGGGCCAGGACAGCGACAGCGATCAG
CTGTTTTACACCAAGATCTTCTTGGACCCGGAGAAGAGGGAGCAGATCAATATCACCCTG
GACCACCGCTGCCGTATCTTCCAGAACCTGGATGGAGCCTTGGATGAGGTCGTGCTCAAG
TTTGAAATGGGCCATGTGAGAGCGAGGAACCTGGCCTATGACACCCTCCCGGTCCTGATC
CATGGCAACGGGCCAACCAAGCTGCAGTTGAACTACCTGGGCAACTACATCCCGCGCTTC
TGGACCTTCGAAACAGGCTGCACCGTGTGTGACGAAGGCTTGCGCAGCCTCAAGGGCATT
GGGGATGAAGCTCTGCCCACGGTCCTGGTCGGCGTGTTCATCGAACAGCCCACGCCGTTT
GTGTCCCTGTTCTTCCAGCGGCTCCTGCGGCTCCACTACCCCCAGAAACACATGCGACTT
TTCATCCACAACCACGAGCAGCACCACAAGGCTCAGGTGGAAGAGTTCCTGGCACAGCAT
GGCAGCGAGTACCAGTCTGTGAAGCTGGTGGGCCCTGAGGTGCGGATGGCGAATGCAGAT
GCCAGGAACATGGGCGCAGACCTGTGCCGGCAGGACCGCAGCTGCACCTACTACTTCAGC
GTGGATGCTGACGTGGCCCTGACCGAGCCCAACAGCCTGCGGCTGCTGATCCAACAGAAC
AAGAATGTCATTGCCCCGCTGATGACCCGGCATGGGAGGCTGTGGTCGAACTTCTGGGGG
GCTCTCAGTGCAGATGGCTACTATGCCCGTTCCGAGGACTACGTGGACATTGTGCAGGGG
CGGCGTGTTGGTGTCTGGAATGTGCCCTATATTTCAAACATCTACTTGATCAAGGGCAGT
GCCCTGCGGGGTGAGCTGCAGTCCTCAGATCTCTTCCACCACAGCAAGCTGGACCCCGAC
ATGGCCTTCTGTGCCAACATCCGGCAGCAGGATGTGTTCATGTTCCTGACCAACCGGCAC
ACCCTTGGCCATCTGCTCTCCCTAGACAGCTACCGCACCACCCACCTGCACAACGACCTC
TGGGAGGTGTTCAGCAACCCCGAGGACTGGAAGGAGAAGTACATCCACCAGAACTACACC
AAAGCCCTGGCAGGGAAGCTGGTGGAGACGCCCTGCCCGGATGTCTATTGGTTCCCCATC
TTCACGGAGGTGGCCTGTGATGAGCTGGTGGAGGAGATGGAGCACTTTGGCCAGTGGTCT
CTGGGCAACAACAAGGACAACCGCATCCAGGGTGGCTACGAGAACGTGCCGACTATTGAC
ATCCACATGAACCAGATCGGCTTTGAGCGGGAGTGGCACAAATTCCTGCTGGAGTACATT
GCGCCCATGACGGAGAAGCTCTACCCCGGCTACTACACCAGGGCCCAGTTTGACCTGGCC
TTTGTCGTCCGCTACAAGCCTGATGAGCAGCCCTCACTGATGCCACACCATGATGCCTCC
ACCTTCACCATCAACATCGCCCTGAACCGAGTCGGGGTGGATTACGAGGGCGGGGGCTGT
CGGTTCCTGCGCTACAACTGTTCCATCCGAGCCCCAAGGAAGGGCTGGACCCTCATGCAC
CCTGGACGACTCACGCATTACCATGAGGGGCTCCCCACCACCAGGGGCACCCGCTACATC
GCAGTCTCCTTCGTCGATCCCTAA
Enzyme 6 GenBank Gene ID L06419 Link Image
Enzyme 6 GeneCard ID PLOD1 Link Image
Enzyme 6 GenAtlas ID PLOD1 Link Image
Enzyme 6 HGNC ID HGNC:9081 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1p36.3-p36.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Hautala T, Byers MG, Eddy RL, Shows TB, Kivirikko KI, Myllyla R: Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3----p36.2. Genomics. 1992 May;13(1):62-9. [PubMed Link Image]
  2. Heikkinen J, Hautala T, Kivirikko KI, Myllyla R: Structure and expression of the human lysyl hydroxylase gene (PLOD): introns 9 and 16 contain Alu sequences at the sites of recombination in Ehlers-Danlos syndrome type VI patients. Genomics. 1994 Dec;24(3):464-71. [PubMed Link Image]
  3. Pirskanen A, Kaimio AM, Myllyla R, Kivirikko KI: Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity. J Biol Chem. 1996 Apr 19;271(16):9398-402. [PubMed Link Image]
  4. Ha VT, Marshall MK, Elsas LJ, Pinnell SR, Yeowell HN: A patient with Ehlers-Danlos syndrome type VI is a compound heterozygote for mutations in the lysyl hydroxylase gene. J Clin Invest. 1994 Apr;93(4):1716-21. [PubMed Link Image]
  5. Brinckmann J, Acil Y, Feshchenko S, Katzer E, Brenner R, Kulozik A, Kugler S: Ehlers-Danlos syndrome type VI: lysyl hydroxylase deficiency due to a novel point mutation (W612C). Arch Dermatol Res. 1998 Apr;290(4):181-6. [PubMed Link Image]
  6. Yeowell HN, Allen JD, Walker LC, Overstreet MA, Murad S, Thai SF: Deletion of cysteine 369 in lysyl hydroxylase 1 eliminates enzyme activity and causes Ehlers-Danlos syndrome type VI. Matrix Biol. 2000 Feb;19(1):37-46. [PubMed Link Image]
Enzyme 6 Metabolite References
  1. Myllyla R, Majamaa K, Gunzler V, Hanauske-Abel HM, Kivirikko KI: Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J Biol Chem. 1984 May 10;259(9):5403-5. [PubMed Link Image]
Enzyme 7 [top]
Enzyme 7 ID 5700
Enzyme 7 Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 precursor
Enzyme 7 Synonyms
  1. Lysyl hydroxylase 2
  2. LH2
Enzyme 7 Gene Name PLOD2
Enzyme 7 Protein Sequence >Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 precursor 
MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAK
YFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAG
GPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIV
QQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARA
KNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSI
GVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKHEIKTIKIV
GPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTR
HGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGVWNVPYMANVYLIKGKTLRSEMNERN
YFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDW
KEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGKWSGGKHHDSRIS
GGYENVPTDDIHMKQVDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQ
RSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEG
LPVKNGTRYIAVSFIDP
Enzyme 7 Number of Residues 737
Enzyme 7 Molecular Weight 84686
Enzyme 7 Theoretical pI 6.69
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
  • procollagen-lysine 5-dioxygenase activity
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
  • endoplasmic reticulum
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • organelle
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links
Enzyme 7 Pathways
Enzyme 7 Reactions
  • procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-25
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 2138314 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O00469 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PLOD2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2214 bp 
ATGGGGGGATGCACGGTGAAGCCTCAGCTGCTGCTCCTGGCGCTCGTCCTCCACCCCTGG
AATCCCTGTCTGGGTGCGGACTCGGAGAAGCCCTCGAGCATCCCCACAGATAAATTATTA
GTCATAACTGTAGCAACAAAAGAAAGTGATGGATTCCATCGATTTATGCAGTCAGCCAAA
TATTTCAATTATACTGTGAAGGTCCTTGGTCAAGGAGAAGAATGGAGAGGTGGTGATGGA
ATTAATAGTATTGGAGGGGGCCAGAAAGTGAGATTAATGAAAGAAGTCATGGAACACTAT
GCTGATCAAGATGATCTGGTTGTCATGTTTACTGAATGCTTTGATGTCATATTTGCTGGT
GGTCCAGAAGAAGTTCTAAAAAAATTCCAAAAGGCAAACCACAAAGTGGTCTTTGCAGCA
GATGGAATTTTGTGGCCAGATAAAAGACTAGCAGACAAGTATCCTGTTGTGCACATTGGG
AAACGCTATCTGAATTCAGGAGGATTTATTGGCTATGCTCCATATGTCAACCGTATAGTT
CAACAATGGAATCTCCAGGATAATGATGATGATCAGCTCTTTTACACTAAAGTTTACATT
GATCCACTGAAAAGGGAAGCTATTAACATCACATTGGATCACAAATGCAAAATTTTCCAG
ACCTTAAATGGAGCTGTAGATGAAGTTGTTTTAAAATTTGAAAATGGCAAAGCCAGAGCT
AAGAATACATTTTATGAAACATTACCAGTGGCAATTAATGGAAATGGACCCACCAAGATT
CTCCTGAATTATTTTGGAAACTATGTACCCAATTCATGGACACAGGATAATGGCTGCACT
CTTTGTGAATTCGATACAGTCGACTTGTCTGCAGTAGATGTCCATCCAAACGTATCAATA
GGTGTTTTTATTGAGCAACCAACCCCTTTTCTACCTCGGTTTCTGGACATATTGTTGACA
CTGGATTACCCAAAAGAAGCACTTAAACTTTTTATTCATAACAAAGAAGTTTATCATGAA
AAGGACATCAAGGTATTTTTTGATAAAGCTAAGCATGAAATCAAAACTATAAAAATAGTA
GGACCAGAAGAAAATCTAAGTCAAGCGGAAGCCAGAAACATGGGAATGGACTTTTGCCGT
CAGGATGAAAAGTGTGATTATTACTTTAGTGTGGATGCAGATGTTGTTTTGACAAATCCA
AGGACTTTAAAAATTTTGATTGAACAAAACAGAAAGATCATTGCTCCTCTTGTAACTCGT
CATGGAAAGCTGTGGTCCAATTTCTGGGGAGCATTGAGTCCTGATGGATACTATGCACGA
TCTGAAGATTATGTGGATATTGTTCAAGGGAATAGAGTAGGAGTATGGAATGTCCCATAT
ATGGCTAATGTGTACTTAATTAAAGGAAAGACACTCCGATCAGAGATGAATGAAAGGAAC
TATTTTGTTCGTGATAAACTGGATCCTGATATGGCTCTTTGCCGAAATGCTAGAGAAATG
GGTGTATTTATGTACATTTCTAATAGACATGAATTTGGAAGGCTATTATCCACTGCTAAT
TACAATACTTCCCATTATAACAATGACCTCTGGCAGATTTTTGAAAATCCTGTGGACTGG
AAGGAAAAGTATATAAACCGTGATTATTCAAAGATTTTCACTGAAAATATAGTTGAACAG
CCCTGTCCAGATGTCTTTTGGTTCCCCATATTTTCTGAAAAAGCCTGTGATGAATTGGTA
GAAGAAATGGAACATTACGGCAAATGGTCTGGGGGAAAACATCATGATAGCCGTATATCT
GGTGGTTATGAAAATGTCCCAACTGATGATATCCACATGAAGCAAGTTGATCTGGAGAAT
GTATGGCTTGATTTTATCCGGGAGTTCATTGCACCAGTTACACTGAAGGTCTTTGCAGGC
TATTATACGAAGGGATTTGCACTACTGAATTTTGTAGTAAAATACTCCCCTGAACGACAG
CGTTCTCTTCGTCCTCATCATGATGCTTCTACATTTACCATAAACATTGCACTTAATAAC
GTGGGAGAAGACTTTCAGGGAGGTGGTTGCAAATTTCTAAGGTACAATTGCTCTATTGAG
TCACCACGAAAAGGCTGGAGCTTCATGCATCCTGGGAGACTCACACATTTGCATGAAGGA
CTTCCTGTTAAAAATGGAACAAGATACATTGCAGTGTCATTTATAGATCCCTAA
Enzyme 7 GenBank Gene ID U84573 Link Image
Enzyme 7 GeneCard ID PLOD2 Link Image
Enzyme 7 GenAtlas ID PLOD2 Link Image
Enzyme 7 HGNC ID HGNC:9082 Link Image
Enzyme 7 Chromosome Location 3
Enzyme 7 Locus 3q23-q24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Valtavaara M, Papponen H, Pirttila AM, Hiltunen K, Helander H, Myllyla R: Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. J Biol Chem. 1997 Mar 14;272(11):6831-4. [PubMed Link Image]
  2. Yeowell HN, Walker LC: Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene. Matrix Biol. 1999 Apr;18(2):179-87. [PubMed Link Image]
  3. van der Slot AJ, Zuurmond AM, Bardoel AF, Wijmenga C, Pruijs HE, Sillence DO, Brinckmann J, Abraham DJ, Black CM, Verzijl N, DeGroot J, Hanemaaijer R, TeKoppele JM, Huizinga TW, Bank RA: Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis. J Biol Chem. 2003 Oct 17;278(42):40967-72. Epub 2003 Jul 24. [PubMed Link Image]
Enzyme 7 Metabolite References
  1. Myllyla R, Majamaa K, Gunzler V, Hanauske-Abel HM, Kivirikko KI: Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J Biol Chem. 1984 May 10;259(9):5403-5. [PubMed Link Image]
Enzyme 8 [top]
Enzyme 8 ID 5701
Enzyme 8 Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 precursor
Enzyme 8 Synonyms
  1. Lysyl hydroxylase 3
  2. LH3
Enzyme 8 Gene Name PLOD3
Enzyme 8 Protein Sequence >Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 precursor 
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAE
FFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAG
SPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIV
RQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRI
RNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFL
AVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLV
GPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSR
HGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRD
VFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDW
KEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRL
AGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDE
QPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHE
GLPTTWGTRYIMVSFVDP
Enzyme 8 Number of Residues 738
Enzyme 8 Molecular Weight 84786
Enzyme 8 Theoretical pI 5.95
Enzyme 8 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
  • procollagen-lysine 5-dioxygenase activity
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
  • endoplasmic reticulum
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • organelle
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links
Enzyme 8 Pathways
Enzyme 8 Reactions
  • procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-24
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 3153235 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O60568 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PLOD3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2217 bp 
ATGACCTCCTCGGGGCCTGGACCCCGGTTCCTGCTGCTGCTGCCGCTGCTGCTGCCCCCT
GCGGCCTCAGCCTCCGACCGGCCCCGGGGCCGAGACCCGGTCAACCCAGAGAAGCTGCTG
GTGATCACTGTGGCCACAGCTGAAACCGAGGGGTACCTGCGTTTCCTGCGCTCTGCGGAG
TTCTTCAACTACACTGTGCGGACCCTGGGCCTGGGAGAGGAGTGGCGAGGGGGTGATGTG
GCTCGAACAGTTGGTGGAGGACAGAAGGTCCGGTGGTTAAAGAAGGAAATGGAGAAATAC
GCTGACCGGGAGGATATGATCATCATGTTTGTGGATAGCTACGACGTGATTCTGGCCGGC
AGCCCCACAGAGCTGCTGAAGAAGTTCGTCCAGAGTGGCAGCCGCCTGCTCTTCTCTGCA
GAGAGCTTCTGCTGGCCCGAGTGGGGGCTGGCGGAGCAGTACCCTGAGGTGGGCACGGGG
AAGCGCTTCCTCAATTCTGGTGGATTCATCGGTTTTGCCACCACCATCCACCAAATCGTG
CGCCAGTGGAAGTACAAGGATGATGACGACGACCAGCTGTTCTACACACGGCTCTACCTG
GACCCAGGACTGAGGGAGAAACTCAGCCTTAATCTGGATCATAAGTCTCGGATCTTTCAG
AACCTCAACGGGGCTTTAGATGAAGTGGTTTTAAAGTTTGATCGGAACCGTGTGCGTATC
CGGAACGTGGCCTACGACACGCTCCCCATTGTGGTCCATGGAAACGGTCCCACTAAGCTG
CAGCTCAACTACCTGGGAAACTACGTCCCCAATGGCTGGACTCCTGAGGGAGGCTGTGGC
TTCTGCAACCAGGACCGGAGGACACTCCCGGGGGGGCAGCCTCCCCCCCGGGTGTTTCTG
GCCGTGTTTGTGGAACAGCCTACTCCGTTTCTGCCCCGCTTCCTGCAGCGGCTGCTACTC
CTGGACTATCCCCCCGACAGGGTCACCCTTTTCCTGCACAACAACGAGGTCTTCCATGAA
CCCCACATCGCTGACTCCTGGCCGCAGCTCCAGGACCACTTCTCAGCTGTGAAGCTCGTG
GGGCCGGAGGAGGCTCTGAGCCCAGGCGAGGCCAGGGACATGGCCATGGACCTGTGTCGG
CAGGACCCCGAGTGTGAGTTCTACTTCAGCCTGGACGCCGACGCTGTCCTCACCAACCTG
CAGACCCTGCGTATCCTCATTGAGGAGAACAGGAAGGTGATCGCCCCCATGCTGTCCCGC
CACGGCAAGCTGTGGTCCAACTTCTGGGGCGCCCTGAGCCCCGATGAGTACTACGCCCGC
TCCGAGGACTACGTGGAGCTGGTGCAGCGGAAGCGAGTGGGTGTGTGGAATGTACCATAC
ATCTCCCAGGCCTATGTGATCCGGGGTGATACCCTGCGGATGGAGCTGCCCCAGAGGGAT
GTGTTCTCGGGCAGTGACACAGACCCGGACATGGCCTTCTGTAAGAGCTTTCGAGACAAG
GGCATCTTCCTCCATCTGAGCAATCAGCATGAATTTGGCCGGCTCCTGGCCACTTCCAGA
TACGACACGGAGCACCTGCACCCCGACCTCTGGCAGATCTTCGACAACCCCGTCGACTGG
AAGGAGCAGTACATCCACGAGAACTACAGCCGGGCCCTGGAAGGGGAAGGAATCGTGGAG
CAGCCATGCCCGGACGTGTACTGGTTCCCACTGCTGTCAGAACAAATGTGTGATGAGCTG
GTGGCAGAGATGGAGCACTACGGCCAGTGGTCAGGCGGCCGGCATGAGGATTCAAGGCTG
GCTGGAGGCTACGAGAATGTGCCCACCGTGGACATCCACATGAAGCAGGTGGGGTACGAG
GACCAGTGGCTGCAGCTGCTGCGGACGTATGTGGGCCCCATGACCGAGAGCCTGTTTCCC
GGTTACCACACCAAGGCGCGGGCGGTGATGAACTTTGTGGTTCGCTACCGGCCAGACGAG
CAGCCGTCTCTGCGGCCACACCACGACTCATCCACCTTCACCCTCAACGTTGCCCTCAAC
CACAAGGGCCTGGACTATGAGGGAGGTGGCTGCCGCTTCCTGCGCTACGACTGTGTGATC
TCCTCCCCGAGGAAGGGCTGGGCACTCCTGCACCCCGGCCGCCTCACCCACTACCACGAG
GGGCTGCCAACGACCTGGGGCACACGCTACATCATGGTGTCCTTTGTCGACCCCTGA
Enzyme 8 GenBank Gene ID AF046889 Link Image
Enzyme 8 GeneCard ID PLOD3 Link Image
Enzyme 8 GenAtlas ID PLOD3 Link Image
Enzyme 8 HGNC ID HGNC:9083 Link Image
Enzyme 8 Chromosome Location 7
Enzyme 8 Locus 7q22
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Valtavaara M, Szpirer C, Szpirer J, Myllyla R: Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) J Biol Chem. 1998 May 22;273(21):12881-6. [PubMed Link Image]
  2. Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko KI: Cloning and characterization of a third human lysyl hydroxylase isoform. Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10482-6. [PubMed Link Image]
  3. Rautavuoma K, Passoja K, Helaakoski T, Kivirikko KI: Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3). Matrix Biol. 2000 Feb;19(1):73-9. [PubMed Link Image]
  4. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
Enzyme 8 Metabolite References
  1. Myllyla R, Majamaa K, Gunzler V, Hanauske-Abel HM, Kivirikko KI: Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J Biol Chem. 1984 May 10;259(9):5403-5. [PubMed Link Image]
Enzyme 9 [top]
Enzyme 9 ID 8308
Enzyme 9 Name Protein disulfide-isomerase precursor
Enzyme 9 Synonyms
  1. PDI
  2. Prolyl 4- hydroxylase subunit beta
  3. Cellular thyroid hormone-binding protein
  4. p55
Enzyme 9 Gene Name P4HB
Enzyme 9 Protein Sequence >Protein disulfide-isomerase precursor 
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALA
PEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGR
EADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAID
DIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEF
TEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQR
ILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQEL
PEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENI
VIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGD
DDDLEDLEEAEEPDMEEDDDQKAVKDEL
Enzyme 9 Number of Residues 508
Enzyme 9 Molecular Weight 57117
Enzyme 9 Theoretical pI 4.49
Enzyme 9 GO Classification
Function
  • catalytic activity
  • electron transporter activity
  • isomerase activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
  • endoplasmic reticulum
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • organelle
Enzyme 9 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 9 Specific Function This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • Catalyses the rearrangement of -S-S- bonds in proteins
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-17
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 35655 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P07237 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PDIA1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1527 bp 
ATGCTGCGCCGCGCTCTGCTGTGCCTGCCGTGGNCCGCCCTGGTGCGCGCCGACGCCCCC
GAGGAGGAGGACCACGTCTTGGTGCTGCGGAAAAGCAACTTCGCGGAGGCGCTGGCGGCC
CACAAGTACCCGCCGGTGGAGTTCCATGCCCCCTGGTGTGGCCACTGCAAGGCTCTGGCC
CCTGAGTATGCCAAAGCCGCTGGGAAGCTGAAGGCAGAAGGTTCCGAGATCAGGTTGGCC
AAGGTGGACGCCACGGAGGAGTCTGACCTAGCCCAGCAGTACGGCGTGCGCGGCTATCCC
ACCATCAAGTTCTTCAGGAATGGAGACACGGCTTCCCCCAAGGAATATACAGCTGGCAGA
GAGGCTGATGACATCGTGAACTGGCTGAAGAAGCGCACGGGCCCGGCTGCCACCACCCTG
CCTGACGGCGCAGCTGCAGAGTCCTTGGTGGAGTCCAGCGAGGTGGCCGTCATCGGCTTC
TTCAAGGACGTGGAGTCGGACTCTGCCAAGCAGTTTTTGCAGGCAGCAGAGGCCATCGAT
GACATACCATTTGGGATCACTTCCAACAGTGACGTGTTCTCCAAATACCAGCTCGACAAA
GATGGGGTTGTCCTCTTTAAGAAGTTTGATGAAGGCCGGAACAACTTTGAAGGGGAGGTC
ACCAAGGAGAACCTGCTGGACTTTATCAAACACAACCAGCTGCCCCTTGTCATCGAGTTC
ACCGAGCAGACAGCCCCGAAGATTTTTGGAGGTGAAATCAAGACTCACATCCTGCTGTTC
TTGCCCAAGAGTGTGTCTGACTATGACGGCAAACTGAGCAACTTCAAAACAGCAGCCGAG
AGCTTCAAGGGCAAGATCCTGTTCATCTTCATCGACAGCGACCACACCGACAACCAGCGC
ATCCTCGAGTTCTTTGGCCTGAAGAAGGAAGAGTGCCCGGCCGTGCGCCTCATCACCTTG
GAGGAGGAGATGACCAAGTACAAGCCCGAATCGGAGGAGCTGACGGCAGAGAGGATCACA
GAGTTCTGCCACCGCTTCCTGGAGGGCAAAATCAAGCCCCACCTGATGAGCCAGGAGCTG
CCGGAGGACTGGGACAAGCAGCCTGTCAAGGTGCTTGTTGGGAAGAACTTTGAAGACGTG
GCTTTTGATGAGAAAAAAAACGTCTTTGTGGAGTTCTATGCCCCATGGTGTGGTCACTGC
AAACAGTTGGCTCCCATTTGGGATAAACTGGGAGAGACGTACAAGGACCATGAGAACATC
GTCATCGCCAAGATGGACTCGACTGCCAACGAGGTGGAGGCCGTCAAAGTGCACGGCTTC
CCCACACTCGGGTTCTTTCCTGCCAGTGCCGACAGGACGGTCATTGATTACAACGGGGAA
CGCACGCTGGATGGTTTTAAGAAATTCCTAGAGAGCGGTGGCCAAGATGGGGCAGGGGAT
GTTGACGACCTCGAGGACCTCGAAGAAGCAGAGGAGCCAGACATGGAGGAAGACGATGAC
CAGAAAGCTGTGAAAGATGAACTGTAA
Enzyme 9 GenBank Gene ID X05130 Link Image
Enzyme 9 GeneCard ID P4HB Link Image
Enzyme 9 GenAtlas ID P4HB Link Image
Enzyme 9 HGNC ID HGNC:8548 Link Image
Enzyme 9 Chromosome Location 17
Enzyme 9 Locus 17q25
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Pihlajaniemi T, Helaakoski T, Tasanen K, Myllyla R, Huhtala ML, Koivu J, Kivirikko KI: Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 1987 Mar;6(3):643-9. [PubMed Link Image]
  2. Cheng SY, Gong QH, Parkison C, Robinson EA, Appella E, Merlino GT, Pastan I: The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum. J Biol Chem. 1987 Aug 15;262(23):11221-7. [PubMed Link Image]
  3. Tasanen K, Parkkonen T, Chow LT, Kivirikko KI, Pihlajaniemi T: Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase. J Biol Chem. 1988 Nov 5;263(31):16218-24. [PubMed Link Image]
  4. Tasanen K, Oikarinen J, Kivirikko KI, Pihlajaniemi T: Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements. J Biol Chem. 1992 Jun 5;267(16):11513-9. [PubMed Link Image]
  5. Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed Link Image]
  6. 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]
  7. Ward LD, Hong J, Whitehead RH, Simpson RJ: Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis. 1990 Oct;11(10):883-91. [PubMed Link Image]
  8. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  9. Urade R, Oda T, Ito H, Moriyama T, Utsumi S, Kito M: Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease. J Biochem (Tokyo). 1997 Oct;122(4):834-42. [PubMed Link Image]
  10. Morris JI, Varandani PT: Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase). Biochim Biophys Acta. 1988 Feb 28;949(2):169-80. [PubMed Link Image]
  11. Bauw G, Rasmussen HH, van den Bulcke M, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes. Electrophoresis. 1990 Jul;11(7):528-36. [PubMed Link Image]
  12. Ko HS, Uehara T, Nomura Y: Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death. J Biol Chem. 2002 Sep 20;277(38):35386-92. Epub 2002 Jul 2. [PubMed Link Image]
  13. Kemmink J, Darby NJ, Dijkstra K, Scheek RM, Creighton TE: Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase. Protein Sci. 1995 Dec;4(12):2587-93. [PubMed Link Image]
  14. Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE: Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry. 1996 Jun 18;35(24):7684-91. [PubMed Link Image]
  15. Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, Darby NJ: The structure in solution of the b domain of protein disulfide isomerase. J Biomol NMR. 1999 Apr;13(4):357-68. [PubMed Link Image]
Enzyme 9 Metabolite References
  1. 8198555;6325436
Enzyme 10 [top]
Enzyme 10 ID 8667
Enzyme 10 Name Solute carrier family 23 member 1
Enzyme 10 Synonyms
  1. Sodium-dependent vitamin C transporter 1
  2. hSVCT1
  3. Na(+/L-ascorbic acid transporter 1
  4. Yolk sac permease-like molecule 3
Enzyme 10 Gene Name SLC23A1
Enzyme 10 Protein Sequence >Solute carrier family 23 member 1 
MRAQEDLEGRTQHETTRDPSTPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTI
AVPFLLAEALCVGHDQHMVSQLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKA
ILALERWKCPPEEEIYGNWSLPLNTSHIWHPRIREVQGAIMVSSVVEVVIGLLGLPGALL
NYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIILFSQYLRNLTFLLPVYRW
GKGLTLLRIQIFKMFPIMLAIMTVWLLCYVLTLTDVLPTDPKAYGFQARTDARGDIMAIA
PWIRIPYPCQWGLPTVTAAAVLGMFSATLAGIIESIGDYYACARLAGAPPPPVHAINRGI
FTEGICCIIAGLLGTGNGSTSSSPNIGVLGITKVGSRRVVQYGAAIMLVLGTIGKFTALF
ASLPDPILGGMFCTLFGMITAVGLSNLQFVDMNSSRNLFVLGFSMFFGLTLPNYLESNPG
AINTGILEVDQILIVLLTTEMFVGGCLAFILDNTVPGSPEERGLIQWKAGAHANSDMSSS
LKSYDFPIGMGIVKRITFLKYIPICPVFKGFSSSSKDQIAIPEDTPENTETASVCTKV
Enzyme 10 Number of Residues 598
Enzyme 10 Molecular Weight 64816
Enzyme 10 Theoretical pI 6.58
Enzyme 10 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 10 General Function Nucleotide transport and metabolism
Enzyme 10 Specific Function Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-274
Enzyme 10 Transmembrane Regions
  • 53-73 82-102 104-124 160-180 208-228 251-271 313-333 359-379 403-423 427-447 458-478 491-511
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 3789785 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9UHI7 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name S23A1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1797 bp 
ATGAGGGCCCAGGAGGACCTCGAGGGCCGGACACAGCATGAAACCACCAGGGACCCCTCG
ACCCCGCTACCCACAGAGCCTAAGTTTGACATGTTGTACAAGATCGAGGACGTGCCACCT
TGGTACCTGTGCATCCTGCTAGGGTTCCAGCACATCCATGACTGCTTACGTGGTACCATC
GCCGTGCCCTTCCTGCTGGCTGAGGCGCTGTGTGTGGGCCACAGCCAGACACTCCATTGT
CAGCTCATCGGCACCATCTTCACGTGCGTGGGCATCACCACTCTCATCCAGACCACCGTG
GGCATCCGGCTGCCGCTGTTCCAGGCCAGTGCCTTTGCATTTCTGGTTCCAGCCAAAGCC
ATACTGGCTCTGGAGAGATGGAAATGCCCCCCGGAAGAGGAGATCTACGGTAACTCCAGT
CTGCCCCTGAACACCTCTCATATTTGGCACCCACGGAATCGGGAGGTCCAGGGTGCAATC
ATGGTGTCCAGCGTGGTGGAGGTGGTGATTGGCCTGCTGGGGCTGCCTGGGGCCCTGCTC
AACTCACTTGGGCCTCTCACAGTCACCCCCACTGTCTCCCTCATTGGCCTTTCTGTCTTC
CAAGCTGCTGGCGACCGACCTGGCTCCCACTGGGGCATCTCAGCTTGCTCCATTCTCCTG
ATCATCCTCTTCTCCCAGTACCTGCGCAACCTCACCTTCCTGCTGCCTGTCTACCGCTGG
GGCAAGGGGCTCACTCTCCTCCGCATCCAGATCTTCAAAATGTTTCCTATCATGCTGGCC
ATCATGACCGTGTGGCTGCTCTGCATTGTCCTGACCTTGACAGACGTGCTGCCCACAGAC
CCAAAAGCCATTGGCTTCCAGGCACGAACCGATGCCCGTGGTGACATCATGGCTATTGCA
CCCTGGATCCGCATCCCCTACCCCTGTCAGTGGGGCCTGCCCACGGTGACTGCGGCTGCT
GTCCTGGGAATGTTCAGCGCCACTCTGGCAGGCATCATTGAGTCCATCGGAGATTACTAC
GCCTGTGCCCGCCTGGCTGGTGCACCACCCCCTCCAGTACATGCTATCAACAGGGGCATC
TTCACCGAAGGCATTTGCTGCATCATCGCGGGGCTATTGGGCACGGGCAACGGGTCCACC
TCGTCCAGTCCCAACATTGGCGTCCTGGGAATTACCAAGGTGGGCAGCCGGCGCGTGGTG
CAGTATGGTGCGGCTATCATGCTGGTCCTGGGCACCATCGGCAAGTTCACGGCCCTCTTC
GCCTCGCTCCCTGACCCCATCCTGGGGGGCATGTTCTGCAGTCTCTTTGGCATGATTACA
GCTGTGGGGCTGTCCAACCTGCAATTTGTGGCACTGAACTCCTCTCGCAACCTCTTCGTG
CTGGGATTTTCCATGTTCTTCGGGCTCACGCTGCCCAATTACCTGGAGTCCAACCCTGGC
GCCATCAATACAGGCATTCTTGAAGTGGATCAGATTCTGATTGTGCTGCTGACCACGGAG
ATGTTTGTGGGCGGGTGCCTTGCTTTCATACTTGACAACACAGTGCCAGGGAGCCCAGAG
GAGCGTGGTCTGATACAGTGGAAAGCTGGGGCTCATGCCAACAGTGACATGTCTTCCAGC
CTGAAGAGCTACGATTTCCCATTTGGGATGGGCATAGTAAAAAGAATTACCTTTCTGAAA
TACATTCCTATCTGCCCAGTCTTCAAAGGATTTTCTTCAAGTTCAAAAGATCAGATTGCA
ATTCCAGAAGACACTCCAGAAAATACAGAAACTGCATCTGTGTGCACCAAGGTCTGA
Enzyme 10 GenBank Gene ID AF058317 Link Image
Enzyme 10 GeneCard ID SLC23A1 Link Image
Enzyme 10 GenAtlas ID SLC23A1 Link Image
Enzyme 10 HGNC ID HGNC:10974 Link Image
Enzyme 10 Chromosome Location 5
Enzyme 10 Locus 5q31.2-q31.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Faaland CA, Race JE, Ricken G, Warner FJ, Williams WJ, Holtzman EJ: Molecular characterization of two novel transporters from human and mouse kidney and from LLC-PK1 cells reveals a novel conserved family that is homologous to bacterial and Aspergillus nucleobase transporters. Biochim Biophys Acta. 1998 Nov 8;1442(2-3):353-60. [PubMed Link Image]
  2. Wang H, Dutta B, Huang W, Devoe LD, Leibach FH, Ganapathy V, Prasad PD: Human Na(+)-dependent vitamin C transporter 1 (hSVCT1): primary structure, functional characteristics and evidence for a non-functional splice variant. Biochim Biophys Acta. 1999 Nov 9;1461(1):1-9. [PubMed Link Image]
  3. Daruwala R, Song J, Koh WS, Rumsey SC, Levine M: Cloning and functional characterization of the human sodium-dependent vitamin C transporters hSVCT1 and hSVCT2. FEBS Lett. 1999 Nov 5;460(3):480-4. [PubMed Link Image]
  4. Wang Y, Mackenzie B, Tsukaguchi H, Weremowicz S, Morton CC, Hediger MA: Human vitamin C (L-ascorbic acid) transporter SVCT1. Biochem Biophys Res Commun. 2000 Jan 19;267(2):488-94. [PubMed Link Image]
  5. Erichsen HC, Eck P, Levine M, Chanock S: Characterization of the genomic structure of the human vitamin C transporter SVCT1 (SLC23A2). J Nutr. 2001 Oct;131(10):2623-7. [PubMed Link Image]
  6. Liang WJ, Johnson D, Jarvis SM: Vitamin C transport systems of mammalian cells. Mol Membr Biol. 2001 Jan-Mar;18(1):87-95. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 8682
Enzyme 11 Name Solute carrier family 23 member 2
Enzyme 11 Synonyms
  1. Sodium-dependent vitamin C transporter 2
  2. hSVCT2
  3. Na(+/L-ascorbic acid transporter 2
  4. Yolk sac permease-like molecule 2
  5. Nucleobase transporter-like 1 protein
Enzyme 11 Gene Name SLC23A2
Enzyme 11 Protein Sequence >Solute carrier family 23 member 2 
MMGIGKNTTSKSMEAGSSTEGKYEDEAKHPAFFTLPVVINGGATSSGEQDNEDTELMAIY
TTENGIAEKSSLAETLDSTGSLDPQRSDMIYTIEDVPPWYLCIFLGLQHYLTCFSGTIAV
PFLLADAMCVGYDQWATSQLIGTIFFCVGITTLLQTTFGCRLPLFQASAFAFLAPARAIL
SLDKWKCNTTDVSVANGTAELLHTEHIWYPRIREIQGAIIMSSLIEVVIGLLGLPGALLK
YIGPLTITPTVALIGLSGFQAAGERAGKHWGIAMLTIFLVLLFSQYARNVKFPLPIYKSK
KGWTAYKLQLFKMFPIILAILVSWLLCFIFTVTDVFPPDSTKYGFYARTDARQGVLLVAP
WFKVPYPFQWGLPTVSAAGVIGMLSAVVASIIESIGDYYACARLSCAPPPPIHAINRGIF
VEGLSCVLDGIFGTGNGSTSSSPNIGVLGITKVGSRRVIQCGAALMLALGMIGKFSALFA
SLPDPVLGALFCTLFGMITAVGLSNLQFIDLNSSRNLFVLGFSIFFGLVLPSYLRQNPLV
TGITGIDQVLNVLLTTAMFVGGCVAFILDNTIPGTPEERGIRKWKKGVGKGNKSLDGMES
YNLPFGMNIIKKYRCFSYLPISPTFVGYTWKGLRKSDNSRSSDEDSQATG
Enzyme 11 Number of Residues 650
Enzyme 11 Molecular Weight 70338
Enzyme 11 Theoretical pI 7.74
Enzyme 11 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 11 General Function Nucleotide transport and metabolism
Enzyme 11 Specific Function Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-333
Enzyme 11 Transmembrane Regions
  • 103-123 140-160 162-182 219-239 242-262 267-287 313-333 372-392 462-482 486-506 514-534 548-568
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 3789789 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9UGH3 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name S23A2_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1953 bp 
ATGATGGGTATTGGTAAGAATACCACATCCAAATCAATGGAGGCTGGAAGTTCAACAGAA
GGCAAATACGAAGACGAGGCAAAGCACCCAGCTTTCTTCACTCTTCCGGTGGTGATAAAT
GGAGGCGCCACCTCCAGCGGTGAGCAGGACAATGAGGACACTGAGCTCATGGCGATCTAC
ACTACGGAAAACGGCATTGCAGAAAAGAGCTCTCTCGCTGAGACCCTGGATAGCACTGGC
AGTCTGGACCCCCAGCGATCAGACATGATTTATACCATAGAAGATGTTCCTCCCTGGTAC
CTGTGTATATTTCTGGGGCTACAGCACTACCTGACATGCTTCAGCGGCACGATCGCAGTG
CCCTTCCTGTTGGCCGATGCCATGTGTGTGGGGTACGACCAGTGGGCCACCAGCCAGCTC
ATTGGGACCATTTTCTTCTGTGTGGGAATCACTACTTTGCTACAGACAACGTTTGGATGC
AGGTTACCCCTGTTTCAGACCAGTGCTTTTGCATTTTTGGCCCCTGCTCGAGCCATCCTG
TCTTTAGATAAATGGAAATGTAACACCACAGATGTTTCAGTTGCCAATGGAACAGCAGAG
CTGTTGCACACAGAACACATCTGGTATCCCCGGATCCGAGAGATCCAGGGGGCCATCATC
ATGTCCTCACTGATAGAAGTAGTCATCGGCCTCCTCGGCCTGCCTGGGGCTCTACTGAAG
TACATCGGTCCCTTGACCATTACACCCACGGTGGCCCTAATTGGCCTCTCTGGTTTCCAG
GCAGCGGGGGAGAGAGCCGGGAAGCACTGGGGCATTGCCATGCTGACAATATTCCTAGTA
TTACTGTTTTCTCAATACGCCAGAAATGTTAAATTTCCTCTCCCGATTTATAAATCCAAG
AAAGGATGGACTGCGTACAAGTTACAGCTGTTCAAAATGTTCCCTATCATCCTGGCCATC
CTGGTATCCTGGCTGCTCTGCTTCATCTTCACGGTGACAGATGTCTTCCCTCCCGACAGC
ACAAAGTATGGCTTCTATGCTCGCACAGATGCCAGGCAAGGCGTGCTTCTGGTAGCCCCG
TGGTTTAAGGTTCCATACCCATTTCAGTGGGGACTGCCCACCGTGTCTGCGGCCGGTGTC
ATCGGCATGCTCAGTGCCGTGGTCGCCAGCATCATCGAGTCTATTGGTGACTACTACGCC
TGTGCACGGCTGTCCTGTGCCCCACCCCCCCCCATCCACGCAATAAACAGGGGAATTTTC
GTGGAAGGCCTCTCCTGTGTTCTTGATGGCATATTTGGTACTGGGAATGGCTCTACTTCA
TCCAGTCCCAACATTGGAGTTTTGGGAATTACAAAGGTCGGCAGCCGCCGCGTGATACAG
TGCGGAGCAGCCCTCATGCTCGCTCTGGGCATGATCGGGAAGTTCAGCGCCCTCTTTGCG
TCCCTTCCGGATCCTGTGCTGGGAGCCCTGTTCTGCACGCTCTTTGGAATGATCACAGCT
GTTGGCCTCTCTAACCTGCAGTTCATTGATTTAAATTCTTCCCGGAACCTCTTTGTGCTT
GGATTTTCGATCTTCTTTGGGCTCGTCCTTCCAAGTTACCTCAGACAGAACCCTCTGGTC
ACAGGGATAACAGGAATCGATCAAGTGTTGAACGTCCTTCTCACAACTGCTATGTTTGTA
GGGGGCTGTGTGGCTTTTATCCTGGATAACACCATCCCAGGCACTCCAGAGGAAAGAGGA
ATCCGGAAATGGAAGAAGGGTGTGGGCAAAGGGAACAAATCACTCGACGGCATGGAGTCG
TACAATTTGCCATTTGGCATGAACATTATAAAAAAATACAGATGCTTCAGCTACTTACCC
ATCAGCCCAACCTTTGTGGGCTACACATGGAAAGGCCTCAGGAAGAGCGACAACAGCCGG
AGTTCAGATGAAGACTCCCAGGCCACGGGATAG
Enzyme 11 GenBank Gene ID AF058319 Link Image
Enzyme 11 GeneCard ID SLC23A2 Link Image
Enzyme 11 GenAtlas ID SLC23A2 Link Image
Enzyme 11 HGNC ID HGNC:10973 Link Image
Enzyme 11 Chromosome Location 20
Enzyme 11 Locus 20p13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Faaland CA, Race JE, Ricken G, Warner FJ, Williams WJ, Holtzman EJ: Molecular characterization of two novel transporters from human and mouse kidney and from LLC-PK1 cells reveals a novel conserved family that is homologous to bacterial and Aspergillus nucleobase transporters. Biochim Biophys Acta. 1998 Nov 8;1442(2-3):353-60. [PubMed Link Image]
  2. Rajan DP, Huang W, Dutta B, Devoe LD, Leibach FH, Ganapathy V, Prasad PD: Human placental sodium-dependent vitamin C transporter (SVCT2): molecular cloning and transport function. Biochem Biophys Res Commun. 1999 Sep 7;262(3):762-8. [PubMed Link Image]
  3. Daruwala R, Song J, Koh WS, Rumsey SC, Levine M: Cloning and functional characterization of the human sodium-dependent vitamin C transporters hSVCT1 and hSVCT2. FEBS Lett. 1999 Nov 5;460(3):480-4. [PubMed Link Image]
  4. Hogue DL, Ling V: A human nucleobase transporter-like cDNA (SLC23A1): member of a transporter family conserved from bacteria to mammals. Genomics. 1999 Jul 1;59(1):18-23. [PubMed Link Image]
  5. Liang WJ, Johnson D, Jarvis SM: Vitamin C transport systems of mammalian cells. Mol Membr Biol. 2001 Jan-Mar;18(1):87-95. [PubMed Link Image]
  6. Nagase T, Seki N, Ishikawa K, Ohira M, Kawarabayasi Y, Ohara O, Tanaka A, Kotani H, Miyajima N, Nomura N: Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 1996 Oct 31;3(5):321-9, 341-54. [PubMed Link Image]
  7. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  8. 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 9242
Enzyme 12 Name Trimethyllysine dioxygenase, mitochondrial precursor
Enzyme 12 Synonyms
  1. Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
  2. TML-alpha- ketoglutarate dioxygenase
  3. TML hydroxylase
  4. TML dioxygenase
  5. TMLD
Enzyme 12 Gene Name TMLHE
Enzyme 12 Protein Sequence >Trimethyllysine dioxygenase, mitochondrial precursor 
MWYHRLSHLHSRLQDLLKGGVIYPALPQPNFKSLLPLAVHWHHTASKSLTCAWQQHEDHF
ELKYANTVMRFDYVWLRDHCRSASCYNSKTHQRSLDTASVDLCIKPKTIRLDETTLFFTW
PDGHVTKYDLNWLVKNSYEGQKQKVIQPRILWNAEIYQQAQVPSVDCQSFLETNEGLKKF
LQNFLLYGIAFVENVPPTQEHTEKLAERISLIRETIYGRMWYFTSDFSRGDTAYTKLALD
RHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAEQVLQKAPEEFELLSKVPLKHE
YIEDVGECHNHMIGIGPVLNIYPWNKELYLIRYNNYDRAVINTVPYDVVHRWYTAHRTLT
IELRRPENEFWVKLKPGRVLFIDNWRVLHGRECFTGYRQLCGCYLTRDDVLNTARLLGLQ
A
Enzyme 12 Number of Residues 421
Enzyme 12 Molecular Weight 49518
Enzyme 12 Theoretical pI Not Available
Enzyme 12 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 12 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 12 Specific Function Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML)
Enzyme 12 Pathways
Enzyme 12 Reactions
  • 2-Oxoglutarate + O2 + N6,N6,N6-Trimethyl-L-lysine --> 3-Hydroxy-N6,N6,N6-trimethyl-L-lysine + CO2 + Succinate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 15553435 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9NVH6 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name TMLH_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AF373407 Link Image
Enzyme 12 GeneCard ID Not Available
Enzyme 12 GenAtlas ID TMLHE Link Image
Enzyme 12 HGNC ID HGNC:18308 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Vaz FM, Ofman R, Westinga K, Back JW, Wanders RJ: Molecular and Biochemical Characterization of Rat epsilon -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis. J Biol Chem. 2001 Sep 7;276(36):33512-7. Epub 2001 Jun 28. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 14359
Enzyme 13 Name CDNA PSEC0259 fis, clone NT2RP3003789, weakly similar to CYTOCHROME B561
Enzyme 13 Synonyms
  1. Cytochrome b, ascorbate dependent 3, isoform CRA_a
  2. Cytochrome b, ascorbate dependent 3
Enzyme 13 Gene Name CYBASC3
Enzyme 13 Protein Sequence >CDNA PSEC0259 fis, clone NT2RP3003789, weakly similar to CYTOCHROME B561 
MVSGRFYLSCLLLGSLGSMCILFTIYWMQYWRGGFAWNGSIYMFNWHPVLMVAGMVVFYG
GASLVYRLPQSWVGPKLPWKLLHAALHLMAFVLTVVGLVAVFTFHNHGRTANLYSLHSWL
GITTVFLFACQWFLGFAVFLLPWASMWLRSLLKPIHVFFGAAILSLSIASVISGINEKLF
FSLKNTTRPYHSLPSEAVFANSTGMLVVAFGLLVLYILLASSWKRPEPGILTDRQPLLHD
GE
Enzyme 13 Number of Residues 242
Enzyme 13 Molecular Weight 27215
Enzyme 13 Theoretical pI 9.90
Enzyme 13 GO Classification
Function
—
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-36
Enzyme 13 Transmembrane Regions
  • 7-29
  • 44-66
  • 82-104
  • 119-141
  • 154-176
  • 198-220
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 37515296 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q8NBI2 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name Q8NBI2_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >729 bp 
ATGGTGTCTGGACGGTTCTACTTGTCCTGCCTGCTGCTGGGGTCCCTGGGCTCTATGTGC
ATCCTCTTCACTATCTACTGGATGCAGTACTGGCGTGGTGGCTTTGCCTGGAATGGCAGC
ATCTACATGTTCAACTGGCACCCAGTGCTTATGGTTGCTGGCATGGTGGTATTCTATGGA
GGTGCGTCACTGGTGTACCGCCTGCCCCAGTCGTGGGTGGGGCCCAAACTGCCCTGGAAA
CTCCTCCATGCAGCGCTGCACCTGATGGCCTTCGTCCTCACTGTTGTGGGGCTGGTTGCT
GTCTTTACGTTTCACAACCATGGAAGGACTGCCAACCTCTACTCCCTTCACAGCTGGCTG
GGCATCACCACTGTCTTCCTCTTCGCCTGCCAGTGGTTCCTGGGCTTTGCTGTCTTCCTC
CTGCCCTGGGCGTCCATGTGGCTGCGCAGCCTCCTAAAACCTATCCACGTCTTTTTTGGA
GCCGCCATCCTCTCTCTGTCCATCGCATCCGTCATTTCGGGCATTAATGAGAAGCTTTTC
TTCAGTTTGAAAAACACCACCAGGCCATACCACAGCCTGCCCAGTGAGGCGGTCTTTGCC
AACAGCACCGGGATGCTGGTGGTGGCCTTTGGGCTGCTGGTGCTCTACATCCTTCTGGCT
TCATCTTGGAAGCGCCCAGAGCCGGGGATCCTGACCGACAGACAGCCCCTGCTGCATGAT
GGGGAGTGA
Enzyme 13 GenBank Gene ID BC014045 Link Image
Enzyme 13 GeneCard ID Q8NBI2 Link Image
Enzyme 13 GenAtlas ID CYBASC3 Link Image
Enzyme 13 HGNC ID HGNC:23014 Link Image
Enzyme 13 Chromosome Location 11
Enzyme 13 Locus 11q12.2
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 14388
Enzyme 14 Name Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3
Enzyme 14 Synonyms
  1. Alkylated DNA repair protein alkB homolog 3
  2. Prostate cancer antigen 1
  3. DEPC-1
Enzyme 14 Gene Name ALKBH3
Enzyme 14 Protein Sequence >Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 
MEEKRRRARVQGAWAAPVKSQAIAQPATTAKSHLHQKPGQTWKNKEHHLSDREFVFKEPQ
QVVRRAPEPRVIDREGVYEISLSPTGVSRVCLYPGFVDVKEADWILEQLCQDVPWKQRTG
IREDITYQQPRLTAWYGELPYTYSRITMEPNPHWHPVLRTLKNRIEENTGHTFNSLLCNL
YRNEKDSVDWHSDDEPSLGRCPIIASLSFGATRTFEMRKKPPPEENGDYTYVERVKIPLD
HGTLLIMEGATQADWQHRVPKEYHSREPRVNLTFRTVYPDPRGAPW
Enzyme 14 Number of Residues 286
Enzyme 14 Molecular Weight 33375
Enzyme 14 Theoretical pI 8.58
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Replication, recombination and repair
Enzyme 14 Specific Function Dioxygenase that repairs alkylated DNA containing 1- methyladenine and 3-methylcytosine by oxidative demethylation. Has a strong preference for single-stranded DNA. May also act on RNA. Requires molecular oxygen, alpha-ketoglutarate and iron
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function Not Available
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 16326129 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q96Q83 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name ALKB3_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >861 bp 
ATGGAGGAAAAAAGACGGCGAGCCCGAGTTCAGGGAGCCTGGGCTGCCCCTGTTAAAAGC
CAGGCCATTGCTCAGCCAGCTACCACTGCTAAGAGCCATCTCCACCAGAAGCCTGGCCAG
ACCTGGAAGAACAAAGAGCATCATCTCTCTGACAGAGAGTTTGTGTTCAAAGAACCTCAG
CAGGTAGTACGTAGAGCTCCTGAGCCACGAGTGATTGACAGAGAGGGTGTGTATGAAATC
AGCCTGTCACCCACAGGTGTATCTAGGGTCTGTTTGTATCCTGGCTTTGTTGACGTGAAA
GAAGCTGACTGGATATTGGAACAGCTTTGTCAAGATGTTCCCTGGAAACAGAGGACCGGC
ATCAGAGAGGATATAACTTATCAGCAACCAAGACTTACAGCATGGTATGGAGAACTTCCT
TACACTTATTCAAGAATCACTATGGAACCAAATCCTCACTGGCACCCTGTGCTGCGCACA
CTAAAGAACCGCATTGAAGAGAACACTGGCCACACCTTCAACTCCTTACTCTGCAATCTT
TATCGCAATGAGAAGGACAGCGTGGACTGGCACAGTGATGATGAACCCTCACTAGGGAGG
TGCCCCATTATTGCTTCACTAAGTTTTGGTGCCACACGCACATTTGAGATGAGAAAGAAG
CCACCACCAGAAGAGAATGGAGACTACACATATGTGGAAAGAGTGAAGATACCCTTGGAT
CATGGGACCTTGTTAATCATGGAAGGAGCGACACAAGCTGACTGGCAGCATCGAGTGCCC
AAAGAATACCACTCTAGAGAACCGAGAGTGAACCTGACCTTTCGGACAGTCTATCCAGAC
CCTCGAGGGGCACCCTGGTGA
Enzyme 14 GenBank Gene ID AB042029 Link Image
Enzyme 14 GeneCard ID Q96Q83 Link Image
Enzyme 14 GenAtlas ID ALKBH3 Link Image
Enzyme 14 HGNC ID HGNC:30141 Link Image
Enzyme 14 Chromosome Location 11
Enzyme 14 Locus 11p11.2
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 14401
Enzyme 15 Name Prolyl 3-hydroxylase 1 precursor
Enzyme 15 Synonyms
  1. Leucine- and proline- enriched proteoglycan 1
  2. Leprecan-1
  3. Growth suppressor 1
Enzyme 15 Gene Name LEPRE1
Enzyme 15 Protein Sequence >Prolyl 3-hydroxylase 1 precursor 
MAVRALKLLTTLLAVVAAASQAEVESEAGWGMVTPDLLFAEGTAAYARGDWPGVVLSMER
ALRSRAALRALRLRCRTQCAADFPWELDPDWSPSPAQASGAAALRDLSFFGGLLRRAACL
RRCLGPPAAHSLSEEMELEFRKRSPYNYLQVAYFKINKLEKAVAAAHTFFVGNPEHMEMQ
QNLDYYQTMSGVKEADFKDLETQPHMQEFRLGVRLYSEEQPQEAVPHLEAALQEYFVAYE
ECRALCEGPYDYDGYNYLEYNADLFQAITDHYIQVLNCKQNCVTELASHPSREKPFEDFL
PSHYNYLQFAYYNIGNYTQAVECAKTYLLFFPNDEVMNQNLAYYAAMLGEEHTRSIGPRE
SAKEYRQRSLLEKELLFFAYDVFGIPFVDPDSWTPEEVIPKRLQEKQKSERETAVRISQE
IGNLMKEIETLVEEKTKESLDVSRLTREGGPLLYEGISLTMNSKLLNGSQRVVMDGVISD
HECQELQRLTNVAATSGDGYRGQTSPHTPNEKFYGVTVFKALKLGQEGKVPLQSAHLYYN
VTEKVRRIMESYFRLDTPLYFSYSHLVCRTAIEEVQAERKDDSHPVHVDNCILNAETLVC
VKEPPAYTFRDYSAILYLNGDFDGGNFYFTELDAKTVTAEVQPQCGRAVGFSSGTENPHG
VKAVTRGQRCAIALWFTLDPRHSERDRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEP
AQESLSGSESKPKDEL
Enzyme 15 Number of Residues 736
Enzyme 15 Molecular Weight 83395
Enzyme 15 Theoretical pI 4.79
Enzyme 15 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro- Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218] ALL_REAC R03218
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-22
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 11127636 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q32P28 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name P3H1_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1092 bp 
ATGGCGGTACGCGCGTTGAAGCTGCTGACCACACTGCTGGCTGTCGTGGCCGCTGCCTCC
CAAGCCGAGGTCGAGTCCGAGGCAGGATGGGGCATGGTGACGCCTGATCTGCTCTTCGCC
GAGGGGACCGCAGCCTACGCGCGCGGGGACTGGCCCGGGGTGGTCCTGAGCATGGAACGG
GCGCTGCGCTCCCGGGCAGCCCTCCGCGCCCTTCGCCTGCGCTGCCGCACCCAGTGTGCC
GCCGACTTCCCGTGGGAGCTGGACCCCGACTGGTCCCCCAGCCCGGCCCAGGCCTCGGGC
GCCGGCGCCCTGCGCGACCTGAGCTTCTTCGGGGGCCTTCTGCGTCGCGCTGCCTGCCTG
CGCCGCTGCCTCGGGCCGCCGGCCGCCCACTCGCTCAGCGAAGAGATGGAGCTGGAGTTC
CGCAAGCGGAGCCCCTACAACTACCTGCAGGTCGCCTACTTCAAGATCAACAAGTTGGAG
AAAGCTGTTGCTGCAGCACACACCTTCTTCGTGGGCAATCCTGAGCACATGGAAATGCAG
CAGAACCTAGACTATTACCAAACCATGTCTGGAGTGAAGGAGGCCGACTTCAAGGATCTT
GAGACTCAACCCCATATGCAAGAATTTCGACTGGGAGTGCGACTCTACTCAGAGGAACAG
CCACAGGAAGCTGTGCCCCACCTAGAGGCGGCGCTGCAAGAATACTTTGTGGCCTATGAG
GAGTGCCGTGCCCTCTGCGAAGGGCCCTATGACTACGATGGCTACAACTACCTTGAGTAC
AACGCTGACCTCTTCCAGGCCATCACAGATCATTACATCCAGGTCCTCAACTGTAAGCAG
AACTGTGTCACGGAGCTTGCTTCCCACCCAAGTCGAGAGAAGCCCTTTGAAGACTTCCTC
CCATCGCATTATAATTATCTGCAGTTTGCCTACTATAACATTGGGAATTATACACAAGCT
GGTGAATGTGCCAAGACCTATCTTCTCTTCTTCCCCAATGACGAGGTGATGAACCAAAAT
TTGGCCTATTATGCAGCTATGCTTGGAGAAGAACACACCAGATCCATCGGCCCCCGTGAG
CAGGGCACCTAG
Enzyme 15 GenBank Gene ID AF097431 Link Image
Enzyme 15 GeneCard ID Q32P28 Link Image
Enzyme 15 GenAtlas ID LEPRE1 Link Image
Enzyme 15 HGNC ID HGNC:19316 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Kaul SC, Sugihara T, Yoshida A, Nomura H, Wadhwa R: Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan. Oncogene. 2000 Jul 27;19(32):3576-83. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 14402
Enzyme 16 Name Prolyl 3-hydroxylase 2 precursor
Enzyme 16 Synonyms
  1. Leprecan-like protein 1
  2. Myxoid liposarcoma-associated protein 4
Enzyme 16 Gene Name LEPREL1
Enzyme 16 Protein Sequence >Prolyl 3-hydroxylase 2 precursor 
MRERIWAPPLLLLLPLLLPPPLWGGPPDSPRRELELEPGPLQPFDLLYASGAAAYYSGDY
ERAVRDLEAALRSHRRLREIRTRCARHCAARHPLPPPPPGEGPGAELPLFRSLLGRARCY
RSCETQRLGGPASRHRVSEDVRSDFQRRVPYNYLQRAYIKLNQLEKAVEAAHTFFVANPE
HMEMQQNIENYRATAGVEALQLVDREAKPHMESYNAGVKHYEADDFEMAIRHFEQALREY
FVEDTECRTLCEGPQRFEEYEYLGYKAGLYEAIADHYMQVLVCQHECVRELATRPGRLSP
IENFLPLHYDYLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSIDPA
SIEAREDLTMFVKRHKLESELIKSAAEGLGFSYTEPNYWIRYGGRQDENRVPSGVNVEGA
EVHGFSMGKKLSPKIDRDLREGGPLLYENITFVYNSEQLNGTQRVLLDNVLSEEQCRELH
SVASGIMLVGDGYRGKTSPHTPNEKFEGATVLKALKSGYEGRVPLKSARLFYDISEKARR
IVESYFMLNSTLYFSYTHMVCRTALSGQQDRRNDLSHPIHADNCLLDPEANECWKEPPAY
TFRDYSALLYMNDDFEGGEFIFTEMDAKTVTASIKPKCGRMISFSSGGENPHGVKAVTKG
KRCAVALWFTLDPLYRELERIQADEVIAILDQEQQGKHELNINPKDEL
Enzyme 16 Number of Residues 708
Enzyme 16 Molecular Weight 80985
Enzyme 16 Theoretical pI 5.47
Enzyme 16 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218] ALL_REAC R03218
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-24
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 27526730 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q8IVL5 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name P3H2_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >2127 bp 
ATGCGGGAGCGCATCTGGGCGCCGCCGCTGCTGCTGCTGCTGCCGCTGCTACTGCCGCCG
CCACTGTGGGGCGGCCCCCCGGACAGCCCACGCCGGGAGCTGGAGCTGGAGCCCGGGCCT
CTGCAGCCCTTCGACCTGCTCTACGCCAGCGGCGCGGCCGCCTACTACAGCGGAGACTAC
GAGCGAGCGGTGCGCGACTTGGAAGCGGCGCTGCGCAGCCACCGGCGCCTGCGGGAAATC
CGCACGCGCTGTGCCCGCCACTGCGCGGCGCGCCACCCGCTCCCGCCCCCGCCCCCCGGC
GAGGGCCCCGGCGCTGAGCTGCCCCTTTTCCGCTCCTTGTTGGGGCGGGCGCGCTGTTAT
CGCAGCTGTGAGACCCAGCGCCTCGGGGGCCCCGCATCCCGCCACCGCGTCAGCGAGGAT
GTGCGCAGCGACTTCCAGCGCAGAGTGCCCTACAACTACCTGCAGCGGGCCTACATCAAG
CTTAACCAGCTCGAAAAAGCAGTGGAAGCAGCTCACACATTTTTCGTGGCTAACCCTGAG
CACATGGAAATGCAGCAGAACATTGAGAATTACAGGGCGACAGCTGGTGTTGAAGCATTG
CAGTTGGTAGACAGAGAAGCCAAGCCACACATGGAGAGTTACAATGCAGGAGTTAAACAT
TATGAGGCTGATGACTTTGAGATGGCTATCAGGCATTTCGAACAAGCCTTAAGAGAATAT
TTCGTTGAAGATACAGAATGCCGGACCCTATGTGAGGGGCCTCAGAGATTTGAAGAATAT
GAGTATTTAGGGTATAAGGCTGGTCTGTATGAAGCTATTGCAGATCACTACATGCAGGTG
CTTGTTTGTCAGCATGAATGTGTGAGGGAACTTGCCACCCGCCCTGGCCGCCTCTCTCCC
ATCGAGAATTTTCTTCCTCTGCACTATGATTACCTACAGTTTGCCTACTATCGAGTTGGT
GAGTATGTGAAAGCCCTGGAGTGTGCCAAAGCCTATCTTCTATGCCATCCAGATGATGAG
GATGTCCTAGACAATGTGGATTACTATGAGAGTCTGCTGGATGATAGCATTGACCCGGCA
TCCATTGAGGCCAGAGAGGATTTAACAATGTTTGTGAAACGTCATAAGCTGGAGTCTGAG
CTGATAAAATCAGCTGCAGAAGGTCTGGGGTTTTCATACACTGAACCGAATTATTGGATC
AGATATGGAGGACGACAGGATGAGAATCGGGTCCCTTCAGGAGTGAACGTAGAGGGAGCA
GAAGTTCATGGATTCTCAATGGGAAAAAAGCTATCACCCAAGATAGATCGAGACCTAAGA
GAAGGTGGTCCTCTACTCTATGAGAACATCACATTCGTCTACAACTCGGAGCAGCTGAAC
GGGACTCAGCGGGTTCTCCTGGATAACGTCCTGTCGGAAGAACAGTGCCGGGAGCTCCAC
AGCGTGGCCAGTGGAATCATGCTTGTTGGTGATGGATACAGAGGAAAAACTTCACCCCAT
ACACCCAATGAAAAGTTTGAAGGTGCAACTGTCCTGAAAGCACTCAAATCTGGTTATGAA
GGTCGAGTCCCACTGAAGAGCGCTCGTCTGTTTTATGACATCAGCGAAAAGGCTCGAAGG
ATTGTAGAATCTTATTTTATGCTGAACTCAACTCTGTATTTTTCCTATACACACATGGTC
TGCCGAACAGCCCTGTCTGGTCAGCAGGATAGAAGAAATGACCTCAGTCATCCCATCCAT
GCTGACAACTGTTTGTTGGATCCAGAGGCCAACGAATGCTGGAAGGAGCCTCCTGCTTAC
ACATTTCGAGACTATAGTGCTCTCCTATATATGAATGATGACTTTGAAGGAGGAGAATTC
ATATTCACAGAGATGGATGCTAAGACTGTGACTGCCTCTATAAAACCAAAATGTGGGCGC
ATGATCAGCTTCTCATCTGGAGGAGAGAACCCTCATGGGGTGAAGGCAGTCACCAAGGGA
AAGAGGTGTGCTGTGGCTCTGTGGTTCACCTTGGACCCACTTTATAGAGAATTGGAGCGA
ATACAGGCTGATGAAGTGATTGCAATTCTGGATCAAGAACAGCAAGGGAAGCATGAACTG
AATATCAACCCTAAAGATGAGCTATAA
Enzyme 16 GenBank Gene ID AJ430351 Link Image
Enzyme 16 GeneCard ID Q8IVL5 Link Image
Enzyme 16 GenAtlas ID LEPREL1 Link Image
Enzyme 16 HGNC ID HGNC:19317 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 14403
Enzyme 17 Name Prolyl 3-hydroxylase 3 precursor
Enzyme 17 Synonyms
  1. Leprecan-like protein 2
  2. Protein B
Enzyme 17 Gene Name LEPREL2
Enzyme 17 Protein Sequence >Prolyl 3-hydroxylase 3 precursor 
MLRLLRPLLLLLLLPPPGSPEPPGLTQLSPGAPPQAPDLLYADGLRAYAAGAWAPAVALL
REALRSQAALGRVRLDCGASCAADPGAALPAVLLGAPEPDSGPGPTQGSWERQLLRAALR
RADCLTQCAARRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAAAAAHTF
FVANPMHLQMREDMAKYRRMSGVRPQSFRDLETPPHWAAYDTGLELLGRQEAGLALPRLE
EALQGSLAQMESCRADCEGPEEQQGAEEEEDGAASQGGLYEAIAGHWIQVLQCRQRCVGE
TATRPGRSFPVPDFLPNQLRRLHEAHAQVGNLSQAIENVLSVLLFYPEDEAAKRALNQYQ
AQLGEPRPGLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDPWTPAALIPEALREK
LREDQEKRPWDHEPVKPKPLTYWKDVLLLEGVTLTQDSRQLNGSERAVLDGLLTPAECGV
LLQLAKDAAGAGARSGYRGRRSPHTPHERFEGLTVLKAAQLARAGTVGSQGAKLLLEVSE
RVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWRE
PPAYTYRDYSGLLYLNDDFQGGDLFFTEPNALTVTARVRPRCGRLVAFSSGVENPHGVWA
VTRGRRCALALWHTWAPEHREQEWIEAKELLQESQEEEEEEEEEMPSKDPSPEPPSRRHQ
RVQDKTGRAPRVREEL
Enzyme 17 Number of Residues 736
Enzyme 17 Molecular Weight 81837
Enzyme 17 Theoretical pI 6.26
Enzyme 17 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218] ALL_REAC R03218
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-20
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 1200503 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q8IVL6 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name P3H3_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1656 bp 
ATGCACCTGCAGATGCGGGAGGACATGGCTAAGTACAGACGAATGTCGGGAGTTCGGCCC
CAGAGCTTCCGGGACCTGGAGACGCCCCCACACTGGGCAGCCTATGACACTGGCCTGGAG
CTACTGGGGCGCCAGGAGGCAGGACTGGCACTGCCCAGGCTAGAGGAGGCTCTTCAGGGG
AGCCTGGCCCAGATGGAGAGCTGCCGTGCTGACTGTGAGGGGCCTGAGGAGCAGCAGGGG
GCTGAAGAAGAGGAGGATGGGGCTGCGAGCCAGGGGGGCCTCTATGAGGCCATTGCAGGA
CACTGGATTCAGGTCCTGCAGTGCCGGCAACGCTGTGTGGGGGAAACAGCCACACGCCCT
GGTCGCAGCTTCCCTGTCCCAGACTTCCTTCCCAACCAGCTGAGGCGGCTACATGAGGCC
CATGCTCAGGTGGGCAATCTGTCCCAGGCTATAGAAAATGTCCTGAGTGTCCTGCTCTTC
TACCCGGAGGATGAGGCTGCCAAGAGGGCTCTGAACCAGTACCAGGCCCAGCTGGGAGAG
CCGAGACCTGGCCTCGGACCCAGAGAGGACATCCAGCGCTTCATCCTCCGATCCCTGGGG
GAGAAGAGGCAGCTCTACTATGCCATGGAGCACCTGGGGACCAGCTTCAAGGATCCTGAC
CCCTGGACCCCTGCAGCTCTCATCCCTGAGGCACTTAGAGAAAAGCTCAGAGAGGATCAA
GAGAAGAGGCCTTGGGACCATGAGCCCGTGAAGCCAAAGCCCTTGACCTACTGGAAGGAT
GTCCTTCTCCTGGAGGGTGTGACCTTGACCCAGGATTCCAGGCAGCTGAATGGGTCGGAG
CGGGCGGTGTTGGATGGGCTGCTCACCCCAGCCGAGTGTGGGGTGCTGCTGCAGCTGGCT
AAGGATGCAGCTGGGGCTGGAGCCAGGTCTGGCTATCGTGGTCGCCGCTCCCCTCACACC
CCCCATGAACGCTTCGAGGGGCTCACGGTGCTTAAGGCTGCGCAGCTGGCCCGGGCTGGG
ACAGTGGGCAGTCAGGGTGCTAAGCTGCTTCTGGAGGTGAGCGAGCGGGTGCGGACCTTG
ACCCAGGCCTACTTCTCCCCGGAACGGCCCCTGCATCTGTCCTTCACCCACCTGGTGTGC
CGCAGCGCCATAGAAGGAGAGCAAGAGCAGCGCATGGACCTGAGTCACCCAGTGCACGCA
GACAACTGCGTCCTGGACCCTGACACGGGAGAGTGCTGGCGGGAGCCCCCAGCCTACACC
TATCGGGACTACAGCGGACTCCTCTACCTCAACGATGACTTCCAGGGTGGGGACCTGTTC
TTCACGGAGCCCAACGCCCTCACTGTCACGGCTCGGGTGCGTCCTCGCTGTGGGCGCCTT
GTGGCCTTCAGCTCCGGTGTCGAGAATCCCCATGGGGTGTGGGCCGTGACTCGGGGACGG
CGCTGTGCCCTGGCACTGTGGCACACGTGGGCACCTGAGCACAGGGAGCAGGAGTGGATA
GAAGCCAAAGAACTGCTGCAGGAGTCACAGGAGGAGGAGGAAGAGGAAGAGGAAGAAATG
CCCAGCAAAGACCCTTCCCCAGAGCCCCCTAGCCGCAGGCACCAGAGGGTCCAAGACAAG
ACTGGAAGGGCACCTCGGGTTCGGGAGGAGCTGTGA
Enzyme 17 GenBank Gene ID U47924 Link Image
Enzyme 17 GeneCard ID Q8IVL6 Link Image
Enzyme 17 GenAtlas ID LEPREL2 Link Image
Enzyme 17 HGNC ID HGNC:19318 Link Image
Enzyme 17 Chromosome Location 12
Enzyme 17 Locus 12q13
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed Link Image]
  2. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 14854
Enzyme 18 Name Solute carrier family 23 member 3
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name SLC23A3
Enzyme 18 Protein Sequence >Solute carrier family 23 member 3 
MSRSPLNPSQLRSVGSQDALAPLPPPAPQNPSTHSWDPLCGSLPWGLSCLLALQHVLVMA
SLLCVSHLLLLCSLSPGGLSYSPSQLLASSFFSCGMSTILQTWMGSRLPLVQAPSLEFLI
PALVLTSQKLPRAIQTPGNSSLMLHLCRGPSCHGLGHWNTSLQEVSGAVVVSGLLQGMMG
LLGSPGHVFPHCGPLVLAPSLVVAGLSAHREVAQFCFTHWGLALLTWAPASFMCAPGGEL
QRHQLTLLSLSSGSFRNCLPPPRHHGFGCLTQAGSQQVAHLVGLLCVGLGLSPRLAQLLT
TIPLPVVGGVLGVTQAVVLSAGFSSFYLADIDSGRNIFIVGFSIFMALLLPRWFREAPVL
FSTGWSPLDVLLHSLLTQPIFLAGLSGFLLENTIPGTQLERGLGQGLPSPFTAQEARMPQ
KPREKAQVYRLPFPIQNLCPCIPQPLHCLCPLPEDPGDEEGGSSEPEEMADLLPGSGEPC
PESSREGFRSQK
Enzyme 18 Number of Residues 492
Enzyme 18 Molecular Weight 52291
Enzyme 18 Theoretical pI 7.04
Enzyme 18 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 18 General Function Nucleotide transport and metabolism
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 20988420 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q6PIS1 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name Q6PIS1_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1479 bp 
ATGAGCCGATCACCCCTCAATCCCAGCCAACTCCGATCAGTGGGCTCCCAGGATGCCCTG
GCCCCCTTGCCTCCACCTGCTCCCCAGAATCCCTCCACCCACTCTTGGGACCCTTTGTGT
GGATCTCTGCCTTGGGGCCTCAGCTGTCTTCTGGCTCTGCAGCATGTCTTGGTCATGGCT
TCTCTGCTCTGTGTCTCCCACCTGCTCCTGCTTTGCAGTCTCTCCCCAGGAGGACTCTCT
TACTCCCCTTCTCAGCTCCTGGCCTCCAGCTTCTTTTCATGTGGTATGTCTACCATCCTG
CAAACTTGGATGGGCAGCAGGCTGCCTCTTGTCCAGGCTCCATCCTTAGAGTTCCTTATC
CCTGCTCTGGTGCTGACCAGCCAGAAGCTACCCCGGGCCATCCAGACACCTGGAAACTCC
TCCCTCATGCTGCACCTTTGTAGGGGACCTAGCTGCCATGGCCTGGGGCACTGGAACACT
TCTCTCCAGGAGGTGTCCGGGGCAGTGGTAGTATCTGGGCTGCTGCAGGGCATGATGGGG
CTGCTGGGGAGTCCCGGCCACGTGTTCCCCCACTGTGGGCCCCTGGTGCTGGCTCCCAGC
CTGGTTGTGGCAGGGCTCTCTGCCCACAGGGAGGTAGCCCAGTTCTGCTTCACACACTGG
GGGTTGGCCTTGCTCACCTGGGCTCCTGCCAGTTTCATGTGTGCCCCTGGAGGCGAGCTT
CAACGTCATCAACTCACACTCCTCTCCCTGTCTTCCGGCTCCTTTCGGAACTGTCTGCCC
CCACCAAGGCACCATGGATTTGGCTGCCTCACCCAGGCTGGATCTCAGCAAGTGGCTCAC
TTAGTGGGGCTACTCTGCGTGGGGCTTGGACTCTCCCCCAGGTTGGCTCAGCTCCTCACC
ACCATCCCACTGCCTGTTGTTGGTGGGGTGCTGGGGGTGACCCAGGCTGTGGTTTTGTCT
GCTGGATTCTCCAGCTTCTACCTGGCTGACATAGACTCTGGGCGAAATATCTTCATTGTG
GGCTTCTCCATCTTCATGGCCTTGCTGCTGCCAAGATGGTTTCGGGAAGCCCCAGTCCTG
TTCAGCACAGGCTGGAGCCCCTTGGATGTATTACTGCACTCACTGCTGACACAGCCCATC
TTCCTGGCTGGACTCTCAGGCTTCCTACTGGAGAACACGATTCCTGGCACACAGCTTGAG
CGAGGCCTAGGTCAAGGGCTACCATCTCCTTTCACTGCCCAAGAGGCTCGAATGCCTCAG
AAGCCCAGGGAGAAGGCTCAAGTGTACAGACTTCCTTTCCCCATCCAAAACCTCTGTCCC
TGCATCCCCCAGCCTCTCCACTGCCTCTGCCCACTGCCTGAAGACCCTGGGGATGAGGAA
GGAGGCTCCTCTGAGCCAGAAGAGATGGCAGACTTGCTGCCTGGCTCAGGGGAGCCATGC
CCTGAATCTAGCAGAGAAGGGTTTAGGTCCCAGAAATGA
Enzyme 18 GenBank Gene ID BC030243 Link Image
Enzyme 18 GeneCard ID Q6PIS1 Link Image
Enzyme 18 GenAtlas ID SLC23A3 Link Image
Enzyme 18 HGNC ID HGNC:20601 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 14855
Enzyme 19 Name Prolyl 4-hydroxylase subunit alpha-3
Enzyme 19 Synonyms
  1. 4-PH alpha-3
Enzyme 19 Gene Name P4HA3
Enzyme 19 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-3 
MGPGARLAALLAVLALGTGDPERAAARGDTFSALTSVARALAPERRLLGLLRRYLRGEEA
RLRDLTRFYDKVLSLHEDSTTPVANPLLAFTLIKRLQSDWRNVVHSLEASENIRALKDGY
EKVEQDLPAFEDLEGAARALMRLQDVYMLNVKGLARGVFQRVTGSAITDLYSPKRLFSLT
GDDCFQVGKVAYDMGDYYHAIPWLEEAVSLFRGSYGEWKTEDEASLEDALDHLAFAYFRA
GNVSCALSLSREFLLYSPDNKRMARNVLKYERLLAESPNHVVAEAVIQRPNIPHLQTRDT
YEGLCQTLGSQPTLYQIPSLYCSYETNSNAYLLLQPIRKEVIHLEPYIALYHDFVSDSEA
QKIRELAEPWLQRSVVASGEKQLQVEYRISKSAWLKDTVDPKLVTLNHRIAALTGLDVRP
PYAEYLQVVNYGIGGHYEPHFDHATSPSSPLYRMKSGNRVATFMIYLSSVEAGGATAFIY
ANLSVPVVRNAALFWWNLHRSGEGDSDTLHAGCPVLVGDKWVANKWIHEYGQEFRRPCSS
SPED
Enzyme 19 Number of Residues 544
Enzyme 19 Molecular Weight 61127
Enzyme 19 Theoretical pI 6.46
Enzyme 19 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways
Enzyme 19 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 [RN:R03219] ALL_REAC R03219
  • (other) R01252
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 109658570 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q7Z4N8 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name Q7Z4N8_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1635 bp 
ATGGGTCCTGGGGCGCGGCTGGCGGCGCTGCTGGCGGTGCTGGCGCTCGGGACAGGAGAC
CCAGAAAGGGCTGCGGCTCGGGGCGACACGTTCTCGGCGCTGACCAGCGTGGCGCGCGCC
CTGGCGCCCGAGCGCCGGCTGCTGGGGCTGCTGAGGCGGTACCTGCGCGGGGAGGAGGCG
CGGCTGCGGGACCTGACTAGATTCTACGACAAGGTACTTTCTTTGCATGAGGATTCAACA
ACCCCTGTGGCTAACCCTCTGCTTGCATTTACTCTCATCAAACGCCTGCAGTCTGACTGG
AGGAATGTGGTACATAGTCTGGAGGCCAGTGAGAACATCCGAGCTCTGAAGGATGGCTAT
GAGAAGGTGGAGCAAGACCTTCCAGCCTTTGAGGACCTTGAGGGAGCAGCAAGGGCCCTG
ATGCGGCTGCAGGACGTGTACATGCTCAATGTGAAAGGCCTGGCCCGAGGTGTCTTTCAG
AGAGTCACTGGCTCTGCCATCACTGACCTGTACAGCCCCAAACGGCTCTTTTCTCTCACA
GGGGATGACTGCTTCCAAGTTGGCAAGGTGGCCTATGACATGGGGGATTATTACCATGCC
ATTCCATGGCTGGAGGAGGCTGTCAGTCTCTTCCGAGGATCTTACGGAGAGTGGAAGACA
GAGGATGAGGCAAGTCTAGAAGATGCCTTGGATCACTTGGCCTTTGCTTATTTCCGGGCA
GGAAATGTTTCGTGTGCCCTCAGCCTCTCTCGGGAGTTTCTTCTCTACAGCCCAGATAAT
AAGAGGATGGCCAGGAATGTCTTGAAATATGAAAGGCTCTTGGCAGAGAGCCCCAACCAC
GTGGTAGCTGAGGCTGTCATCCAGAGGCCCAATATACCCCACCTGCAGACCAGAGACACC
TACGAGGGGCTATGTCAGACCCTGGGTTCCCAGCCCACTCTCTACCAGATCCCTAGCCTC
TACTGTTCCTATGAGACCAATTCCAACGCCTACCTGCTGCTCCAGCCCATCCGGAAGGAG
GTCATCCACCTGGAGCCCTACATTGCTCTCTACCATGACTTCGTCAGTGACTCAGAGGCT
CAGAAAATTAGAGAACTTGCAGAACCATGGCTACAGAGGTCAGTGGTGGCATCAGGGGAG
AAGCAGTTACAAGTGGAGTACCGCATCAGCAAAAGTGCCTGGCTGAAGGACACTGTTGAC
CCAAAACTGGTGACCCTCAACCACCGCATTGCTGCCCTCACAGGCCTTGATGTCCGGCCT
CCCTATGCAGAGTATCTGCAGGTGGTGAACTATGGCATCGGAGGACACTATGAGCCTCAC
TTTGACCATGCTACGTCACCAAGCAGCCCCCTCTACAGAATGAAGTCAGGAAACCGAGTT
GCAACATTTATGATCTATCTGAGCTCGGTGGAAGCTGGAGGAGCCACAGCCTTCATCTAT
GCCAACCTCAGCGTGCCTGTGGTTAGGAATGCAGCACTGTTTTGGTGGAACCTGCACAGG
AGTGGTGAAGGGGACAGTGACACACTTCATGCTGGCTGTCCTGTCCTGGTGGGAGATAAG
TGGGTGGCCAACAAGTGGATACATGAGTATGGACAGGAATTCCGCAGACCCTGCAGCTCC
AGCCCTGAAGACTGA
Enzyme 19 GenBank Gene ID BC117333 Link Image
Enzyme 19 GeneCard ID Q7Z4N8 Link Image
Enzyme 19 GenAtlas ID P4HA3 Link Image
Enzyme 19 HGNC ID HGNC:30135 Link Image
Enzyme 19 Chromosome Location 11
Enzyme 19 Locus 11q13.4
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Van Den Diepstraten C, Papay K, Bolender Z, Brown A, Pickering JG: Cloning of a novel prolyl 4-hydroxylase subunit expressed in the fibrous cap of human atherosclerotic plaque. Circulation. 2003 Aug 5;108(5):508-11. Epub 2003 Jul 21. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Kukkola L, Hieta R, Kivirikko KI, Myllyharju J: Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme. J Biol Chem. 2003 Nov 28;278(48):47685-93. Epub 2003 Sep 18. [PubMed Link Image]
Enzyme 19 Metabolite References
  1. 8198555;6325436
Enzyme 20 [top]
Enzyme 20 ID 14992
Enzyme 20 Name Egl nine homolog 1
Enzyme 20 Synonyms
  1. Hypoxia-inducible factor prolyl hydroxylase 2
  2. HIF-prolyl hydroxylase 2
  3. HIF-PH2
  4. HPH-2
  5. Prolyl hydroxylase domain-containing protein 2
  6. PHD2
  7. SM-20
Enzyme 20 Gene Name EGLN1
Enzyme 20 Protein Sequence >Egl nine homolog 1 
MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQG
SEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADP
AAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLR
PNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQL
VSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMV
ACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKF
DRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDS
VGKDVF
Enzyme 20 Number of Residues 426
Enzyme 20 Molecular Weight 46021
Enzyme 20 Theoretical pI 8.66
Enzyme 20 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 20 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 20 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF-1 alpha at 'Pro-402' and 'Pro-564', and HIF-2 alpha. Functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 11345052 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9GZT9 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name EGLN1_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1281 bp 
ATGGCCAATGACAGCGGCGGGCCCGGCGGGCCGAGCCCGAGCGAGCGAGACCGGCAGTAC
TGCGAGCTGTGCGGGAAGATGGAGAACCTGCTGCGCTGCAGCCGCTGCCGCAGCTCCTTC
TACTGCTGCAAGGAGCACCAGCGTCAGGACTGGAAGAAGCACAAGCTCGTGTGCCAGGGC
AGCGAGGGCGCCCTCGGCCACGGAGTGGGCCCACACCAGCATTCCGGCCCCGCGCCGCCG
GCTGCAGTGCCGCCGCCCAGGGCCGGGGCCCGGGAGCCCAGGAAGGCAGCGGCGCGCCGG
GACAACGCCTCCGGGGACGCGGCCAAGGGAAAAGTAAAGGCCAAGCCCCCGGCCGACCCA
GCGGCGGCCGCGTCGCCGTGTCGTGCGGCCGCCGGCGGCCAGGGCTCGGCGGTGGCTGCC
GAAGCCGAGCCCGGCAAGGAGGAGCCGCCGGCCCGCTCATCGCTGTTCCAGGAGAAGGCG
AACCTGTACCCCCCAAGCAACACGCCCGGGGATGCGCTGAGCCCCGGCGGCGGCCTGCGG
CCCAACGGGCAGACGAAGCCCCTGCCGGCGCTGAAGCTGGCGCTCGAGTACATCGTGCCG
TGCATGAACAAGCACGGCATCTGTGTGGTGGACGACTTCCTCGGCAAGGAGACCGGACAG
CAGATCGGCGACGAGGTGCGCGCCCTGCACGACACCGGGAAGTTCACGGACGGGCAGCTG
GTCAGCCAGAAGAGTGACTCGTCCAAGGACATCCGAGGCGATAAGATCACCTGGATCGAG
GGCAAGGAGCCCGGCTGCGAAACCATTGGGCTGCTCATGAGCAGCATGGACGACCTGATA
CGCCACTGTAACGGGAAGCTGGGCAGCTACAAAATCAATGGCCGGACGAAAGCCATGGTT
GCTTGTTATCCGGGCAATGGAACGGGTTATGTACGTCATGTTGATAATCCAAATGGAGAT
GGAAGATGTGTGACATGTATATATTATCTTAATAAAGACTGGGATGCCAAGGTAAGTGGA
GGTATACTTCGAATTTTTCCAGAAGGCAAAGCCCAGTTTGCTGACATTGAACCCAAATTT
GATAGACTGCTGTTTTTCTGGTCTGACCGTCGCAACCCTCATGAAGTACAACCAGCATAT
GCTACAAGGTACGCAATAACTGTTTGGTATTTTGATGCAGATGAGAGAGCACGAGCTAAA
GTAAAATATCTAACAGGTGAAAAAGGTGTGAGGGTTGAACTCAATAAACCTTCAGATTCG
GTCGGTAAAGACGTCTTCTAG
Enzyme 20 GenBank Gene ID AF246631 Link Image
Enzyme 20 GeneCard ID Q9GZT9 Link Image
Enzyme 20 GenAtlas ID EGLN1 Link Image
Enzyme 20 HGNC ID HGNC:1232 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Dupuy D, Aubert I, Duperat VG, Petit J, Taine L, Stef M, Bloch B, Arveiler B: Mapping, characterization, and expression analysis of the SM-20 human homologue, c1orf12, and identification of a novel related gene, SCAND2. Genomics. 2000 Nov 1;69(3):348-54. [PubMed Link Image]
  2. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed Link Image]
  3. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed Link Image]
  4. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed Link Image]
  5. Ivan M, Haberberger T, Gervasi DC, Michelson KS, Gunzler V, Kondo K, Yang H, Sorokina I, Conaway RC, Conaway JW, Kaelin WG Jr: Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13459-64. Epub 2002 Sep 26. [PubMed Link Image]
  6. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
  7. Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR: Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells. Biochem Biophys Res Commun. 2003 Apr 11;303(3):947-53. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 14993
Enzyme 21 Name Egl nine homolog 2
Enzyme 21 Synonyms
  1. Hypoxia-inducible factor prolyl hydroxylase 1
  2. HIF-prolyl hydroxylase 1
  3. HIF-PH1
  4. HPH-3
  5. Prolyl hydroxylase domain-containing protein 1
  6. PHD1
  7. Estrogen-induced tag 6
Enzyme 21 Gene Name EGLN2
Enzyme 21 Protein Sequence >Egl nine homolog 2 
MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAG
SGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVTKGCQRLAAQGARPEAPKRK
WAEDGGDAPSPSKRPWARQENQEAEREGGMSCSCSSGSGEASAGLMEEALPSAPERLALD
YIVPCMRYYGICVKDSFLGAALGGRVLAEVEALKRGGRLRDGQLVSQRAIPPRSIRGDQI
AWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGSYVINGRTKAMVACYPGNGLGYVRHVDN
PHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEV
KPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT
Enzyme 21 Number of Residues 407
Enzyme 21 Molecular Weight 43651
Enzyme 21 Theoretical pI 7.97
Enzyme 21 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 21 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 21 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF-1 alpha at 'Pro-402' and 'Pro-564', and HIF-2 alpha. Functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. May play a role in cell growth regulation
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 14547148 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q96KS0 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name EGLN2_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1224 bp 
ATGGACAGCCCGTGCCAGCCGCAGCCCCTAAGTCAGGCTCTCCCTCAGTTACCAGGGTCT
TCGTCAGAGCCCTTGGAGCCTGAGCCTGGCCGGGCCAGGATGGGAGTGGAGAGTTACCTG
CCCTGTCCCCTGCTCCCCTCCTACCACTGTCCAGGAGTGCCTAGTGAGGCCTCGGCAGGG
AGTGGGACCCCCAGAGCCACAGCCACCTCTACCACTGCCAGCCCTCTTCGGGACGGTTTT
GGCGGGCAGGATGGTGGTGAGCTGCGGCCGCTGCAGAGTGAAGGCGCTGCAGCGCTGGTC
ACCAAGGGGTGCCAGCGATTGGCAGCCCAGGGCGCACGGCCTGAGGCCCCCAAACGGAAA
TGGGCCGAGGATGGTGGGGATGCCCCTTCACCCAGCAAACGGCCCTGGGCCAGGCAAGAG
AACCAGGAGGCAGAGCGGGAGGGTGGCATGAGCTGCAGCTGCAGCAGTGGCAGTGGTGAG
GCCAGTGCTGGGCTGATGGAGGAGGCGCTGCCCTCTGCGCCCGAGCGCCTGGCCCTGGAC
TATATCGTGCCCTGCATGCGGTACTACGGCATCTGCGTCAAGGACAGCTTCCTGGGGGCA
GCACTGGGCGGTCGCGTGCTGGCCGAGGTGGAGGCCCTCAAACGGGGTGGGCGCCTGCGA
GACGGGCAGCTAGTGAGCCAGAGGGCGATCCCGCCGCGCAGCATCCGTGGGGACCAGATT
GCCTGGGTGGAAGGCCATGAACCAGGCTGTCGAAGCATTGGTGCCCTCATGGCCCATGTG
GACGCCGTCATCCGCCACTGCGCAGGGCGGCTGGGCAGCTATGTCATCAACGGGCGCACC
AAGGCCATGGTGGCGTGTTACCCAGGCAACGGGCTCGGGTACGTAAGGCACGTTGACAAT
CCCCACGGCGATGGGCGCTGCATCACCTGTATCTATTACCTGAATCAGAACTGGGACGTT
AAGGTGCATGGCGGCCTGCTGCAGATCTTCCCTGAGGGCCGGCCCGTGGTAGCCAACATC
GAGCCACTCTTTGACCGGTTGCTCATTTTCTGGTCTGACCGGCGGAACCCCCACGAGGTG
AAGCCAGCCTATGCCACCAGGTACGCCATCACTGTCTGGTATTTTGATGCCAAGGAGCGG
GCAGCAGCCAAAGACAAGTATCAGCTAGCATCAGGACAGAAAGGTGTCCAAGTACCTGTA
TCACAGCCGCCTACGCCCACCTAG
Enzyme 21 GenBank Gene ID AJ310544 Link Image
Enzyme 21 GeneCard ID Q96KS0 Link Image
Enzyme 21 GenAtlas ID EGLN2 Link Image
Enzyme 21 HGNC ID HGNC:14660 Link Image
Enzyme 21 Chromosome Location 19
Enzyme 21 Locus 19q13.2
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed Link Image]
  2. Seth P, Krop I, Porter D, Polyak K: Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression). Oncogene. 2002 Jan 24;21(5):836-43. [PubMed Link Image]
  3. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed Link Image]
  4. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed Link Image]
  5. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
  6. McNeill LA, Hewitson KS, Gleadle JM, Horsfall LE, Oldham NJ, Maxwell PH, Pugh CW, Ratcliffe PJ, Schofield CJ: The use of dioxygen by HIF prolyl hydroxylase (PHD1). Bioorg Med Chem Lett. 2002 Jun 17;12(12):1547-50. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 14994
Enzyme 22 Name Egl nine homolog 3
Enzyme 22 Synonyms
  1. Hypoxia-inducible factor prolyl hydroxylase 3
  2. HIF-prolyl hydroxylase 3
  3. HIF-PH3
  4. HPH-1
  5. Prolyl hydroxylase domain-containing protein 3
  6. PHD3
Enzyme 22 Gene Name EGLN3
Enzyme 22 Protein Sequence >Egl nine homolog 3 
MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHCTGALRDGQ
LAGPRAGVSKRHLRGDQITWIGGNEEGCEAISFLLSLIDRLVLYCGSRLGKYYVKERSKA
MVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEP
IFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALTED
Enzyme 22 Number of Residues 239
Enzyme 22 Molecular Weight 27262
Enzyme 22 Theoretical pI 7.70
Enzyme 22 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 22 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 22 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF-1 alpha at 'Pro-564', and HIF-2 alpha. Functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. May play a role in cell growth regulation in muscle cells and in apoptosis in neuronal tissue. Promotes cell death through a caspase-dependent mechanism
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 14547150 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q9H6Z9 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name EGLN3_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >720 bp 
ATGCCCCTGGGACACATCATGAGGCTGGACCTGGAGAAAATTGCCCTGGAGTACATCGTG
CCCTGTCTGCACGAGGTGGGCTTCTGCTACCTGGACAACTTCCTGGGCGAGGTGGTGGGC
GACTGCGTCCTGGAGCGCGTCAAGCAGCTGCACTGCACCGGGGCCCTGCGGGACGGCCAG
CTGGCGGGGCCGCGCGCCGGCGTCTCCAAGCGACACCTGCGGGGCGACCAGATCACGTGG
ATCGGGGGCAACGAGGAGGGCTGCGAGGCCATCAGCTTCCTCCTGTCCCTCATCGACAGG
CTGGTCCTCTACTGCGGGAGCCGGCTGGGCAAATACTACGTCAAGGAGAGGTCTAAGGCA
ATGGTGGCTTGCTATCCGGGAAATGGAACAGGTTATGTTCGCCACGTGGACAACCCCAAC
GGTGATGGTCGCTGCATCACCTGCATCTACTATCTGAACAAGAATTGGGATGCCAAGCTA
CATGGTGGGATCCTGCGGATATTTCCAGAGGGGAAATCATTCATAGCAGATGTGGAGCCC
ATTTTTGACAGACTCCTGTTCTTCTGGTCAGATCGTAGGAACCCACACGAAGTGCAGCCC
TCTTACGCAACCAGATATGCTATGACTGTCTGGTACTTTGATGCTGAAGAAAGGGCAGAA
GCCAAAAAGAAATTCAGGAATTTAACTAGGAAAACTGAATCTGCCCTCACTGAAGACTGA
Enzyme 22 GenBank Gene ID AJ310545 Link Image
Enzyme 22 GeneCard ID Q9H6Z9 Link Image
Enzyme 22 GenAtlas ID EGLN3 Link Image
Enzyme 22 HGNC ID HGNC:14661 Link Image
Enzyme 22 Chromosome Location 14
Enzyme 22 Locus 14q13.1
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed Link Image]
  2. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed Link Image]
  3. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed Link Image]
  4. Bruick RK, McKnight SL: A conserved family of prolyl-4-hydroxylases that modify HIF. Science. 2001 Nov 9;294(5545):1337-40. Epub 2001 Oct 11. [PubMed Link Image]
  5. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
  6. Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR: Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells. Biochem Biophys Res Commun. 2003 Apr 11;303(3):947-53. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 14995
Enzyme 23 Name Putative HIF-prolyl hydroxylase PH-4
Enzyme 23 Synonyms
  1. Hypoxia-inducible factor prolyl 4-hydroxylase
Enzyme 23 Gene Name PH4
Enzyme 23 Protein Sequence >Putative HIF-prolyl hydroxylase PH-4 
MAAAAVTGQRPETAAAEEASRPQWAPPDHCQAQAAAGLGDGEDAPVRPLCKPRGICSRAY
FLVLMVFVHLYLGNVLALLLFVHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVG
HERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYE
EAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDG
DGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRL
TRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYM
TVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVF
WYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLARE
GGTDSQPEWALDRAYRDARVEL
Enzyme 23 Number of Residues 502
Enzyme 23 Molecular Weight 56662
Enzyme 23 Theoretical pI 5.99
Enzyme 23 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function May catalyze the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 28566186 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q9NXG6 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name EGLX_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1509 bp 
ATGGCGGCAGCGGCGGTGACAGGCCAGCGGCCTGAGACCGCGGCGGCCGAGGAGGCCTCG
AGGCCGCAGTGGGCGCCGCCAGACCACTGCCAGGCTCAGGCGGCGGCCGGGCTGGGCGAC
GGCGAGGACGCACCGGTGCGTCCGCTGTGCAAGCCCCGCGGCATCTGCTCGCGCGCCTAC
TTCCTGGTGCTGATGGTGTTCGTGCACCTGTACCTGGGTAACGTGCTGGCGCTGCTGCTC
TTCGTGCACTACAGCAACGGCGACGAAAGCAGCGATCCCGGGCCCCAACACCGTGCCCAG
GGCCCCGGGCCCGAGCCCACCTTAGGTCCCCTCACCCGGCTGGAGGGCATCAAGGTGGGG
CACGAGCGTAAGGTCCAGCTGGTCACCGACAGGGATCACTTCATCCGAACCCTCAGCCTC
AAGCCGCTGCTCTTCGAAATCCCCGGCTTCCTGACTGATGAAGAGTGTCGGCTCATCATC
CATCTGGCGCAGATGAAGGGGTTACAGCGCAGCCAGATCCTGCCTACTGAAGAGTATGAA
GAGGCAATGAGCACTATGCAGGTCAGCCAGCTGGACCTCTTCCGGCTGCTGGACCAGAAC
CGTGATGGGCACCTTCAGCTCCGTGAGGTTCTGGCCCAGACTCGCCTGGGAAATGGATGG
TGGATGACTCCAGAGAGCATTCAGGAGATGTACGCCGCGATCAAGGCTGACCCTGATGCT
GACGGAGTGCTGAGTCTGCAGGAGTTCTCCAACATGGACCTTCGGGACTTCCACAAGTAC
ATGAGGAGCCACAAGGCAGAGTCCAGTGAGCTGGTGCGGAACAGCCACCATACCTGGCTC
TACCAGGGTGAGGGTGCCCACCACATCATGCGTGCCATCCGCCAGAGGGTGCTGCGCCTC
ACTCGCCTGTCGCCTGAGATCGTGGAGCTCAGCGAGCCGCTGCAGGTTGTTCGATATGGT
GAGGGGGGCCACTACCATGCCCACGTGGACAGTGGGCCTGTGTACCCAGAGACCATCTGC
TCCCATACCAAGCTGGTAGCCAACGAGTCTGTACCCTTCGAGACCTCCTGCCGCTACATG
ACAGTGCTGTTTTATTTGAACAACGTCACTGGTGGGGGCGAGACTGTTTTCCCTGTAGCA
GATAACAGAACCTACGATGAAATGAGTCTGATTCAGGATGACGTGGACCTCCGTGACACA
CGGAGGCACTGTGACAAGGGAAACCTGCGTGTCAAGCCCCAACAGGGCACAGCAGTCTTC
TGGTACAACTACCTGCCTGATGGGCAAGGTTGGGTGGGTGACGTAGACGACTACTCGCTG
CACGGGGGCTGCCTGGTCACGCGCGGCACCAAGTGGATTGCCAACAACTGGATTAATGTG
GACCCCAGCCGAGCGCGGCAAGCGCTGTTCCAACAGGAGATGGCCCGCCTTGCCCGAGAA
GGGGGCACCGACTCACAGCCCGAGTGGGCTCTGGACCGGGCCTACCGCGATGCGCGCGTG
GAACTCTGA
Enzyme 23 GenBank Gene ID AY198406 Link Image
Enzyme 23 GeneCard ID Q9NXG6 Link Image
Enzyme 23 GenAtlas ID Not Available
Enzyme 23 HGNC ID Not Available
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 15069
Enzyme 24 Name Uncharacterized protein PAM
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name PAM
Enzyme 24 Protein Sequence >Uncharacterized protein PAM 
MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALD
IRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWF
CDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKD
CSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHH
LGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATH
IGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHE
HHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESES
DLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQ
PPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSF
DSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALH
QVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFS
PSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVR
EIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFD
MPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMEN
KPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGGKNS
EHKLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESE
EEYSAPLPALAPSSS
Enzyme 24 Number of Residues 975
Enzyme 24 Molecular Weight 108517
Enzyme 24 Theoretical pI 6.49
Enzyme 24 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • copper ion binding
  • ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
  • peptidylglycine monooxygenase activity
  • transition metal ion binding
Process
  • cellular metabolism
  • metabolism
  • peptide metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID A6NMR0 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name A6NMR0_HUMAN Link Image
Enzyme 24 PDB ID 1SDW Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID AC010250 Link Image
Enzyme 24 GeneCard ID A6NMR0 Link Image
Enzyme 24 GenAtlas ID PAM Link Image
Enzyme 24 HGNC ID HGNC:8596 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 16431
Enzyme 25 Name Putative uncharacterized protein
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name BBOX1
Enzyme 25 Protein Sequence >Putative uncharacterized protein 
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDV
NIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSEL
QLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHT
WQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQK
LKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISR
HLEGAYADWDVVMSRLRILRQRVENGN
Enzyme 25 Number of Residues 387
Enzyme 25 Molecular Weight 44715
Enzyme 25 Theoretical pI 6.73
Enzyme 25 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein Not Available
Enzyme 25 UniProtKB/Swiss-Prot ID B2R8L7 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name B2R8L7_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence Not Available
Enzyme 25 GenBank Gene ID AK313422 Link Image
Enzyme 25 GeneCard ID B2R8L7 Link Image
Enzyme 25 GenAtlas ID Not Available
Enzyme 25 HGNC ID Not Available
Enzyme 25 Chromosome Location 11
Enzyme 25 Locus 11p14.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 16432
Enzyme 26 Name cDNA, FLJ93151, Homo sapiens procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3 (PLOD3), mRNA (Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3)
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name PLOD3
Enzyme 26 Protein Sequence >cDNA, FLJ93151, Homo sapiens procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3 (PLOD3), mRNA (Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3) 
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAE
FFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAG
SPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIV
RQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRI
RNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFL
AVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLV
GPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSR
HGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRD
VFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDW
KEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRL
AGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDE
QPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHE
GLPTTWGTRYIMVSFVDP
Enzyme 26 Number of Residues 738
Enzyme 26 Molecular Weight 84786
Enzyme 26 Theoretical pI 5.95
Enzyme 26 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
  • procollagen-lysine 5-dioxygenase activity
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
  • endoplasmic reticulum
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • organelle
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein Not Available
Enzyme 26 UniProtKB/Swiss-Prot ID B2R6W6 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name B2R6W6_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence Not Available
Enzyme 26 GenBank Gene ID AK312743 Link Image
Enzyme 26 GeneCard ID B2R6W6 Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID Not Available
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 16890
Enzyme 27 Name 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1
Enzyme 27 Synonyms
  1. Termination and polyadenylation 1 homolog
Enzyme 27 Gene Name OGFOD1
Enzyme 27 Protein Sequence >2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1 
MNGKRPAEPGPARVGKKGKKEVMAEFSDAVTEETLKKQVAEAWSRRTPFSHEVIVMDMDP
FLHCVIPNFIQSQDFLEGLQKELMNLDFHEKYNDLYKFQQSDDLKKRREPHISTLRKILF
EDFRSWLSDISKIDLESTIDMSCAKYEFTDALLCHDDELEGRRIAFILYLVPPWDRSMGG
TLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSPVSFHQVSEVLSEEKSRLSISGWFHGP
SLTRPPNYFEPPIPRSPHIPQDHEILYDWINPTYLDMDYQVQIQEEFEESSEILLKEFLK
PEKFTKVCEALEHGHVEWSSRGPPNKRFYEKAEESKLPEILKECMKLFRSEALFLLLSNF
TGLKLHFLAPSEEDEMNDKKEAETTDITEEGTSHSPPEPENNQMAISNNSQQSNEQTDPE
PEENETKKESSVPMCQGELRHWKTGHYTLIHDHSKAEFALDLILYCGCEGWEPEYGGFTS
YIAKGEDEELLTVNPESNSLALVYRDRETLKFVKHINHRSLEQKKTFPNRTGFWDFSFIY
YE
Enzyme 27 Number of Residues 542
Enzyme 27 Molecular Weight 63247
Enzyme 27 Theoretical pI 4.77
Enzyme 27 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID Q8N543 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name OGFD1_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID AB046832 Link Image
Enzyme 27 GeneCard ID Q8N543 Link Image
Enzyme 27 GenAtlas ID OGFOD1 Link Image
Enzyme 27 HGNC ID HGNC:25585 Link Image
Enzyme 27 Chromosome Location 16
Enzyme 27 Locus 16q13
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Aug 31;7(4):273-81. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 16891
Enzyme 28 Name 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name OGFOD2
Enzyme 28 Protein Sequence >2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2 
MATVGAPRHFCRCACFCTDNLYVARYGLHVRFRGEQQLRRDYGPILRSRGCVSAKDFQQL
LAELEQEVERRQRLGQESAARKALIASSYHPARPEVYDSLQDAALAPEFLAVTEYSVSPD
ADLKGLLQRLETVSEEKRIYRVPVFTAPFCQALLEELEHFEQSDMPKGRPNTMNNYGVLL
HELGLDEPLMTPLRERFLQPLMALLYPDCGGGRLDSHRAFVVKYAPGQDLELGCHYDNAE
LTLNVALGKVFTGGALYFGGLFQAPTALTEPLEVEHVVGQGVLHRGGQLHGARPLGTGER
WNLVVWLRASAVRNSLCPMCCREPDLVDDEGFGDGFTREEPATVDVCALT
Enzyme 28 Number of Residues 350
Enzyme 28 Molecular Weight 38997
Enzyme 28 Theoretical pI 5.44
Enzyme 28 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID Q6N063 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name OGFD2_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID AK023553 Link Image
Enzyme 28 GeneCard ID Q6N063 Link Image
Enzyme 28 GenAtlas ID OGFOD2 Link Image
Enzyme 28 HGNC ID HGNC:25823 Link Image
Enzyme 28 Chromosome Location 12
Enzyme 28 Locus 12q24.31
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available