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Human Metabolome Database Version 2.5

 

Showing metabocard for Glycogen (HMDB00757)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:13
Accession Number HMDB00757
Secondary Accession Numbers Not Available
Common Name Glycogen
Description Glycogen is a highly-branched polymer of about 30,000 glucose residues and has a molecular weight between 106 and 107 daltons (4.8 million approx.). Most of Glc units are linked by alpha-1,4 glycosidic bonds, approximately 1 in 12 Glc residues also makes -1,6 glycosidic bond with a second Glc which results in the creation of a branch. Glycogen only has one reducing end and a large number of non-reducing ends with a free hydroxyl group at carbon 4. The glycogen granules contain both glycogen and the enzymes of glycogen synthesis (glycogenesis) and degradation (glycogenolysis). The enzymes are nested between the outer branches of the glycogen molecules and act on the non-reducing ends. Therefore, the many non-reducing end-branches of glycogen facilitate its rapid synthesis and breakdown. In hypoglycemia caused by excessive insulin, liver glycogen levels are high, but the high insulin level prevents the glycogenolysis necessary to maintain normal blood sugar levels. Glucagon is a common treatment for this type of hypoglycemia. Glycogen is a polysaccharide that is the principal storage form of glucose (Glc) in animal and human cells. Glycogen is found in the form of granules in the cytosol in many cell types. Hepatocytes (liver cells) have the highest concentration of it - up to 8% of the fresh weight in well fed state, or 100 to 120 g in an adult - giving liver a distinctive, 'starchy taste'. In the muscles, glycogen is found in a much lower concentration (1% of the muscle mass), but the total amount exceeds that in liver. Small amounts of glycogen are found in the kidneys, and even smaller amounts in certain glial cells in the brain and white blood cells.
Synonyms
  1. Animal starch
  2. Glycogen
  3. Liver starch
  4. Lyoglycogen
  5. Phytoglycogen
Chemical IUPAC Name (2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-6-[(2R,3S,4R,5R,6S)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-2-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxymethyl]oxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
Chemical Formula C24H42O21
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Tetrasaccharides
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • acetal
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • heterocyclic compound
Biofunction
  • Component of Starch and sucrose metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 666.578
Monoisotopic Molecular Weight 666.221863
Isomeric SMILES OC[C@H]1O[C@H](OC[C@H]2O[C@H](O[C@@H]3[C@@H](CO)O[C@H](O)[C@H](O)[C@H]3O)[C@H](O)[C@@H](O)[C@@H]2O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1O
Canonical SMILES OCC1OC(OCC2OC(OC3C(CO)OC(O)C(O)C3O)C(O)C(O)C2OC2OC(CO)C(O)C(O)C2O)C(O)C(O)C1O
KEGG Compound ID C00182 Link Image
BioCyc ID CPD0-971 Link Image
BiGG ID Not Available
Wikipedia Link Glycogen Link Image
NuGOwiki Link HMDB00757 Link Image
Metagene Link HMDB00757 Link Image
METLIN ID 160 Link Image
PubChem Compound 439177 Link Image
PubChem Substance 3157432 Link Image
ChEBI ID 28087 Link Image
CAS Registry Number 9005-79-2
InChI Identifier InChI=1/C24H42O21/c25-1-5-9(28)11(30)16(35)22(41-5)39-4-8-20(45-23-17(36)12(31)10(29)6(2-26)42-23)14(33)18(37)24(43-8)44-19-7(3-27)40-21(38)15(34)13(19)32/h5-38H,1-4H2/t5-,6-,7-,8-,9-,10-,11+,12+,13-,14-,15-,16-,17-,18-,19-,20-,21+,22+,23-,24-/m1/s1
Synthesis Reference Parodi A J; Krisman C R; Mordoh J In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process. Archives of biochemistry and biophysics (1970), 141(1), 219-27.
Melting Point (Experimental) 270-280 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 343.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.67 [Predicted by ALOGPS]; -7.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Blood
Tissue Location
Tissue References
Adipose Tissue —
Adrenal Cortex —
Adrenal Gland —
Adrenal Medulla —
Brain —
Epidermis —
Fibroblasts —
Kidney —
Liver —
Muscle —
Myelin —
Nerve Cells —
Neuron —
Pancreas —
Placenta —
Platelet —
Skeletal Muscle —
Stratum Corneum —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 39.1 +/- 3.1 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 43.3 +/- 3.4 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Starch and Sucrose Metabolism SMP00058 Link Image map00500 Link Image
General References
  1. Zderic TW, Schenk S, Davidson CJ, Byerley LO, Coyle EF: Manipulation of dietary carbohydrate and muscle glycogen affects glucose uptake during exercise when fat oxidation is impaired by beta-adrenergic blockade. Am J Physiol Endocrinol Metab. 2004 Dec;287(6):E1195-201. Epub 2004 Aug 17. [PubMed Link Image]
  2. Schaart G, Hesselink RP, Keizer HA, van Kranenburg G, Drost MR, Hesselink MK: A modified PAS stain combined with immunofluorescence for quantitative analyses of glycogen in muscle sections. Histochem Cell Biol. 2004 Aug;122(2):161-9. Epub 2004 Aug 3. [PubMed Link Image]
  3. Wee SL, Williams C, Tsintzas K, Boobis L: Ingestion of a high-glycemic index meal increases muscle glycogen storage at rest but augments its utilization during subsequent exercise. J Appl Physiol. 2005 Aug;99(2):707-14. Epub 2005 Apr 14. [PubMed Link Image]
  4. Zehnder M, Muelli M, Buchli R, Kuehne G, Boutellier U: Further glycogen decrease during early recovery after eccentric exercise despite a high carbohydrate intake. Eur J Nutr. 2004 Jun;43(3):148-59. Epub 2004 Jan 6. [PubMed Link Image]
  5. Koopman R, Manders RJ, Jonkers RA, Hul GB, Kuipers H, van Loon LJ: Intramyocellular lipid and glycogen content are reduced following resistance exercise in untrained healthy males. Eur J Appl Physiol. 2006 Mar;96(5):525-34. Epub 2005 Dec 21. [PubMed Link Image]
  6. Jentjens R, Jeukendrup A: Determinants of post-exercise glycogen synthesis during short-term recovery. Sports Med. 2003;33(2):117-44. [PubMed Link Image]
  7. Ouwens DM, van der Zon GC, Maassen JA: Modulation of insulin-stimulated glycogen synthesis by Src Homology Phosphatase 2. Mol Cell Endocrinol. 2001 Apr 25;175(1-2):131-40. [PubMed Link Image]
  8. Koppersmith DL, Powers JM, Hennigar GR: Angiomatoid neuroblastoma with cytoplasmic glycogen: a case report and histogenetic considerations. Cancer. 1980 Feb;45(3):553-60. [PubMed Link Image]
  9. Kohler G, Boutellier U: Glycogen reduction in non-exercising muscle depends on blood lactate concentration. Eur J Appl Physiol. 2004 Aug;92(4-5):548-54. [PubMed Link Image]
  10. Crosson SM, Khan A, Printen J, Pessin JE, Saltiel AR: PTG gene deletion causes impaired glycogen synthesis and developmental insulin resistance. J Clin Invest. 2003 May;111(9):1423-32. [PubMed Link Image]
  11. Dube SN, Nayak BB, Das PK: Effect of foot-electroshock stress on cholinergic activity, tissue glycogen and blood sugar in albino rats. Indian J Physiol Pharmacol. 1978 Jan-Mar;22(1):24-32. [PubMed Link Image]
  12. Chryssanthopoulos C, Williams C, Nowitz A, Bogdanis G: Skeletal muscle glycogen concentration and metabolic responses following a high glycaemic carbohydrate breakfast. J Sports Sci. 2004 Nov-Dec;22(11-12):1065-71. [PubMed Link Image]
  13. Steinberg GR, Watt MJ, McGee SL, Chan S, Hargreaves M, Febbraio MA, Stapleton D, Kemp BE: Reduced glycogen availability is associated with increased AMPKalpha2 activity, nuclear AMPKalpha2 protein abundance, and GLUT4 mRNA expression in contracting human skeletal muscle. Appl Physiol Nutr Metab. 2006 Jun;31(3):302-12. [PubMed Link Image]
  14. Hudson ER, Pan DA, James J, Lucocq JM, Hawley SA, Green KA, Baba O, Terashima T, Hardie DG: A novel domain in AMP-activated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias. Curr Biol. 2003 May 13;13(10):861-6. [PubMed Link Image]
  15. van Loon LJ, Murphy R, Oosterlaar AM, Cameron-Smith D, Hargreaves M, Wagenmakers AJ, Snow R: Creatine supplementation increases glycogen storage but not GLUT-4 expression in human skeletal muscle. Clin Sci (Lond). 2004 Jan;106(1):99-106. [PubMed Link Image]
  16. Tomihira M, Kawasaki E, Nakajima H, Imamura Y, Sato Y, Sata M, Kage M, Sugie H, Nunoi K: Intermittent and recurrent hepatomegaly due to glycogen storage in a patient with type 1 diabetes: genetic analysis of the liver glycogen phosphorylase gene (PYGL). Diabetes Res Clin Pract. 2004 Aug;65(2):175-82. [PubMed Link Image]
  17. McVie-Wylie AJ, Ding EY, Lawson T, Serra D, Migone FK, Pressley D, Mizutani M, Kikuchi T, Chen YT, Amalfitano A: Multiple muscles in the AMD quail can be "cross-corrected" of pathologic glycogen accumulation after intravenous injection of an [E1-, polymerase-] adenovirus vector encoding human acid-alpha-glucosidase. J Gene Med. 2003 May;5(5):399-406. [PubMed Link Image]
  18. Price TB, Laurent D, Petersen KF: 13C/31P NMR studies on the role of glucose transport/phosphorylation in human glycogen supercompensation. Int J Sports Med. 2003 May;24(4):238-44. [PubMed Link Image]
  19. Tanis AA, Rietveld T, Wattimena JL, van den Berg JW, Swart GR: The 13CO2 breath test for liver glycogen oxidation after 3-day labeling of the liver with a naturally 13C-enriched diet. Nutrition. 2003 May;19(5):432-7. [PubMed Link Image]
  20. Devries MC, Hamadeh MJ, Graham TE, Tarnopolsky MA: 17beta-estradiol supplementation decreases glucose rate of appearance and disappearance with no effect on glycogen utilization during moderate intensity exercise in men. J Clin Endocrinol Metab. 2005 Nov;90(11):6218-25. Epub 2005 Aug 23. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Glycogen debranching enzyme
  2. Glycogen phosphorylase, brain form
  3. Glycogenin-2
  4. Serine/threonine-protein phosphatase PP1-beta catalytic subunit
  5. Laforin
  6. Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
  7. Salivary alpha-amylase precursor
  8. Maltase-glucoamylase, intestinal [Includes: Maltase
  9. Glucan , branching enzyme 1 variant
  10. Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
  11. Protein phosphatase 1 regulatory subunit 3C
  12. Protein phosphatase 1 regulatory subunit 3B
Enzyme 1 [top]
Enzyme 1 ID 5603
Enzyme 1 Name Glycogen debranching enzyme
Enzyme 1 Synonyms
  1. Glycogen debrancher[Includes: 4-alpha- glucanotransferase
  2. Oligo-1,4-1,4-glucantransferase
  3. Amylo-alpha-1,6-glucosidase
  4. Amylo-1,6-glucosidase
  5. Dextrin 6-alpha-D-glucosidase]
Enzyme 1 Gene Name AGL
Enzyme 1 Protein Sequence >Glycogen debranching enzyme 
MGHSKQIRILLLNEMEKLEKTLFRLEQGYELQFRLGPTLQGKAVTVYTNYPFPGETFNRE
KFRSLDWENPTEREDDSDKYCKLNLQQSGSFQYYFLQGNEKSGGGYIVVDPILRVGADNH
VLPLDCVTLQTFLAKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSCYSLANQLE
LNPDFSRPNRKYTWNDVGQLVEKLKKEWNVICITDVVYNHTAANSKWIQEHPECAYNLVN
SPHLKPAWVLDRALWRFSCDVAEGKYKEKGIPALIENDHHMNSIRKIIWEDIFPKLKLWE
FFQVDVNKAVEQFRRLLTQENRRVTKSDPNQHLTIIQDPEYRRFGCTVDMNIALTTFIPH
DKGPAAIEECCNWFHKRMEELNSEKHRLINYHQEQAVNCLLGNVFYERLAGHGPKLGPVT
RKHPLVTRYFTFPFEEIDFSMEESMIHLPNKACFLMAHNGWVMGDDPLRNFAEPGSEVYL
RRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATYFQGVRLDNCHSTPLHVAEYML
DAARNLQPNLYVVAELFTGSEDLDNVFVTRLGISSLIREAMSAYNSHEEGRLVYRYGGEP
VGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSTTIVSMACCASGSTRGY
DELVPHQISVVSEERFYTKWNPEALPSNTGEVNFQSGIIAARCAISKLHQELGAKGFIQV
YVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEAR
TIERNTKPYRKDENSINGTPDITVEIREHIQLNESKIVKQAGVATKGPNEYIQEIEFENL
SPGSVIIFRVSLDPHAQVAVGILRNHLTQFSPHFKSGSLAVDNADPILKIPFASLASRLT
LAELNQILYRCESEEKEDGGGCYDIPNWSALKYAGLQGLMSVLAEIRPKNDLGHPFCNNL
RSGDWMIDYVSNRLISRSGTIAEVGKWLQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLD
TAWKQMSSFVQNGSTFVKHLSLGSVQLCGVGKFPSLPILSPALMDVPYRLNEITKEKEQC
CVSLAAGLPHFSSGIFRCWGRDTFIALRGILLITGRYVEARNIILAFAGTLRHGLIPNLL
GEGIYARYNCRDAVWWWLQCIQDYCKMVPNGLDILKCPVSRMYPTDDSAPLPAGTLDQPL
FEVIQEAMQKHMQGIQFRERNAGPQIDRNMKDEGFNITAGVDEETGFVYGGNRFNCGTWM
DKMGESDRARNRGIPATPRDGSAVEIVGLSKSAVRWLLELSKKNIFPYHEVTVKRHGKAI
KVSYDEWNRKIQDNFEKLFHVSEDPSDLNEKHPNLVHKRGIYKDSYGASSPWCDYQLRPN
FTIAMVVAPELFTTEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGIYDNALDNDNYNLA
KGFNYHQGPEWLWPIGYFLRAKLYFSRLMGPETTAKTIVLVKNVLSRHYVHLERSPWKGL
PELTNENAQYCPFSCETQAWSIATILETLYDL
Enzyme 1 Number of Residues 1532
Enzyme 1 Molecular Weight 174766
Enzyme 1 Theoretical pI 6.74
Enzyme 1 GO Classification
Function
  • 4-alpha-glucanotransferase activity
  • amylo-alpha-1,6-glucosidase activity
  • catalytic activity
  • glycogen debranching enzyme activity
Process
  • carbohydrate metabolism
  • cellular polysaccharide metabolism
  • glucan metabolism
  • glycogen biosynthesis
  • glycogen metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide metabolism
Component
—
Enzyme 1 General Function Carbohydrate transport and metabolism
Enzyme 1 Specific Function Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6- glucosidase in glycogen degradation
Enzyme 1 Pathways
Enzyme 1 Reactions
  • Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 187577 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P35573 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GDE_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >4548 bp 
ATGAGTTTATTAACATGTGCTTTTTATTTAGGGTATGAGCTACAGTTCCGATTAGGCCCA
ACTTTACAGGGAAAAGCAGTTACCGTGTATACAAATTACCCATTTCCTGGAGAAACATTT
AATAGAGAAAAATTCCGTTCTCTGGATTGGGAAAATCCAACAGAAAGAGAAGATGATTCT
GATAAATACTGTAAACTTAATCTGCAACAATCTGGTTCATTTCAGTATTATTTCCTTCAA
GGAAATGAGAAAAGTGGTGGAGGTTACATAGTTGTGGACCCCATTTTACGTGTTGGTGCT
GATAATCATGTGCTACCCTTGGACTGTGTTACTCTTCAGACATTTTTAGCTAAGTGTTTG
GGACCTTTTGATGAATGGGAAAGCAGACTTAGGGTTGCAAAAGAATCAGGCTACAACATG
ATTCATTTTACCCCATTGCAGACTCTTGGACTATCTAGGTCATGCTACTCCCTTGCCAAT
CAGTTAGAATTAAATCCTGACTTTTCAAGACCTAATAGAAAGTATACCTGGAATGATGTT
GGACAGCTAGTGGAAAAATTAAAAAAGGAATGGAATGTTATTTGTATTACTGATGTTGTC
TACAATCATACTGCTGCTAATAGTAAATGGATCCAGGAACATCCAGAATGTGCCTATAAT
CTTGTGAATTCTCCACACTTAAAACCTGCCTGGGTCTTAGACAGAGCACTTTGGCGTTTC
TCCTGTGATGTTGCAGAAGGGAAATACAAAGAAAAGGGAATACCTGCTTTGATTGAAAAT
GATCACCATATGAATTCCATCCGAAAAATAATTTGGGAGGATATTTTTCCAAAGCTTAAA
CTCTGGGAATTTTTCCAAGTAGATGTCAACAAAGCGGTTGAGCAATTTAGAAGACTTCTT
ACACAAGAAAATAGGCGAGTAACCAAGTCTGATCCAAACCAACACCTTACGATTATTCAA
GATCCTGAATACAGACGGTTTGGCTGTACTGTAGATATGAACATTGCACTAACGACTTTC
ATACCACATGACAAGGGGCCAGCAGCAATTGAAGAATGCTGTAATTGGTTTCATAAAAGA
ATGGAGGAATTAAATTCAGAGAAGCATCGACTCATTAACTATCATCAGGAACAGGCAGTT
AATTGCCTTTTGGGAAATGTGTTTTATGAACGACTGGCTGGCCATGGTCCAAAACTAGGA
CCTGTCACTAGAAAGCATCCTTTAGTTACCAGGTATTTTACTTTCCCATTTGAAGAGATA
GACTTCTCCATGGAAGAATCTATGATTCATCTGCCAAATAAAGCTTGTTTTCTGATGGCA
CACAATGGATGGGTAATGGGAGATGATCCTCTTCGAAACTTTGCTGAACCGGGTTCAGAA
GTTTACCTAAGGAGAGAACTTATTTGCTGGGGAGACAGTGTTAAATTACGCTATGGGAAT
AAACCAGAGGACTGTCCTTATCTCTGGGCACACATGAAAAAATACACTGAAATAACTGCA
ACTTATTTCCAGGGAGTACGTCTTGATAACTGCCACTCAACACCTCTTCACGTAGCTGAG
TACATGTTGGATGCTGCTAGGAATTTGCAACCCAATTTATATGTAGTAGCTGAACTGTTC
ACAGGAAGTGAAGATCTGGACAATGTCTTTGTTACTAGACTGGGCATTAGTTCCTTAATA
AGAGAGGCAATGAGTGCATATAATAGTCATGAAGAGGGCAGATTAGTTTACCGATATGGA
GGAGAACCTGTTGGATCCTTTGTTCAGCCCTGTTTGAGGCCTTTAATGCCAGCTATTGCA
CATGCCCTGTTTATGGATATTACGCATGATAATGAGTGTCCTATTGTGCATAGATCAGCG
TATGATGCTCTTCCAAGTACTACAATTGTTTCTATGGCATGTTGTGCTAGTGGAAGTACA
AGAGGCTATGATGAATTAGTGCCTCATCAGATTTCAGTGGTTTCTGAAGAACGGTTTTAC
ACTAAGTGGAATCCTGAAGCATTGCCTTCAAACACAGGTGAAGTTAATTTCCAAAGCGGC
ATTATTGCAGCCAGGTGTGCTATCAGTAAACTTCATCAGGAGCTTGGAGCCAAGGGTTTT
ATTCAGGTGTATGTGGATCAAGTTGATGAAGACATAGTGGCAGTAACAAGACACTCACCT
AGCATCCATCAGTCTGTTGTGGCTGTATCTAGAACTGCTTTCAGGAATCCCAAGACTTCA
TTTTACAGCAAGGAAGTGCCTCAAATGTGCATCCCTGGCAAAATTGAAGAAGTAGTTCTT
GAAGCTAGAACTATTGAGAGAAACACGAAACCTTATAGGAAGGATGAGAATTCAATCAAT
GGAACACCAGATATCACAGTAGAAATTAGAGAACATATTCAGCTTAATGAAAGTAAAATT
GTTAAACAAGCTGGAGTTGCCACAAAAGGGCCCAATGAATATATTCAAGAAATAGAATTT
GAAAACTTGTCTCCAGGAAGTGTTATTATATTCAGAGTTAGTCTTGATCCACATGCACAA
GTCGCTGTTGGAATTCTTCGAAATCATCTGACACAATTCAGTCCTCACTTTAAATCTGGC
AGCCTAGCTGTTGACAATGCAGATCCTATATTAAAAATTCCTTTTGCTTCTCTTGCCTCC
AGATTAACTTTGGCTGAGCTAAATCAGATCCTTTACCGATGTGAATCAGAAGAAAAGGAA
GATGGTGGAGGGTGCTATGACATACCAAACTGGTCAGCCCTTAAATATGCAGGTCTTCAA
GGTTTAATGTCTGTATTGGCAGAAATAAGACCAAAGAATGACTTGGGGCATCCTTTTTGT
AATAATTTGAGATCTGGAGATTGGATGATTGACTATGTCAGTAACCGGCTTATTTCACGA
TCAGGAACTATTGCTGAAGTTGGTAAATGGTTGCAGGCTATGTTCTTCTACCTGAAGCAG
ATCCCACGTTACCTTATCCCATGTTACTTTGATGCTATATTAATTGGTGCATATACCACT
CTTCTGGATACAGCATGGAAGCAGATGTCAAGCTTTGTTCAGAATGGTTCAACCTTTGTG
AAACACCTTTCATTGGGTTCAGTTCAACTGTGTGGAGTAGGAAAATTCCCTTCCCTGCCA
ATTCTTTCACCTGCCCTAATGGATGTACCTTATAGGTTAAATGAGATCACAAAAGAAAAG
GAGCAATGTTGTGTTTCTCTAGCTGCAGGCTTACCTCATTTTTCTTCTGGTATTTTCCGC
TGCTGGGGAAGGGATACTTTTATTGCACTTAGAGGTATACTGCTGATTACTGGACGCTAT
GTAGAAGCCAGGAATATTATTTTAGCATTTGCGGGTACCCTGAGGCATGGTCTCATTCCT
AATCTACTGGGTGAAGGGATTTATGCCAGATACAATTGTCGGGATGCTGTGTGGTGGTGG
CTGCAGTGTATCCAGGATTACTGTAAAATGGTTCCAAATGGTCTAGACATTCTCAAGTGC
CCAGTTTCCAGAATGTATCCTACAGATGATTCTGCTCCTTTGCCTGCTGGCACACTGGAT
CAGCCATTGTTTGAAGTCATACAGGAAGCAATGCAAAAACACATGCAGGGCATACAGTTC
CGAGAAAGGAATGCTGGTCCCCAGATAGATCGAAACATGAAGGACGAAGGTTTTAATATA
ACTGCAGGAGTTGATGAAGAAACAGGATTTGTTTATGGAGGAAATCGTTTCAATTGTGGC
ACATGGATGGATAAAATGGGAGAAAGTGACAGAGCTAGAAACAGAGGAATCCCAGCCACA
CCAAGAGATGGGTCTGCTGTGGAAATTGTGGGCCTGAGTAAATCTGCTGTTCGCTGGTTG
CTGGAATTATCCAAAAAAAATATTTTCCCTTATCATGAAGTCACAGTAAAAAGACATGGA
AAGGCTATAAAGGTCTCATATGATGAGTGGAACAGAAAAATACAAGACAACTTTGAAAAG
CTATTTCATGTTTCCGAAGACCCTTCAGATTTAAATGAAAAGCATCCAAATCTGGTTCAC
AAACGTGGCATATACAAAGATAGTTATGGAGCTTCAAGTCCTTGGTGTGACTATCAGCTC
AGGCCTAATTTTACCATAGCAATGGTTGTGGCCCCTGAGCTCTTTACTACAGAAAAAGCA
GGGAAAGCTTTGGAGATTGCAGAAAAAAAATTGCTTGGTCCCCTTGGCATGAAAACTTTA
GATCCAGATGATATGGTTTACTGTGGAATTTATGACAATGCATTAGACAATGACAACTAC
AATCTTGCTAAAGGTTTCAATTATCACCAAGGACCTGAGTGGCTGTGGCCTATTGGGTAT
TTTCTTCGTGCAAAATTATATTTTTCCAGATTGATGGGCCCGGAGACTACTGCAAAGACT
ATAGTTTTGGTTAAAAATGTTCTTTCCCGACATTATGTTCATCTTGAGAGATCCCCTTGG
AAAGGACTTCCAGAACTGACCAATGAGAATGCCCAGTACTGTCCTTTCAGCTGTGAAACA
CAAGCCTGGTCAATTGCTACTATTCTTGAGACACTTTATGATTTATAG
Enzyme 1 GenBank Gene ID M85168 Link Image
Enzyme 1 GeneCard ID AGL Link Image
Enzyme 1 GenAtlas ID AGL Link Image
Enzyme 1 HGNC ID HGNC:321 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Yang BZ, Ding JH, Enghild JJ, Bao Y, Chen YT: Molecular cloning and nucleotide sequence of cDNA encoding human muscle glycogen debranching enzyme. J Biol Chem. 1992 May 5;267(13):9294-9. [PubMed Link Image]
  2. Bao Y, Dawson TL Jr, Chen YT: Human glycogen debranching enzyme gene (AGL): complete structural organization and characterization of the 5' flanking region. Genomics. 1996 Dec 1;38(2):155-65. [PubMed Link Image]
  3. Bao Y, Yang BZ, Dawson TL Jr, Chen YT: Isolation and nucleotide sequence of human liver glycogen debranching enzyme mRNA: identification of multiple tissue-specific isoforms. Gene. 1997 Sep 15;197(1-2):389-98. [PubMed Link Image]
  4. Okubo M, Horinishi A, Takeuchi M, Suzuki Y, Sakura N, Hasegawa Y, Igarashi T, Goto K, Tahara H, Uchimoto S, Omichi K, Kanno H, Hayasaka K, Murase T: Heterogeneous mutations in the glycogen-debranching enzyme gene are responsible for glycogen storage disease type IIIa in Japan. Hum Genet. 2000 Jan;106(1):108-15. [PubMed Link Image]
  5. Okubo M, Kanda F, Horinishi A, Takahashi K, Okuda S, Chihara K, Murase T: Glycogen storage disease type IIIa: first report of a causative missense mutation (G1448R) of the glycogen debranching enzyme gene found in a homozygous patient. Hum Mutat. 1999 Dec;14(6):542-3. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5612
Enzyme 2 Name Glycogen phosphorylase, brain form
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name PYGB
Enzyme 2 Protein Sequence >Glycogen phosphorylase, brain form 
MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTV
RDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDL
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEA
DDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVN
TMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKV
DWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFP
GDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKF
QNKTNGITPRRWLLLCNPGLADTIVEKIGEEFLTDLSQLKKLLPLVSDEVFIRDVAKVKQ
ENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKRDPAKAFV
PRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLKVIFLENYRVSLAEKVIPA
ADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVE
ALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDIVNMLMHHDRFKVFADYEA
YMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNI
PRD
Enzyme 2 Number of Residues 843
Enzyme 2 Molecular Weight 96697
Enzyme 2 Theoretical pI 6.85
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • phosphorylase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
  • vitamin binding
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Carbohydrate transport and metabolism
Enzyme 2 Specific Function Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 307200 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P11216 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PYGB_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2592 bp 
ATGGGCGAACCGCTGACGGACAGCGAGAAGCGGAAGCAGATCAGCGTGCGCGGCCTGGCG
GGGCTAGGCGACGTGGCCGAGGTGCGGAAGAGCTTCAACCGGCACTTGCACTTCACGCTG
GTCAAGGACCGCAATGTGGCCACGCCCCGCGACTACTTCTTCGCGCTGGCGCACACGGTG
CGCGACCACCTCGTGGGCCGCTGGATCCGCACGCAGCAGCACTACTACGAGCGCGACCCC
AAGCGAATTTATTATCTTTCCCTGGAATTCTACATGGGTCGCACGCTGCAGAACACGATG
GTGAACCTGGGCCTTCAGAATGCCTGCGATGAAGCCATCTATCAGTTGGGGTTAGACTTG
GAGGAACTCGAGGAGATAGAAGAAGATGCTGGCCTTGGGAATGGAGGCCTGGGGAGGCTG
GCAGCGTGTTTCCTTGACTCAATGGCTACCTTGGGCCTGGCAGCATACGGCTATGGAATC
CGCTATGAATTTGGGATTTTTAACCAGAAGATTGTCAATGGCTGGCAGGTAGAGGAGGCC
GATGACTGGCTGCGCTACGGCAACCCCTGGGAGAAAGCGCGGCCTGAGTATATGCTTCCC
GTGCACTTCTACGGACGCGTGGAGCACACCCCCGACGGCGTGAAGTGGCTGGACACACAG
GTGGTGCTGGCCATGCCCTACGACACCCCAGTGCCCGGCTACAAGAACAACACCGTCAAC
ACCATGCGGCTGTGGTCCGCAAGGGCTCCCAACGACTTCAAGCTGCAGGACTTCAACGTG
GGAGACTACATCGAGGCGGTCCTGGACCGGAACTTGGCTGAGAACATCTCCAGGGTCCTG
TATCCAAATGATAACTTCTTTGAGGGGAAGGAGCTGCGGCTGAAGCAGGAGTACTTCGTG
GTGGGCGCCACGCTCCAGGACATCATCCGCCGCTTCAAGTCGTCCAAGTTCGGCTGCCGG
GACCCTGTGAGAACCTGTTTCGAGACGTTCCCAGACAAGGTGGCCATCCAGCTGAACGAC
ACCCACCCCGCCCTCTCCATCCCTGAGCTCATGCGGATCCTGGTGGACGTGGAGAAGGTG
GACTGGGACAAGGCCTGGGAAATCACGAAGAAGACCTGTGCATACACCAACCACACTGTG
CTGCCTGAGGCCTTGGAGCGCTGGCCCGTGTCCATGTTTGAGAAGCTGCTGCCGCGGCAC
CTGGAGATAATCTATGCCATCAACCAGCGGCACCTGGACCACGTGGCCGCGCTGTTTCCC
GGCGATGTGGACCGCCTGCGCAGGATGTCTGTGATCGAGGAGGGGGACTGCAAGCGGATC
AACATGGCCCACCTGTGTGTGATTGGGTCCCATGCTGTCAATGGTGTGGCGAGGATCCAC
TCGGAGATCGTGAAACAGTCGGTCTTTAAGGATTTTTATGAACTGGAGCCAGAGAAGTTC
CAGAATAAGACCAATGGCATCACCCCCCGCCGGTGGCTGCTGCTGTGCAACCCGGGGCTG
GCCGATACCATCGTGGAGAAAATTGGGGAGGAGTTCCTGACTGACCTGAGCCAGCTGAAG
AAGCTGCTGCCGCTGGTCAGTGACGAGGTGTTCATCAGGGACGTGGCCAAGGTCAAACAG
GAGAACAAGCTCAAGTTCTCGGCCTTCCTGGAGAAGGAGTACAAGGTGAAGATCAACCCC
TCCTCCATGTTCGATGTGCATGTGAAGAGGATCCACGAGTACAAGCGGCAGCTGCTCAAC
TGCCTGCACGTCGTCACCCTGTACAATCGAATCAAGAGAGACCCGGCCAAGGCTTTTGTG
CCCAGGACTGTTATGATTGGGGGCAAGGCAGCGCCCGGTTACCACATGGCCAAGCTGATC
ATCAAGTTGGTCACCTCCATCGGCGACGTCGTCAATCATGACCCAGTTGTGGGTGACAGG
TTGAAAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGATCCCGGCC
GCTGATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGGCAACATG
AAGTTCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGTGGAGATG
GCCGAGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGATGTCGAG
GCCTTGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGAGCTGAAG
CAGGCCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTGCTTCAAG
GACATCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTATGAAGCC
TACATGCAGTGCCAGGCACAGGTGGACCAGCTGTACCGGAACCCCAAGGAGTGGACCAAG
AAGGTCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCATCACGGAG
TATGCACGGGAGATCTGGGGTGTGGAGCCCTCCGACCTGCAGCTTCAGCACCTGCCCCAC
CCAGAGTGGGAGTCAGGTGGAGCCACCTGCTGGGCTCCCCCAGAACTTTGCACACATCTT
GCTATGTATTAG
Enzyme 2 GenBank Gene ID J03544 Link Image
Enzyme 2 GeneCard ID PYGB Link Image
Enzyme 2 GenAtlas ID PYGB Link Image
Enzyme 2 HGNC ID HGNC:9723 Link Image
Enzyme 2 Chromosome Location 20
Enzyme 2 Locus 20p11.2-p11.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Newgard CB, Littman DR, van Genderen C, Smith M, Fletterick RJ: Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes. J Biol Chem. 1988 Mar 15;263(8):3850-7. [PubMed Link Image]
  2. Gelinas RP, Froman BE, McElroy F, Tait RC, Gorin FA: Human brain glycogen phosphorylase: characterization of fetal cDNA and genomic sequences. Brain Res Mol Brain Res. 1989 Nov;6(2-3):177-85. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6384
Enzyme 3 Name Glycogenin-2
Enzyme 3 Synonyms
  1. GN-2
  2. GN2
Enzyme 3 Gene Name GYG2
Enzyme 3 Protein Sequence >Glycogenin-2 
MSETEFHHGAQAGLELLRSSNSPTSASQSAGMTVTDQAFVTLATNDIYCQGALVLGQSLR
RHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLAFLKRPELGLTLTKL
HCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPDPGWPDCFNSGVFVFQPSLHTHK
LLLQHAMEHGSFDGADQGLLNSFFRNWSTTDIHKHLPFIYNLSSNTMYTYSPAFKQFGSS
AKVVHFLGSMKPWNYKYNPQSGSVLEQGSASSSQHQAAFLHLWWTVYQNNVLPLYKSVQA
GEARASPGHTLCHSDVGGPCADSASGVGEPCENSTPSAGVPCANSPLGSNQPAQGLPEPT
QIVDETLSLPEGRRSEDMIACPETETPAVITCDPLSQPSPQPADFTETETILQPANKVES
VSSEETFEPSQELPAEALRDPSLQDALEVDLAVSVSQISIEEKVKELSPEEERRKWEEGR
IDYMGKDAFARIQEKLDRFLQ
Enzyme 3 Number of Residues 501
Enzyme 3 Molecular Weight 55184
Enzyme 3 Theoretical pI 4.74
Enzyme 3 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • UDP-glucose + glycogenin = UDP + glucosylglycogenin
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2618766 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O15488 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GLYG2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1506 bp 
ATGTCGGAGACAGAGTTTCACCATGGTGCCCAGGCTGGTCTCGAACTCCTGAGGTCAAGC
AATTCACCCACCTCAGCCTCCCAAAGTGCTGGAATGACAGTGACTGATCAGGCTTTTGTC
ACACTAGCCACCAATGACATCTACTGCCAGGGCGCCCTGGTCCTGGGGCAGTCACTGAGG
AGACACAGGCTGACGAGGAAGCTGGTGGTGTTGATCACTCCTCAGGTGTCCAGCCTGCTC
AGGGTCATCCTCTCGAAGGTGTTCGATGAAGTCATTGAAGTGAATCTAATCGATAGTGCC
GACTACATCCACCTGGCCTTTCTGAAGAGACCTGAGCTCGGGCTCACCCTCACCAAGCTT
CACTGTTGGACTCTCACTCACTACAGCAAGTGTGTCTTCCTGGATGCAGACACTCTGGTG
CTGTCCAATGTCGATGAGCTGTTTGACAGGGGAGAGTTTTCTGCGGCCCCGGACCCCGGA
TGGCCGGATTGCTTCAATAGCGGGGTGTTTGTCTTCCAGCCTTCTCTCCACACGCATAAA
CTCCTGCTACAGCACGCCATGGAACACGGCAGCTTTGACGGGGCAGACCAAGGCTTACTG
AATAGTTTCTTCAGGAACTGGTCGACCACAGACATCCACAAGCACCTGCCGTTCATCTAT
AACTTGAGTAGTAACACGATGTACACTTACAGCCCTGCCTTCAAGCAATTCGGTTCCAGT
GCAAAGGTCGTCCACTTTTTGGGGTCCATGAAACCTTGGAACTACAAGTACAATCCACAG
AGTGGCTCGGTGTTGGAGCAAGGCTCAGTGTCCAGCAGCCAGCACCAGGCGGCATTCCTT
CATCTCTGGTGGACGGTCTACCAGAACAACGTGCTGCCCCTTTATAAAAGCGTCCAAGCG
GGGGAAGCACGCGCGTCTCCTGGTCACACACTTTGCCACAGTGATGTGGGGGGGCCGTGT
GCGGATTCAGCCTCTGGTGTTGGAGAGCCGTGTGAAAATTCAACACCCAGTGCGGGCGTG
CCGTGTGCAAATTCACCACTGGGTTCTAACCAGCCTGCTCAGGGCCTTCCGGAGCCGACC
CAGATAGTGGATGAGACCCTGTCCCTACCTGAAGGACGCCGTTCAGAAGATATGATAGCT
TGTCCTGAAACTGAGACTCCTGCCGTGATAACGTGTGACCCACTGTCCCAGCCTTCCCCT
CAGCCTGCAGACTTCACAGAGACTGAAACCATCTTGCAGCCAGCAAATAAAGTCGAAAGT
GTCTCATCCGAGGAAACCTTCGAACCAAGCCAGGAACTCCCTGCTGAGGCTCTCAGGGAC
CCCAGTCTGCAGGATGCACTGGAGGTCGACCTGGCCGTCTCTGTTTCCCAGATCTCCATC
GAAGAGAAGGTGAAGGAATTGAGCCCCGAGGAAGAGAGGAGGAAGTGGGAGGAAGGCCGT
ATCGACTACATGGGGAAGGACGCGTTTGCTCGCATCCAGGAGAAGCTGGACCGGTTCCTG
CAGTAA
Enzyme 3 GenBank Gene ID U94362 Link Image
Enzyme 3 GeneCard ID GYG2 Link Image
Enzyme 3 GenAtlas ID GYG2 Link Image
Enzyme 3 HGNC ID HGNC:4700 Link Image
Enzyme 3 Chromosome Location X
Enzyme 3 Locus Xp22.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Mu J, Skurat AV, Roach PJ: Glycogenin-2, a novel self-glucosylating protein involved in liver glycogen biosynthesis. J Biol Chem. 1997 Oct 31;272(44):27589-97. [PubMed Link Image]
  2. Zhai L, Mu J, Zong H, DePaoli-Roach AA, Roach PJ: Structure and chromosomal localization of the human glycogenin-2 gene GYG2. Gene. 2000 Jan 25;242(1-2):229-35. [PubMed Link Image]
  3. Mu J, Roach PJ: Characterization of human glycogenin-2, a self-glucosylating initiator of liver glycogen metabolism. J Biol Chem. 1998 Dec 25;273(52):34850-6. [PubMed Link Image]
  4. Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ: Cluster analysis of an extensive human breast cancer cell line protein expression map database. Proteomics. 2002 Feb;2(2):212-23. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 7128
Enzyme 4 Name Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Enzyme 4 Synonyms
  1. PP-1B
Enzyme 4 Gene Name PPP1CB
Enzyme 4 Protein Sequence >Serine/threonine-protein phosphatase PP1-beta catalytic subunit 
MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKI
CGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL
RGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ
SMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDL
DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEK
KAKYQYGGLNSGRPVTPPRTANPPKKR
Enzyme 4 Number of Residues 327
Enzyme 4 Molecular Weight 37187
Enzyme 4 Theoretical pI 6.06
Enzyme 4 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 4 General Function Signal transduction mechanisms
Enzyme 4 Specific Function Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • A phosphoprotein + H2O = a protein + phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 531476 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P62140 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PP1B_HUMAN Link Image
Enzyme 4 PDB ID 1S70 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >984 bp 
ATGGCGGACGGGGAGCTGAACGTGGACAGCCTCATCACCCGGCTGCTGGAGGTACGAGGA
TGTCGTCCAGGAAAGATTGTGCAGATGACTGAAGCAGAAGTTCGAGGCTTATGTATCAAG
TCTCGGGAGATCTTTCTCAGCCAGCCTATTCTTTTGGAATTGGAAGCACCGCTGAAAATT
TGTGGAGATATTCATGGACAATATACAGATTTACTGAGATTATTTGAATATGGAGGTTTC
CCACCAGAAGCCAACTATCTTTTCTTAGGAGATTATGTGGACAGAGGAAAGCAGTCTTTG
GAAACCATTTGTTTGCTATTGGCTTATAAAATCAAATATCCAGAGAACTTCTTTCTCTTA
AGAGGAAACCATGAGTGTGCTAGCATCAATCGCATTTATGGATTCTATGATGAATGCAAA
CGAAGATTTAATATTAAATTGTGGAAGACCTTCACTGATTGTTTTAACTGTCTGCCTATA
GCAGCCATTGTGGATGAGAAGATCTTCTGTTGTCATGGAGGATTGTCACCAGACCTGCAA
TCTATGGAGCAGATTCGGAGAATTATGAGACCTACTGATGTCCCTGATACAGGTTTGCTC
TGTGATTTGCTATGGTCTGATCCAGATAAGGATGTGCAAGGCTGGGGAGAAAATGATCGT
GGTGTTTCCTTTACTTTTGGAGCTGATGTAGTCAGTAAATTTCTGAATCGTCATGATTTA
GATTTGATTTGTCGAGCTCATCAGGTGGTGGAAGATGGATATGAATTTTTTGCTAAACGA
CAGTTGGTAACCTTATTTTCAGCCCCAAATTACTGTGGCGAGTTTGATAATGCTGGTGGA
ATGATGAGTGTGGATGAAACTTTGATGTGTTCATTTCAGATATTGAAACCATCTGAAAAG
AAAGCTAAATACCAGTATGGTGGACTGAATTCTGGACGTCCTGTCACTCCACCTCGAACA
GCTAATCCGCCGAAGAAAAGGTGA
Enzyme 4 GenBank Gene ID X80910 Link Image
Enzyme 4 GeneCard ID PPP1CB Link Image
Enzyme 4 GenAtlas ID PPP1CB Link Image
Enzyme 4 HGNC ID HGNC:9282 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 2p23
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Barker HM, Brewis ND, Street AJ, Spurr NK, Cohen PT: Three genes for protein phosphatase 1 map to different human chromosomes: sequence, expression and gene localisation of protein serine/threonine phosphatase 1 beta (PPP1CB). Biochim Biophys Acta. 1994 Jan 13;1220(2):212-8. [PubMed Link Image]
  2. Prochazka M, Mochizuki H, Baier LJ, Cohen PT, Bogardus C: Molecular and linkage analysis of type-1 protein phosphatase catalytic beta-subunit gene: lack of evidence for its major role in insulin resistance in Pima Indians. Diabetologia. 1995 Apr;38(4):461-6. [PubMed Link Image]
  3. 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]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 7291
Enzyme 5 Name Laforin
Enzyme 5 Synonyms
  1. Lafora PTPase
  2. LAFPTPase
Enzyme 5 Gene Name EPM2A
Enzyme 5 Protein Sequence >Laforin 
MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLW
LGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDG
VYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKL
KHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYREEGLAYIWMPTPDMSTEG
RVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKR
PAVYIDEEALARAQEDFFQKFGKVRSSVCSL
Enzyme 5 Number of Residues 331
Enzyme 5 Molecular Weight 37158
Enzyme 5 Theoretical pI 6.64
Enzyme 5 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoprotein phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
  • protein tyrosine/serine/threonine phosphatase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid dephosphorylation
  • protein modification
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Dual specificity protein phosphatase. May be involved in the control of glycogen metabolism, particularly in monitoring for and preventing the formation of poorly branched glycogen molecules (polyglucosans)
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-15
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 6005986 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O95278 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name EPM2A_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >996 bp 
ATGCGCTTCCGCTTTGGGGTGGTGGTGCCACCCGCCGTGGCCGGCGCCCGGCCGGAGCTG
CTGGTGGTGGGGTCGCGGCCCGAGCTGGGGCGTTGGGAGCCGCGCGGTGCCGTCCGCCTG
AGGCCGGCCGGCACCGCGGCGGGCGACGGGGCCCTGGCGCTGCAGGAGCCGGGCCTGTGG
CTCGGGGAGGTGGAGCTGGCGGCCGAGGAGGCGGCGCAGGACGGGGCGGAGCCGGGCCGC
GTGGACACGTTCTGGTACAAGTTCCTGAAGCGGGAGCCGGGAGGAGAGCTCTCCTGGGAA
GGCAATGGACCTCATCATGACCGTTGCTGTACTTACAATGAAAACAACTTGGTGGATGGT
GTGTATTGTCTCCCAATAGGACACTGGATTGAGGCCACTGGGCACACCAATGAAATGAAG
CACACAACAGACTTCTATTTTAATATTGCAGGCCACCAAGCCATGCATTATTCAAGAATT
CTACCAAATATCTGGCTGGGTAGCTGCCCTCGTCAGGTGGAACATGTAACCATCAAACTG
AAGCATGAATTGGGGATTACAGCTGTAATGAATTTCCAGACTGAATGGGATATTGTACAG
AATTCCTCAGGCTGTAACCGCTACCCAGAGCCCATGACTCCAGACACTATGATTAAACTA
TATAGGGAAGAAGGCTTGGCCTACATCTGGATGCCAACACCAGATATGAGCACCGAAGGC
CGAGTACAGATGCTGCCCCAGGCGGTGTGCCTGCTGCATGCGCTGCTGGAGAAGGGACAC
ATCGTGTACGTGCACTGCAACGCTGGGGTGGGCCGCTCCACCGCGGCTGTCTGCGGCTGG
CTCCAGTATGTGATGGGCTGGAATCTGAGGAAGGTGCAGTATTTCCTCATGGCCAAGAGG
CCGGCTGTCTACATTGACGAAGAGGCCTTGGCCCGGGCACAAGAAGATTTTTTCCAGAAA
TTTGGGAAGGTTCGTTCTTCTGTGTGTAGCCTGTAG
Enzyme 5 GenBank Gene ID AF084535 Link Image
Enzyme 5 GeneCard ID EPM2A Link Image
Enzyme 5 GenAtlas ID EPM2A Link Image
Enzyme 5 HGNC ID HGNC:3413 Link Image
Enzyme 5 Chromosome Location 6
Enzyme 5 Locus 6q24
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Minassian BA, Lee JR, Herbrick JA, Huizenga J, Soder S, Mungall AJ, Dunham I, Gardner R, Fong CY, Carpenter S, Jardim L, Satishchandra P, Andermann E, Snead OC 3rd, Lopes-Cendes I, Tsui LC, Delgado-Escueta AV, Rouleau GA, Scherer SW: Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat Genet. 1998 Oct;20(2):171-4. [PubMed Link Image]
  2. Ganesh S, Agarwala KL, Ueda K, Akagi T, Shoda K, Usui T, Hashikawa T, Osada H, Delgado-Escueta AV, Yamakawa K: Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes. Hum Mol Genet. 2000 Sep 22;9(15):2251-61. [PubMed Link Image]
  3. Serratosa JM, Gomez-Garre P, Gallardo ME, Anta B, de Bernabe DB, Lindhout D, Augustijn PB, Tassinari CA, Malafosse RM, Topcu M, Grid D, Dravet C, Berkovic SF, de Cordoba SR: A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2). Hum Mol Genet. 1999 Feb;8(2):345-52. [PubMed Link Image]
  4. Ganesh S, Suzuki T, Yamakawa K: Alternative splicing modulates subcellular localization of laforin. Biochem Biophys Res Commun. 2002 Mar 15;291(5):1134-7. [PubMed Link Image]
  5. Wang J, Stuckey JA, Wishart MJ, Dixon JE: A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen. J Biol Chem. 2002 Jan 25;277(4):2377-80. Epub 2001 Dec 5. [PubMed Link Image]
  6. Ianzano L, Zhao XC, Minassian BA, Scherer SW: Identification of a novel protein interacting with laforin, the EPM2a progressive myoclonus epilepsy gene product. Genomics. 2003 Jun;81(6):579-87. [PubMed Link Image]
  7. Fernandez-Sanchez ME, Criado-Garcia O, Heath KE, Garcia-Fojeda B, Medrano-Fernandez I, Gomez-Garre P, Sanz P, Serratosa JM, Rodriguez de Cordoba S: Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. Hum Mol Genet. 2003 Dec 1;12(23):3161-71. Epub 2003 Oct 7. [PubMed Link Image]
  8. Gomez-Garre P, Sanz Y, Rodriguez De Cordoba SR, Serratosa JM: Mutational spectrum of the EPM2A gene in progressive myoclonus epilepsy of Lafora: high degree of allelic heterogeneity and prevalence of deletions. Eur J Hum Genet. 2000 Dec;8(12):946-54. [PubMed Link Image]
  9. Ganesh S, Shoda K, Amano K, Uchiyama A, Kumada S, Moriyama N, Hirose S, Yamakawa K: Mutation screening for Japanese Lafora's disease patients: identification of novel sequence variants in the coding and upstream regulatory regions of EPM2A gene. Mol Cell Probes. 2001 Oct;15(5):281-9. [PubMed Link Image]
  10. Ganesh S, Delgado-Escueta AV, Suzuki T, Francheschetti S, Riggio C, Avanzini G, Rabinowicz A, Bohlega S, Bailey J, Alonso ME, Rasmussen A, Thomson AE, Ochoa A, Prado AJ, Medina MT, Yamakawa K: Genotype-phenotype correlations for EPM2A mutations in Lafora's progressive myoclonus epilepsy: exon 1 mutations associate with an early-onset cognitive deficit subphenotype. Hum Mol Genet. 2002 May 15;11(11):1263-71. [PubMed Link Image]
  11. Ki CS, Kong SY, Seo DW, Hong SB, Kim HJ, Kim JW: Two novel mutations in the EPM2A gene in a Korean patient with Lafora's progressive myoclonus epilepsy. J Hum Genet. 2003;48(1):51-4. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 7293
Enzyme 6 Name Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Enzyme 6 Synonyms
  1. PP-1G
  2. Protein phosphatase 1C catalytic subunit
Enzyme 6 Gene Name PPP1CC
Enzyme 6 Protein Sequence >Serine/threonine-protein phosphatase PP1-gamma catalytic subunit 
MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE
KKKPNATRPVTPPRGMITKQAKK
Enzyme 6 Number of Residues 323
Enzyme 6 Molecular Weight 36984
Enzyme 6 Theoretical pI 6.50
Enzyme 6 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 6 General Function Signal transduction mechanisms
Enzyme 6 Specific Function Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • A phosphoprotein + H2O = a protein + phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 402778 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P36873 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PP1G_HUMAN Link Image
Enzyme 6 PDB ID 1IT6 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >972 bp 
ATGGCGGATTTAGATAAACTCAACATCGACAGCATTATCCAACGGCTGCTGGAAGTGAGA
GGGTCCAAGCCTGGTAAGAATGTCCAGCTTCAGGAGAATGAAATCAGAGGACTGTGCTTA
AAGTCTCGTGAAATCTTTCTCAGTCAGCCTATCCTACTAGAACTTGAAGCACCACTCAAA
ATATGTGGTGACATCCATGGACAATACTATGATTTGCTGCGACTTTTTGAGTACGGTGGT
TTCCCACCAGAAAGCAACTACCTGTTTCTTGGGGACTATGTGGACAGGGGAAAGCAGTCA
TTGGAGACGATCTGCCTCTTACTGGCCTACAAAATAAAATATCCTGAGAATTTTTTTCTT
CTCAGAGGGAACCATGAATGTGCCAGCATCAACAGAATTTATGGATTTTATGATGAATGT
AAAAGAAGATACAACATTAAACTATGGAAAACTTTCACAGACTGTTTTAACTGTTTACCG
ATAGCAGCCATCGTGGATGAGAAGATATTCTGCTGTCATGGAGGTTTATCACCAGATCTT
CAATCTATGGAGCAGATTCGGCGAATTATGCGACCAACTGATGTACCAGATCAAGGTCTT
CTTTGTGATCTTTTGTGGTCTGACCCCGATAAAGATGTCTTAGGCTGGGGTGAAAATGAC
AGAGGAGTGTCCTTCACATTTGGTGCAGAAGTGGTTGCAAAATTTCTCCATAAGCATGAT
TTGGATCTTATATGTAGAGCCCATCAGGTGGTTGAAGATGGATATGAATTTTTTGCAAAG
AGGCAGTTGGTCACTCTGTTTTCTGCGCCCAATTATTGCGGAGAGTTTGACAATGCAGGT
GCCATGATGAGTGTGGATGAAACACTAATGTGTTCTTTTCAGATTTTAAAGCCTGCAGAG
AAAAAGAAGCCAAATGCCACGAGACCTGTAACGCCTCCAAGGGGTATGATCACAAAGCAA
GCAAAGAAATAG
Enzyme 6 GenBank Gene ID X74008 Link Image
Enzyme 6 GeneCard ID PPP1CC Link Image
Enzyme 6 GenAtlas ID PPP1CC Link Image
Enzyme 6 HGNC ID HGNC:9283 Link Image
Enzyme 6 Chromosome Location 12
Enzyme 6 Locus 12q24.1-q24.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Barker HM, Craig SP, Spurr NK, Cohen PT: Sequence of human protein serine/threonine phosphatase 1 gamma and localization of the gene (PPP1CC) encoding it to chromosome bands 12q24.1-q24.2. Biochim Biophys Acta. 1993 Aug 18;1178(2):228-33. [PubMed Link Image]
  2. Norman SA, Mott DM: Molecular cloning and chromosomal localization of a human skeletal muscle PP-1 gamma 1 cDNA. Mamm Genome. 1994 Jan;5(1):41-5. [PubMed Link Image]
  3. Armstrong CG, Browne GJ, Cohen P, Cohen PT: PPP1R6, a novel member of the family of glycogen-targetting subunits of protein phosphatase 1. FEBS Lett. 1997 Nov 24;418(1-2):210-4. [PubMed Link Image]
  4. Egloff MP, Cohen PT, Reinemer P, Barford D: Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J Mol Biol. 1995 Dec 15;254(5):942-59. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 7564
Enzyme 7 Name Salivary alpha-amylase precursor
Enzyme 7 Synonyms
  1. 1,4-alpha-D-glucan glucanohydrolase
Enzyme 7 Gene Name AMY1A
Enzyme 7 Protein Sequence >Salivary alpha-amylase precursor 
MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP
NENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN
AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGL
LDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEG
SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG
FMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP
RYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQP
FTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGI
KIYVSDDGKAHFSISNSAEDPFIAIHAESKL
Enzyme 7 Number of Residues 511
Enzyme 7 Molecular Weight 57768
Enzyme 7 Theoretical pI 6.92
Enzyme 7 GO Classification
Function
  • alpha-amylase activity
  • amylase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Carbohydrate transport and metabolism
Enzyme 7 Specific Function Endohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides
Enzyme 7 Pathways
Enzyme 7 Reactions
  • Endohydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides containing three or more 1,4-alpha-linked D-glucose units
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-15
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 178585 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P04745 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name AMYS_HUMAN Link Image
Enzyme 7 PDB ID 1MFV Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1536 bp 
ATGAAGCTCTTTTGGTTGCTTTTCACCATTGGGTTCTGCTGGGCTCAGTATTCCTCAAAT
ACACAACAAGGACGAACATCTATTGTTCATCTGTTTGAATGGCGATGGGTTGATATTGCT
CTTGAATGTGAGCGATATTTAGCTCCCAAGGGATTTGGAGGGGTTCAGGTCTCTCCACCA
AATGAAAATGTTGCCATTCACAACCCTTTCAGACCTTGGTGGGAAAGATACCAACCAGTT
AGCTATAAATTATGCACAAGATCTGGAAATGAAGATGAATTTAGAAACATGGTGACTAGA
TGCAACAATGTTGGGGTTCGTATTTATGTGGATGCTGTAATTAATCATATGTGTGGTAAT
GCTGTGAGTGCAGGAACAAGCAGTACCTGTGGAAGTTACTTCAACCCTGGAAGTAGGGAC
TTTCCAGCAGTCCCATATTCTGGATGGGATTTTAATGATGGTAAATGTAAAACTGGAAGT
GGAGATATCGAGAACTATAATGATGCTACTCAGGTCAGAGATTGTCGTCTGTCTGGTCTT
CTCGATCTTGCACTGGGGAAGGATTATGTGCGTTCTAAGATTGCCGAATATATGAACCAT
CTCATTGACATTGGTGTTGCAGGGTTCAGAATTGATGCTTCCAAGCACATGTGGCCTGGA
GACATAAAGGCAATTTTGGACAAACTGCATAATCTAAACAGTAACTGGTTCCCGGAAGGT
AGTAAACCTTTCATTTACCAGGAGGTAATTGATCTGGGTGGTGAGCCAATTAAAAGCAGT
GACTACTTTGGTAATGGCCGGGTGACAGAATTCAAGTATGGTGCAAAACTCGGCACAGTT
ATTCGCAAGTGGAATGGAGAGAAGATGTCTTACTTAAAGAACTGGGGAGAAGGTTGGGGT
TTCATGCCTTCTGACAGAGCGCTTGTCTTTGTGGATAACCATGACAATCAACGAGGACAT
GGCGCTGGAGGAGCCTCTATACTTACCTTCTGGGATGCTAGGCTGTACAAAATGGCAGTT
GGATTTATGCTTGCTCATCCTTATGGATTTACACGAGTAATGTCAAGCTACCGTTGGCCA
AGATATTTTGAAAATGGAAANGATGTTAATGATTGGGTTGGGCCACCAAATGATAATGGA
GTAACTAAAGAAGTTACTATTAATCCAGACACTACTTGTGGCAATGACTGGGTCTGTGAA
CATCGATGGCGCCAAATAAGGAACATGGTTAATTTCCGCAATGTAGTGGATGGCCAGCCT
TTTACAAACTGGTATGATAATGGGAGCAACCAAGTGGCTTTTGGGAGAGGAAACAGAGGA
TTCATTGTTTTCAACAATGATGACTGGACATTTTCTTTAACTTTGCAAACTGGTCTTCCT
GCTGGCACATACTGTGATGTCATTTCTGGAGATAAAATTAATGGCAACTGCACAGGCATT
AAAATCTACGTTTCTGATGATGGCAAAGCTCATTTTTCTATTAGTAACTCTGCTGAAGAT
CCATTTATTGCAATTCATGCTGAATCTAAATTGTAA
Enzyme 7 GenBank Gene ID M18786 Link Image
Enzyme 7 GeneCard ID AMY1A Link Image
Enzyme 7 GenAtlas ID AMY1A Link Image
Enzyme 7 HGNC ID HGNC:474 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1p21
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Nishide T, Nakamura Y, Emi M, Yamamoto T, Ogawa M, Mori T, Matsubara K: Primary structure of human salivary alpha-amylase gene. Gene. 1986;41(2-3):299-304. [PubMed Link Image]
  2. Nishide T, Emi M, Nakamura Y, Matsubara K: Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected] Gene. 1984 May;28(2):263-70. [PubMed Link Image]
  3. Gumucio DL, Wiebauer K, Caldwell RM, Samuelson LC, Meisler MH: Concerted evolution of human amylase genes. Mol Cell Biol. 1988 Mar;8(3):1197-205. [PubMed Link Image]
  4. Bank RA, Hettema EH, Arwert F, Amerongen AV, Pronk JC: Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase. Electrophoresis. 1991 Jan;12(1):74-9. [PubMed Link Image]
  5. Ramasubbu N, Ragunath C, Mishra PJ: Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. J Mol Biol. 2003 Jan 31;325(5):1061-76. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 8603
Enzyme 8 Name Maltase-glucoamylase, intestinal [Includes: Maltase
Enzyme 8 Synonyms
  1. Alpha-glucosidase
  2. Glucoamylase
  3. Glucan 1,4-alpha- glucosidase]
Enzyme 8 Gene Name MGAM
Enzyme 8 Protein Sequence >Maltase-glucoamylase, intestinal [Includes: Maltase 
MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTP
DPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWN
PQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTS
NRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDS
SIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLY
GAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVV
QEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDER
RDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNS
SDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGS
VSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKT
VFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICG
FALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLL
PYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAY
VPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGL
IIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFN
EIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRD
EEKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADIS
LKSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEG
QLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHR
SYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPL
PALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIA
SLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAI
SGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYV
AFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDAS
LNHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEV
TGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFF
QDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLY
TLMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRA
RWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIAL
DDEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIE
IWGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL
Enzyme 8 Number of Residues 1857
Enzyme 8 Molecular Weight 209855
Enzyme 8 Theoretical pI 5.14
Enzyme 8 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing
Enzyme 8 Pathways
Enzyme 8 Reactions
  • Hydrolysis of terminal, non-reducing 1,4-linked alpha-D-glucose residues with release of alpha-D-glucose
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-35
Enzyme 8 Transmembrane Regions
  • 14-34
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 17648144 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O43451 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name MGA_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >5574 bp 
ATGGCAAGAAAGAAGCTGAAAAAATTTACTACTTTGGAGATTGTGCTCAGTGTTCTTCTG
CTTGTGTTGTTTATCATCAGTATTGTTCTAATTGTGCTTTTAGCCAAAGAGTCACTGAAA
TCAACAGCCCCAGATCCTGGGACAACTGGTACCCCAGATCCTGGGACAACTGGTACCCCA
GATCCTGGAACAACTGGTACCACACATGCTAGGACAACGGGTCCCCCAGATCCTGGAACA
ACTGGTACCACTCCTGTTTCTGCTGAATGTCCAGTGGTAAATGAATTGGAACGAATTAAT
TGCATCCCTGACCAGCCGCCAACAAAGGCCACATGTGACCAACGTGGCTGTTGCTGGAAT
CCCCAGGGAGCTGTAAGTGTTCCCTGGTGCTACTATTCCAAGAATCATAGCTACCATGTA
GAGGGCAACCTTGTCAACACAAATGCAGGATTCACAGCCCGGTTGAAAAATCTGCCTTCT
TCACCAGTGTTTGGAAGCAATGTTGACAATGTTCTTCTCACAGCAGAATATCAGACATCT
AATCGTTTCCACTTTAAGTTGACTGACCAAACCAATAACAGGTTTGAAGTGCCCCACGAA
CACGTGCAGTCCTTCAGTGGAAATGCTGCTGCTTCTTTGACCTACCAAGTTGAAATCTCC
AGACAGCCATTTAGCATCAAAGTGACCAGAAGAAGCAACAATCGTGTTTTGTTTGACTCG
AGCATTGGGCCCCTACTGTTTGCTGACCAGTTCTTGCAGCTCTCCACTCGACTGCCTAGC
ACTAACGTGTATGGCCTGGGAGAGCATGTGCACCAGCAGTATCGGCATGATATGAATTGG
AAGACCTGGCCCATATTTAACAGAGACACAACTCCCAATGGAAACGGAACTAATTTGTAT
GGTGCGCAGACATTCTTCTTGTGCCTTGAAGATGCTAGTGGATTGTCCTTTGGGGTGTTT
CTGATGAACAGCAATGCCATGGAGGTTGTCCTTCAGCCTGCGCCAGCCATCACTTACCGC
ACCATTGGGGGCATTCTCGACTTCTATGTGTTCTTGGGAAACACTCCAGAGCAAGTTGTT
CAAGAATATCTAGAGCTCATTGGGCGGCCAGCCCTTCCCTCCTACTGGGCGCTTGGATTT
CACCTCAGTCGTTACGAATATGGAACCTTAGACAACATGAGGGAAGTCGTGGAGAGAAAT
CGCGCAGCACAGCTCCCTTATGATGTTCAGCATGCTGATATTGATTATATGGATGAGAGA
AGGGACTTCACTTATGATTCAGTGGATTTTAAAGGCTTCCCTGAATTTGTCAACGAGTTA
CACAATAATGGACAGAAGCTTGTCATCATTGTGGATCCAGCCATCTCCAACAACTCTTCC
TCAAGTAAACCCTATGGCCCATATGACAGGGGTTCAGATATGAAGATATGGGTGAATAGT
TCAGATGGAGTGACTCCACTCATTGGGGAGGTCTGGCCTGGACAAACTGTGTTTCCTGAT
TATACCAATCCCAACTGTGCTGTTTGGTGGACAAAGGAATTTGAGCTTTTTCACAATCAA
GTAGAGTTTGATGGAATCTGGATTGATATGAATGAAGTCTCCAACTTTGTTGATGGTTCG
GTCTCAGGATGTTCCACAAACAACCTAAATAATCCCCCATTCACTCCCAGAATCCTGGAT
GGGTACCTGTTCTGCAAGACTCTCTGTATGGATGCAGTGCAGCACTGGGGCAAGCAGTAT
GACATTCACAATCTGTATGGCTACTCCATGGCGGTCGCCACAGCAGAAGCTGCCAAGACT
GTGTTCCCTAATAAGAGAAGCTTCATTCTGACCCGTTCTACCTTTGCGGGCTCTGGCAAG
TTTGCAGCACATTGGTTAGGAGACAACACTGCCACCTGGGATGACCTGAGATGGTCCATC
CCTGGCGTGCTTGAGTTCAACCTTTTTGGCATCCCAATGGTGGGTCCTGACATATGTGGC
TTTGCTTTGGACACCCCTGAGGAGCTCTGTAGGCGGTGGATGCAGTTGGGTGCATTTTAT
CCGTTTTCTAGAAATCACAATGGCCAAGGCTACAAGGACCAGGATCCTGCCTCCTTTGGA
GCTGACTCCCTGCTGTTGAATTCCTCCAGGCACTACCTTAACATCCGCTATACTCTATTG
CCCTACCTATACACCCTTTTCTTCCGTGCTCACAGCCGAGGGGACACGGTGGCCAGGCCC
CTTTTGCATGAGTTCTACGAGGACAACAGCACTTGGGATGTGCACCAACAGTTCTTATGG
GGGCCCGGCCTCCTCATCACTCCAGTTCTGGATGAAGGTGCAGAGAAAGTGATGGCATAT
GTGCCTGATGCTGTCTGGTATGACTACGAGACTGGGAGCCAAGTGAGATGGAGGAAGCAA
AAAGTCGAGATGGAACTTCCTGGAGACAAAATTGGACTTCACCTTCGAGGAGGCTACATC
TTCCCCACACAGCAGCCAAATACAACCACTCTGGCCAGTCGAAAGAACCCTCTTGGTCTT
ATCATTGCCCTAGATGAGAACAAAGAAGCAAAAGGAGAACTTTTCTGGGATGATGGGGAA
ACGAAGGATACTGTGGCCAATAAAGTGTATCTTTTATGTGAGTTTTCTGTCACTCAAAAC
CGCTTGGAGGTGAATATTTCACAATCAACCTACAAGGACCCCAATAATTTAGCATTTAAT
GAGATTAAAATTCTTGGGACGGAGGAACCTAGCAATGTTACAGTGAAACACAATGGTGTC
CCAAGTCAGACTTCTCCTACAGTCACTTATGATTCTAACCTGAAGGTTGCCATTATCACA
GATATTGATCTTCTCCTGGGAGAAGCATACACAGTGGAATGGAGCATAAAGATAAGGGAT
GAAGAAAAAATAGACTGTTACCCTGATGAGAATGGTGCTTCTGCCGAAAACTGCACTGCC
CGTGGCTGTATCTGGGAGGCATCCAATTCTTCTGGAGTCCCTTTTTGCTATTTTGTCAAC
GACCTATACTCTGTCAGTGATGTTCAGTATAATTCCCATGGGGCCACAGCTGACATCTCC
TTAAAGTCTTCCGTTTATGCCAATGCCTTCCCCTCCACACCCGTGAACCCCCTTCGCCTG
GATGTCACTTACCATAAGAATGAAATGCTGCAGTTCAAGATTTATGATCCCAACAAGAAT
CGGTATGAAGTTCCAGTCCCTCTGAACATACCCAGCATGCCATCCAGCACCCCTGAGGGT
CAACTCTATGATGTGCTCATTAAGAAGAATCCATTTGGGATTGAAATTCGCCGGAAGAGT
ACAGGCACTATAATTTGGGACTCTCAGCTCCTTGGCTTTACCTTCAGTGACATGTTTATC
CGCATCTCCACCCGCCTTCCCTCCAAGTACCTCTATGGCTTTGGGGAAACTGAGCACAGG
TCCTATAGGAGAGACTTGGAGTGGCACACTTGGGGGATGTTCTCCCGAGACCAGCCCCCA
GGGTACAAGAAGAATTCCTATGGTGTCCACCCCTACTACATGGGGCTGGAGGAGGACGGC
AGTGCCCATGGAGTGCTCCTGCTGAACAGCAATGCCATGGATGTGACGTTCCAGCCCCTG
CCTGCCTTGACATACCGCACCACAGGGGGAGTTCTGGACTTTTATGTGTTCTTGGGGCCG
ACTCCAGAGCTTGTCACCCAGCAGTACACTGAGTTGATTGGCCGGCCTGTGATGGTACCT
TACTGGTCTTTGGGGTTCCAGCTGTGTCGCTATGGCTACCAGAATGACTCTGAGATCGCC
AGCTTGTATGATGAGATGGTGGCTGCCCAGATCCCTTATGATGTGCAGTACTCAGACATC
GACTACATGGAGCGGCAGCTGGACTTCACCCTCAGCCCCAAGTTTGCTGGGTTTCCAGCT
CTGATCAATCGCATGAAGGCTGATGGGATGCGGGTCATCCTCATTCTGGATCCAGCCATT
TCTGGCAATGAGACACAGCCTTATCCTGCCTTCACTCGGGGCGTGGAGGATGACGTCTTC
ATCAAATACCCAAATGATGGAGACATTGTCTGGGGAAAGGTCTGGCCTGATTTTCCTGAT
GTTGTTGTGAATGGGTCTCTAGACTGGGACAGCCAAGTGGAGCTATATCGAGCTTATGTG
GCCTTCCCAGACTTTTTCCGTAATTCAACTGCCAAGTGGTGGAAGAGGGAAATAGAAGAA
CTATACAACAATCCACAGAATCCAGAGAGGAGCTTGAAGTTTGATGGCATGTGGATTGAT
ATGAATGAACCATCAAGCTTCGTGAATGGGGCAGTTTCTCCAGGCTGCAGGGACGCCTCT
CTGAACCACCCTCCCTACATGCCACATTTGGAGTCCAGGGACAGGGGCCTGAGCAGCAAG
ACCCTTTGTATGGAGAGTCAGCAGATCCTCCCAGACGGCTCCCTGGTGCAGCACTACAAC
GTGCACAACCTGTATGGGTGGTCCCAGACCAGACCCACATACGAAGCCGTGCAGGAGGTG
ACGGGACAGCGAGGGGTCGTCATCACCCGCTCCACATTTCCCTCTTCTGGCCGCTGGGCA
GGACATTGGCTGGGAGACAACACGGCCGCATGGGATCAGCTGAAGAAGTCTATCATTGGC
ATGATGGAGTTCAGCCTCTTCGGCATATCCTATACGGGAGCAGATATCTGTGGGTTCTTT
CAAGATGCTGAATATGAGATGTGTGTTCGCTGGATGCAGCTGGGGGCCTTTTACCCCTTC
TCAAGAAACCACAACACCATTGGGACCAGGAGACAAGACCCTGTGTCCTGGGATGTTGCT
TTTGTGAATATTTCCAGAACTGTCCTGCAGACCAGATACACCCTGTTGCCATATCTGTAT
ACCTTGATGCATAAGGCCCACACGGAGGGCGTCACTGTTGTGCGGCCTCTGCTCCATGAA
TTTGTGTCAGACCAGGTGACATGGGACATAGACAGTCAGTTCCTGCTGGGCCCAGCCTTC
CTGGTCAGCCCTGTCCTGGAGCGTAATGCCAGAAATGTCACTGCATATTTCCCTAGAGCC
CGCTGGTATGATTACTACACGGGTGTGGATATTAATGCAAGAGGAGAGTGGAAGACCTTG
CCAGCCCCTCTTGACCACATTAATCTTCATGTCCGTGGGGGCTACATCCTGCCCTGGCAA
GAGCCTGCACTGAACACCCACTTAAGCCGCCAGAAATTCATGGGCTTCAAAATTGCCTTG
GATGATGAAGGAACTGCTGGGGGCTGGCTCTTCTGGGATGATGGGCAAAGCATTGATACC
TATGGGAAAGGACTCTATTACTTGGCCAGCTTTTCTGCCAGCCAGAATACGATGCAAAGC
CATATAATTTTCAACAATTACATCACTGGTACAAATCCTTTGAAACTGGGCTACATTGAA
ATCTGGGGAGTGGGCAGTGTCCCCGTTACCAGTGTCAGCATCTCTGTGAGTGGCATGGTC
ATAACACCCTCCTTCAACAATGACCCCACGACACAGGTATTAAGCATCGATGTGACTGAC
AGAAACATCAGCCTACATAATTTTACTTCATTGACGTGGATAAGCACTCTGTGA
Enzyme 8 GenBank Gene ID AF016833 Link Image
Enzyme 8 GeneCard ID MGAM Link Image
Enzyme 8 GenAtlas ID MGAM Link Image
Enzyme 8 HGNC ID HGNC:7043 Link Image
Enzyme 8 Chromosome Location 7
Enzyme 8 Locus 7q34
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E: Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. J Biol Chem. 1998 Jan 30;273(5):3076-81. [PubMed Link Image]
  2. Naim HY, Sterchi EE, Lentze MJ: Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase. J Biol Chem. 1988 Dec 25;263(36):19709-17. [PubMed Link Image]
  3. Danielsen EM: Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte. EMBO J. 1987 Oct;6(10):2891-6. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 13111
Enzyme 9 Name Glucan , branching enzyme 1 variant
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name Not Available
Enzyme 9 Protein Sequence >Glucan , branching enzyme 1 variant 
RAPDRRGSPRLASTRLGALRLRPSRRVPARAPAPAQAPLDPLGPRLLGLRRNMAAPMTPA
ARPEDYEAALNAALADVPELARLLEIDPYLKPYAVDFQRRYKQFSQILKNIGENEGGIDK
FSRGYESFGVHRCADGGLYCKEWAPGAEGVFLTGDFNGWNPFSYPYKKLDYGKWELYIPP
KQNKSVLVPHGSKLKVVITSKSGEILYRISPWAKYVVREGDNVNYDWIHWDPEHSYEFKH
SRPKKPRSLRIYESHVGISSHEGKVASYKHFTCNVLPRIKGLGYNCIQLMAIMEHAYYAS
FGYQITSFFAASSRYGTPEELQELVDTAHSMGIIVLLDVVHSHASKNSADGLNMFDGTDS
CYFHSGPRGTHDLWDSRLFAYSSWEVLRFLLSNIRWWLEEYRFDGFRFDGVTSMLYHHHG
VGQGFSGDYSEYFGLQVDEDALTYLMLANHLVHTLCPDSITIAEDVSGMPALCSPISQGG
GGFDYRLAMAIPDKWIQLLKEFKDEDWNMGDIVYTLTNRRYLEKCIAYAESHDQALVGDK
SLAFWLMDAEMYTNMSVLTPFTPVIDRGIQLHKMIRLITHGLGGEGYLNFMGNEFGHPEW
LDFPRKGNNESYHYARRQFHLTDDDLLRYKFLNNFDRDMNRLEERYGWLAAPQAYVSEKH
EGNKIIAFERAGLLFIFNFHPSKSYTDYRVGTALPGKFKIVLDSDAAEYGGHQRLDHSTD
FFSEAFEHNGRPYSLLVYIPSRVALILQNVDLPN
Enzyme 9 Number of Residues 754
Enzyme 9 Molecular Weight 86114
Enzyme 9 Theoretical pI 6.93
Enzyme 9 GO Classification
Function
  • alpha-amylase activity
  • amylase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 9 General Function Carbohydrate transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 62089042 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q59ET0 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q59ET0_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AB209731 Link Image
Enzyme 9 GeneCard ID Q59ET0 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID HGNC:4180 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs Not Available
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 14405
Enzyme 10 Name Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Enzyme 10 Synonyms
  1. PP-1A
Enzyme 10 Gene Name PPP1CA
Enzyme 10 Protein Sequence >Serine/threonine-protein phosphatase PP1-alpha catalytic subunit 
MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
KNKGKYGQFSGLNPGGRPITPPRNSAKAKK
Enzyme 10 Number of Residues 330
Enzyme 10 Molecular Weight 37512
Enzyme 10 Theoretical pI 6.25
Enzyme 10 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 10 General Function Signal transduction mechanisms
Enzyme 10 Specific Function Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II
Enzyme 10 Pathways
Enzyme 10 Reactions
  • a phosphoprotein + H2O = a protein + phosphate [RN:R00164] ALL_REAC R00164
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 35451 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P62136 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PP1A_HUMAN Link Image
Enzyme 10 PDB ID 1FJM Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >993 bp 
ATGTCCGACAGCGAGAAGCTCAACCTGGACTCGATCATCGGGCGCCTGCTGGAAGTGCAG
GGCTCGCGGCCTGGCAAGAATGTACAGCTGACAGAGAACGAGATCCGCGGTCTGTGCCTG
AAATCCCGGGAGATTTTTCTGAGCCAGCCCATTCTTCTGGAGCTGGAGGCACCCCTCAAG
ATCTGCGGTGACATACACGGCCAGTACTACGACCTTCTGCGACTATTTGAGTATGGCGGT
TTCCCTCCCGAGAGCAACTACCTCTTTCTGGGGGACTATGTGGACAGGGGCAAGCAGTCC
TTGGAGACCATCTGCCTGCTGCTGGCCTATAAGATCAAGTACCCCGAGAACTTCTTCCTG
CTCCGTGGGAACCACGAGTGTGCCAGCATCAACCGCATCTATGGTTTCTACGATGAGTGC
AAGAGACGCTACAACATCAAACTGTGGAAAACCTTCACTGACTGCTTCAACTGCCTGCCC
ATCGCGGCCATAGTGGACGAAAAGATCTTCTGCTGCCACGGAGGCCTGTCCCCGGACCTG
CAGTCTATGGAGCAGATTCGGCGGATCATGCGGCCCACAGATGTGCCTGACCAGGGCCTG
CTGTGTGACCTGCTGTGGTCTGACCCTGACAAGGACGTGCAGGGCTGGGGCGAGAACGAC
CGTGGCGTCTCTTTTACCTTTGGAGCCGAGGTGGTGGCCAAGTTCCTCCACAAGCACGAC
TTGGACCTCATCTGCCGAGCACACCAGGTGGTAGAAGACGGCTACGAGTTCTTTGCCAAG
CGGCAGCTGGTGACACTTTTCTCAGCTCCCAACTACTGTGGCGAGTTTGACAATGCTGGC
GCCATGATGAGTGTGGACGAGACCCTCATGTGCTCTTTCCAGATCCTCAAGCCCGCCGAC
AAGAACAAGGGGAAGTACGGGCAGTTCAGTGGCCTGAACCCTGGAGGCCGACCCATCACC
CCACCCCGCAATTCCGCCAAAGCCAAGAAATAG
Enzyme 10 GenBank Gene ID X70848 Link Image
Enzyme 10 GeneCard ID P62136 Link Image
Enzyme 10 GenAtlas ID PPP1CA Link Image
Enzyme 10 HGNC ID HGNC:9281 Link Image
Enzyme 10 Chromosome Location 11
Enzyme 10 Locus 11q13
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Song Q, Khanna KK, Lu H, Lavin MF: Cloning and characterization of a human protein phosphatase 1-encoding cDNA. Gene. 1993 Jul 30;129(2):291-5. [PubMed Link Image]
  2. Barker HM, Jones TA, da Cruz e Silva EF, Spurr NK, Sheer D, Cohen PT: Localization of the gene encoding a type I protein phosphatase catalytic subunit to human chromosome band 11q13. Genomics. 1990 Jun;7(2):159-66. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16936
Enzyme 11 Name Protein phosphatase 1 regulatory subunit 3C
Enzyme 11 Synonyms
  1. Protein phosphatase 1 regulatory subunit 5
  2. R5
  3. Protein targeting to glycogen
  4. PTG
Enzyme 11 Gene Name PPP1R3C
Enzyme 11 Protein Sequence >Protein phosphatase 1 regulatory subunit 3C 
MSCTRMIQVLDPRPLTSSVMPVDVAMRLCLAHSPPVKSFLGPYDEFQRRHFVNKLKPLKS
CLNIKHKAKSQNDWKCSHNQAKKRVVFADSKGLSLTAIHVFSDLPEEPAWDLQFDLLDLN
DISSALKHHEEKNLILDFPQPSTDYLSFRSHFQKNFVCLENCSLQERTVTGTVKVKNVSF
EKKVQIRITFDSWKNYTDVDCVYMKNVYGGTDSDTFSFAIDLPPVIPTEQKIEFCISYHA
NGQVFWDNNDGQNYRIVHVQWKPDGVQTQMAPQDCAFHQTSPKTELESTIFGSPRLASGL
FPEWQSWGRMENLASYR
Enzyme 11 Number of Residues 317
Enzyme 11 Molecular Weight 36446
Enzyme 11 Theoretical pI 7.52
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID Q9UQK1 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PPR3C_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID Y18207 Link Image
Enzyme 11 GeneCard ID Q9UQK1 Link Image
Enzyme 11 GenAtlas ID PPP1R3C Link Image
Enzyme 11 HGNC ID HGNC:9293 Link Image
Enzyme 11 Chromosome Location 10
Enzyme 11 Locus 10q23-q24
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Doherty MJ, Young PR, Cohen PT: Amino acid sequence of a novel protein phosphatase 1 binding protein (R5) which is related to the liver- and muscle-specific glycogen binding subunits of protein phosphatase 1. FEBS Lett. 1996 Dec 16;399(3):339-43. [PubMed Link Image]
  2. Permana PA, Luczy-Bachman G, Bogardus C: Protein targeting to glycogen/PPP1R5: screening of coding and flanking genomic regions for polymorphisms and association analysis with insulin action in Pima Indians. Biochem Biophys Res Commun. 1999 Apr 29;258(1):184-6. [PubMed Link Image]
  3. Fernandez-Sanchez ME, Criado-Garcia O, Heath KE, Garcia-Fojeda B, Medrano-Fernandez I, Gomez-Garre P, Sanz P, Serratosa JM, Rodriguez de Cordoba S: Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. Hum Mol Genet. 2003 Dec 1;12(23):3161-71. Epub 2003 Oct 7. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16937
Enzyme 12 Name Protein phosphatase 1 regulatory subunit 3B
Enzyme 12 Synonyms
  1. Protein phosphatase 1 regulatory subunit 4
  2. R4
  3. Protein phosphatase 1 subunit GL
  4. Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL
Enzyme 12 Gene Name PPP1R3B
Enzyme 12 Protein Sequence >Protein phosphatase 1 regulatory subunit 3B 
MMAVDIEYRYNCMAPSLRQERFAFKISPKPSKPLRPCIQLSSKNEASGMVAPAVQEKKVK
KRVSFADNQGLALTMVKVFSEFDDPLDMPFNITELLDNIVSLTTAESESFVLDFSQPSAD
YLDFRNRLQADHVCLENCVLKDKAIAGTVKVQNLAFEKTVKIRMTFDTWKSYTDFPCQYV
KDTYAGSDRDTFSFDISLPEKIQSYERMEFAVYYECNGQTYWDSNRGKNYRIIRAELKST
QGMTKPHSGPDLGISFDQFGSPRCSYGLFPEWPSYLGYEKLGPYY
Enzyme 12 Number of Residues 285
Enzyme 12 Molecular Weight 32695
Enzyme 12 Theoretical pI 5.92
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID Q86XI6 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PPR3B_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK024067 Link Image
Enzyme 12 GeneCard ID Q86XI6 Link Image
Enzyme 12 GenAtlas ID PPP1R3B Link Image
Enzyme 12 HGNC ID HGNC:14942 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available