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Human Metabolome Database Version 2.5

 

Showing metabocard for Dihydroxyacetone phosphate (HMDB01473)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:48
Accession Number HMDB01473
Secondary Accession Numbers HMDB11735
Common Name Dihydroxyacetone phosphate
Description An important intermediate in lipid biosynthesis and in glycolysis.
Synonyms
  1. 1,3-Dihydroxy-2-propanone phosphate
  2. 1,3-Dihydroxyacetone 1-phosphate
  3. 1,3-dihydroxy-2-Propanone mono(dihydrogen phosphate)
  4. 1-Hydroxy-3-(phosphonooxy)acetone
  5. 1-hydroxy-3-(phosphonooxy)-2-Propanone
  6. Dihydroxy-Acetone-P
  7. Dihydroxyacetone monophosphate
  8. Dihydroxyacetone phosphate
  9. Dihydroxyacetone phosphic acid
  10. Glycerone phosphate
  11. Phosphoric acid ester with 1,3-dihydroxy-2-propanone
  12. di-OH-acetone-P
  13. dihydroxy-acetone-phosphate
  14. dihydroxyacetone 3-phosphate
  15. dihydroxyacetone-P
  16. dihydroxyacetone-phosphate
  17. glycerone-phosphate;DHAP
Chemical IUPAC Name (3-hydroxy-2-oxo-propoxy)phosphonic acid
Chemical Formula C3H7O6P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Glycerophosphates
Family
  • Mammalian Metabolite
Species
  • ketone
  • primary alcohol
  • phosphoric acid ester
Biofunction
  • Component of Fructose and mannose metabolism
  • Component of Glycerophospholipid metabolism
  • Component of Inositol metabolism
Application
Source
  • Endogenous
Average Molecular Weight 170.058
Monoisotopic Molecular Weight 169.998032
Isomeric SMILES OCC(=O)COP(O)(O)=O
Canonical SMILES OCC(=O)COP(O)(O)=O
KEGG Compound ID C00111 Link Image
BioCyc ID DIHYDROXY-ACETONE-PHOSPHATE Link Image
BiGG ID 33898 Link Image
Wikipedia Link Dihydroxyacetone phosphate Link Image
NuGOwiki Link HMDB01473 Link Image
Metagene Link HMDB01473 Link Image
METLIN ID 6262 Link Image
PubChem Compound 668 Link Image
PubChem Substance 8145644 Link Image
ChEBI ID 15835 Link Image
CAS Registry Number 57-04-5
InChI Identifier InChI=1/C3H7O6P/c4-1-3(5)2-9-10(6,7)8/h4H,1-2H2,(H2,6,7,8)
Synthesis Reference Ballou, Clinton E.; Fischer, Hermann O. L. The synthesis of dihydroxyacetone phosphate. Journal of the American Chemical Society (1956), 78 1659-61.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 21.900002 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.49 [Predicted by ALOGPS]; -3.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • peroxisome
Biofluid Location
  • Blood
  • Cellular Cytoplasm
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 12.1 +/- 5.1 uM
Age Newborn:0-30 days 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 Blood
Value 15.6 +/- 4.56 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Huck JH, Struys EA, Verhoeven NM, Jakobs C, van der Knaap MS: Profiling of pentose phosphate pathway intermediates in blood spots by tandem mass spectrometry: application to transaldolase deficiency. Clin Chem. 2003 Aug;49(8):1375-80. [PubMed Link Image]
Biofluid Cellular Cytoplasm
Value 140 (60-220) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 1.88 +/- 0.34 uM
Age Adult:>18 yrs old
Sex Both
Condition Transaldolase deficiency
Comments Not Available
References
  • Huck JH, Struys EA, Verhoeven NM, Jakobs C, van der Knaap MS: Profiling of pentose phosphate pathway intermediates in blood spots by tandem mass spectrometry: application to transaldolase deficiency. Clin Chem. 2003 Aug;49(8):1375-80. [PubMed Link Image]
Associated Disorders
Condition References
Transaldolase deficiency
  • Huck JH, Struys EA, Verhoeven NM, Jakobs C, van der Knaap MS: Profiling of pentose phosphate pathway intermediates in blood spots by tandem mass spectrometry: application to transaldolase deficiency. Clin Chem. 2003 Aug;49(8):1375-80. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Fructose and Mannose Degradation SMP00064 Link Image map00051 Link Image
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Glycerol Phosphate Shuttle SMP00124 Link Image
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
Glycolysis SMP00040 Link Image map00010 Link Image
Mitochondrial Electron Transport Chain SMP00355 Link Image map00190 Link Image
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Roberts NB, Dutton J, Helliwell T, Rothwell PJ, Kavanagh JP: Pyrophosphate in synovial fluid and urine and its relationship to urinary risk factors for stone disease. Ann Clin Biochem. 1992 Sep;29 ( Pt 5):529-34. [PubMed Link Image]
  2. Yamamoto T, Moriwaki Y, Takahashi S, Ohata H, Nakano T, Yamakita J, Higashino K: Effect of glucagon on the xylitol-induced increase in the plasma concentration and urinary excretion of purine bases. Metabolism. 1996 Nov;45(11):1354-9. [PubMed Link Image]
  3. Schutgens RB, Wanders RJ, Heymans HS, Schram AW, Tager JM, Schrakamp G, van den Bosch H: Zellweger syndrome: biochemical procedures in diagnosis, prevention and treatment. J Inherit Metab Dis. 1987;10 Suppl 1:33-45. [PubMed Link Image]
  4. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
  5. Wikipedia Link Image
Metabolic Enzymes
  1. Alkaline phosphatase, placental type
  2. Intestinal-type alkaline phosphatase
  3. Alkaline phosphatase, tissue-nonspecific isozyme
  4. Alkaline phosphatase, placental-like
  5. Glycerol-3-phosphate dehydrogenase, mitochondrial
  6. Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
  7. Fructose-bisphosphate aldolase A
  8. Fructose-bisphosphate aldolase C
  9. Fructose-bisphosphate aldolase B
  10. Dihydroxyacetone phosphate acyltransferase
  11. Triosephosphate isomerase
  12. Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
  13. Glycerol-3-phosphate dehydrogenase 1-like protein
  14. cDNA FLJ75492, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
  15. Triosephosphate isomerase
  16. cDNA, FLJ93658, highly similar to Homo sapiens alkaline phosphatase, intestinal (ALPI), mRNA (Alkaline phosphatase, intestinal, isoform CRA_a)
  17. cDNA, FLJ92580, Homo sapiens aldolase C, fructose-bisphosphate (ALDOC), mRNA (Aldolase C, fructose-bisphosphate, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5322
Enzyme 1 Name Alkaline phosphatase, placental type
Enzyme 1 Synonyms
  1. Alkaline phosphatase Regan isozyme
  2. Placental alkaline phosphatase 1
  3. PLAP-1
Enzyme 1 Gene Name ALPP
Enzyme 1 Protein Sequence >Alkaline phosphatase, placental type
MLGPCMLLLLLLLGLRLQLSLGIIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLII
FLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALSKTYNVDKHVPDSGATATA
YLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAG
TYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYP
DDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEI
HRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAI
ERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPG
YVLKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFI
AHVMAFAACLEPYTACDLAPPAGTTDAAHPGRSVVPALLPLLAGTLLLLETATAP
Enzyme 1 Number of Residues 535
Enzyme 1 Molecular Weight 57953.3
Enzyme 1 Theoretical pI 6.24
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
  • metabolic process
Component
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 1 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 1 Reactions
  • a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-22
Enzyme 1 Transmembrane Regions
  • 513-529
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 178474 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P05187 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PPB1_HUMAN Link Image
Enzyme 1 PDB ID 1EW2 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1608 bp
ATGCTGGGGCCCTGCATGCTGCTGCTGCTGCTGCTGCTGGGCCTGAGGCTACAGCTCTCC
CTGGGCATCATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCGAGGCAGCCGAG
GCCCTGGGTGCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATC
TTCCTGGGCGATGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAG
AAGAAGGACAAACTGGGGCCTGAGATACCCCTGGCCATGGACCGCTTCCCATATGTGGCT
CTGTCCAAGACATACAATGTAGACAAACATGTGCCAGACAGTGGAGCCACAGCCACGGCC
TACCTGTGCGGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTT
AACCAGTGCAACACGACACGCGGCAACGAGGTCATCTCCGTGATGAATCGGGCCAAGAAA
GCAGGGAAGTCAGTGGGAGTGGTAACCACCACACGAGTGCAGCACGCCTCGCCAGCCGGC
ACCTACGCCCACACGGTGAACCGCAACTGGTACTCGGACGCCGACGTGCCTGCCTCGGCC
CGCCAGGAGGGGTGCCAGGACATCGCTACGCAGCTCATCTCCAACATGGACATTGACGTG
ATCCTAGGTGGAGGCCGAAAGTACATGTTTCCCATGGGAACCCCAGACCCTGAGTACCCA
GATGACTACAGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTG
GCGAAGCGCCAGGGTGCCCGGTATGTGTGGAACCGCACTGAGCTCATGCAGGCTTCCCTG
GACCCGTCTGTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATC
CACCGAGACTCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCGCCTG
CTGAGCAGGAACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGT
CATCATGAAAGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATT
GAGAGGGCGGGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCAC
TCCCACGTCTTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCC
CCTGGCAAGGCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGC
TATGTGCTCAAGGACGGCGCCCGGCCGGATGTTACCGAGAGCGAGAGCGGGAGCCCCGAG
TATCGGCAGCAGTCAGCAGTGCCCCTGGACGAAGAGACCCACGCAGGCGAGGACGTGGCG
GTGTTCGCGCGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATA
GCGCACGTCATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCC
CCCGCCGGCACCACCGACGCCGCGCACCCGGGGCGGTCCGTGGTCCCCGCGTTGCTTCCT
CTGCTGGCCGGGACCCTGCTGCTGCTGGAGACGGCCACTGCTCCCTGA
Enzyme 1 GenBank Gene ID M13077 Link Image
Enzyme 1 GeneCard ID ALPP Link Image
Enzyme 1 GenAtlas ID ALPP Link Image
Enzyme 1 HGNC ID HGNC:439 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q37
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Knoll BJ, Rothblum KN, Longley M: Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution. J Biol Chem. 1988 Aug 25;263(24):12020-7. [PubMed Link Image]
  2. Millan JL: Molecular cloning and sequence analysis of human placental alkaline phosphatase. J Biol Chem. 1986 Mar 5;261(7):3112-5. [PubMed Link Image]
  3. Henthorn PS, Knoll BJ, Raducha M, Rothblum KN, Slaughter C, Weiss M, Lafferty MA, Fischer T, Harris H: Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids. Proc Natl Acad Sci U S A. 1986 Aug;83(15):5597-601. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Kam W, Clauser E, Kim YS, Kan YW, Rutter WJ: Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8715-9. [PubMed Link Image]
  7. Ezra E, Blacher R, Udenfriend S: Purification and partial sequencing of human placental alkaline phosphatase. Biochem Biophys Res Commun. 1983 Nov 15;116(3):1076-83. [PubMed Link Image]
  8. Ovitt CE, Strauss AW, Alpers DH, Chou JY, Boime I: Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells. Proc Natl Acad Sci U S A. 1986 Jun;83(11):3781-5. [PubMed Link Image]
  9. Micanovic R, Bailey CA, Brink L, Gerber L, Pan YC, Hulmes JD, Udenfriend S: Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1398-402. [PubMed Link Image]
  10. Micanovic R, Gerber LD, Berger J, Kodukula K, Udenfriend S: Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase. Proc Natl Acad Sci U S A. 1990 Jan;87(1):157-61. [PubMed Link Image]
  11. Lowe ME: Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein. J Cell Biol. 1992 Feb;116(3):799-807. [PubMed Link Image]
  12. Kozlenkov A, Manes T, Hoylaerts MF, Millan JL: Function assignment to conserved residues in mammalian alkaline phosphatases. J Biol Chem. 2002 Jun 21;277(25):22992-9. Epub 2002 Apr 5. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Le Du MH, Stigbrand T, Taussig MJ, Menez A, Stura EA: Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity. J Biol Chem. 2001 Mar 23;276(12):9158-65. Epub 2000 Dec 20. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5325
Enzyme 2 Name Intestinal-type alkaline phosphatase
Enzyme 2 Synonyms
  1. IAP
  2. Intestinal alkaline phosphatase
Enzyme 2 Gene Name ALPI
Enzyme 2 Protein Sequence >Intestinal-type alkaline phosphatase
MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLG
DGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLC
GVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYA
HTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADA
SQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRD
PTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERA
GQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVF
NSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHV
MAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP
Enzyme 2 Number of Residues 528
Enzyme 2 Molecular Weight 56811.7
Enzyme 2 Theoretical pI 5.70
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
  • metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 2 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 2 Reactions
  • a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-19
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 178432 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P09923 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PPBI_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1587 bp
ATGCAGGGGCCCTGGGTGCTGCTGCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCGTC
ATCCCAGCTGAGGAGGAGAACCCGGCCTTCTGGAACCGCCAGGCAGCTGAGGCCCTGGAT
GCTGCCAAGAAGCTGCAGCCCATCCAGAAGGTCGCCAAGAACCTCATCCTCTTCCTGGGC
GATGGGTTGGGGGTGCCCACGGTGACAGCCACCAGGATCCTAAAGGGGCAGAAGAATGGC
AAACTGGGGCCTGAGACGCCCCTGGCCATGGACCGCTTCCCATACCTGGCTCTGTCCAAG
ACATACAATGTGGACAGACAGGTGCCAGACAGCGCAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGCCAACTTCCAGACCATCGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAATGAGGTCATCTCCGTGATGAACCGGGCCAAGCAAGCAGGAAAG
TCAGTAGGAGTGGTGACCACCACACGGGTGCAGCACGCCTCGCCAGCCGGCACCTACGCA
CACACAGTGAACCGCAACTGGTACTCAGATGCTGACATGCCTGCCTCAGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACTCAGCTCATCTCCAACATGGACATTGACGTGATCCTTGGC
GGAGGCCGCAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGCTGATGCC
AGCCAGAATGGAATCAGGCTGGACGGGAAGAACCTGGTGCAGGAATGGCTGGCAAAGCAC
CAGGGTGCCTGGTATGTGTGGAACCGCACTGAGCTCATGCAGGCGTCCCTGGACCAGTCT
GTGACCCATCTCATGGGCCTCTTTGAGCCCGGAGACACGAAATATGAGATCCTCCGAGAC
CCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCGCCTGCTGAGCAGG
AACCCCCGCGGCTTCTACCTCTTTGTGGAGGGCGGCCGCATCGACCATGGTCATCATGAG
GGTGTGGCTTACCAGGCAGTCACTGAGGCGGTCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGACCCTCGTCACCGCTGACCACTCCCATGTC
TTCTCCTTTGGTGGCTACACCTTGCGAGGGAGCTCCATCTTCGGGTTGGCCCCCAGCAAG
GCTCAGGACAGCAAAGCCTACACGTCCATCCTGTACGGCAATGGCCCGGGCTACGTGTTC
AACTCAGGCGTGCGACCAGACGTGAATGAGAGCGAGAGCGGGAGCCCCGATTACCAGCAG
CAGGCGGCGGTGCCCCTGTCGTCCGAGACCCACGGAGGCGAAGACGTGGCGGTGTTTGCG
CGCGGCCCGCAGGCGCACCTGGTGCATGGTGTGCAGGAGCAGAGCTTCGTAGCGCATGTC
ATGGCCTTCGCTGCCTGTCTGGAGCCCTACACGGCCTGCGACCTGGCGCTCCCCGCCTGC
ACCACCGACGCCGCGCACCCAGTTGCCGCGTCGCTGCCACTGCTGGCCGGGACCCTGCTG
CTGCTGGGGGCGTCCGCTGCTCCCTGA
Enzyme 2 GenBank Gene ID M15694 Link Image
Enzyme 2 GeneCard ID ALPI Link Image
Enzyme 2 GenAtlas ID ALPI Link Image
Enzyme 2 HGNC ID HGNC:437 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2q37.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Berger J, Garattini E, Hua JC, Udenfriend S: Cloning and sequencing of human intestinal alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1987 Feb;84(3):695-8. [PubMed Link Image]
  2. Henthorn PS, Raducha M, Edwards YH, Weiss MJ, Slaughter C, Lafferty MA, Harris H: Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1234-8. [PubMed Link Image]
  3. Henthorn PS, Raducha M, Kadesch T, Weiss MJ, Harris H: Sequence and characterization of the human intestinal alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12011-9. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Millan JL: Promoter structure of the human intestinal alkaline phosphatase gene. Nucleic Acids Res. 1987 Dec 23;15(24):10599. [PubMed Link Image]
  8. Knoll BJ, Rothblum KN, Longley M: Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene. 1987;60(2-3):267-76. [PubMed Link Image]
  9. Hua JC, Berger J, Pan YC, Hulmes JD, Udenfriend S: Partial sequencing of human adult, human fetal, and bovine intestinal alkaline phosphatases: comparison with the human placental and liver isozymes. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2368-72. [PubMed Link Image]
  10. Nishihara Y, Hayashi Y, Adachi T, Koyama I, Stigbrand T, Hirano K: Chemical nature of intestinal-type alkaline phosphatase in human kidney. Clin Chem. 1992 Dec;38(12):2539-42. [PubMed Link Image]
  11. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5328
Enzyme 3 Name Alkaline phosphatase, tissue-nonspecific isozyme
Enzyme 3 Synonyms
  1. AP-TNAP
  2. TNSALP
  3. Alkaline phosphatase liver/bone/kidney isozyme
Enzyme 3 Gene Name ALPL
Enzyme 3 Protein Sequence >Alkaline phosphatase, tissue-nonspecific isozyme
MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGD
GMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCG
VKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAH
SADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDE
KARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELN
RNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIG
QAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPG
YKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYV
PHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF
Enzyme 3 Number of Residues 524
Enzyme 3 Molecular Weight 57304.4
Enzyme 3 Theoretical pI 6.66
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
  • metabolic process
Component
Enzyme 3 General Function Involved in catalytic activity
Enzyme 3 Specific Function This isozyme may play a role in skeletal mineralization
Enzyme 3 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 3 Reactions
  • a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-17
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 28738 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P05186 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PPBT_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1575 bp
ATGATTTCACCATTCTTAGTACTGGCCATTGGCACCTGCCTTACTAACTCCTTAGTGCCA
GAGAAAGAGAAAGACCCCAAGTACTGGCGAGACCAAGCGCAAGAGACACTGAAATATGCC
CTGGAGCTTCAGAAGCTCAACACCAACGTGGCTAAGAATGTCATCATGTTCCTGGGAGAT
GGGATGGGTGTCTCCACAGTGACGGCTGCCCGCATCCTCAAGGGTCAGCTCCACCACAAC
CCTGGGGAGGAGACCAGGCTGGAGATGGACAAGTTCCCCTTCGTGGCCCTCTCCAAGACG
TACAACACCAAAGCCCAGGTCCCTGACAGCGCCGGCACCGCCACCGCCTACCTGTGTGGG
GTGAAGGCCAATGAGGGCACCGTGGGGGTAAGCGCAGCCACTGAGCGTTCCCGGTGCAAC
ACCACCCAGGGGAACGAGGTCACCTCCATCCTGCGCTGGGCCAAGGACGCTGGGAAATCT
GTGGGCATTGTGACCACCACGAGAGTGAACCATGCCACCCCCAGCGCCGCCTACGCCCAC
TCGGCTGACCGGGACTGGTACTCAGACAACGAGATGCCCCCTGAGGCCTTGAGCCAGGGC
TGTAAGGACATCGCCTACCAGCTCATGCATAACATCAGGGACATTGACGTGATCATGGGG
GGTGGCCGGAAATACATGTACCCCAAGAATAAAACTGATGTGGAGTATGAGAGTGACGAG
AAAGCCAGGGGCACGAGGCTGGACGGCCTGGACCTCGTTGACACCTGGAAGAGCTTCAAA
CCGAGACACAAGCACTCCCACTTCATCTGGAACCGCACGGAACTCCTGACCCTTGACCCC
CACAATGTGGACTACCTATTGGGTCTCTTCGAGCCGGGGGACATGCAGTACGAGCTGAAC
AGGAACAACGTGACGGACCCGTCACTCTCCGAGATGGTGGTGGTGGCCATCCAGATCCTG
CGGAAGAACCCCAAAGGCTTCTTCTTGCTGGTGGAAGGAGGCAGAATTGACCACGGGCAC
CATGAAGGAAAAGCCAAGCAGGCCCTGCATGAGGCGGTGGAGATGGACCGGGCCATCGGG
CAGGCAGGCAGCTTGACCTCCTCGGAAGACACTCTGACCGTGGTCACTGCGGACCATTCC
CACGTCTTCACATTTGGTGGATACACCCCCCGTGGCAACTCTATCTTTGGTCTGGCCCCC
ATGCTGAGTGACACAGACAAGAAGCCCTTCACTGCCATCCTGTATGGCAATGGGCCTGGC
TACAAGGTGGTGGGCGGTGAACGAGAGAATGTCTCCATGGTGGACTATGCTCACAACAAC
TACCAGGCGCAGTCTGCTGTGCCCCTGCGCCACGAGACCCACGGCGGGGAGGACGTGGCC
GTCTTCTCCAAGGGCCCCATGGCGCACCTGCTGCACGGCGTCCACGAGCAGAACTACGTC
CCCCACGTGATGGCGTATGCAGCCTGCATCGGGGCCAACCTCGGCCACTGTGCTCCTGCC
AGCTCGGCAGGCAGCCTTGCTGCAGGCCCCCTGCTGCTCGCGCTGGCCCTCTACCCCCTG
AGCGTCCTGTTCTGA
Enzyme 3 GenBank Gene ID X14174 Link Image
Enzyme 3 GeneCard ID ALPL Link Image
Enzyme 3 GenAtlas ID ALPL Link Image
Enzyme 3 HGNC ID HGNC:438 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p36.12
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Weiss MJ, Henthorn PS, Lafferty MA, Slaughter C, Raducha M, Harris H: Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7182-6. [PubMed Link Image]
  2. Weiss MJ, Ray K, Henthorn PS, Lamb B, Kadesch T, Harris H: Structure of the human liver/bone/kidney alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12002-10. [PubMed Link Image]
  3. Kishi F, Matsuura S, Kajii T: Nucleotide sequence of the human liver-type alkaline phosphatase cDNA. Nucleic Acids Res. 1989 Mar 11;17(5):2129. [PubMed Link Image]
  4. Sugimoto N, Iwamoto S, Hoshino Y, Kajii E: A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia. J Hum Genet. 1998;43(3):160-4. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Garattini E, Hua JC, Pan YC, Udenfriend S: Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme. Arch Biochem Biophys. 1986 Mar;245(2):331-7. [PubMed Link Image]
  8. Nishihara Y, Hayashi Y, Adachi T, Koyama I, Stigbrand T, Hirano K: Chemical nature of intestinal-type alkaline phosphatase in human kidney. Clin Chem. 1992 Dec;38(12):2539-42. [PubMed Link Image]
  9. Elortza F, Nuhse TS, Foster LJ, Stensballe A, Peck SC, Jensen ON: Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins. Mol Cell Proteomics. 2003 Dec;2(12):1261-70. Epub 2003 Sep 29. [PubMed Link Image]
  10. Elortza F, Mohammed S, Bunkenborg J, Foster LJ, Nuhse TS, Brodbeck U, Peck SC, Jensen ON: Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment. J Proteome Res. 2006 Apr;5(4):935-43. [PubMed Link Image]
  11. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  12. Weiss MJ, Cole DE, Ray K, Whyte MP, Lafferty MA, Mulivor RA, Harris H: A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7666-9. [PubMed Link Image]
  13. Henthorn PS, Raducha M, Fedde KN, Lafferty MA, Whyte MP: Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9924-8. [PubMed Link Image]
  14. Greenberg CR, Taylor CL, Haworth JC, Seargeant LE, Philipps S, Triggs-Raine B, Chodirker BN: A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites. Genomics. 1993 Jul;17(1):215-7. [PubMed Link Image]
  15. Orimo H, Hayashi Z, Watanabe A, Hirayama T, Hirayama T, Shimada T: Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia. Hum Mol Genet. 1994 Sep;3(9):1683-4. [PubMed Link Image]
  16. Ozono K, Yamagata M, Michigami T, Nakajima S, Sakai N, Cai G, Satomura K, Yasui N, Okada S, Nakayama M: Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia. J Clin Endocrinol Metab. 1996 Dec;81(12):4458-61. [PubMed Link Image]
  17. Mornet E, Taillandier A, Peyramaure S, Kaper F, Muller F, Brenner R, Bussiere P, Freisinger P, Godard J, Le Merrer M, Oury JF, Plauchu H, Puddu R, Rival JM, Superti-Furga A, Touraine RL, Serre JL, Simon-Bouy B: Identification of fifteen novel mutations in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in European patients with severe hypophosphatasia. Eur J Hum Genet. 1998 Jul-Aug;6(4):308-14. [PubMed Link Image]
  18. Goseki-Sone M, Orimo H, Iimura T, Takagi Y, Watanabe H, Taketa K, Sato S, Mayanagi H, Shimada T, Oida S: Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients. Hum Mutat. 1998;Suppl 1:S263-7. [PubMed Link Image]
  19. Zurutuza L, Muller F, Gibrat JF, Taillandier A, Simon-Bouy B, Serre JL, Mornet E: Correlations of genotype and phenotype in hypophosphatasia. Hum Mol Genet. 1999 Jun;8(6):1039-46. [PubMed Link Image]
  20. Taillandier A, Zurutuza L, Muller F, Simon-Bouy B, Serre JL, Bird L, Brenner R, Boute O, Cousin J, Gaillard D, Heidemann PH, Steinmann B, Wallot M, Mornet E: Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia. Mutations in brief no. 217. Online. Hum Mutat. 1999;13(2):171-2. [PubMed Link Image]
  21. Mochizuki H, Saito M, Michigami T, Ohashi H, Koda N, Yamaguchi S, Ozono K: Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene. Eur J Pediatr. 2000 May;159(5):375-9. [PubMed Link Image]
  22. Taillandier A, Cozien E, Muller F, Merrien Y, Bonnin E, Fribourg C, Simon-Bouy B, Serre JL, Bieth E, Brenner R, Cordier MP, De Bie S, Fellmann F, Freisinger P, Hesse V, Hennekam RC, Josifova D, Kerzin-Storrar L, Leporrier N, Zabot MT, Mornet E: Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S, 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with hypophosphatasia. Hum Mutat. 2000 Mar;15(3):293. [PubMed Link Image]
  23. Muller HL, Yamazaki M, Michigami T, Kageyama T, Schonau E, Schneider P, Ozono K: Asp361Val Mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme. J Clin Endocrinol Metab. 2000 Feb;85(2):743-7. [PubMed Link Image]
  24. Sergi C, Mornet E, Troeger J, Voigtlaender T: Perinatal hypophosphatasia: radiology, pathology and molecular biology studies in a family harboring a splicing mutation (648+1A) and a novel missense mutation (N400S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene. Am J Med Genet. 2001 Oct 15;103(3):235-40. [PubMed Link Image]
  25. Lia-Baldini AS, Muller F, Taillandier A, Gibrat JF, Mouchard M, Robin B, Simon-Bouy B, Serre JL, Aylsworth AS, Bieth E, Delanote S, Freisinger P, Hu JC, Krohn HP, Nunes ME, Mornet E: A molecular approach to dominance in hypophosphatasia. Hum Genet. 2001 Jul;109(1):99-108. [PubMed Link Image]
  26. Taillandier A, Lia-Baldini AS, Mouchard M, Robin B, Muller F, Simon-Bouy B, Serre JL, Bera-Louville A, Bonduelle M, Eckhardt J, Gaillard D, Myhre AG, Kortge-Jung S, Larget-Piet L, Malou E, Sillence D, Temple IK, Viot G, Mornet E: Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia. Hum Mutat. 2001;18(1):83-4. [PubMed Link Image]
  27. Orimo H, Girschick HJ, Goseki-Sone M, Ito M, Oda K, Shimada T: Mutational analysis and functional correlation with phenotype in German patients with childhood-type hypophosphatasia. J Bone Miner Res. 2001 Dec;16(12):2313-9. [PubMed Link Image]
  28. Watanabe H, Hashimoto-Uoshima M, Goseki-Sone M, Orimo H, Ishikawa I: A novel point mutation (C571T) in the tissue-non-specific alkaline phosphatase gene in a case of adult-type hypophosphatasia. Oral Dis. 2001 Nov;7(6):331-5. [PubMed Link Image]
  29. Litmanovitz, Reish O, Dolfin T, Arnon S, Regev R, Grinshpan G, Yamazaki M, Ozono K: Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline phosphatase gene in neonatal hypophosphatasia associated with convulsions. J Inherit Metab Dis. 2002 Feb;25(1):35-40. [PubMed Link Image]
  30. Mumm S, Jones J, Finnegan P, Henthorn PS, Podgornik MN, Whyte MP: Denaturing gradient gel electrophoresis analysis of the tissue nonspecific alkaline phosphatase isoenzyme gene in hypophosphatasia. Mol Genet Metab. 2002 Feb;75(2):143-53. [PubMed Link Image]
  31. Spentchian M, Merrien Y, Herasse M, Dobbie Z, Glaser D, Holder SE, Ivarsson SA, Kostiner D, Mansour S, Norman A, Roth J, Stipoljev F, Taillemite JL, van der Smagt JJ, Serre JL, Simon-Bouy B, Taillandier A, Mornet E: Severe hypophosphatasia: characterization of fifteen novel mutations in the ALPL gene. Hum Mutat. 2003 Jul;22(1):105-6. [PubMed Link Image]
  32. Herasse M, Spentchian M, Taillandier A, Keppler-Noreuil K, Fliorito AN, Bergoffen J, Wallerstein R, Muti C, Simon-Bouy B, Mornet E: Molecular study of three cases of odontohypophosphatasia resulting from heterozygosity for mutations in the tissue non-specific alkaline phosphatase gene. J Med Genet. 2003 Aug;40(8):605-9. [PubMed Link Image]
  33. Draguet C, Gillerot Y, Mornet E: [Childhood hypophosphatasia: a case report due to a novel mutation] Arch Pediatr. 2004 May;11(5):440-3. [PubMed Link Image]
  34. Brun-Heath I, Taillandier A, Serre JL, Mornet E: Characterization of 11 novel mutations in the tissue non-specific alkaline phosphatase gene responsible for hypophosphatasia and genotype-phenotype correlations. Mol Genet Metab. 2005 Mar;84(3):273-7. Epub 2004 Dec 19. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5331
Enzyme 4 Name Alkaline phosphatase, placental-like
Enzyme 4 Synonyms
  1. ALP-1
  2. Alkaline phosphatase Nagao isozyme
  3. Germ cell alkaline phosphatase
  4. GCAP
  5. Placental alkaline phosphatase-like
  6. PLAP-like
Enzyme 4 Gene Name ALPPL2
Enzyme 4 Protein Sequence >Alkaline phosphatase, placental-like
MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLG
DGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLC
GVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYA
HTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDY
SQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRD
STLDPSLMEMTEAALLLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERA
GQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVL
KDGARPDVTESESGSPEYRQQSAVPLDGETHAGEDVAVFARGPQAHLVHGVQEQTFIAHV
MAFAACLEPYTACDLAPRAGTTDAAHPGPSVVPALLPLLAGTLLLLGTATAP
Enzyme 4 Number of Residues 532
Enzyme 4 Molecular Weight 57376.5
Enzyme 4 Theoretical pI 6.31
Enzyme 4 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
  • metabolic process
Component
Enzyme 4 General Function Involved in catalytic activity
Enzyme 4 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 4 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 4 Reactions
  • a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-19
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 62988701 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P10696 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PPBN_HUMAN Link Image
Enzyme 4 PDB ID 1EW2 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1599 bp
ATGCAGGGGCCCTGGGTGCTGCTCCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCATC
ATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCCAGGCAGCCGAGGCCCTGGGT
GCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATCTTCCTGGGT
GACGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAGAAGAAGGAC
AAACTGGGGCCTGAGACCTTCCTGGCCATGGACCGCTTCCCGTACGTGGCTCTGTCCAAG
ACATACAGTGTAGACAAGCATGTGCCAGACAGTGGAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAACGAGGTCATCTCCGTGATGAATCGGGCCAAGAAAGCAGGAAAG
TCAGTGGGAGTGGTAACCACCACACGGGTGCAGCATGCCTCGCCAGCCGGCGCCTACGCC
CACACGGTGAACCGCAACTGGTACTCGGATGCCGACGTGCCTGCCTCGGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACGCAGCTCATCTCCAACATGGACATTGATGTGATCCTAGGT
GGAGGCCGAAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGATGACTAC
AGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTGGCGAAGCAC
CAGGGTGCCCGGTACGTGTGGAACCGCACTGAGCTCCTGCAGGCTTCCCTGGACCCGTCT
GTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATCCACCGAGAC
TCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCTCCTGCTGAGCAGG
AACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGTCATCATGAA
AGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCACTCCCACGTC
TTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCCCCTGGCAAG
GCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGCTATGTGCTC
AAGGACGGCGCCCGGCCGGATGTTACGGAGAGCGAGAGCGGGAGCCCCGAGTATCGGCAG
CAGTCAGCAGTGCCCCTGGACGGAGAGACCCACGCAGGCGAGGACGTGGCGGTGTTCGCG
CGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATAGCGCACGTC
ATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCCCGCGCCGGC
ACCACCGACGCCGCGCACCCGGGGCCGTCCGTGGTCCCCGCGTTGCTTCCTCTGCTGGCA
GGGACCTTGCTGCTGCTGGGGACGGCCACTGCTCCCTGA
Enzyme 4 GenBank Gene ID AC068134 Link Image
Enzyme 4 GeneCard ID ALPPL2 Link Image
Enzyme 4 GenAtlas ID ALPPL2 Link Image
Enzyme 4 HGNC ID HGNC:441 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 2q37
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Millan JL, Manes T: Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc Natl Acad Sci U S A. 1988 May;85(9):3024-8. [PubMed Link Image]
  2. Watanabe S, Watanabe T, Li WB, Soong BW, Chou JY: Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells. J Biol Chem. 1989 Jul 25;264(21):12611-9. [PubMed Link Image]
  3. Gum JR, Hicks JW, Sack TL, Kim YS: Molecular cloning of complementary DNAs encoding alkaline phosphatase in human colon cancer cells. Cancer Res. 1990 Feb 15;50(4):1085-91. [PubMed Link Image]
  4. Lowe ME, Strauss AW: Expression of a Nagao-type, phosphatidylinositol-glycan anchored alkaline phosphatase in human choriocarcinomas. Cancer Res. 1990 Jul 1;50(13):3956-62. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Knoll BJ, Rothblum KN, Longley M: Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene. 1987;60(2-3):267-76. [PubMed Link Image]
  9. Shen LP, Liu H, Kan YW, Kam W: 5' nucleotide sequence of a putative human placental alkaline phosphatase-like gene. Nucleic Acids Res. 1988 Jun 24;16(12):5694. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5429
Enzyme 5 Name Glycerol-3-phosphate dehydrogenase, mitochondrial
Enzyme 5 Synonyms
  1. GPD-M
  2. GPDH-M
  3. mtGPD
Enzyme 5 Gene Name GPD2
Enzyme 5 Protein Sequence >Glycerol-3-phosphate dehydrogenase, mitochondrial
MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQ
LLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVR
YLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLY
DLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYG
AATANYMEVVSLLKKTDPQTGKVRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKM
DDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTD
VTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNH
VVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY
IRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYG
IKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLY
YEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMD
ENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPV
DRSCGGL
Enzyme 5 Number of Residues 727
Enzyme 5 Molecular Weight 80852.0
Enzyme 5 Theoretical pI 7.77
Enzyme 5 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • glycerol-3-phosphate dehydrogenase activity
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor
Process
  • alcohol metabolic process
  • alditol metabolic process
  • glycerol metabolic process
  • glycerol-3-phosphate metabolic process
  • metabolic process
  • oxidation reduction
  • polyol metabolic process
  • small molecule metabolic process
Component
  • glycerol-3-phosphate dehydrogenase complex
  • macromolecular complex
  • protein complex
Enzyme 5 General Function Involved in calcium ion binding
Enzyme 5 Specific Function sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol
Enzyme 5 Pathways
Enzyme 5 Reactions
  • sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol [RN:R00849]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 285002233 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P43304 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GPDM_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2184 bp
ATGGCATTTCAAAAGGCAGTGAAAGGGACGATTCTTGTTGGAGGAGGTGCTCTTGCAACT
GTTTTAGGACTTTCTCAGTTTGCTCATTACAGAAGGAAACAAATGAACCTGGCCTATGTT
AAAGCAGCAGACTGCATTTCAGAACCAGTTAACAGGGAGCCTCCTTCCAGAGAAGCTCAG
CTACTGACTTTGCAAAACACATCTGAATTTGATATCCTTGTTATTGGAGGAGGAGCAACA
GGAAGTGGCTGTGCGCTAGATGCTGTCACCAGAGGACTAAAAACAGCCCTTGTAGAAAGA
GATGATTTCTCATCAGGGACCAGCAGCAGAAGCACTAAATTGATCCATGGTGGTGTGAGA
TATCTGCAGAAGGCCATCATGAAGTTGGATATTGAGCAGTATAGGATGGTAAAAGAAGCC
CTTCATGAGCGTGCCAACCTGCTAGAAATTGCTCCCCATTTATCAGCTCCATTGCCTATA
ATGCTTCCAGTTTACAAGTGGTGGCAGTTACCTTACTACTGGGTAGGAATCAAGCTGTAT
GATTTGGTTGCAGGAAGCAATTGCCTAAAAAGCAGTTATGTCCTCAGCAAATCAAGAGCC
CTTGAACATTTCCCAATGCTCCAGAAGGACAAACTGGTAGGAGCAATTGTCTACTATGAC
GGACAACATAACGATGCACGGATGAACCTTGCCATTGCTCTGACTGCTGCCAGGTATGGG
GCTGCCACAGCCAATTACATGGAGGTAGTGAGCTTGCTCAAGAAGACAGACCCCCAGACA
GGGAAAGTGCGTGTGAGCGGCGCACGGTGCAAGGATGTCCTCACAGGGCAGGAATTTGAC
GTGAGAGCCAAATGTGTTATCAATGCCACGGGACCTTTCACGGACTCTGTGCGCAAAATG
GATGATAAAGACGCAGCAGCTATCTGCCAGCCAAGTGCTGGTGTCCATATTGTGATGCCT
GGTTATTACAGCCCAGAGAGCATGGGACTTCTTGACCCAGCGACCAGTGATGGGCGAGTT
ATTTTCTTCTTACCCTGGCAAAAGATGACGATCGCTGGCACTACTGATACTCCAACTGAT
GTTACACACCATCCAATTCCTTCAGAAGAAGATATCAACTTCATTTTGAATGAAGTGCGT
AATTACCTGAGTTGTGATGTTGAAGTGAGAAGAGGGGATGTCCTGGCAGCATGGAGTGGA
ATCCGTCCTCTTGTTACAGACCCCAAATCTGCAGATACTCAGTCTATCTCCCGAAATCAT
GTTGTTGATATCAGTGAGAGTGGCCTTATTACTATAGCAGGTGGAAAGTGGACAACTTAT
CGGTCTATGGCAGAAGATACCATAAATGCTGCTGTCAAAACTCATAATTTAAAAGCAGGA
CCAAGTAGAACAGTTGGGCTTTTCCTTCAAGGGGGTAAAGATTGGAGCCCCACACTCTAC
ATTAGGCTTGTGCAGGATTATGGACTTGAAAGCGAGGTGGCACAGCATCTTGCCGCCACC
TATGGTGATAAGGCCTTTGAGGTGGCCAAAATGGCAAGTGTGACTGGCAAAAGGTGGCCT
ATTGTTGGAGTACGTCTTGTGTCAGAATTTCCATATATTGAAGCAGAGGTGAAATATGGG
ATTAAGGAGTATGCCTGCACTGCTGTGGATATGATTTCACGTCGTACTCGCCTGGCCTTT
CTAAATGTCCAGGCAGCAGAGGAAGCCCTACCCAGGATTGTTGAACTGATGGGCAGGGAA
CTGAATTGGGATGATTATAAGAAGCAGGAACAACTTGAAACAGCCAGGAAGTTTCTATAT
TATGAAATGGGCTATAAATCTCGATCAGAACAGTTAACAGATCGCTCTGAAATTAGCCTA
CTGCCTTCAGACATTGACAGGTATAAGAAGAGATTTCATAAGTTTGATGCAGACCAGAAA
GGCTTTATTACCATTGTTGATGTTCAGCGTGTATTAGAGAGTATCAATGTCCAAATGGAT
GAAAATACACTCCATGAAATTCTAAATGAAGTTGATTTGAATAAAAATGGACAGGTTGAA
CTCAATGAATTTTTGCAGCTGATGAGTGCTATTCAAAAAGGAAGGGTATCTGGAAGCCGG
CTTGCTATACTAATGAAAACTGCAGAAGAGAACCTCGACAGAAGAGTTCCAATTCCAGTG
GACCGTAGTTGTGGAGGATTGTGA
Enzyme 5 GenBank Gene ID NM_000408.4 Link Image
Enzyme 5 GeneCard ID GPD2 Link Image
Enzyme 5 GenAtlas ID GPD2 Link Image
Enzyme 5 HGNC ID HGNC:4456 Link Image
Enzyme 5 Chromosome Location 2
Enzyme 5 Locus 2q24.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Lehn DA, Brown LJ, Simonson GD, Moran SM, MacDonald MJ: The sequence of a human mitochondrial glycerol-3-phosphate dehydrogenase-encoding cDNA. Gene. 1994 Dec 15;150(2):417-8. [PubMed Link Image]
  2. Ferrer J, Aoki M, Behn P, Nestorowicz A, Riggs A, Permutt MA: Mitochondrial glycerol-3-phosphate dehydrogenase. Cloning of an alternatively spliced human islet-cell cDNA, tissue distribution, physical mapping, and identification of a polymorphic genetic marker. Diabetes. 1996 Feb;45(2):262-6. [PubMed Link Image]
  3. Brown LJ, Stoffel M, Moran SM, Fernald AA, Lehn DA, LeBeau MM, MacDonald MJ: Structural organization and mapping of the human mitochondrial glycerol phosphate dehydrogenase-encoding gene and pseudogene. Gene. 1996 Jun 26;172(2):309-12. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  6. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6118
Enzyme 6 Name Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
Enzyme 6 Synonyms
  1. GPD-C
  2. GPDH-C
Enzyme 6 Gene Name GPD1
Enzyme 6 Protein Sequence >Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
MASKKVCIVGSGNWGSAIAKIVGGNAAQLAQFDPRVTMWVFEEDIGGKKLTEIINTQHEN
VKYLPGHKLPPNVVAVPDVVQAAEDADILIFVVPHQFIGKICDQLKGHLKANATGISLIK
GVDEGPNGLKLISEVIGERLGIPMSVLMGANIASEVADEKFCETTIGCKDPAQGQLLKEL
MQTPNFRITVVQEVDTVEICGALKNVVAVGAGFCDGLGFGDNTKAAVIRLGLMEMIAFAK
LFCSGPVSSATFLESCGVADLITTCYGGRNRKVAEAFARTGKSIEQLEKELLNGQKLQGP
ETARELYSILQHKGLVDKFPLFMAVYKVCYEGQPVGEFIHCLQNHPEHM
Enzyme 6 Number of Residues 349
Enzyme 6 Molecular Weight 37567.4
Enzyme 6 Theoretical pI 6.10
Enzyme 6 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • glycerol-3-phosphate dehydrogenase [NAD+] activity
  • glycerol-3-phosphate dehydrogenase [NAD+] activity
  • identical protein binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • protein binding
  • protein homodimerization activity
Process
  • alcohol metabolic process
  • alditol metabolic process
  • carbohydrate metabolic process
  • glycerol metabolic process
  • glycerol-3-phosphate catabolic process
  • glycerol-3-phosphate metabolic process
  • metabolic process
  • oxidation reduction
  • polyol metabolic process
  • primary metabolic process
  • small molecule metabolic process
Component
  • cell part
  • cytoplasm
  • glycerol-3-phosphate dehydrogenase complex
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 6 General Function Involved in oxidoreductase activity
Enzyme 6 Specific Function sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH
Enzyme 6 Pathways
Enzyme 6 Reactions
  • sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+ [RN:R00842]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 21594877 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P21695 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name GPDA_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1050 bp
ATGGCTAGCAAGAAAGTCTGCATTGTAGGCTCCGGGAACTGGGGCTCAGCCATCGCCAAG
ATCGTGGGTGGCAATGCAGCCCAGCTGGCACAGTTTGACCCACGGGTGACCATGTGGGTA
TTTGAGGAAGACATTGGAGGCAAAAAGCTGACTGAGATCATCAACACGCAGCATGAGAAT
GTCAAATACCTGCCAGGGCACAAGTTGCCCCCAAATGTGGTGGCTGTCCCAGATGTGGTC
CAGGCTGCAGAGGATGCTGACATCCTGATCTTTGTGGTGCCCCATCAGTTCATCGGCAAG
ATCTGTGACCAGCTCAAGGGCCATCTGAAGGCAAACGCCACTGGCATATCTCTTATTAAG
GGGGTAGACGAGGGCCCCAATGGGCTGAAGCTCATCTCGGAAGTGATTGGGGAGCGCCTC
GGCATCCCCATGAGTGTGCTGATGGGGGCCAACATTGCCAGCGAGGTGGCTGATGAGAAG
TTCTGTGAGACAACCATTGGCTGCAAGGACCCGGCCCAGGGACAACTCCTGAAAGAGCTG
ATGCAGACACCAAACTTCCGTATCACAGTGGTGCAAGAGGTGGACACAGTAGAGATCTGT
GGAGCCTTAAAGAATGTAGTGGCCGTGGGGGCTGGCTTCTGTGATGGCCTGGGCTTTGGC
GACAACACCAAGGCGGCAGTGATCCGGCTGGGACTCATGGAGATGATAGCCTTCGCCAAG
CTCTTCTGCAGTGGCCCTGTGTCCTCTGCCACCTTCTTGGAGAGCTGTGGTGTTGCTGAC
CTGATCACTACCTGCTATGGAGGGCGGAACCGGAAAGTGGCTGAGGCCTTTGCGCGTACA
GGAAAGTCCATTGAGCAGCTGGAGAAAGAGTTGCTGAATGGGCAGAAACTGCAGGGGCCC
GAGACAGCCCGGGAGCTATACAGCATCCTCCAGCACAAGGGCCTGGTAGACAAGTTTCCC
TTGTTCATGGCTGTGTACAAGGTGTGCTACGAGGGCCAGCCAGTGGGTGAATTCATCCAC
TGCCTGCAGAATCATCCAGAACATATGTGA
Enzyme 6 GenBank Gene ID BC032234 Link Image
Enzyme 6 GeneCard ID GPD1 Link Image
Enzyme 6 GenAtlas ID GPD1 Link Image
Enzyme 6 HGNC ID HGNC:4455 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 12q12-q13
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Menaya J, Gonzalez-Manchon C, Parrilla R, Ayuso MS: Molecular cloning, sequencing and expression of a cDNA encoding a human liver NAD-dependent alpha-glycerol-3-phosphate dehydrogenase. Biochim Biophys Acta. 1995 May 17;1262(1):91-4. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Gwynn B, Lyford KA, Birkenmeier EH: Sequence conservation and structural organization of the glycerol-3-phosphate dehydrogenase promoter in mice and humans. Mol Cell Biol. 1990 Oct;10(10):5244-56. [PubMed Link Image]
  4. Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z: Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1). J Mol Biol. 2006 Mar 31;357(3):858-69. Epub 2006 Jan 18. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6266
Enzyme 7 Name Fructose-bisphosphate aldolase A
Enzyme 7 Synonyms
  1. Lung cancer antigen NY-LU-1
  2. Muscle-type aldolase
Enzyme 7 Gene Name ALDOA
Enzyme 7 Protein Sequence >Fructose-bisphosphate aldolase A
MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYR
QLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTN
GETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQ
NGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHAC
TQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTF
SYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVS
NHAY
Enzyme 7 Number of Residues 364
Enzyme 7 Molecular Weight 39419.7
Enzyme 7 Theoretical pI 8.20
Enzyme 7 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • fructose-bisphosphate aldolase activity
  • lyase activity
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 7 General Function Involved in fructose-bisphosphate aldolase activity
Enzyme 7 Specific Function D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate [RN:R01068]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 178351 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P04075 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ALDOA_HUMAN Link Image
Enzyme 7 PDB ID 4ALD Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1095 bp
ATGCCCTACCAATATCCAGCACTGACCCCGGAGCAGAAGAAGGAGCTGTCTGACATCGCT
CACCGCATCGTGGCACCTGGCAAGGGCATCCTGGCTGCAGATGAGTCCACTGGGAGCATT
GCCAAGCGGCTGCAGTCCATTGGCACCGAGAACACCGAGGAGAACCGGCGCTTCTACCGC
CAGCTGCTGCTGACAGCTGACGACCGCGTGAACCCCTGCATTGGGGGTGTCATCCTCTTC
CATGAGACACTCTACCAGAAGGCGGATGATGGGCGTCCCTTCCCCCAAGTTATCAAATCC
AAGGGCGGTGTTGTGGGCATCAAGGTAGACAAGGGCGTGGTCCCCCTGGCAGGGACAAAT
GGCGAGACTACCACCCAAGGGTTGGATGGGCTGTCTGAGCGCTGTGCCCAGTACAAGAAG
GACGGAGCTGACTTCGCCAAGTGGCGTTGTGTGCTGAAGATTGGGGAACACACCCCCTCA
GCCCTCGCCATCATGGAAAATGCCAATGTTCTGGCCCGTTATGCCAGTATCTGCCAGCAG
AATGGCATTGTGCCCATCGTGGAGCCTGAGATCCTCCCTGATGGGGACCATGACTTGAAG
CGCTGCCAGTATGTGACCGAGAAGGTGCTGGCTGCTGTCTACAAGGCTCTGAGTGACCAC
CACATCTACCTGGAAGGCACCTTGCTGAAGCCCAACATGGTCACCCCAGGCCATGCTTGC
ACTCAGAAGTTTTCTCATGAGGAGATTGCCATGGCGACCGTCACAGCGCTGCGCCGCACA
GTGCCCCCCGCTGTCACTGGGATCACCTTCCTGTCTGGAGGCCAGAGTGAGGAGGAGGCG
TCCATCAACCTCAATGCCATTAACAAGTGCCCCCTGCTGAAGCCCTGGGCCCTGACCTTC
TCCTACGGCCGAGCCCTGCAGGCCTCTGCCCTGAAGGCCTGGGGCGGGAAGAAGGAGAAC
CTGAAGGCTGCGCAGGAGGAGTATGTCAAGCGAGCCCTGGCCAACAGCCTTGCCTGTCAA
GGAAAGTACACTCCGAGCGGTCAGGCTGGGGCTGCTGCCAGCGAGTCCCTCTTCGTCTCT
AACCACGCCTATTAA
Enzyme 7 GenBank Gene ID M11560 Link Image
Enzyme 7 GeneCard ID ALDOA Link Image
Enzyme 7 GenAtlas ID ALDOA Link Image
Enzyme 7 HGNC ID HGNC:414 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 16p11.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Sakakibara M, Mukai T, Hori K: Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in the liver. Biochem Biophys Res Commun. 1985 Aug 30;131(1):413-20. [PubMed Link Image]
  2. Izzo P, Costanzo P, Lupo A, Rippa E, Borghese AM, Paolella G, Salvatore F: A new human species of aldolase A mRNA from fibroblasts. Eur J Biochem. 1987 Apr 1;164(1):9-13. [PubMed Link Image]
  3. Izzo P, Costanzo P, Lupo A, Rippa E, Paolella G, Salvatore F: Human aldolase A gene. Structural organization and tissue-specific expression by multiple promoters and alternate mRNA processing. Eur J Biochem. 1988 Jul 1;174(4):569-78. [PubMed Link Image]
  4. Mukai T, Arai Y, Yatsuki H, Joh K, Hori K: An additional promoter functions in the human aldolase A gene, but not in rat. Eur J Biochem. 1991 Feb 14;195(3):781-7. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Maire P, Gautron S, Hakim V, Gregori C, Mennecier F, Kahn A: Characterization of three optional promoters in the 5' region of the human aldolase A gene. J Mol Biol. 1987 Oct 5;197(3):425-38. [PubMed Link Image]
  8. Freemont PS, Dunbar B, Fothergill-Gilmore LA: The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase. Biochem J. 1988 Feb 1;249(3):779-88. [PubMed Link Image]
  9. Freemont PS, Dunbar B, Fothergill LA: Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments. Arch Biochem Biophys. 1984 Jan;228(1):342-52. [PubMed Link Image]
  10. 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]
  11. Lee KN, Maxwell MD, Patterson MK Jr, Birckbichler PJ, Conway E: Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe. Biochim Biophys Acta. 1992 Jul 22;1136(1):12-6. [PubMed Link Image]
  12. Tolan DR, Niclas J, Bruce BD, Lebo RV: Evolutionary implications of the human aldolase-A, -B, -C, and -pseudogene chromosome locations. Am J Hum Genet. 1987 Nov;41(5):907-24. [PubMed Link Image]
  13. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  14. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed Link Image]
  15. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  16. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  17. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  18. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  19. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  20. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  21. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  22. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  23. Gamblin SJ, Cooper B, Millar JR, Davies GJ, Littlechild JA, Watson HC: The crystal structure of human muscle aldolase at 3.0 A resolution. FEBS Lett. 1990 Mar 26;262(2):282-6. [PubMed Link Image]
  24. Gamblin SJ, Davies GJ, Grimes JM, Jackson RM, Littlechild JA, Watson HC: Activity and specificity of human aldolases. J Mol Biol. 1991 Jun 20;219(4):573-6. [PubMed Link Image]
  25. Dalby A, Dauter Z, Littlechild JA: Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications. Protein Sci. 1999 Feb;8(2):291-7. [PubMed Link Image]
  26. Kishi H, Mukai T, Hirono A, Fujii H, Miwa S, Hori K: Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8623-7. [PubMed Link Image]
  27. Takasaki Y, Takahashi I, Mukai T, Hori K: Human aldolase A of a hemolytic anemia patient with Asp-128----Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G. J Biochem (Tokyo). 1990 Aug;108(2):153-7. [PubMed Link Image]
  28. Kreuder J, Borkhardt A, Repp R, Pekrun A, Gottsche B, Gottschalk U, Reichmann H, Schachenmayr W, Schlegel K, Lampert F: Brief report: inherited metabolic myopathy and hemolysis due to a mutation in aldolase A. N Engl J Med. 1996 Apr 25;334(17):1100-4. [PubMed Link Image]
  29. Yao DC, Tolan DR, Murray MF, Harris DJ, Darras BT, Geva A, Neufeld EJ: Hemolytic anemia and severe rhabdomyolysis caused by compound heterozygous mutations of the gene for erythrocyte/muscle isozyme of aldolase, ALDOA(Arg303X/Cys338Tyr). Blood. 2004 Mar 15;103(6):2401-3. Epub 2003 Nov 13. [PubMed Link Image]
  30. Esposito G, Vitagliano L, Costanzo P, Borrelli L, Barone R, Pavone L, Izzo P, Zagari A, Salvatore F: Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function. Biochem J. 2004 May 15;380(Pt 1):51-6. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6267
Enzyme 8 Name Fructose-bisphosphate aldolase C
Enzyme 8 Synonyms
  1. Brain-type aldolase
Enzyme 8 Gene Name ALDOC
Enzyme 8 Protein Sequence >Fructose-bisphosphate aldolase C
MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYR
QVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGIVVGIKVDKGVVPLAGTD
GETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISERTPSALAILENANVLARYASICQQ
NGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHAC
PIKYTPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASFNLNAINRCPLPRPWALTF
SYGRALQASALNAWRGQRDNAGAATEEFIKRAEVNGLAAQGKYEGSGEDGGAAAQSLYIA
NHAY
Enzyme 8 Number of Residues 364
Enzyme 8 Molecular Weight 39455.5
Enzyme 8 Theoretical pI 6.86
Enzyme 8 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • fructose-bisphosphate aldolase activity
  • lyase activity
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 8 General Function Involved in fructose-bisphosphate aldolase activity
Enzyme 8 Specific Function D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Enzyme 8 Pathways
Enzyme 8 Reactions
  • D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate [RN:R01068]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID P09972 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ALDOC_HUMAN Link Image
Enzyme 8 PDB ID 1XFB Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1095 bp
ATGCCTCACTCGTACCCAGCCCTTTCTGCTGAGCAGAAGAAGGAGTTGTCTGACATTGCC
CTGCGGATTGTAGCCCCGGGCAAAGGCATTCTGGCTGCGGATGAGTCTGTAGGCAGCATG
GCCAAGCGGCTGAGCCAAATTGGGGTGGAAAACACAGAGGAGAACCGCCGGCTGTACCGC
CAGGTCCTGTTCAGTGCTGATGACCGTGTGAAAAAGTGCATTGGAGGCGTCATTTTCTTC
CATGAGACCCTCTACCAGAAAGATGATAATGGTGTTCCCTTCGTCCGAACCATCCAGGAT
AAGGGCATCGTCGTGGGCATCAAGGTTGACAAGGGTGTGGTGCCTCTAGCTGGGACTGAT
GGAGAAACCACCACTCAAGGGCTGGATGGGCTCTCAGAACGCTGTGCCCAATACAAGAAG
GATGGTGCTGACTTTGCCAAGTGGCGCTGTGTGCTGAAAATCAGTGAGCGTACACCCTCT
GCACTTGCCATTCTGGAGAACGCCAACGTGCTGGCCCGTTATGCCAGTATCTGCCAGCAG
AATGGCATTGTGCCTATTGTGGAACCTGAAATATTGCCTGATGGAGACCACGACCTCAAA
CGTTGTCAGTATGTTACAGAGAAGGTCTTGGCTGCTGTGTACAAGGCCCTGAGTGACCAT
CATGTATACCTGGAGGGGACCCTGCTCAAGCCCAACATGGTGACCCCGGGCCATGCCTGT
CCCATCAAGTATACCCCAGAGGAGATTGCCATGGCAACTGTCACTGCCCTGCGTCGCACT
GTGCCCCCAGCTGTCCCAGGAGTGACCTTCCTGTCTGGGGGTCAGAGCGAAGAAGAGGCA
TCATTCAACCTCAATGCCATCAACCGCTGCCCCCTTCCCCGACCCTGGGCGCTTACCTTC
TCCTATGGGCGTGCCCTGCAAGCCTCTGCACTCAATGCCTGGCGAGGGCAACGGGACAAT
GCTGGGGCTGCCACTGAGGAGTTCATCAAGCGGGCTGAGGTGAATGGGCTTGCAGCCCAG
GGCAAGTATGAAGGCAGTGGAGAAGATGGTGGAGCAGCAGCACAGTCACTCTACATTGCC
AACCATGCCTACTGA
Enzyme 8 GenBank Gene ID AF054987 Link Image
Enzyme 8 GeneCard ID ALDOC Link Image
Enzyme 8 GenAtlas ID ALDOC Link Image
Enzyme 8 HGNC ID HGNC:418 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 17cen-q12
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Rottmann WH, Deselms KR, Niclas J, Camerato T, Holman PS, Green CJ, Tolan DR: The complete amino acid sequence of the human aldolase C isozyme derived from genomic clones. Biochimie. 1987 Feb;69(2):137-45. [PubMed Link Image]
  2. Buono P, Paolella G, Mancini FP, Izzo P, Salvatore F: The complete nucleotide sequence of the gene coding for the human aldolase C. Nucleic Acids Res. 1988 May 25;16(10):4733. [PubMed Link Image]
  3. Buono P, Mancini FP, Izzo P, Salvatore F: Characterization of the transcription-initiation site and of the promoter region within the 5' flanking region of the human aldolase C gene. Eur J Biochem. 1990 Sep 24;192(3):805-11. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Lu M, Holliday LS, Zhang L, Dunn WA Jr, Gluck SL: Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump. J Biol Chem. 2001 Aug 10;276(32):30407-13. Epub 2001 Jun 8. [PubMed Link Image]
  7. Kim JH, Lee S, Kim JH, Lee TG, Hirata M, Suh PG, Ryu SH: Phospholipase D2 directly interacts with aldolase via Its PH domain. Biochemistry. 2002 Mar 12;41(10):3414-21. [PubMed Link Image]
  8. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Arakaki TL, Pezza JA, Cronin MA, Hopkins CE, Zimmer DB, Tolan DR, Allen KN: Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function. Protein Sci. 2004 Dec;13(12):3077-84. Epub 2004 Nov 10. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6268
Enzyme 9 Name Fructose-bisphosphate aldolase B
Enzyme 9 Synonyms
  1. Liver-type aldolase
Enzyme 9 Gene Name ALDOB
Enzyme 9 Protein Sequence >Fructose-bisphosphate aldolase B
MAHRFPALTQEQKKELSEIAQSIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFR
EILFSVDSSINQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTN
KETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQ
NGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHAC
TKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSF
SYGRALQASALAAWGGKAANKEATQEAFMKRAMANCQAAKGQYVHTGSSGAASTQSLFTA
CYTY
Enzyme 9 Number of Residues 364
Enzyme 9 Molecular Weight 39472.7
Enzyme 9 Theoretical pI 7.96
Enzyme 9 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • fructose-bisphosphate aldolase activity
  • lyase activity
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 9 General Function Involved in fructose-bisphosphate aldolase activity
Enzyme 9 Specific Function D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Enzyme 9 Pathways
Enzyme 9 Reactions
  • D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate [RN:R01068]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 55958631 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P05062 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name ALDOB_HUMAN Link Image
Enzyme 9 PDB ID 1QO5 Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1095 bp
ATGGCCCACCGATTTCCAGCCCTCACCCAGGAGCAGAAGAAGGAGCTCTCAGAAATTGCC
CAGAGCATTGTTGCCAATGGAAAGGGGATCCTGGCTGCAGATGAATCTGTAGGTACCATG
GGGAACCGCCTGCAGAGGATCAAGGTGGAAAACACTGAAGAGAACCGCCGGCAGTTCCGA
GAAATCCTCTTCTCTGTGGACAGTTCCATCAACCAGAGCATCGGGGGTGTGATCCTTTTC
CACGAGACCCTCTACCAGAAGGACAGCCAGGGAAAGCTGTTCAGAAACATCCTCAAGGAA
AAGGGGATCGTGGTGGGAATCAAGTTAGACCAAGGAGGTGCTCCTCTTGCAGGAACAAAC
AAAGAAACCACCATTCAAGGGCTTGATGGCCTCTCAGAGCGCTGTGCTCAGTACAAGAAA
GATGGTGTTGACTTTGGGAAGTGGCGTGCTGTGCTGAGGATTGCCGACCAGTGTCCATCC
AGCCTCGCTATCCAGGAAAACGCCAACGCCCTGGCTCGCTACGCCAGCATCTGTCAGCAG
AATGGACTGGTACCTATTGTTGAACCAGAGGTAATTCCTGATGGAGACCATGACCTGGAA
CACTGCCAGTATGTTACTGAGAAGGTCCTGGCTGCTGTCTACAAGGCCCTGAATGACCAT
CATGTTTACCTGGAGGGCACCCTGCTAAAGCCCAACATGGTGACTGCTGGACATGCCTGC
ACCAAGAAGTATACTCCAGAACAAGTAGCTATGGCCACCGTAACAGCTCTCCACCGTACT
GTTCCTGCAGCTGTTCCTGGCATCTGCTTTTTGTCTGGTGGCATGAGTGAAGAGGATGCC
ACTCTCAACCTCAATGCTATCAACCTTTGCCCTCTACCAAAGCCCTGGAAACTAAGTTTC
TCTTATGGACGGGCCCTGCAGGCCAGTGCACTGGCTGCCTGGGGTGGCAAGGCTGCAAAC
AAGGAGGCAACCCAGGAGGCTTTTATGAAGCGGGCCATGGCTAACTGCCAGGCGGCCAAA
GGACAGTATGTTCACACGGGTTCTTCTGGGGCTGCTTCCACCCAGTCGCTCTTCACAGCC
TGCTATACCTACTAG
Enzyme 9 GenBank Gene ID AL353621 Link Image
Enzyme 9 GeneCard ID ALDOB Link Image
Enzyme 9 GenAtlas ID ALDOB Link Image
Enzyme 9 HGNC ID HGNC:417 Link Image
Enzyme 9 Chromosome Location 9
Enzyme 9 Locus 9q21.3-q22.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Paolella G, Santamaria R, Izzo P, Costanzo P, Salvatore F: Isolation and nucleotide sequence of a full-length cDNA coding for aldolase B from human liver. Nucleic Acids Res. 1984 Oct 11;12(19):7401-10. [PubMed Link Image]
  2. Sakakibara M, Mukai T, Yatsuki H, Hori K: Human aldolase isozyme gene: the structure of multispecies aldolase B mRNAs. Nucleic Acids Res. 1985 Jul 25;13(14):5055-69. [PubMed Link Image]
  3. Rottmann WH, Tolan DR, Penhoet EE: Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones. Proc Natl Acad Sci U S A. 1984 May;81(9):2738-42. [PubMed Link Image]
  4. Mukai T, Yatsuki H, Arai Y, Joh K, Matsuhashi S, Hori K: Human aldolase B gene: characterization of the genomic aldolase B gene and analysis of sequences required for multiple polyadenylations. J Biochem (Tokyo). 1987 Nov;102(5):1043-51. [PubMed Link Image]
  5. Tolan DR, Penhoet EE: Characterization of the human aldolase B gene. Mol Biol Med. 1986 Jun;3(3):245-64. [PubMed Link Image]
  6. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  7. Sakakibara M, Takahashi I, Takasaki Y, Mukai T, Hori K: Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host. Biochim Biophys Acta. 1989 Apr 12;1007(3):334-42. [PubMed Link Image]
  8. Besmond C, Dreyfus JC, Gregori C, Frain M, Zakin MM, Sala Trepat J, Kahn A: Nucleotide sequence of a cDNA clone for human aldolase B. Biochem Biophys Res Commun. 1983 Dec 16;117(2):601-9. [PubMed Link Image]
  9. Dalby AR, Tolan DR, Littlechild JA: The structure of human liver fructose-1,6-bisphosphate aldolase. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1526-33. Epub 2001 Oct 25. [PubMed Link Image]
  10. Tolan DR: Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene. Hum Mutat. 1995;6(3):210-8. [PubMed Link Image]
  11. Cross NC, Tolan DR, Cox TM: Catalytic deficiency of human aldolase B in hereditary fructose intolerance caused by a common missense mutation. Cell. 1988 Jun 17;53(6):881-5. [PubMed Link Image]
  12. Cross NC, de Franchis R, Sebastio G, Dazzo C, Tolan DR, Gregori C, Odievre M, Vidailhet M, Romano V, Mascali G, et al.: Molecular analysis of aldolase B genes in hereditary fructose intolerance. Lancet. 1990 Feb 10;335(8685):306-9. [PubMed Link Image]
  13. Brooks CC, Tolan DR: A partially active mutant aldolase B from a patient with hereditary fructose intolerance. FASEB J. 1994 Jan;8(1):107-13. [PubMed Link Image]
  14. Ali M, Cox TM: Diverse mutations in the aldolase B gene that underlie the prevalence of hereditary fructose intolerance. Am J Hum Genet. 1995 Apr;56(4):1002-5. [PubMed Link Image]
  15. Ali M, Sebastio G, Cox TM: Identification of a novel mutation (Leu 256-->Pro) in the human aldolase B gene associated with hereditary fructose intolerance. Hum Mol Genet. 1994 Jan;3(1):203-4. [PubMed Link Image]
  16. Cross NC, Stojanov LM, Cox TM: A new aldolase B variant, N334K, is a common cause of hereditary fructose intolerance in Yugoslavia. Nucleic Acids Res. 1990 Apr 11;18(7):1925. [PubMed Link Image]
  17. Lau J, Tolan DR: Screening for hereditary fructose intolerance mutations by reverse dot-blot. Mol Cell Probes. 1999 Feb;13(1):35-40. [PubMed Link Image]
  18. Santamaria R, Esposito G, Vitagliano L, Race V, Paglionico I, Zancan L, Zagari A, Salvatore F: Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase. Biochem J. 2000 Sep 15;350 Pt 3:823-8. [PubMed Link Image]
  19. Sanchez-Gutierrez JC, Benlloch T, Leal MA, Samper B, Garcia-Ripoll I, Feliu JE: Molecular analysis of the aldolase B gene in patients with hereditary fructose intolerance from Spain. J Med Genet. 2002 Sep;39(9):e56. [PubMed Link Image]
  20. Esposito G, Santamaria R, Vitagliano L, Ieno L, Viola A, Fiori L, Parenti G, Zancan L, Zagari A, Salvatore F: Six novel alleles identified in Italian hereditary fructose intolerance patients enlarge the mutation spectrum of the aldolase B gene. Hum Mutat. 2004 Dec;24(6):534. [PubMed Link Image]
  21. Santer R, Rischewski J, von Weihe M, Niederhaus M, Schneppenheim S, Baerlocher K, Kohlschutter A, Muntau A, Posselt HG, Steinmann B, Schneppenheim R: The spectrum of aldolase B (ALDOB) mutations and the prevalence of hereditary fructose intolerance in Central Europe. Hum Mutat. 2005 Jun;25(6):594. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6839
Enzyme 10 Name Dihydroxyacetone phosphate acyltransferase
Enzyme 10 Synonyms
  1. DAP-AT
  2. DHAP-AT
  3. Acyl-CoA:dihydroxyacetonephosphateacyltransferase
  4. Glycerone-phosphate O-acyltransferase
Enzyme 10 Gene Name GNPAT
Enzyme 10 Protein Sequence >Dihydroxyacetone phosphate acyltransferase
MESSSSSNSYFSVGPTSPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVY
KGITPCKPIDIKCSVLNSEEIHYVIKQLSKESLQSVDVLREEVSEILDEMSHKLRLGAIR
FCAFTLSKVFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDL
PVPVIAAGMDFLGMKMVGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEF
FLEGTRSRSAKTLTPKFGLLNIVMEPFFKREVFDTYLVPISISYDKILEETLYVYELLGV
PKPKESTTGLLKARKILSENFGSIHVYFGDPVSLRSLAAGRMSRSSYNLVPRYIPQKQSE
DMHAFVTEVAYKMELLQIENMVLSPWTLIVAVLLQNRPSMDFDALVEKTLWLKGLTQAFG
GFLIWPDNKPAEEVVPASILLHSNIASLVKDQVILKVDSGDSEVVDGLMLQHITLLMCSA
YRNQLLNIFVRPSLVAVALQMTPGFRKEDVYSCFRFLRDVFADEFIFLPGNTLKDFEEGC
YLLCKSEAIQVTTKDILVTEKGNTVLEFLVGLFKPFVESYQIICKYLLSEEEDHFSEEQY
LAAVRKFTSQLLDQGTSQCYDVLSSDVQKNALAACVRLGVVEKKKINNNCIFNVNEPATT
KLEEMLGCKTPIGKPATAKL
Enzyme 10 Number of Residues 680
Enzyme 10 Molecular Weight 77187.2
Enzyme 10 Theoretical pI 6.52
Enzyme 10 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 10 General Function Lipid transport and metabolism
Enzyme 10 Specific Function Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
Enzyme 10 Pathways
Enzyme 10 Reactions
  • acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate [RN:R01013]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 3258645 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O15228 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name GNPAT_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2043 bp
ATGGAGTCTTCCAGTTCATCTAACTCTTATTTCTCCGTTGGCCCAACCAGTCCCAGCGCT
GTCGTGCTCCTCTACTCGAAGGAGCTCAAAAAGTGGGATGAGTTTGAAGATATTTTAGAA
GAGAGGAGGCATGTCAGTGACTTGAAATTTGCAATGAAATGCTACACACCTCTTGTCTAT
AAGGGAATTACTCCATGTAAACCAATTGATATTAAATGTAGTGTTCTCAATTCTGAGGAG
ATTCATTATGTCATTAAACAGCTTTCCAAGGAATCCCTTCAATCTGTGGATGTCCTCCGA
GAGGAAGTGAGTGAGATCTTAGATGAAATGAGTCACAAACTGCGTCTTGGAGCCATTCGG
TTTTGTGCCTTCACCCTGAGCAAAGTATTTAAACAAATTTTCTCGAAGGTGTGTGTAAAT
GAAGAAGGTATTCAGAAACTACAAAGAGCCATCCAGGAGCATCCTGTTGTTCTGCTGCCT
AGTCATCGAAGTTACATTGACTTCCTCATGTTGTCTTTTCTTCTATACAATTATGATTTG
CCTGTGCCAGTTATAGCAGCAGGAATGGACTTCCTGGGAATGAAAATGGTTGGTGAGCTG
CTACGAATGTCGGGTGCCTTTTTCATGCGGCGTACCTTTGGTGGCAATAAACTCTACTGG
GCTGTATTCTCTGAATATGTAAAAACTATGTTACGGAATGGTTATGCTCCTGTTGAATTT
TTCCTCGAAGGGACAAGAAGCCGCTCTGCCAAGACATTGACTCCTAAATTTGGTCTTCTG
AATATTGTGATGGAGCCATTTTTTAAAAGAGAAGTTTTTGATACCTACCTTGTCCCAATT
AGTATCAGTTATGATAAGATCTTGGAAGAAACTCTTTATGTGTATGAGCTTCTAGGGGTT
CCTAAACCAAAAGAATCTACAACTGGGTTGCTGAAAGCCAGAAAGATTCTCTCTGAAAAT
TTTGGAAGCATCCATGTGTACTTTGGAGATCCTGTGTCACTTCGATCTTTGGCAGCTGGG
AGGATGAGTCGGAGCTCATATAACTTGGTTCCAAGATACATTCCTCAGAAACAGTCTGAG
GACATGCATGCCTTTGTCACTGAAGTTGCCTACAAAATGGAGCTTCTGCAAATTGAAAAC
ATGGTTTTGAGCCCCTGGACCCTAATAGTTGCTGTTCTGCTTCAGAACCGGCCATCCATG
GACTTTGATGCTCTGGTGGAAAAGACTTTATGGCTAAAAGGCTTAACCCAGGCATTTGGA
GGGTTTCTCATTTGGCCTGATAATAAACCTGCTGAAGAAGTTGTCCCGGCCAGCATTCTT
CTGCATTCCAACATTGCCAGCCTTGTCAAAGACCAGGTGATTCTGAAAGTGGACTCCGGA
GACTCGGAAGTGGTCGATGGGCTTATGCTCCAGCACATCACTCTCCTCATGTGCTCAGCT
TATAGGAACCAGCTGCTCAACATTTTTGTGCGCCCATCCTTAGTAGCAGTAGCATTGCAG
ATGACACCAGGGTTCAGGAAAGAGGATGTCTACAGTTGCTTTCGCTTCCTACGTGATGTT
TTTGCAGATGAGTTCATCTTCCTTCCAGGAAACACACTAAAGGACTTTGAAGAAGGCTGT
TACCTGCTTTGTAAAAGTGAAGCCATACAAGTGACTACGAAAGACATCCTAGTTACAGAG
AAAGGAAATACTGTGTTAGAATTTTTAGTAGGACTCTTTAAACCTTTTGTGGAAAGCTAT
CAGATAATTTGCAAGTACCTTTTGAGTGAAGAAGAGGACCACTTCAGTGAGGAACAGTAC
TTGGCTGCAGTCAGAAAATTCACAAGTCAGCTTCTCGATCAAGGTACCTCTCAATGTTAT
GATGTATTATCTTCTGATGTGCAGAAAAACGCCTTAGCAGCCTGTGTGAGGCTCGGAGTA
GTGGAGAAGAAGAAGATAAATAATAACTGTATATTTAATGTGAATGAACCTGCCACAACC
AAATTAGAAGAAATGCTTGGTTGTAAGACACCAATAGGAAAACCAGCCACTGCAAAACTT
TAA
Enzyme 10 GenBank Gene ID AF043937 Link Image
Enzyme 10 GeneCard ID GNPAT Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1q42
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Thai TP, Heid H, Rackwitz HR, Hunziker A, Gorgas K, Just WW: Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase. FEBS Lett. 1997 Dec 29;420(2-3):205-11. [PubMed Link Image]
  2. Ofman R, Hettema EH, Hogenhout EM, Caruso U, Muijsers AO, Wanders RJ: Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2. Hum Mol Genet. 1998 May;7(5):847-53. [PubMed Link Image]
  3. Ofman R, Lajmir S, Wanders RJ: Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human gnpat gene and its use in the identification of novel mutations. Biochem Biophys Res Commun. 2001 Mar 2;281(3):754-60. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  7. Thai TP, Rodemer C, Jauch A, Hunziker A, Moser A, Gorgas K, Just WW: Impaired membrane traffic in defective ether lipid biosynthesis. Hum Mol Genet. 2001 Jan 15;10(2):127-36. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6880
Enzyme 11 Name Triosephosphate isomerase
Enzyme 11 Synonyms
  1. TIM
  2. Triose-phosphate isomerase
Enzyme 11 Gene Name TPI1
Enzyme 11 Protein Sequence >Triosephosphate isomerase
MAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKI
AVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAE
GLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ
QAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE
FVDIINAKQ
Enzyme 11 Number of Residues 249
Enzyme 11 Molecular Weight 26669.3
Enzyme 11 Theoretical pI 6.91
Enzyme 11 GO Classification
Function
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, interconverting aldoses and ketoses
  • isomerase activity
  • triose-phosphate isomerase activity
Process
  • metabolic process
Component
Enzyme 11 General Function Involved in catalytic activity
Enzyme 11 Specific Function D-glyceraldehyde 3-phosphate = glycerone phosphate
Enzyme 11 Pathways
Enzyme 11 Reactions
  • D-glyceraldehyde 3-phosphate = glycerone phosphate [RN:R01015]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 339841 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P60174 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name TPIS_HUMAN Link Image
Enzyme 11 PDB ID 1HTI Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >750 bp
ATGGCGCCCTCCAGGAAGTTCTTCGTTGGGGGAAACTGGAAGATGAACGGGCGGAAGCAG
AGTCTGGGGGAGCTCATCGGCACTCTGAACGCGGCCAAGGTGCCGGCCGACACCGAGGTG
GTTTGTGCTCCCCCTACTGCCTATATCGACTTCGCCCGGCAGAAGCTAGATCCCAAGATT
GCTGTGGCTGCGCAGAACTGCTACAAAGTGACTAATGGGGCTTTTACTGGGGAGATCAGC
CCTGGCATGATCAAAGACTGCGGAGCCACGTGGGTGGTCCTGGGACACTCAGAGAGAAGG
CATGTCTTTGGGGAGTCAGATGAGCTGATTGGGCAGAAAGTGGCCCATGCTCTGGCAGAG
GGACTCGGAGTAATCGCCTGCATTGGGGAGAAGCTAGATGAAAGGGAAGCTGGCATCACT
GAGAAGGTTGTTTTCGAGCAGACAAAGGTCATCGCAGATAACGTGAAGGACTGGAGCAAG
GTCGTCCTCGCCTATGAGCCTGTGTGGGCCATTGGTACTGGCAAGACTGCAACACCCCAA
CAGGCCCAGGAAGTACACGAGAAGCTCCGAGGATGGCTGAAGTCCAACGTCTCTGATGCG
GTGGCTCAGAGCACCCGTATCATTTATGGAGGCTCTGTGACTGGGGCAACCTGCAAGGAG
CTGGCCAGCCAGCCTGATGTGGATGGCTTCCTTGTGGGTGGTGCTTCCCTCAAGCCCGAA
TTCGTGGACATCATCAATGCCAAACAATGA
Enzyme 11 GenBank Gene ID M10036 Link Image
Enzyme 11 GeneCard ID TPI1 Link Image
Enzyme 11 GenAtlas ID TPI1 Link Image
Enzyme 11 HGNC ID HGNC:12009 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 12p13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Lu HS, Yuan PM, Gracy RW: Primary structure of human triosephosphate isomerase. J Biol Chem. 1984 Oct 10;259(19):11958-68. [PubMed Link Image]
  2. Maquat LE, Chilcote R, Ryan PM: Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man. J Biol Chem. 1985 Mar 25;260(6):3748-53. [PubMed Link Image]
  3. Brown JR, Daar IO, Krug JR, Maquat LE: Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family. Mol Cell Biol. 1985 Jul;5(7):1694-706. [PubMed Link Image]
  4. 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]
  5. 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]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed Link Image]
  9. 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]
  10. Boyer TG, Krug JR, Maquat LE: Transcriptional regulatory sequences of the housekeeping gene for human triosephosphate isomerase. J Biol Chem. 1989 Mar 25;264(9):5177-87. [PubMed Link Image]
  11. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  12. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  13. Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F: Phosphoproteomic analysis of the human pituitary. Pituitary. 2006;9(2):109-20. [PubMed Link Image]
  14. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  15. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed Link Image]
  16. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  17. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed Link Image]
  18. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  19. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  20. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  21. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  22. Mande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WG: Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme. Protein Sci. 1994 May;3(5):810-21. [PubMed Link Image]
  23. Kinoshita T, Maruki R, Warizaya M, Nakajima H, Nishimura S: Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt 4):346-9. Epub 2005 Mar 24. [PubMed Link Image]
  24. Rodriguez-Almazan C, Arreola R, Rodriguez-Larrea D, Aguirre-Lopez B, de Gomez-Puyou MT, Perez-Montfort R, Costas M, Gomez-Puyou A, Torres-Larios A: Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. J Biol Chem. 2008 Aug 22;283(34):23254-63. Epub 2008 Jun 18. [PubMed Link Image]
  25. Daar IO, Artymiuk PJ, Phillips DC, Maquat LE: Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7903-7. [PubMed Link Image]
  26. Perry BA, Mohrenweiser HW: Human triosephosphate isomerase: substitution of Arg for Gly at position 122 in a thermolabile electromorph variant, TPI-Manchester. Hum Genet. 1992 Mar;88(6):634-8. [PubMed Link Image]
  27. Chang ML, Artymiuk PJ, Wu X, Hollan S, Lammi A, Maquat LE: Human triosephosphate isomerase deficiency resulting from mutation of Phe-240. Am J Hum Genet. 1993 Jun;52(6):1260-9. [PubMed Link Image]
  28. Watanabe M, Zingg BC, Mohrenweiser HW: Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus. Am J Hum Genet. 1996 Feb;58(2):308-16. [PubMed Link Image]
  29. Arya R, Lalloz MR, Bellingham AJ, Layton DM: Evidence for founder effect of the Glu104Asp substitution and identification of new mutations in triosephosphate isomerase deficiency. Hum Mutat. 1997;10(4):290-4. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 8052
Enzyme 12 Name Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
Enzyme 12 Synonyms
  1. ATP-dependent dihydroxyacetone kinase
  2. DHA kinase
  3. Glycerone kinase
  4. FAD-AMP lyase (cyclizing)
  5. FAD-AMP lyase (cyclic FMN forming)
  6. FMN cyclase
Enzyme 12 Gene Name DAK
Enzyme 12 Protein Sequence >Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
MTSKKLVNSVAGCADDALAGLVACNPNLQLLQGHRVALRSDLDSLKGRVALLSGGGSGHE
PAHAGFIGKGMLTGVIAGAVFTSPAVGSILAAIRAVAQAGTVGTLLIVKNYTGDRLNFGL
AREQARAEGIPVEMVVIGDDSAFTVLKKAGRRGLCGTVLIHKVAGALAEAGVGLEEIAKQ
VNVVTKAMGTLGVSLSSCSVPGSKPTFELSADEVELGLGIHGEAGVRRIKMATADEIVKL
MLDHMTNTTNASHVPVQPGSSVVMMVNNLGGLSFLELGIIADATVRSLEGRGVKIARALV
GTFMSALEMPGISLTLLLVDEPLLKLIDAETTAAAWPNVAAVSITGRKRSRVAPAEPQEA
PDSTAAGGSASKRMALVLERVCSTLLGLEEHLNALDRAAGDGDCGTTHSRAARAIQEWLK
EGPPPASPAQLLSKLSVLLLEKMGGSSGALYGLFLTAAAQPLKAKTSLPAWSAAMDAGLE
AMQKYGKAAPGDRTMLDSLWAAGQELQAWKSPGADLLQVLTKAVKSAEAAAEATKNMEAG
AGRASYISSARLEQPDPGAVAAAAILRAILEVLQS
Enzyme 12 Number of Residues 575
Enzyme 12 Molecular Weight 58976.5
Enzyme 12 Theoretical pI 7.56
Enzyme 12 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • glycerone kinase activity
  • kinase activity
  • nucleoside binding
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • alditol metabolic process
  • glycerol metabolic process
  • metabolic process
  • polyol metabolic process
  • small molecule metabolic process
Component
Enzyme 12 General Function Carbohydrate transport and metabolism
Enzyme 12 Specific Function Catalyzes both the phosphorylation of dihydroxyacetone and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate
Enzyme 12 Pathways
Enzyme 12 Reactions
  • FAD = AMP + riboflavin cyclic-4',5'-phosphate [RN:R07636]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 10435998 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q3LXA3 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name DHAK_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1728 bp
ATGACCTCCAAGAAGCTGGCGAACTCGGTGGCTGGCTGTGCTGATGACGCTCTTGCTGGC
CTGGTGGCCTGCAACCCCAACCTGCAGCTCCTGCAGGGCCACCGCGTGGCCCTCCGTTCT
GACCTGGACAGCCTCAAGGGCCGGGTGGCACTGCTGTCGGGTGGGGGCTCTGGCCATGAG
CCTGCCCATGCTGGTTTCATAGGGAAGGGGATGCTGACTGGGGCCATCGCGGGAGCTGTG
TTCACCTCCCCGGCAGTGGGCAGCATCCTGGCAGCCATCAGGGCCGTGGCCCAGGCCGGC
ACAGTGGGGACGCTCCTTATCGTGAAGAACTACACTGGGGATCGGCTCAACTTCGGCCTG
GCCCGGGAGCAGGCCCGGGCTGAAGGCATCCCGGTGGAGATGGTGGTGATTGGGGACGAC
AGCGCCTTCACTGTCCTGAAGAAGGCAGGCCGGCGGGGGCTGTGCGGCACCGTGCTTATA
CACAAGGTGGCAGGTGCTCTGGCTGAGGCTGGTGTGGGGCTGGAGGAGATCGCAAAGCAG
GTGAACGTGGTCACCAAGGCCATGGGTACCCTGGGGGTGAGCTTATCCTCCTGCAGCGTC
CCTGGTTCCAAACCCACCTTCGAGCTCTCAGCCGACGAGGTGGAGCTGGGCCTGGGGATC
CACGGGGAAGCTGGTGTGCGCCGGATAAAGATGGCAACCGCCGATGAGATTGTGAAACTC
ATGCTCGACCACATGACAAACACCACCAACGCGTCCCATGTGCCTGTGCAGCCCGGCTCC
TCAGTTGTGATGATGGTCAACAACCTGGGTGGCCTGTCATTCCTGGAACTGGGCATCATA
GCCGACGCTACCGTCCGCTCCCTGGAGGGCCGCGGGGTGAAGATTGCCCGTGCCCTGGTG
GGCACCTTCATGTCAGCACTGGAGATGCCTGGCATTTCTCTCACCCTCCTGCTGGTGGAT
GAGCCTCTCCTGAAACTGATAGATGCTGAAACCACTGCAGCAGCCTGGCCTAACGTGGCT
GCAGTCTCCATTACTGGGCGGAAGCGGAGCCGGGTAGCCCCTGCCGAGCCCCAGGAGGCC
CCTGATTCCACTGCTGCAGGAGGCTCAGCCTCGAAGCGGATGGCGCCGGTGCTGGAACGG
GTGTGCAGCACTCTCCTGGGCCTGGAGGAACACCTGAATGCCCTGGACCGGGCTGCTGGT
GACGGCGACTGTGGCACCACCCACAGCCGTGCGGCCAGAGCAATCCAGGAGTGGCTGAAG
GAGGGCCCACCCCCTGCCAGCCCTGCCCAGCTGCTCTCCAAGTTGTCTGTTCTGCTCCTG
GAGAAGATGGGAGGCTCATCTGGGGCGCTCTATGGCCTGTTCCTGACTGCGGCTGCACAG
CCCCTGAAGGCCAAGACCAGCCTCCCAGCCTGGTCTGCTGCCATGGATGCCGGCCTGGAA
GCCATGCAGAAGTATGGCAAGGCTGCTCCAGGGGACAGGACTATGCTGGGTTCTCTGTGG
GCAGCGGGGCAGGAGCTCCAAGCCTGGAAGAGCCCAGGAGCTGATCTGTTACAAGTCCTG
ACCAAAGCAGTCAAGAGTGCCGAAGCTGCAGCCGAGGCCACCAAGAATATGGAAGCTGGA
GCCGGAAGAGCCAGTTATATCAGCTCAGCACGGCTGGAGCAGCCAGACCCCGGGGCGGTG
GCAGCTGCTGCCATCCTCCGGGCCATCTTGGAGGTCTTGCAGAGCTAG
Enzyme 12 GenBank Gene ID AK023915 Link Image
Enzyme 12 GeneCard ID DAK Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 11q12.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Cabezas A, Costas MJ, Pinto RM, Couto A, Cameselle JC: Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases. Biochem Biophys Res Commun. 2005 Dec 30;338(4):1682-9. Epub 2005 Nov 2. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 12879
Enzyme 13 Name Glycerol-3-phosphate dehydrogenase 1-like protein
Enzyme 13 Synonyms
  1. GPD1-L
Enzyme 13 Gene Name GPD1L
Enzyme 13 Protein Sequence >Glycerol-3-phosphate dehydrogenase 1-like protein
MAAAPLKVCIVGSGNWGSAVAKIIGNNVKKLQKFASTVKMWVFEETVNGRKLTDIINNDH
ENVKYLPGHKLPENVVAMSNLSEAVQDADLLVFVIPHQFIHRICDEITGRVPKKALGITL
IKGIDEGPEGLKLISDIIREKMGIDISVLMGANIANEVAAEKFCETTIGSKVMENGLLFK
ELLQTPNFRITVVDDADTVELCGALKNIVAVGAGFCDGLRCGDNTKAAVIRLGLMEMIAF
ARIFCKGQVSTATFLESCGVADLITTCYGGRNRRVAEAFARTGKTIEELEKEMLNGQKLQ
GPQTSAEVYRILKQKGLLDKFPLFTAVYQICYESRPVQEMLSCLQSHPEHT
Enzyme 13 Number of Residues 351
Enzyme 13 Molecular Weight 38418.4
Enzyme 13 Theoretical pI 7.03
Enzyme 13 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • glycerol-3-phosphate dehydrogenase [NAD+] activity
  • glycerol-3-phosphate dehydrogenase [NAD+] activity
  • identical protein binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • protein binding
  • protein homodimerization activity
Process
  • alcohol metabolic process
  • alditol metabolic process
  • carbohydrate metabolic process
  • glycerol metabolic process
  • glycerol-3-phosphate catabolic process
  • glycerol-3-phosphate metabolic process
  • metabolic process
  • oxidation reduction
  • polyol metabolic process
  • primary metabolic process
  • small molecule metabolic process
Component
  • cell part
  • cytoplasm
  • glycerol-3-phosphate dehydrogenase complex
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 13 General Function Involved in oxidoreductase activity
Enzyme 13 Specific Function Play a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3-phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L
Enzyme 13 Pathways
Enzyme 13 Reactions
  • sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+ [RN:R00842]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 158259077 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q8N335 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name GPD1L_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1056 bp
ATGGCAGCGGCGCCCCTGAAAGTGTGCATCGTGGGCTCGGGGAACTGGGGTTCAGCTGTT
GCAAAAATAATTGGTAATAATGTCAAGAAACTTCAGAAATTTGCCTCCACAGTCAAGATG
TGGGTCTTTGAAGAAACAGTGAATGGCAGAAAACTGACAGACATCATAAATAATGACCAT
GAAAATGTAAAATATCTTCCTGGACACAAGCTGCCAGAAAATGTGGTTGCCATGTCAAAT
CTTAGCGAGGCTGTGCAGGATGCAGACCTGCTGGTGTTTGTCATTCCCCACCAGTTCATT
CACAGAATCTGTGATGAGATCACTGGGAGAGTGCCCAAGAAAGCGCTGGGAATCACCCTC
ATCAAGGGCATAGACGAGGGCCCCGAGGGGCTGAAGCTCATTTCTGACATCATCCGTGAG
AAGATGGGTATTGACATCAGTGTGCTGATGGGAGCCAACATTGCCAATGAGGTGGCTGCA
GAGAAGTTCTGTGAGACCACCATCGGCAGCAAAGTAATGGAGAACGGCCTTCTCTTCAAA
GAACTTCTGCAGACTCCAAATTTTCGAATTACCGTGGTTGATGATGCAGACACTGTTGAA
CTCTGTGGTGCGCTTAAGAACATCGTAGCTGTGGGAGCTGGGTTCTGCGACGGCCTCCGC
TGTGGAGACAACACCAAAGCGGCCGTCATCCGCCTGGGACTCATGGAAATGATTGCTTTT
GCCAGGATCTTCTGCAAAGGCCAAGTGTCTACAGCCACCTTCCTAGAGAGCTGCGGGGTG
GCCGACCTGATCACCACCTGTTACGGAGGGCGGAACCGCAGGGTGGCCGAGGCCTTCGCC
AGAACTGGGAAGACCATTGAAGAGTTGGAGAAGGAGATGCTGAATGGGCAAAAGCTCCAA
GGACCGCAGACTTCTGCTGAAGTGTACCGCATCCTCAAACAGAAGGGACTACTGGACAAG
TTTCCATTGTTTACTGCAGTGTATCAGATCTGCTACGAAAGCAGACCAGTTCAAGAGATG
TTGTCTTGTCTTCAGAGCCATCCAGAGCATACATAA
Enzyme 13 GenBank Gene ID AK292808 Link Image
Enzyme 13 GeneCard ID GPD1L Link Image
Enzyme 13 GenAtlas ID GPD1L Link Image
Enzyme 13 HGNC ID HGNC:28956 Link Image
Enzyme 13 Chromosome Location 3
Enzyme 13 Locus 3p22.3
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Valdivia CR, Ueda K, Ackerman MJ, Makielski JC: GPD1L links redox state to cardiac excitability by PKC-dependent phosphorylation of the sodium channel SCN5A. Am J Physiol Heart Circ Physiol. 2009 Oct;297(4):H1446-52. Epub 2009 Aug 7. [PubMed Link Image]
  5. Liu M, Sanyal S, Gao G, Gurung IS, Zhu X, Gaconnet G, Kerchner LJ, Shang LL, Huang CL, Grace A, London B, Dudley SC Jr: Cardiac Na+ current regulation by pyridine nucleotides. Circ Res. 2009 Oct 9;105(8):737-45. Epub 2009 Sep 10. [PubMed Link Image]
  6. Van Norstrand DW, Valdivia CR, Tester DJ, Ueda K, London B, Makielski JC, Ackerman MJ: Molecular and functional characterization of novel glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) mutations in sudden infant death syndrome. Circulation. 2007 Nov 13;116(20):2253-9. Epub 2007 Oct 29. [PubMed Link Image]
  7. London B, Michalec M, Mehdi H, Zhu X, Kerchner L, Sanyal S, Viswanathan PC, Pfahnl AE, Shang LL, Madhusudanan M, Baty CJ, Lagana S, Aleong R, Gutmann R, Ackerman MJ, McNamara DM, Weiss R, Dudley SC Jr: Mutation in glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) decreases cardiac Na+ current and causes inherited arrhythmias. Circulation. 2007 Nov 13;116(20):2260-8. Epub 2007 Oct 29. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 13047
Enzyme 14 Name cDNA FLJ75492, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
Enzyme 14 Synonyms
  1. mitochondrial
  2. GPD2, mRNA
  3. Glycerol-3-phosphate dehydrogenase 2
  4. Mitochondrial, isoform CRA_b
  5. cDNA FLJ78257, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
  6. mitochondrial
  7. GPD2, mRNA
Enzyme 14 Gene Name GPD2
Enzyme 14 Protein Sequence >cDNA FLJ75492, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQ
LLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVR
YLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLY
DLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYG
AATANYMEVVSLLKKTDPQTGKVHVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKM
DDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTD
VTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNH
VVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY
IRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYG
IKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLY
YEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMD
ENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPV
DRSCGGL
Enzyme 14 Number of Residues 727
Enzyme 14 Molecular Weight 80835
Enzyme 14 Theoretical pI 7.58
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Energy production and conversion
Enzyme 14 Specific Function Not Available
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 158255566 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID A8K4V0 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name A8K4V0_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AK291065 Link Image
Enzyme 14 GeneCard ID A8K4V0 Link Image
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
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 15832
Enzyme 15 Name Triosephosphate isomerase
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name Not Available
Enzyme 15 Protein Sequence >Triosephosphate isomerase
MAPSRKFFVGGNWKMNGRKQSLRELVRTLNAAKVPADTEVVCTPPTAYIDFARQKLDPKI
AVAAQNCYKVTNGAFTGEISPGMIKDCRATWVVLGHSERRHVFGESDELIGQKVAHALAE
GLGVIACTGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ
QDQEVHDKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPGVDGFLVGGASLKPE
FVDIINAKQ
Enzyme 15 Number of Residues 249
Enzyme 15 Molecular Weight 26942.6
Enzyme 15 Theoretical pI 8.21
Enzyme 15 GO Classification
Function
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, interconverting aldoses and ketoses
  • isomerase activity
  • triose-phosphate isomerase activity
Process
  • metabolic process
Component
Enzyme 15 General Function Involved in catalytic activity
Enzyme 15 Specific Function D-glyceraldehyde 3-phosphate = glycerone phosphate
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions
  • D-glyceraldehyde 3-phosphate = glycerone phosphate [RN:R01015]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 83674980 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q2QD09 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q2QD09_HUMAN Link Image
Enzyme 15 PDB ID 1HTI Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >747 bp
ATGGCGCCCTCCAGGAAGTTCTTCGTTGGGGGGAACTGGAAGATGAACGGGCGAAAGCAG
AGTCTGCGGGAGCTCGTCCGCACTCTGAACGCGGCCAAGGTGCCGGCCGACACCGAGGTG
GTTTGTACTCCGCCTACTGCCTATATCGACTTCGCCCGGCAGAAGCTAGATCCCAAGATT
GCTGTGGCTGCGCAGAACTGCTACAAAGTGACTAATGGGGCTTTTACTGGGGAGATCAGC
CCTGGCATGATCAAAGACTGCAGAGCCACGTGGGTGGTCCTGGGGCACTCAGAGAGAAGG
CATGTCTTTGGGGAGTCAGATGAGCTGATTGGGCAGAAAGTGGCCCATGCTCTGGCAGAG
GGACTCGGAGTAATCGCCTGCACTGGGGAGAAGCTAGATGAAAGGGAAGCTGGCATCACT
GAGAAGGTTGTTTTCGAGCAGACAAAGGTCATCGCAGATAACGTGAAGGACTGGAGCAAG
GTCGTCCTGGCCTATGAGCCTGTGTGGGCCATTGGTACTGGCAAGACTGCAACACCCCAA
CAGGACCAGGAAGTACACGACAAGCTCCGAGGATGGCTTAAGTCCAACGTCTCTGATGCG
GTGGCTCAGAGCACCCGTATCATTTATGGAGGCTCTGTGACTGGGGCAACCTGCAAGGAG
CTGGCCAGCCAGCCTGGCGTGGATGGCTTCCTTGTGGGTGGTGCTTCCCTCAAGCCCGAA
TTCGTGGACATCATCAATGCCAAACAA
Enzyme 15 GenBank Gene ID DQ120711 Link Image
Enzyme 15 GeneCard ID Not Available
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID HGNC:12009 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs Not Available
Enzyme 15 General References
  1. Marques AC, Dupanloup I, Vinckenbosch N, Reymond A, Kaessmann H: Emergence of young human genes after a burst of retroposition in primates. PLoS Biol. 2005 Nov;3(11):e357. Epub 2005 Oct 11. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 16709
Enzyme 16 Name cDNA, FLJ93658, highly similar to Homo sapiens alkaline phosphatase, intestinal (ALPI), mRNA (Alkaline phosphatase, intestinal, isoform CRA_a)
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name ALPI
Enzyme 16 Protein Sequence >cDNA, FLJ93658, highly similar to Homo sapiens alkaline phosphatase, intestinal (ALPI), mRNA (Alkaline phosphatase, intestinal, isoform CRA_a)
MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLG
DGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLC
GVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYA
HTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADA
SQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRD
PTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERA
GQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVF
NSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHV
MAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP
Enzyme 16 Number of Residues 528
Enzyme 16 Molecular Weight 56813
Enzyme 16 Theoretical pI 5.70
Enzyme 16 GO Classification
Function
Process
  • metabolism
  • physiological process
Component
Enzyme 16 General Function Inorganic ion transport and metabolism
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID B2R7Y4 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name B2R7Y4_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID AK313163 Link Image
Enzyme 16 GeneCard ID B2R7Y4 Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
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 16713
Enzyme 17 Name cDNA, FLJ92580, Homo sapiens aldolase C, fructose-bisphosphate (ALDOC), mRNA (Aldolase C, fructose-bisphosphate, isoform CRA_a)
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name ALDOC
Enzyme 17 Protein Sequence >cDNA, FLJ92580, Homo sapiens aldolase C, fructose-bisphosphate (ALDOC), mRNA (Aldolase C, fructose-bisphosphate, isoform CRA_a)
MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYR
QVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGIVVGIKVDKGVVPLAGTD
GETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISERTPSALAILENANVLARYASICQQ
NGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHAC
PIKYTPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASFNLNAINRCPLPRPWALTF
SYGRALQASALNAWRGQRDNAGAATEEFIKRAEVNGLAAQGKYEGSGEDGGAAAQSLYIA
NHAY
Enzyme 17 Number of Residues 364
Enzyme 17 Molecular Weight 39456
Enzyme 17 Theoretical pI 6.86
Enzyme 17 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • fructose-bisphosphate aldolase activity
  • lyase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 17 General Function Carbohydrate transport and metabolism
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein Not Available
Enzyme 17 UniProtKB/Swiss-Prot ID B2R5R3 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name B2R5R3_HUMAN Link Image
Enzyme 17 PDB ID 1XFB Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID AK312281 Link Image
Enzyme 17 GeneCard ID B2R5R3 Link Image
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location 17
Enzyme 17 Locus 17cen-q12
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
Enzyme 17 Metabolite References Not Available