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Human Metabolome Database Version 2.5

 

Showing metabocard for D-Mannose (HMDB00169)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-03-11 13:41:08
Accession Number HMDB00169
Secondary Accession Numbers Not Available
Common Name D-Mannose
Description D-Mannose is a carbohydrate. High-mannose-type oligosaccharides have been shown to play important roles in protein quality control. Several intracellular proteins, such as lectins, chaperones and glycan-processing enzymes, are involved in this process. These include calnexin/calreticulin, UDP-glucose:glycoprotein glucosyltransferase (UGGT), cargo receptors (such as VIP36 and ERGIC-53), mannosidase-like proteins (e.g. EDEM and Htm1p) and ubiquitin ligase (Fbs). They are thought to recognize high-mannose-type glycans with subtly different structures. Mannose-binding lectin (MBL) is an important constituent of the innate immune system. This protein binds through multiple lectin domains to the repeating sugar arrays that decorate many microbial surfaces, and is then able to activate the complement system through a specific protease called MBL-associated protease-2. The primary pathway for the formation of L-fucose in procaryotic and eucaryotic cells is from D-mannose via an internal oxidation reduction and then epimerization of GDP-D-mannose to produce GDP-L-fucose. (PMID: 9488699, 16154739, 11414367)
Synonyms
  1. DL-mannose
  2. (+)-mannose
  3. D-Mannopyranose
  4. Carubinose (van)
  5. D-mannose
  6. (+-)-mannose
  7. Mannose (van)
  8. D(+)-mannose
  9. nchembio828-comp8
  10. Seminose
  11. hexose (ACD/Name 4.0)
  12. Carubinose
  13. Mannose
Chemical IUPAC Name (3S,4S,5R,6R)-6-(hydroxymethyl)oxane-2,3,4,5-tetrol
Chemical Formula C6H12O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Monosaccharides
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • heterocyclic compound
Biofunction
  • Component of High-mannose type N-glycan biosynthesis
  • Component of N-Glycan biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 180.156
Monoisotopic Molecular Weight 180.063385
Isomeric SMILES OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O
Canonical SMILES OCC1OC(O)C(O)C(O)C1O
KEGG Compound ID C00159 Link Image
BioCyc ID MANNOSE Link Image
BiGG ID 34085 Link Image
Wikipedia Link D-Mannose Link Image
NuGOwiki Link HMDB00169 Link Image
Metagene Link HMDB00169 Link Image
METLIN ID Not Available
PubChem Compound 18950 Link Image
PubChem Substance 15322061 Link Image
ChEBI ID 16024 Link Image
CAS Registry Number 3458-28-4
InChI Identifier InChI=1/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5+,6?/m1/s1
Synthesis Reference Sowden, John C.; Fischer, Hermann O. L. Condensation of nitromethane with D- and L-arabinose: preparation of L-glucose and L-mannose. Journal of the American Chemical Society (1947), 69 1963-5.
Melting Point (Experimental) 132 oC
Experimental Water Solubility 713.0 mg/mL at 17 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 782.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.57 [Predicted by ALOGPS]; -2.3 [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 (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
  • golgi apparatus
  • lysosome
Biofluid Location
  • Blood
  • Breast Milk
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adrenal Medulla
Bladder
Epidermis
Fibroblasts
Intestine
Kidney
Muscle
Myelin
Pancreas
Placenta
Spleen
Testes
Concentrations (Normal)
Biofluid Blood
Value 39.0 +/- 7.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 64.0 +/- 12.0 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 Breast Milk
Value 66.4 +/- 2.3 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Cavalli C, Teng C, Battaglia FC, Bevilacqua G: Free sugar and sugar alcohol concentrations in human breast milk. J Pediatr Gastroenterol Nutr. 2006 Feb;42(2):215-21. [PubMed Link Image]
Biofluid CSF
Value 64.0 (56.0-72.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 24 +/- 13 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid Urine
Value 11.65 +/- 15.42 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 2.5 (0.0-12.6) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1.25 (0.0-2.5) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Fructose and Mannose Degradation SMP00064 Link Image map00051 Link Image
Galactose Metabolism SMP00043 Link Image map00052 Link Image
General References
  1. Lee SH, Nam SY, Chung BC: Altered profile of endogenous steroids in the urine of patients with prolactinoma. Clin Biochem. 1998 Oct;31(7):529-35. [PubMed Link Image]
  2. Nakagawa F, Schulte BA, Spicer SS: Lectin cytochemical evaluation of somatosensory neurons and their peripheral and central processes in rat and man. Cell Tissue Res. 1986;245(3):579-89. [PubMed Link Image]
  3. Thio CL, Mosbruger T, Astemborski J, Greer S, Kirk GD, O'Brien SJ, Thomas DL: Mannose binding lectin genotypes influence recovery from hepatitis B virus infection. J Virol. 2005 Jul;79(14):9192-6. [PubMed Link Image]
  4. Otter M, Zockova P, Kuiper J, van Berkel TJ, Barrett-Bergshoeff MM, Rijken DC: Isolation and characterization of the mannose receptor from human liver potentially involved in the plasma clearance of tissue-type plasminogen activator. Hepatology. 1992 Jul;16(1):54-9. [PubMed Link Image]
  5. Hu P, Parenti G, Keulemans J, Hoogeveen AT: Lysosomal tartrate sensitive acid phosphatase deficiency in cells which contain lysosomal "high uptake forms". Biochem Biophys Res Commun. 1990 Mar 16;167(2):520-7. [PubMed Link Image]
  6. Hermentin P, Witzel R, Kanzy EJ, Diderrich G, Hoffmann D, Metzner H, Vorlop J, Haupt H: The hypothetical N-glycan charge: a number that characterizes protein glycosylation. Glycobiology. 1996 Mar;6(2):217-30. [PubMed Link Image]
  7. DeRossi C, Bode L, Eklund EA, Zhang F, Davis JA, Westphal V, Wang L, Borowsky AD, Freeze HH: Ablation of mouse phosphomannose isomerase (Mpi) causes mannose 6-phosphate accumulation, toxicity, and embryonic lethality. J Biol Chem. 2006 Mar 3;281(9):5916-27. Epub 2005 Dec 8. [PubMed Link Image]
  8. Miras MT, Aunis D, Mandel P: Studies on the interaction of dopamine beta-hydroxylase from various sources with phytohaemagglutinins. Clin Chim Acta. 1975 Nov 3;64(3):293-302. [PubMed Link Image]
  9. Van der Ploeg AT, Kroos MA, Willemsen R, Brons NH, Reuser AJ: Intravenous administration of phosphorylated acid alpha-glucosidase leads to uptake of enzyme in heart and skeletal muscle of mice. J Clin Invest. 1991 Feb;87(2):513-8. [PubMed Link Image]
  10. Cavallone D, Malagolini N, Monti A, Wu XR, Serafini-Cessi F: Variation of high mannose chains of Tamm-Horsfall glycoprotein confers differential binding to type 1-fimbriated Escherichia coli. J Biol Chem. 2004 Jan 2;279(1):216-22. Epub 2003 Oct 21. [PubMed Link Image]
  11. Adlerberth I, Ahrne S, Johansson ML, Molin G, Hanson LA, Wold AE: A mannose-specific adherence mechanism in Lactobacillus plantarum conferring binding to the human colonic cell line HT-29. Appl Environ Microbiol. 1996 Jul;62(7):2244-51. [PubMed Link Image]
  12. Hung CS, Bouckaert J, Hung D, Pinkner J, Widberg C, DeFusco A, Auguste CG, Strouse R, Langermann S, Waksman G, Hultgren SJ: Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection. Mol Microbiol. 2002 May;44(4):903-15. [PubMed Link Image]
  13. Condaminet B, Peguet-Navarro J, Stahl PD, Dalbiez-Gauthier C, Schmitt D, Berthier-Vergnes O: Human epidermal Langerhans cells express the mannose-fucose binding receptor. Eur J Immunol. 1998 Nov;28(11):3541-51. [PubMed Link Image]
  14. Go S, Sato C, Furuhata K, Kitajima K: Oral ingestion of mannose alters the expression level of deaminoneuraminic acid (KDN) in mouse organs. Glycoconj J. 2006 Jul;23(5-6):411-21. [PubMed Link Image]
  15. Burk MR, Troeger C, Brinkhaus R, Holzgreve W, Hahn S: Severely reduced presence of tissue macrophages in the basal plate of pre-eclamptic placentae. Placenta. 2001 Apr;22(4):309-16. [PubMed Link Image]
  16. Sarkar K, Das PK: Protective effect of neoglycoprotein-conjugated muramyl dipeptide against Leishmania donovani infection: the role of cytokines. J Immunol. 1997 Jun 1;158(11):5357-65. [PubMed Link Image]
  17. Kusmierz J, DeGeorge JJ, Sweeney D, May C, Rapoport SI: Quantitative analysis of polyols in human plasma and cerebrospinal fluid. J Chromatogr. 1989 Dec 29;497:39-48. [PubMed Link Image]
  18. Biessen EA, Noorman F, van Teijlingen ME, Kuiper J, Barrett-Bergshoeff M, Bijsterbosch MK, Rijken DC, van Berkel TJ: Lysine-based cluster mannosides that inhibit ligand binding to the human mannose receptor at nanomolar concentration. J Biol Chem. 1996 Nov 8;271(45):28024-30. [PubMed Link Image]
  19. Smith ME: Phagocytic properties of microglia in vitro: implications for a role in multiple sclerosis and EAE. Microsc Res Tech. 2001 Jul 15;54(2):81-94. [PubMed Link Image]
  20. Della Porta M, Danova M, Rigolin GM, Brugnatelli S, Rovati B, Tronconi C, Fraulini C, Russo Rossi A, Riccardi A, Castoldi G: Dendritic cells and vascular endothelial growth factor in colorectal cancer: correlations with clinicobiological findings. Oncology. 2005;68(2-3):276-84. Epub 2005 Jul 7. [PubMed Link Image]
  21. Patnaik SK, Stanley P: Mouse large can modify complex N- and mucin O-glycans on alpha-dystroglycan to induce laminin binding. J Biol Chem. 2005 May 27;280(21):20851-9. Epub 2005 Mar 23. [PubMed Link Image]
  22. Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
  23. Brysk MM, Miller J: Concanavalin A binding glycoprotein in human stratum corneum. J Invest Dermatol. 1984 Mar;82(3):280-2. [PubMed Link Image]
  24. Takahashi I, Takahashi T, Mikami T, Komatsu M, Ohura T, Schuchman EH, Takada G: Acid sphingomyelinase: relation of 93lysine residue on the ratio of intracellular to secreted enzyme activity. Tohoku J Exp Med. 2005 Aug;206(4):333-40. [PubMed Link Image]
  25. Wu X, Rush JS, Karaoglu D, Krasnewich D, Lubinsky MS, Waechter CJ, Gilmore R, Freeze HH: Deficiency of UDP-GlcNAc:Dolichol Phosphate N-Acetylglucosamine-1 Phosphate Transferase (DPAGT1) causes a novel congenital disorder of Glycosylation Type Ij. Hum Mutat. 2003 Aug;22(2):144-50. [PubMed Link Image]
  26. Akazawa S, Metzger BE, Freinkel N: Relationships between glucose and mannose during late gestation in normal pregnancy and pregnancy complicated by diabetes mellitus: concurrent concentrations in maternal plasma and amniotic fluid. J Clin Endocrinol Metab. 1986 May;62(5):984-9. [PubMed Link Image]
  27. Blach-Olszewska Z: Innate immunity: cells, receptors, and signaling pathways. Arch Immunol Ther Exp (Warsz). 2005 May-Jun;53(3):245-53. [PubMed Link Image]
  28. Pietila EM, Tuusa JT, Apaja PM, Aatsinki JT, Hakalahti AE, Rajaniemi HJ, Petaja-Repo UE: Inefficient maturation of the rat luteinizing hormone receptor. A putative way to regulate receptor numbers at the cell surface. J Biol Chem. 2005 Jul 15;280(28):26622-9. Epub 2005 May 18. [PubMed Link Image]
  29. Carchon HA, Jaeken J: Determination of D-mannose in serum by capillary electrophoresis. Clin Chem. 2001;47(7):1319-21. [PubMed Link Image]
  30. Alton G, Hasilik M, Niehues R, Panneerselvam K, Etchison JR, Fana F, Freeze HH: Direct utilization of mannose for mammalian glycoprotein biosynthesis. Glycobiology. 1998 Mar;8(3):285-95. [PubMed Link Image]
  31. Wikipedia Link Image
Metabolic Enzymes
  1. Glucokinase
  2. Hexokinase-3
  3. Hexokinase-2
  4. Hexokinase-1
  5. Alpha-galactosidase A precursor
  6. Alpha-mannosidase 2
  7. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
  8. Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
  9. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
  10. Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
  11. Glycophorin B precursor
  12. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
  13. cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
  14. N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
Enzyme 1 [top]
Enzyme 1 ID 5442
Enzyme 1 Name Glucokinase
Enzyme 1 Synonyms
  1. Hexokinase-4
  2. Hexokinase type IV
  3. HK IV
  4. HK4
  5. Hexokinase-D
Enzyme 1 Gene Name GCK
Enzyme 1 Protein Sequence >Glucokinase
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
Enzyme 1 Number of Residues 465
Enzyme 1 Molecular Weight 52192
Enzyme 1 Theoretical pI 4.85
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + D-glucose = ADP + D-glucose 6-phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 179427 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P35557 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HXK4_HUMAN Link Image
Enzyme 1 PDB ID 1V4T Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1398 bp
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
Enzyme 1 GenBank Gene ID M88011 Link Image
Enzyme 1 GeneCard ID GCK Link Image
Enzyme 1 GenAtlas ID GCK Link Image
Enzyme 1 HGNC ID HGNC:4195 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7p15.3-p15.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed Link Image]
  2. Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed Link Image]
  3. Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed Link Image]
  4. Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed Link Image]
  5. Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed Link Image]
  6. Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed Link Image]
  7. St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed Link Image]
  8. Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed Link Image]
  9. Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed Link Image]
  10. Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed Link Image]
  11. Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed Link Image]
  12. Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed Link Image]
  13. Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed Link Image]
  14. Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed Link Image]
  15. Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed Link Image]
  16. Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed Link Image]
  17. Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed Link Image]
  18. Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed Link Image]
  19. Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5444
Enzyme 2 Name Hexokinase-3
Enzyme 2 Synonyms
  1. Hexokinase type III
  2. HK III
Enzyme 2 Gene Name HK3
Enzyme 2 Protein Sequence >Hexokinase-3
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSLSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRGNRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
Enzyme 2 Number of Residues 923
Enzyme 2 Molecular Weight 98921
Enzyme 2 Theoretical pI 5.11
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-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 1255788 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P52790 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HXK3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2772 bp
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTAAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGACGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGGGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
Enzyme 2 GenBank Gene ID U51333 Link Image
Enzyme 2 GeneCard ID HK3 Link Image
Enzyme 2 GenAtlas ID HK3 Link Image
Enzyme 2 HGNC ID HGNC:4925 Link Image
Enzyme 2 Chromosome Location 5
Enzyme 2 Locus 5q35.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed Link Image]
  2. Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5445
Enzyme 3 Name Hexokinase-2
Enzyme 3 Synonyms
  1. Hexokinase type II
  2. HK II
  3. Muscle form hexokinase
Enzyme 3 Gene Name HK2
Enzyme 3 Protein Sequence >Hexokinase-2
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
Enzyme 3 Number of Residues 917
Enzyme 3 Molecular Weight 102381
Enzyme 3 Theoretical pI 5.93
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 587202 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P52789 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name HXK2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2754 bp
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCCTTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTACTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCACCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
Enzyme 3 GenBank Gene ID Z46376 Link Image
Enzyme 3 GeneCard ID HK2 Link Image
Enzyme 3 GenAtlas ID HK2 Link Image
Enzyme 3 HGNC ID HGNC:4923 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2p13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [PubMed Link Image]
  2. Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed Link Image]
  3. Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed Link Image]
  4. Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed Link Image]
  5. Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed Link Image]
  6. Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5447
Enzyme 4 Name Hexokinase-1
Enzyme 4 Synonyms
  1. Hexokinase type I
  2. HK I
  3. Brain form hexokinase
Enzyme 4 Gene Name HK1
Enzyme 4 Protein Sequence >Hexokinase-1
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
Enzyme 4 Number of Residues 917
Enzyme 4 Molecular Weight 102487
Enzyme 4 Theoretical pI 6.78
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-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 184021 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P19367 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name HXK1_HUMAN Link Image
Enzyme 4 PDB ID 1HKB Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2754 bp
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGAACGAATATTCCCTAAATGCTGGGAAACAAAGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGATGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
Enzyme 4 GenBank Gene ID M75126 Link Image
Enzyme 4 GeneCard ID HK1 Link Image
Enzyme 4 GenAtlas ID HK1 Link Image
Enzyme 4 HGNC ID HGNC:4922 Link Image
Enzyme 4 Chromosome Location 10
Enzyme 4 Locus 10q22
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Nishi S, Seino S, Bell GI: Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous. Biochem Biophys Res Commun. 1988 Dec 30;157(3):937-43. [PubMed Link Image]
  2. Ruzzo A, Andreoni F, Magnani M: Structure of the human hexokinase type I gene and nucleotide sequence of the 5' flanking region. Biochem J. 1998 Apr 15;331 ( Pt 2):607-13. [PubMed Link Image]
  3. Magnani M, Bianchi M, Casabianca A, Stocchi V, Daniele A, Altruda F, Ferrone M, Silengo L: A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates. Biochem J. 1992 Jul 1;285 ( Pt 1):193-9. [PubMed Link Image]
  4. Magnani M, Serafini G, Bianchi M, Casabianca A, Stocchi V: Human hexokinase type I microheterogeneity is due to different amino-terminal sequences. J Biol Chem. 1991 Jan 5;266(1):502-5. [PubMed Link Image]
  5. Murakami K, Piomelli S: Identification of the cDNA for human red blood cell-specific hexokinase isozyme. Blood. 1997 Feb 1;89(3):762-6. [PubMed Link Image]
  6. Andreoni F, Ruzzo A, Magnani M: Structure of the 5' region of the human hexokinase type I (HKI) gene and identification of an additional testis-specific HKI mRNA. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):19-26. [PubMed Link Image]
  7. Aleshin AE, Zeng C, Fromm HJ, Honzatko RB: Crystallization and preliminary X-ray analysis of human brain hexokinase. FEBS Lett. 1996 Aug 5;391(1-2):9-10. [PubMed Link Image]
  8. Aleshin AE, Zeng C, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate. Structure. 1998 Jan 15;6(1):39-50. [PubMed Link Image]
  9. Aleshin AE, Zeng C, Bartunik HD, Fromm HJ, Honzatko RB: Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate. J Mol Biol. 1998 Sep 18;282(2):345-57. [PubMed Link Image]
  10. Rosano C, Sabini E, Rizzi M, Deriu D, Murshudov G, Bianchi M, Serafini G, Magnani M, Bolognesi M: Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control. Structure. 1999 Nov 15;7(11):1427-37. [PubMed Link Image]
  11. Aleshin AE, Kirby C, Liu X, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. J Mol Biol. 2000 Mar 3;296(4):1001-15. [PubMed Link Image]
  12. Bianchi M, Magnani M: Hexokinase mutations that produce nonspherocytic hemolytic anemia. Blood Cells Mol Dis. 1995;21(1):2-8. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5997
Enzyme 5 Name Alpha-galactosidase A precursor
Enzyme 5 Synonyms
  1. Melibiase
  2. Alpha-D- galactoside galactohydrolase
  3. Alpha-D-galactosidase A
  4. Agalsidase alfa
Enzyme 5 Gene Name GLA
Enzyme 5 Protein Sequence >Alpha-galactosidase A precursor
MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEP
DSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQL
ANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENL
ADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIK
SILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDL
RHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIG
GPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENT
MQMSLKDLL
Enzyme 5 Number of Residues 429
Enzyme 5 Molecular Weight 48767
Enzyme 5 Theoretical pI 5.27
Enzyme 5 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 5 General Function Not Available
Enzyme 5 Specific Function Hydrolysis of terminal, non-reducing alpha-D- galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase
Enzyme 5 Pathways
Enzyme 5 Reactions
  • Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-31
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 757912 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P06280 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AGAL_HUMAN Link Image
Enzyme 5 PDB ID 1R47 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1290 bp
ATGCAGCTGAGGAACCCAGAACTACATCTGGGCTGCGCGCTTGCGCTTCGCTTCCTGGCC
CTCGTTTCCTGGGACATCCCTGGGGCTAGAGCACTGGACAATGGATTGGCAAGGACGCCT
ACCATGGGCTGGCTGCACTGGGAGCGCTTCATGTGCAACCTTGACTGCCAGGAAGAGCCA
GATTCCTGCATCAGTGAGAAGCTCTTCATGGAGATGGCAGAGCTCATGGTCTCAGAAGGC
TGGAAGGATGCAGGTTATGAGTACCTCTGCATTGATGACTGTTGGATGGCTCCCCAAAGA
GATTCAGAAGGCAGACTTCAGGCAGACCCTCAGCGCTTTCCTCATGGGATTCGCCAGCTA
GCTAATTATGTTCACAGCAAAGGACTGAAGCTAGGGATTTATGCAGATGTTGGAAATAAA
ACCTGCGCAGGCTTCCCTGGGAGTTTTGGATACTACGACATTGATGCCCAGACCTTTGCT
GACTGGGGAGTAGATCTGCTAAAATTTGATGGTTGTTACTGTGACAGTTTGGAAAATTTG
GCAGATGGTTATAAGCACATGTCCTTGGCCCTGAATAGGACTGGCAGAAGCATTGTGTAC
TCCTGTGAGTGGCCTCTTTATATGTGGCCCTTTCAAAAGCCCAATTATACAGAAATCCGA
CAGTACTGCAATCACTGGCGAAATTTTGCTGACATTGATGATTCCTGGAAAAGTATAAAG
AGTATCTTGGACTGGACATCTTTTAACCAGGAGAGAATTGTTGATGTTGCTGGACCAGGG
GGTTGGAATGACCCAGATATGTTAGTGATTGGCAACTTTGGCCTCAGCTGGAATCAGCAA
GTAACTCAGATGGCCCTCTGGGCTATCATGGCTGCTCCTTTATTCATGTCTAATGACCTC
CGACACATCAGCCCTCAAGCCAAAGCTCTCCTTCAGGATAAGGACGTAATTGCCATCAAT
CAGGACCCCTTGGGCAAGCAAGGGTACCAGCTTAGACAGGGAGACAACTTTGAAGTGTGG
GAACGACCTCTCTCAGGCTTAGCCTGGGCTGTAGCTATGATAAACCGGCAGGAGATTGGT
GGACCTCGCTCTTATACCATCGCAGTTGCTTCCCTGGGTAAAGGAGTGGCCTGTAATCCT
GCCTGCTTCATCACACAGCTCCTCCCTGTGAAAAGGAAGCTAGGGTTCTATGAATGGACT
TCAAGGTTAAGAAGTCACATAAATCCCACAGGCACTGTTTTGCTTCAGCTAGAAAATACA
ATGCAGATGTCATTAAAAGACTTACTTTAA
Enzyme 5 GenBank Gene ID X05790 Link Image
Enzyme 5 GeneCard ID GLA Link Image
Enzyme 5 GenAtlas ID GLA Link Image
Enzyme 5 HGNC ID HGNC:4296 Link Image
Enzyme 5 Chromosome Location X
Enzyme 5 Locus Xq22
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Tsuji S, Martin BM, Kaslow DC, Migeon BR, Choudary PV, Stubbleflied BK, Mayor JA, Murray GJ, Barranger JA, Ginns EI: Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A. Eur J Biochem. 1987 Jun 1;165(2):275-80. [PubMed Link Image]
  2. Kornreich R, Desnick RJ, Bishop DF: Nucleotide sequence of the human alpha-galactosidase A gene. Nucleic Acids Res. 1989 Apr 25;17(8):3301-2. [PubMed Link Image]
  3. Oeltjen JC, Liu X, Lu J, Allen RC, Muzny D, Belmont JW, Gibbs RA: Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci. Mamm Genome. 1995 May;6(5):334-8. [PubMed Link Image]
  4. Bishop DF, Calhoun DH, Bernstein HS, Hantzopoulos P, Quinn M, Desnick RJ: Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4859-63. [PubMed Link Image]
  5. Quinn M, Hantzopoulos P, Fidanza V, Calhoun DH: A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A. Gene. 1987;58(2-3):177-88. [PubMed Link Image]
  6. Bishop DF, Kornreich R, Desnick RJ: Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3903-7. [PubMed Link Image]
  7. Novo FJ, Kruszewski A, MacDermot KD, Goldspink G, Gorecki DC: Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion. Nucleic Acids Res. 1995 Jul 25;23(14):2636-40. [PubMed Link Image]
  8. Eng CM, Desnick RJ: Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. Hum Mutat. 1994;3(2):103-11. [PubMed Link Image]
  9. Koide T, Ishiura M, Iwai K, Inoue M, Kaneda Y, Okada Y, Uchida T: A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser. FEBS Lett. 1990 Jan 1;259(2):353-6. [PubMed Link Image]
  10. von Scheidt W, Eng CM, Fitzmaurice TF, Erdmann E, Hubner G, Olsen EG, Christomanou H, Kandolf R, Bishop DF, Desnick RJ: An atypical variant of Fabry's disease with manifestations confined to the myocardium. N Engl J Med. 1991 Feb 7;324(6):395-9. [PubMed Link Image]
  11. Sakuraba H, Oshima A, Fukuhara Y, Shimmoto M, Nagao Y, Bishop DF, Desnick RJ, Suzuki Y: Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease. Am J Hum Genet. 1990 Nov;47(5):784-9. [PubMed Link Image]
  12. Bernstein HS, Bishop DF, Astrin KH, Kornreich R, Eng CM, Sakuraba H, Desnick RJ: Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene. J Clin Invest. 1989 Apr;83(4):1390-9. [PubMed Link Image]
  13. Ishii S, Sakuraba H, Suzuki Y: Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease. Hum Genet. 1992 Apr;89(1):29-32. [PubMed Link Image]
  14. Eng CM, Resnick-Silverman LA, Niehaus DJ, Astrin KH, Desnick RJ: Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease. Am J Hum Genet. 1993 Dec;53(6):1186-97. [PubMed Link Image]
  15. Davies JP, Winchester BG, Malcolm S: Mutation analysis in patients with the typical form of Anderson-Fabry disease. Hum Mol Genet. 1993 Jul;2(7):1051-3. [PubMed Link Image]
  16. Davies J, Christomanou H, Winchester B, Malcolm S: Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease. Hum Mol Genet. 1994 Apr;3(4):667-9. [PubMed Link Image]
  17. Eng CM, Niehaus DJ, Enriquez AL, Burgert TS, Ludman MD, Desnick RJ: Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene. Hum Mol Genet. 1994 Oct;3(10):1795-9. [PubMed Link Image]
  18. Okumiya T, Ishii S, Takenaka T, Kase R, Kamei S, Sakuraba H, Suzuki Y: Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease. Biochem Biophys Res Commun. 1995 Sep 25;214(3):1219-24. [PubMed Link Image]
  19. Okumiya T, Ishii S, Kase R, Kamei S, Sakuraba H, Suzuki Y: Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins. Hum Genet. 1995 May;95(5):557-61. [PubMed Link Image]
  20. Madsen KM, Hasholt L, Sorensen SA, Fermer ML, Dahl N: Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease. Hum Mutat. 1995;5(3):277-8. [PubMed Link Image]
  21. Nakao S, Takenaka T, Maeda M, Kodama C, Tanaka A, Tahara M, Yoshida A, Kuriyama M, Hayashibe H, Sakuraba H, et al.: An atypical variant of Fabry's disease in men with left ventricular hypertrophy. N Engl J Med. 1995 Aug 3;333(5):288-93. [PubMed Link Image]
  22. Davies JP, Eng CM, Hill JA, Malcolm S, MacDermot K, Winchester B, Desnick RJ: Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries. Eur J Hum Genet. 1996;4(4):219-24. [PubMed Link Image]
  23. Cariolou MA, Christodoulides M, Manoli P, Kokkofitou A, Tsambaos D: Novel trinucleotide deletion in Fabry's disease. Hum Genet. 1996 Apr;97(4):468-70. [PubMed Link Image]
  24. Germain D, Biasotto M, Tosi M, Meo T, Kahn A, Poenaru L: Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease. Hum Genet. 1996 Dec;98(6):719-26. [PubMed Link Image]
  25. Blanch LC, Meaney C, Morris CP: A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene. Hum Mutat. 1996;8(1):38-43. [PubMed Link Image]
  26. Redonnet-Vernhet I, Ploos van Amstel JK, Jansen RP, Wevers RA, Salvayre R, Levade T: Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene. J Med Genet. 1996 Aug;33(8):682-8. [PubMed Link Image]
  27. Takata T, Okumiya T, Hayashibe H, Shimmoto M, Kase R, Itoh K, Utsumi K, Kamei S, Sakuraba H: Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis. Brain Dev. 1997 Mar;19(2):111-6. [PubMed Link Image]
  28. Eng CM, Ashley GA, Burgert TS, Enriquez AL, D'Souza M, Desnick RJ: Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes. Mol Med. 1997 Mar;3(3):174-82. [PubMed Link Image]
  29. Miyazaki T, Kajita M, Ohmori S, Mizutani N, Niwa T, Murata Y, Seo H: A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease. Hum Mutat. 1998;Suppl 1:S139-40. [PubMed Link Image]
  30. Okumiya T, Kawamura O, Itoh K, Kase R, Ishii S, Kamei S, Sakuraba H: Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote. Hum Mutat. 1998;Suppl 1:S213-6. [PubMed Link Image]
  31. Guffon N, Froissart R, Chevalier-Porst F, Maire I: Mutation analysis in 11 French patients with Fabry disease. Hum Mutat. 1998;Suppl 1:S288-90. [PubMed Link Image]
  32. Germain DP, Poenaru L: Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches. Biochem Biophys Res Commun. 1999 Apr 21;257(3):708-13. [PubMed Link Image]
  33. Beyer EM, Karpova EA, Udalova OV, Ploos van Amstel JK, van Diggelen OP, Tsvetkova IV: The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A. Clin Chim Acta. 1999 Feb;280(1-2):81-9. [PubMed Link Image]
  34. Topaloglu AK, Ashley GA, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease. Mol Med. 1999 Dec;5(12):806-11. [PubMed Link Image]
  35. Lee JK, Kim GH, Kim JS, Kim KK, Lee MC, Yoo HW: Identification of four novel mutations in five unrelated Korean families with Fabry disease. Clin Genet. 2000 Sep;58(3):228-33. [PubMed Link Image]
  36. Ashton-Prolla P, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes. J Investig Med. 2000 Jul;48(4):227-35. [PubMed Link Image]
  37. Germain DP, Salard D, Fellmann F, Azibi K, Caillaud C, Bernard MC, Poenaru L: Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease. Hum Mutat. 2001 Apr;17(4):353. [PubMed Link Image]
  38. Blaydon D, Hill J, Winchester B: Fabry disease: 20 novel GLA mutations in 35 families. Hum Mutat. 2001 Nov;18(5):459. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6149
Enzyme 6 Name Alpha-mannosidase 2
Enzyme 6 Synonyms
  1. Alpha-mannosidase II
  2. Mannosyl- oligosaccharide 1,3-1,6-alpha-mannosidase
  3. MAN II
  4. Golgi alpha- mannosidase II
  5. Mannosidase alpha class 2A member 1
Enzyme 6 Gene Name MAN2A1
Enzyme 6 Protein Sequence >Alpha-mannosidase 2
MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRNPRREGSFPQGQLSMLQEKIDHLER
LLAENNEIISNIRDSVINLSESVEDGPKSSQSNFSQGAGSHLLPSQLSLSVDTADCLFAS
QSGSHNSDVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGW
LKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIEN
GQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYL
LNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTC
GPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLL
APLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRD
KGQSMFPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAH
KYKINKFLSSSLYTALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKIIG
NSAFLLILKDKLTYDSYSPDTFLEMDLKQKSQDSLPQKNIIRLSAEPRYLVVYNPLEQDR
ISLVSVYVSSPTVQVFSASGKPVEVQVSAVWDTANTISETAYEISFRAHIPPLGLKVYKI
LESASSNSHLADYVLYKNKVEDSGIFTIKNMINTEEGITLENSFVLLRFDQTGLMKQMMT
KEDGKHHEVNVQFSWYGTTIKRDKSGAYLFLPDGNAKPYVYTTPPFVRVTHGRIYSEVTC
FFDHVTHRVRLYHIQGIEGQSVEVSNIVDIRKVYNREIAMKISSDIKSQNRFYTDLNGYQ
IQPRMTLSKLPLQANVYPMTTMAYIQDAKHRLTLLSAQSLGVSSLNSGQIEVIMDRRLMQ
DDNRGLEQGIQDNKITANLFRILLEKRSAVNTEEEKKSVSYPSLLSHITSSLMNHPVIPM
ANKFSSPTLELQGEFSPLQSSLPCDIHLVNLRTIQSKVGNGHSNEAALILHRKGFDCRFS
SKGTGLFCSTTQGKILVQKLLNKFIVESLTPSSLSLMHSPPGTQNISEINLSPMEISTFR
IQLR
Enzyme 6 Number of Residues 1144
Enzyme 6 Molecular Weight 131142
Enzyme 6 Theoretical pI 7.61
Enzyme 6 GO Classification
Function
  • alpha-mannosidase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • mannosidase activity
Process
  • alcohol metabolism
  • carbohydrate metabolism
  • cellular metabolism
  • hexose metabolism
  • macromolecule metabolism
  • mannose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 6 General Function Carbohydrate transport and metabolism
Enzyme 6 Specific Function Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway
Enzyme 6 Pathways
Enzyme 6 Reactions
  • Hydrolysis of the terminal 1,3- and 1,6-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-31
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1117827 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q16706 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name MA2A1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >3435 bp
ATGAAGTTAAGCCGCCAGTTCACCGTGTTCGGCAGTGCGATCTTCTGTGTGGTGATTTTC
TCGCTCTACCTGATGCTGGACCGGGGTCACTTAGACTACCCCAGGAACCCGCGCCGCGAG
GGCTCCTTCCCTCAGGGCCAGCTCTCAATGTTGCAAGAAAAAATAGACCATTTGGAGCGT
TTGCTAGCTGAGAATAATGAGATCATCTCAAATATTAGAGACTCAGTCATCAATTTGAGT
GAGTCTGTGGAGGATGGTCCGAAAAGTTCACAAAGCAATTTCAGCCAAGGTGCTGGCTCA
CATCTTCTGCCCTCACAATTATCCCTCTCAGTTGACACTGCAGACTGTCTGTTTGCTTCA
CAAAGTGGAAGTCACAATTCAGATGTGCAGATGTTGGATGTTTACAGTCTAATTTCTTTT
GACAATCCAGATGGTGGAGTTTGGAAGCAAGGATTTGACATTACTTATGAATCTAATGAA
TGGGACACTGAACCCCTTCAAGTCTTTGTGGTGCCTCATTCCCATAACGACCCAGGTTGG
TTGAAGACTTTCAATGACTACTTTAGAGACAAGACTCAGTATATTTTTAATAACATGGTC
CTAAAGCTGAAAGAAGACTCACGGAGGAAGTTTATTTGGTCTGAGATCTCTTACCTTTCA
AAGTGGTGGGATATTATAGATATTCAGAAGAAGGATGCTGTTAAAAGTTTAATAGAAAAT
GGTCAGCTTGAAATTGTGACAGGTGGCTGGGTTATGCCTGATGAAGCTACTCCACATTAT
TTTGCCTTAATTGATCAACTAATTGAAGGACATCAGTGGCTGGAAAATAATATAGGAGTG
AAACCTCGGTCCGGCTGGGCTATTGATCCCTTTGGACACTCACCAACAATGGCTTATCTT
CTAAACCGTGCTGGACTTTCTCACATGCTTATCCAGAGAGTTCATTATGCAGTTAAAAAA
CACTTTGCACTGCATAAAACATTGGAGTTTTTTTGGAGACAGAATTGGGATCTGGGATCT
GTCACAGATATTTTATGCCACATGATGCCCTTCTACAGCTATGACATCCCTCACACTTGT
GGACCTGATCCTAAAATATGCTGCCAGTTTGATTTTAAACGTCTTCCTGGAGGCAGATTT
GGTTGTCCCTGGGGAGTCCCCCCAGAAACAATACATCCTGGAAATGTCCAAAGCAGGGCT
CGGATGCTACTAGATCAGTACCGAAAGAAGTCAAAGCTTTTTCGAACCAAAGTTCTCCTG
GCTCCACTAGGAGATGATTTCCGCTACTGTGAATACACGGAATGGGATTTACAGTTTAAG
AATTATCAGCAGCTTTTTGATTATATGAATTCTCAGTCCAAGTTTAAAGTTAAGATACAG
TTTGGAACTTTATCAGATTTTTTTGATGCGCTGGATAAAGCAGATGAAACTCAGAGAGAC
AAGGGCCAATCGATGTTCCCTGTTTTAAGTGGAGATTTTTTCACTTATGCCGATCGAGAT
GATCATTACTGGAGTGGCTATTTTACATCCAGACCCTTTTACAAACGAATGGACAGAATC
ATGGAATCTCATTTAAGGGCTGCTGAAATTCTTTACTATTTCGCCCTGAGACAAGCTCAC
AAATACAAGATAAATAAATTTCTCTCATCATCACTTTACACGGCACTGACAGAAGCCAGA
AGGAATTTGGGACTGTTTCAACATCATGATGCTATCACAGGAACTGCAAAAGACTGGGTG
GTTGTGGATTATGGTACCAGACTTTTTCATTCGTTAATGGTTTTGGAGAAGATAATTGGA
AATTCTGCATTTCTTCTTATTGGGAAGGACAAACTCACATACGACTCTTACTCTCCTGAT
ACCTTCCTGGAGATGGATTTGAAACAAAAATCACAAGATTCTCTGCCACAAAAAAATATA
ATAAGGCTGAGTGCGGAGCCAAGGTACCTTGTGGTCTATAATCCTTTAGAACAAGACCGA
ATCTCGTTGGTCTCAGTCTATGTGAGTTCCCCGACAGTGCAAGTGTTCTCTGCTTCAGGA
AAACCTGTGGAAGTTCAAGTCAGCGCAGTTTGGGATACAGCAAATACTATTTCAGAAACA
GCCTATGAGATCTCTTTTCGAGCACATATACCGCCATTGGGACTGAAAGTGTATAAGATT
TTGGAATCAGCAAGTTCAAATTCACATTTAGCTGATTATGTCTTGTATAAGAATAAAGTA
GAAGATAGCGGAATTTTCACCATAAAGAATATGATAAATACTGAAGAAGGTATAACACTA
GAGAACTCCTTTGTTTTACTTCGGTTTGATCAAACTGGACTTATGAAGCAAATGATGACT
AAAGAAGATGGTAAACACCATGAAGTAAATGTGCAATTTTCATGGTATGGAACCACAATT
AAAAGAGACAAAAGTGGTGCCTACCTCTTCTTACCTGATGGTAATGCCAAGCCTTATGTT
TACACAACACCGCCCTTTGTCAGAGTGACACATGGAAGGATTTATTCGGAAGTGACTTGC
TTTTTTGACCATGTTACTCATAGAGTCCGACTATACCACATACAGGGAATAGAAGGACAG
TCTGTGGAAGTTTCCAATATTGTGGACATCCGAAAAGTATATAACCGTGAGATTGCAATG
AAAATTTCTTCTGATATAAAAAGCCAAAATAGATTTTATACTGACCTAAATGGGTACCAG
ATTCAACCTAGAATGACACTGAGCAAATTGCCTCTTCAAGCAAATGTCTATCCCATGACC
ACAATGGCCTATATCCAGGATGCCAAACATCGTTTGACACTGCTCTCTGCTCAGTCATTA
GGGGTTTCGAGTTTGAATAGTGGTCAGATTGAAGTTATCATGGATCGAAGACTCATGCAA
GATGATAATCGTGGCCTTGAGCAAGGTATCCAGGATAACAAGATTACAGCTAATCTATTT
CGAATACTACTAGAAAAAAGAAGTGCTGTTAATACGGAAGAAGAAAAGAAGTCGGTCAGT
TATCCTTCTCTCCTTAGCCACATAACTTCTTCTCTCATGAATCATCCAGTCATTCCAATG
GCAAATAAGTTCTCCTCACCTACCCTTGAGCTGCAAGGTGAATTCTCTCCATTACAGTCA
TCTTTGCCTTGTGACATTCATCTGGTTAATTTGAGAACAATACAGTCAAAGGTGGGCAAT
GGGCACTCCAATGAGGCAGCCTTGATCCTCCACAGAAAAGGGTTTGATTGTCGGTTCTCT
AGCAAAGGCACAGGGCTGTTTTGTTCTACTACTCAGGGAAAGATATTGGTACAGAAACTT
TTAAACAAGTTTATTGTCGAAAGTCTCACACCTTCATCACTATCCTTGATGCATTCACCT
CCCGGCACTCAGAATATAAGTGAGATCAACTTGAGTCCAATGGAAATCAGCACATTCCGA
ATCCAGTTGAGGTGA
Enzyme 6 GenBank Gene ID U31520 Link Image
Enzyme 6 GeneCard ID MAN2A1 Link Image
Enzyme 6 GenAtlas ID MAN2A1 Link Image
Enzyme 6 HGNC ID HGNC:6824 Link Image
Enzyme 6 Chromosome Location 5
Enzyme 6 Locus 5q21-q22
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Misago M, Liao YF, Kudo S, Eto S, Mattei MG, Moremen KW, Fukuda MN: Molecular cloning and expression of cDNAs encoding human alpha-mannosidase II and a previously unrecognized alpha-mannosidase IIx isozyme. Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11766-70. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6150
Enzyme 7 Name Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
Enzyme 7 Synonyms
  1. Processing alpha-1,2-mannosidase IB
  2. Alpha-1,2-mannosidase IB
  3. Mannosidase alpha class 1A member 2
Enzyme 7 Gene Name MAN1A2
Enzyme 7 Protein Sequence >Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
MTTPALLPLSGRRIPPLNLGPPSFPHHRATLRLSEKFILLLILSAFITLCFGAFFFLPDS
SKHKRFDLGLEDVLIPHVDAGKGAKNPGVFLIHGPDEHRHREEEERLRNKIRADHEKALE
EAKEKLRKSREEIRAEIQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREK
REKIKEMMKHAWDNYRTYGWGHNELRPIARKGHSPNIFGSSQMGATIVDALDTLYIMGLH
DEFLDGQRWIEDNLDFSVNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLP
AFNTPTGIPWAMVNLKSGVGRNWGWASAGSSILAEFGTLHMEFIHLSYLTGDLTYYKKVM
HIRKLLQKMDRPNGLYPNYLNPRTGRWGQYHTSVGGLGDSFYEYLLKAWLMSDKTDHEAR
KMYDDAIEAIEKHLIKKSRGGLTFIGEWKNGHLEKKMGHLACFAGGMFALGADGSRADKA
GHYLELGAEIARTCHESYDRTALKLGPESFKFDGAVEAVAVRQAEKYYILRPEVIETYWY
LWRFTHDPRYRQWGWEAALAIEKYCRVNGGFSGVKDVYSSTPTHDDVQQSFFLAETLKYL
YLLFSGDDLLPLDHWVFNTEAHPLPVLHLANTTLSGNPAVR
Enzyme 7 Number of Residues 641
Enzyme 7 Molecular Weight 73004
Enzyme 7 Theoretical pI 7.67
Enzyme 7 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • mannosidase activity
  • mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
  • mannosyl-oligosaccharide mannosidase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid N-linked glycosylation
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2)
Enzyme 7 Pathways
Enzyme 7 Reactions
  • Hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 37-57
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 3025750 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O60476 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name MA1A2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >758 bp
ATCATACATCTGTCGGTGGCCTGGGAGACAGTTTTTATGAATACTTACTGAAAGCATGGT
TGATGTCAGATAAAACAGACCATGAGGCAAGAAAGATGTATGATGATGCTATTGAGGCTA
TAGAAAAACATCTTATTAAGAAGTCTCGTGGAGGTCTTACCTTTATTGGAGAATGGAAGA
ATGGGCACTTGGAAAAAAAGATGGGGCATTTGGCCTGCTTTGCTGGGGGAATGTTTGCAC
TAGGAGCAGATGGTTCCAGAGCAGATAAAGCTGGTCATTATTTAGAGCTAGGGGCAGAAA
TTGCACGTACTTGTCATGAGTCATATGACAGAACTGCATTAAAGCTAGGTCCTGAATCAT
TCAAGTTTGATGGTGCAGTGGAGGCTGTGGCTGTCCGGCAGGCTGAAAAGTATTATATCC
TCCGTCCAGAAGTAATTGAAACCTATTGGTACCTATGGCGATTCACTCACGATCCAAGAT
ACAGGCAGTGGGGCTGGGAAGCAGCACTGGCCATTGAAAAGTATTGCCGAGTTAATGGTG
GGTTTTCTGGAGTCAAAGATGTATATTCCTCTACTCCTACACATGATGATGTACAGCAGA
GCTTTTTTCTTGCTGAAACATTAAAATATTTGTATCTGCTGTTCTCCGGTGATGACCTTT
TACCTTTAGACCACTGGGTGTTTAATACAGAGGCTCACCCTCTGCCTGTGTTACATTTAG
CCAACACCACACTTTCAGGTAATCCTGCTGTTCGATGA
Enzyme 7 GenBank Gene ID AF053626 Link Image
Enzyme 7 GeneCard ID MAN1A2 Link Image
Enzyme 7 GenAtlas ID MAN1A2 Link Image
Enzyme 7 HGNC ID HGNC:6822 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1p13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Tremblay LO, Campbell Dyke N, Herscovics A: Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human alpha1,2-mannosidase gene involved in N-glycan maturation. Glycobiology. 1998 Jun;8(6):585-95. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6151
Enzyme 8 Name Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
Enzyme 8 Synonyms
  1. ER alpha-1,2-mannosidase
  2. Mannosidase alpha class 1B member 1
  3. Man9GlcNAc2-specific-processing alpha-mannosidase
Enzyme 8 Gene Name MAN1B1
Enzyme 8 Protein Sequence >Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
MAACEGRRSGALGSSQSDFLTPPVGGAPWAVATTVVMYPPPPPPPHRDFISVTLSFGENY
DNSKSWRRRSCWRKWKQLSRLQRNMILFLLAFLLFCGLLFYINLADHWKALAFRLEEEQK
MRPEIAGLKPANPPVLPAPQKADTDPENLPEISSQKTQRHIQRGPPHLQIRPPSQDLKDG
TQEEATKRQEAPVDPRPEGDPQRTVISWRGAVIEPEQGTELPSRRAEVPTKPPLPPARTQ
GTPVHLNYRQKGVIDVFLHAWKGYRKFAWGHDELKPVSRSFSEWFGLGLTLIDALDTMWI
LGLRKEFEEARKWVSKKLHFEKDVDVNLFESTIRILGGLLSAYHLSGDSLFLRKAEDFGN
RLMPAFRTPSKIPYSDVNIGTGVAHPPRWTSDSTVAEVTSIQLEFRELSRLTGDKKFQEA
VEKVTQHIHGLSGKKDGLVPMFINTHSGLFTHLGVFTLGARADSYYEYLLKQWIQGGKQE
TQLLEDYVEAIEGVRTHLLRHSEPSKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVYHG
LPASHMELAQELMETCYQMNRQMETGLSPEIVHFNLYPQPGRRDVEVKPADRHNLLRPET
VESLFYLYRVTGDRKYQDWGWEILQSFSRFTRVPSGGYSSINNVQDPQKPEPRDKMESFF
LGETLKYLFLLFSDDPNLLSLDAYVFNTEAHPLPIWTPA
Enzyme 8 Number of Residues 699
Enzyme 8 Molecular Weight 79581
Enzyme 8 Theoretical pI 7.80
Enzyme 8 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • mannosidase activity
  • mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
  • mannosyl-oligosaccharide mannosidase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid N-linked glycosylation
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Involved in the maturation of Asn-linked oligosaccharides. Trim a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). The only product is the Man(8)GlcNAc(2) isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. It may be involved in glycoprotein quality control since it is important to target misfolded glycoproteins for degradation
Enzyme 8 Pathways
Enzyme 8 Reactions
  • Hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 85-105
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 6066222 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9UKM7 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name MA1B1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2100 bp
ATGGCTGCCTGCGAGGGCAGGAGAAGCGGAGCTCTCGGTTCCTCTCAGTCGGACTTCCTG
ACGCCGCCAGTGGGCGGGGCCCCTTGGGCCGTCGCCACCACTGTAGTCATGTACCCACCG
CCGCCGCCGCCGCCTCATCGGGACTTCATCTCGGTGACGCTGAGCTTTGGCGAGAGCTAT
GACAACAGCAAGAGTTGGCGGCGGCGCTCGTGCTGGAGGAAATGGAAGCAACTGTCGAGA
TTGCAGCGGAATATGATTCTCTTCCTCCTTGCCTTTCTGCTTTTCTGTGGACTCCTCTTC
TACATCAACTTGGCTGACCATTGGAAAGCTCTGGCTTTCAGGCTAGAGGAAGAGCAGAAG
ATGAGGCCAGAAATTGCTGGGTTAAAACCAGCAAATCCACCCGTCTTACCAGCTCCTCAG
AAGGCGGACACCGACCCTGAGAACTTACCTGAGATTTCGTCACAGAAGACACAAAGACAC
ATCCAGCGGGGACCACCTCACCTGCAGATTAGACCCCCAAGCCAAGACCTGAAGGATGGG
ACCCAGGAGGAGGCCACAAAAAGGCAAGAAGCCCCTGTGGATCCCCGCCCGGAAGGAGAT
CCGCAGAGGACAGTCATCAGCTGGAGGGGAGCGGTGATCGAGCCTGAGCAGGGCACCGAG
CTCCCTTCAAGAAGAGCAGAAGTGCCCACCAAGCCTCCCCTGCCACCGGCCAGGACACAG
GGCACACCAGTGCATCTGAACTATCGCCAGAAGGGCGTGATTGACGTCTTCCTGCATGCA
TGGAAAGGATACCGCAAGTTTGCATGGGGCCATGACGAGCTGAAGCCTGTGTCCAGGTCC
TTCAGTGAGTGGTTTGGCCTCGGTCTCACACTGATCGACGCGCTGGACACCATGTGGATC
TTGGGTCTGAGGAAAGAATTTGAGGAAGCCAGGAAGTGGGTGTCGAAGAAGTTACACTTT
GAAAAGGACGTGGACGTCAACCTGTTTGAGAGCACGATCCGCATCCTGGGGGGGCTCCTG
AGTGCCTACCACCTGTCTGGGGACAGCCTCTTCCTGAGGAAAGCTGAGGATTTTGGAAAT
CGGCTAATGCCTGCCTTCAGAACACCATCCAAGATTCCTTACTCGGATGTGAACATCGGT
ACTGGAGTTGCCCACCCGCCACGGTGGACCTCCGACAGCACTGTGGCCGAGGTGACCAGC
ATTCAGCTGGAGTTCCGGGAGCTCTCCCGTCTCACAGGGGATAAGAAGTTTCAGGAGGCA
GTGGAGAAGGTGACACAGCACATCCACGGCCTGTCTGGGAAGAAGGATGGGCTGGTGCCC
ATGTTCATCAATACCCACAGTGGCCTCTTCACCCACCTGGGCGTATTCACGCTGGGCGCC
AGGGCCGACAGCTACTATGAGTACCTGCTGAAGCAGTGGATCCAGGGCGGGAAGCAGGAG
ACACAGCTGCTGGAAGACTACGTGGAAGCCATCGAGGGTGTCAGAACGCACCTGCTGCGG
CACTCCGAGCCCAGTAAGCTCACCTTTGTGGGGGAGCTTGCCCACGGCCGCTTCAGTGCC
AAGATGGACCACCTGGTGTGCTTCCTGCCAGGGACGCTGGCTCTGGGCGTCTACCACGGC
CTGCCCGCCAGCCACATGGAGCTGGCCCAGGAGCTCATGGAGACTTGTTACCAGATGAAC
CGGCAGATGGAGACGGGGCTGAGTCCCGAGATCGTGCACTTCAACCTTTACCCCCAGCCG
GGCCGTCGGGACGTGGAGGTCAAGCCAGCAGACAGGCACAACCTGCTGCGGCCAGAGACC
GTGGAGAGCCTGTTCTACCTGTACCGCGTCACAGGGGACCGCAAATACCAGGACTGGGGC
TGGGAGATTCTGCAGAGCTTCAGCCGATTCACACGGGTCCCCTCGGGTGGCTATTCTTCC
ATCAACAATGTCCAGGATCCTCAGAAGCCCGAGCCTAGGGACAAGATGGAGAGCTTCTTC
CTGGGGGAGACGCTCAAGTATCTGTTCTTGCTCTTCTCCGATGACCCAAACCTGCTCAGC
CTGGACGCCTACGTGTTCAACACCGAAGCCCACCCTCTGCCTATCTGGACCCCTGCCTAG
Enzyme 8 GenBank Gene ID AF148509 Link Image
Enzyme 8 GeneCard ID MAN1B1 Link Image
Enzyme 8 GenAtlas ID MAN1B1 Link Image
Enzyme 8 HGNC ID HGNC:6823 Link Image
Enzyme 8 Chromosome Location 9
Enzyme 8 Locus 9q34
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Tremblay LO, Herscovics A: Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. Glycobiology. 1999 Oct;9(10):1073-8. [PubMed Link Image]
  2. Gonzalez DS, Karaveg K, Vandersall-Nairn AS, Lal A, Moremen KW: Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis. J Biol Chem. 1999 Jul 23;274(30):21375-86. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6152
Enzyme 9 Name Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
Enzyme 9 Synonyms
  1. Processing alpha-1,2-mannosidase IA
  2. Alpha-1,2-mannosidase IA
  3. Mannosidase alpha class 1A member 1
  4. Man(9-alpha-mannosidase
  5. Man9-mannosidase
Enzyme 9 Gene Name MAN1A1
Enzyme 9 Protein Sequence >Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
MPVGGLLPLFSSPAGGVLGGGLGGGGGRKGSGPAALRLTEKFVLLLVFSAFITLCFGAIF
FLPDSSKLLSGVLFHSSPALQPAADHKPGPGARAEDAAEGRARRREEGAPGDPEAALEDN
LARIRENHERALREAKETLQKLPEEIQRDILLEKKKVAQDQLRDKAPFRGLPPVDFVPPI
GVESREPADAAIREKRAKIKEMMKHAWNNYKGYAWGLNELKPISKGGHSSSLFGNIKGAT
IVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNAEISVFEVNIRFVGGLLSAYYLSGEEI
FRKKAVELGVKLLPAFHTPSGIPWALLNMKSGIGRNWPWASGGSSILAEFGTLHLEFMHL
SHLSGNPIFAEKVMNIRTVLNKLEKPQGLYPNYLNPSSGQWGQHHVSVGGLGDSFYEYLL
KAWLMSDKTDLEAKKMYFDAVQAIETHLIRKSSSGLTYIAEWKGGLLEHKMGHLTCFAGG
MFALGADAAPEGMAQHYLELGAEIARTCHESYNRTFMKLGPEAFRFDGGVEAIATRQNEK
YYILRPEVMETYMYMWRLTHDPKYRKWAWEAVEALENHCRVNGGYSGLRDVYLLHESYDD
VQQSFFLAETLKYLYLIFSDDDLLPLEHWIFNSEAHLLPILPKDKKEVEIREE
Enzyme 9 Number of Residues 653
Enzyme 9 Molecular Weight 72969
Enzyme 9 Theoretical pI 6.44
Enzyme 9 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • mannosidase activity
  • mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
  • mannosyl-oligosaccharide mannosidase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid N-linked glycosylation
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2)
Enzyme 9 Pathways
Enzyme 9 Reactions
  • Hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-19
Enzyme 9 Transmembrane Regions
  • 42-62
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 56202626 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P33908 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name MA1A1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1146 bp
AATGCTGAAATTTCTGTCTTTGAAGTAAATATACGCTTTGTTGGTGGACTACTCTCAGCC
TACTATCTGTCTGGAGAAGAGATTTTTCGAAAGAAAGCAGTGGAACTTGGGGTAAAATTG
CTACCTGCATTTCATACTCCCTCTGGAATACCTTGGGCATTGCTGAATATGAAAAGTGGT
ATTGGAAGGAACTGGCCCTGGGCCTCTGGAGGCAGCAGTATTCTGGCAGAATTTGGAACC
CTGCATTTGGAGTTTATGCACTTGAGCCACTTATCAGGAAACCCCATCTTTGCTGAAAAG
GTAATGAATATTCGAACAGTACTGAACAAACTGGAAAAACCACAAGGCCTTTATCCTAAC
TATCTGAATCCCAGTAGTGGACAGTGGGGTCAACATCATGTATCAGTTGGAGGACTTGGA
GACAGCTTCTATGAGTATTTGCTGAAGGCCTGGTTAATGTCTGACAAGACAGATCTGGAA
GCTAAGAAGATGTATTTTGATGCTGTTCAGGCTATCGAGACTCATTTGATCCGCAAGTCT
AGCAGCGGACTAACTTATATCGCAGAGTGGAAAGGGGGCCTCCTGGAGCACAAGATGGGC
CACCTGACCTGCTTCGCGGGGGGCATGTTCGCACTCGGGGCTGATGCAGCTCCCGAAGGC
ATGGCCCAACACTACCTTGAACTCGGGGCTGAAATTGCCCGTACTTGTCATGAATCATAT
AATCGAACATTTATGAAACTGGGACCAGAAGCTTTCAGATTTGATGGTGGTGTTGAAGCC
ATCGCTACAAGACAAAATGAAAAATACTACATCTTACGGCCAGAAGTTATGGAGACTTAC
ATGTATATGTGGAGACTGACTCATGATCCAAAGTACAGGAAATGGGCCTGGGAAGCCGTA
GAGGCCTTGGAAAACCATTGCAGAGTGAATGGAGGCTATTCAGGCCTAAGGGATGTTTAC
CTTCTTCATGAGAGTTATGATGATGTGCAGCAGAGTTTCTTCCTGGCAGAGACATTGAAA
TATTTGTACCTAATATTTTCTGACGACGATCTTCTTCCACTGGAGCATTGGATCTTCAAT
AGCGAGGCACATCTTCTCCCTATCCTCCCTAAAGATAAAAAGGAAGTTGAAATCAGAGAG
GAATAA
Enzyme 9 GenBank Gene ID AL022722 Link Image
Enzyme 9 GeneCard ID MAN1A1 Link Image
Enzyme 9 GenAtlas ID MAN1A1 Link Image
Enzyme 9 HGNC ID HGNC:6821 Link Image
Enzyme 9 Chromosome Location 6
Enzyme 9 Locus 6q22
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  2. Bause E, Bieberich E, Rolfs A, Volker C, Schmidt B: Molecular cloning and primary structure of Man9-mannosidase from human kidney. Eur J Biochem. 1993 Oct 15;217(2):535-40. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6927
Enzyme 10 Name Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
Enzyme 10 Synonyms
  1. Dol-P-Man-dependent alpha(1-3-mannosyltransferase
  2. Not56-like protein
Enzyme 10 Gene Name ALG3
Enzyme 10 Protein Sequence >Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
MAAGLRKRGRSGSAAQAEGLCKQWLQRAWQERRLLLREPRYTLLVAACLCLAEVGITFWV
IHRVAYTEIDWKAYMAEVEGVINGTYDYTQLQGDTGPLVYPAGFVYIFMGLYYATSRGTD
IRMAQNIFAVLYLATLLLVFLIYHQTCKVPPFVFFFMCCASYRVHSIFVLRLFNDPVAMV
LLFLSINLLLAQRWGWGCCFFSLAVSVKMNVLLFAPGLLFLLLTQFGFRGALPKLGICAG
LQVVLGLPFLLENPSGYLSRSFDLGRQFLFHWTVNWRFLPEALFLHRAFHLALLTAHLTL
LLLFALCRWHRTGESILSLLRDPSKRKVPPQPLTPNQIVSTLFTSNFIGICFSRSLHYQF
YVWYFHTLPYLLWAMPARWLTHLLRLLVLGLIELSWNTYPSTSCSSAALHICHAVILLQL
WLGPQPFPKSTQHSKKAH
Enzyme 10 Number of Residues 438
Enzyme 10 Molecular Weight 50127
Enzyme 10 Theoretical pI 9.69
Enzyme 10 GO Classification
Function
  • catalytic activity
  • mannosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • cell
  • endoplasmic reticulum
  • integral to membrane
  • intracellular membrane-bound organelle
  • intrinsic to membrane
  • membrane
  • membrane-bound organelle
  • organelle
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Adds the first Dol-P-Man derived mannose in an alpha 1,3 linkage to Man5GlcNAc2-PP-Dol
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 41-61 95-115 123-143 149-169 172-192 203-223 231-251 289-309 332-352 356-376 407-427
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 1654000 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q92685 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name ALG3_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1317 bp
ATGGCGGCTGGGCTGCGGAAACGCGGCCGGTCCGGTTCCGCGGCCCAGGCAGAGGGACTC
TGCAAGCAATGGCTGCAGCGCGCCTGGCAAGAGCGGCGCCTGCTGCTGCGGGAGCCGCGC
TACACGCTGCTGGTGGCCGCCTGCCTCTGCCTGGCGGAGGTGGGCATCACCTTCTGGGTC
ATTCACAGGGTGGCATACACAGAGATTGACTGGAAGGCCTACATGGCCGAGGTAGAAGGC
GTCATCAATGGTACCTATGACTATACCCAACTGCAGGGTGACACCGGACCACTTGTGTAC
CCAGCTGGTTTCGTGTACATCTTTATGGGGTTGTACTATGCCACCAGCCGAGGCACTGAC
ATCCGCATGGCCCAGAACATCTTTGCTGTGCTCTACCTGGCTACCTTGCTGCTTGTCTTC
TTGATCTATCACCAGACCTGCAAGGTACCTCCCTTCGTCTTTTTCTTCATGTGCTGCGCC
TCTTACCGTGTCCACTCCATCTTTGTGCTGCGGCTCTTCAATGACCCAGTGGCCATGGTG
CTGCTCTTCCTCAGTATCAACCTCCTGCTGGCCCAGCGCTGGGGCTGGGGCTGCTGCTTT
TTCAGCCTGGCAGTCTCTGTGAAGATGAATGTGCTGCTCTTCGCCCCTGGGTTACTGTTT
CTTCTCCTCACACAGTTTGGCTTCCGTGGGGCCCTCCCCAAGCTGGGAATCTGTGCTGGC
CTTCAGGTGGTGCTGGGGCTGCCCTTCCTGCTGGAGAACCCCAGCGGCTACCTGTCCCGC
TCCTTTGACCTTGGCCGCCAGTTTCTGTTCCACTGGACAGTGAACTGGCGCTTCCTCCCA
GAGGCGCTCTTCCTGCATCGAGCCTTCCACCTGGCCCTGTTGACTGCCCACCTCACCCTG
CTCCTGCTGTTTGCCCTCTGCAGGTGGCACAGGACAGGGGAAAGTATCTTGTCGCTGCTG
AGGGATCCCTCCAAAAGGAAGGTTCCACCCCAGCCCCTTACACCCAACCAGATCGTTTCT
ACCCTCTTCACCTCCAACTTCATTGGCATCTGCTTCAGCCGCTCCCTCCACTACCAGTTC
TACGTCTGGTATTTCCACACACTGCCCTACCTCCTGTGGGCCATGCCTGCACGGTGGCTC
ACACACCTGCTCAGGTTGTTGGTGCTGGGGCTCATCGAGCTCTCCTGGAACACATACCCT
TCCACATCCTGCAGCTCTGCTGCCCTGCACATATGCCATGCCGTCATCCTGCTGCAGCTC
TGGCTGGGCCCGCAGCCTTTCCCCAAGAGCACCCAACACAGCAAGAAAGCCCACTGA
Enzyme 10 GenBank Gene ID Y09022 Link Image
Enzyme 10 GeneCard ID ALG3 Link Image
Enzyme 10 GenAtlas ID ALG3 Link Image
Enzyme 10 HGNC ID HGNC:23056 Link Image
Enzyme 10 Chromosome Location 3
Enzyme 10 Locus 3q27.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Korner C, Knauer R, Stephani U, Marquardt T, Lehle L, von Figura K: Carbohydrate deficient glycoprotein syndrome type IV: deficiency of dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase. EMBO J. 1999 Dec 1;18(23):6816-22. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 7418
Enzyme 11 Name Glycophorin B precursor
Enzyme 11 Synonyms
  1. PAS-3
  2. Sialoglycoprotein delta
  3. SS-active sialoglycoprotein
  4. CD235b antigen
Enzyme 11 Gene Name GYPB
Enzyme 11 Protein Sequence >Glycophorin B precursor
MYGKIIFVLLLSEIVSISALSTTEVAMHTSTSSSVTKSYISSQTNGETGQLVHRFTVPAP
VVIILIILCVMAGIIGTILLISYTIRRLIKA
Enzyme 11 Number of Residues 91
Enzyme 11 Molecular Weight 9796
Enzyme 11 Theoretical pI 9.73
Enzyme 11 GO Classification
Function
Process
Component
  • cell
  • membrane
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function This protein is a minor sialoglycoprotein in erythrocyte membranes
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-19
Enzyme 11 Transmembrane Regions
  • 60-81
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 183313 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P06028 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name GLPB_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >276 bp
ATGTATGGAAAAATAATCTTTGTATTACTATTGTCAGAAATTGTGAGCATATCAGCATTA
AGTACCACTGAGGTGGCAATGCACACTTCAACCTCTTCTTCAGTCACAAAGAGTTACATC
TCATCACAGACAAATGGAGAAACGGGACAACTTGTCCATCGTTTCACTGTACCAGCTCCT
GTAGTGATAATACTCATTATTTTGTGTGTGATGGCTGGTATTATTGGAACGATCCTCTTA
ATTTCTTACACTATTCGCCGACTGATAAAGGCATGA
Enzyme 11 GenBank Gene ID J02982 Link Image
Enzyme 11 GeneCard ID GYPB Link Image
Enzyme 11 GenAtlas ID GYPB Link Image
Enzyme 11 HGNC ID HGNC:4703 Link Image
Enzyme 11 Chromosome Location 4
Enzyme 11 Locus 4q28-q31
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Siebert PD, Fukuda M: Molecular cloning of a human glycophorin B cDNA: nucleotide sequence and genomic relationship to glycophorin A. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6735-9. [PubMed Link Image]
  2. Tate CG, Tanner MJ: Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta. Biochem J. 1988 Sep 15;254(3):743-50. [PubMed Link Image]
  3. Kudo S, Fukuda M: Structural organization of glycophorin A and B genes: glycophorin B gene evolved by homologous recombination at Alu repeat sequences. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4619-23. [PubMed Link Image]
  4. Huang CH, Blumenfeld OO: Molecular genetics of human erythrocyte MiIII and MiVI glycophorins. Use of a pseudoexon in construction of two delta-alpha-delta hybrid genes resulting in antigenic diversification. J Biol Chem. 1991 Apr 15;266(11):7248-55. [PubMed Link Image]
  5. Blanchard D, Dahr W, Hummel M, Latron F, Beyreuther K, Cartron JP: Glycophorins B and C from human erythrocyte membranes. Purification and sequence analysis. J Biol Chem. 1987 Apr 25;262(12):5808-11. [PubMed Link Image]
  6. Dahr W, Beyreuther K, Moulds J, Unger P: Hybrid glycophorins from human erythrocyte membranes. I. Isolation and complete structural analysis of the hybrid sialoglycoprotein from Dantu-positive red cells of the N.E. variety. Eur J Biochem. 1987 Jul 1;166(1):31-6. [PubMed Link Image]
  7. Huang CH, Spruell P, Moulds JJ, Blumenfeld OO: Molecular basis for the human erythrocyte glycophorin specifying the Miltenberger class I (MiI) phenotype. Blood. 1992 Jul 1;80(1):257-63. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 11077
Enzyme 12 Name Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
Enzyme 12 Synonyms
  1. Processing alpha-1,2-mannosidase IC
  2. Alpha-1,2-mannosidase IC
  3. Mannosidase alpha class 1C member 1
  4. HMIC
Enzyme 12 Gene Name MAN1C1
Enzyme 12 Protein Sequence >Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
MLMRKVPGFVPASPWGLRLPQKFLFLLFLSGLVTLCFGALFLLPHSSRLKRLFLAPRTQQ
PGLEVVAEIAGHAPAREQEPPPNPAPAAPAPGEDDPSSWASPRRRKGGLRRTRPTGPREE
ATAARGNSIPASRPGDEGVPFRFDFNAFRSRLRHPVLGTRADESQEPQSQVRAQREKIKE
MMQFAWQSYKRYAMGKNELRPLTKDGYEGNMFGGLSGATVIDSLDTLYLMELKEEFQEAK
AWVGESFHLNVSGEASLFEVNIRYIGGLLSAFYLTGEEVFRIKAIRLGEKLLPAFNTPTG
IPKGVVSFKSGNWGWATAGSSSILAEFGSLHLEFLHLTELSGNQVFAEKVRNIRKVLRKI
EKPFGLYPNFLSPVSGNWVQHHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEA
IETYLLNVSPGGLTYIAEWRGGILDHKMGHLACFSGGMIALGAEDAKEEKRAHYRELAAQ
ITKTCHESYARSDTKLGPEAFWFNSGREAVATQLSESYYILRPEVVESYMYLWRQTHNPI
YREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDL
LSLEDWVFNTEAHPLPVNHSDSSGRAWGRH
Enzyme 12 Number of Residues 630
Enzyme 12 Molecular Weight 70911
Enzyme 12 Theoretical pI Not Available
Enzyme 12 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • mannosidase activity
  • mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
  • mannosyl-oligosaccharide mannosidase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid N-linked glycosylation
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Involved in the maturation of Asn-linked oligosaccharides. Trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce first Man(8)GlcNAc(2) then Man(6)GlcNAc and a small amount of Man(5)GlcNAc
Enzyme 12 Pathways
Enzyme 12 Reactions
  • H2O + (alpha-D-mannosyl)7-beta-D-mannosyl-diacetylchitobiosyl-L-asparagine, isoform A (protein) --> (alpha-D-mannosyl)6-beta-D-mannosyl-diacetylchitobiosyl-L-asparagine (protein) + D-Mannose
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 23-43
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 9664312 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9NR34 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name MA1C1_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 AF261655 Link Image
Enzyme 12 GeneCard ID Not Available
Enzyme 12 GenAtlas ID MAN1C1 Link Image
Enzyme 12 HGNC ID HGNC:19080 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Tremblay LO, Herscovics A: Characterization of a cDNA encoding a novel human Golgi alpha 1, 2-mannosidase (IC) involved in N-glycan biosynthesis. J Biol Chem. 2000 Oct 13;275(41):31655-60. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 15209
Enzyme 13 Name cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQGYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
Enzyme 13 Number of Residues 917
Enzyme 13 Molecular Weight 102388
Enzyme 13 Theoretical pI 6.70
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function Not Available
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 158257456 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID A8K7J7 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name A8K7J7_HUMAN Link Image
Enzyme 13 PDB ID 1HKB Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >2754 bp
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGGACGAATATTCCCTAAATGCTGGGAAACAAGGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGCTGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
Enzyme 13 GenBank Gene ID AK292012 Link Image
Enzyme 13 GeneCard ID A8K7J7 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs Not Available
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 15260
Enzyme 14 Name N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
Enzyme 14 Synonyms
  1. GlcNAc-1-phosphotransferase subunits alpha/beta
  2. Stealth protein GNPTAB
  3. UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
  4. Contains: RecName: N-acetylglucosamine-1-phosphotransferase subunit alpha
  5. Contains: RecName: N-acetylglucosamine-1-phosphotransferase subunit beta
Enzyme 14 Gene Name GNPTAB
Enzyme 14 Protein Sequence >N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
MLFKLLQRQTYTCLSHRYGLYVCFLGVVVTIVSAFQFGEVVLEWSRDQYHVLFDSYRDNI
AGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELQQVREQMEEEQKAMREILGKNTTEPTK
KSEKQLECLLTHCIKVPMLVLDPALPANITLKDLPSLYPSFHSASDIFNVAKPKNPSTNV
SVVVFDSTKDVEDAHSGLLKGNSRQTVWRGYLTTDKEVPGLVLMQDLAFLSGFPPTFKET
NQLKTKLPENLSSKVKLLQLYSEASVALLKLNNPKDFQELNKQTKKNMTIDGKELTISPA
YLLWDLSAISQSKQDEDISASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNL
DNPRVTIVTHQDVFRNLSHLPTFSSPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDF
YSHSKGQKVYLTWPVPNCAEGCPGSWIKDGYCDKACNNSACDWDGGDCSGNSGGSRYIAG
GGGTGSIGVGQPWQFGGGINSVSYCNQGCANSWLADKFCDQACNVLSCGFDAGDCGQDHF
HELYKVILLPNQTHYIIPKGECLPYFSFAEVAKRGVEGAYSDNPIIRHASIANKWKTIHL
IMHSGMNATTIHFNLTFQNTNDEEFKMQITVEVDTREGPKLNSTAQKGYENLVSPITLLP
EAEILFEDIPKEKRFPKFKRHDVNSTRRAQEEVKIPLVNISLLPKDAQLSLNTLDLQLEH
GDITLKGYNLSKSALLRSFLMNSQHAKIKNQAIITDETNDSLVAPQEKQVHKSILPNSLG
VSERLQRLTFPAVSVKVNGHDQGQNPPLDLETTARFRVETHTQKTIGGNVTKEKPPSLIV
PLESQMTKEKKITGKEKENSRMEENAENHIGVTEVLLGRKLQHYTDSYLGFLPWEKKKYF
QDLLDEEESLKTQLAYFTDSKNTGRQLKDTFADSLRYVNKILNSKFGFTSRKVPAHMPHM
IDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFDEVDTD
QSGVLSDREIRTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYD
PNLPPVTKSLVTNCKPVTDKIHKAYKDKNKYRFEIMGEEEIAFKMIRTNVSHVVGQLDDI
RKNPRKFVCLNDNIDHNHKDAQTVKAVLRDFYESMFPIPSQFELPREYRNRFLHMHELQE
WRAYRDKLKFWTHCVLATLIMFTIFSFFAEQLIALKRKIFPRRRIHKEASPNRIRV
Enzyme 14 Number of Residues 1256
Enzyme 14 Molecular Weight 143623
Enzyme 14 Theoretical pI 7.17
Enzyme 14 GO Classification
Function
  • binding
  • calcium ion binding
  • cation binding
  • ion binding
  • protein binding
  • transcription factor binding
Process
  • cell differentiation
  • cellular process
Component
  • cell
  • intracellular membrane-bound organelle
  • membrane
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • 22-42 1215-1235
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 74474848 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q3T906 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name GNPTA_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >3771 bp
ATGCTGTTCAAGCTCCTGCAGAGACAGACCTATACCTGCCTGTCCCACAGGTATGGGCTC
TACGTGTGCTTCTTGGGCGTCGTTGTCACCATCGTCTCCGCCTTCCAGTTCGGAGAGGTG
GTTCTGGAATGGAGCCGAGATCAATACCATGTTTTGTTTGATTCCTATAGAGACAATATT
GCTGGAAAGTCCTTTCAGAATCGGCTTTGTCTGCCCATGCCGATTGACGTTGTTTACACC
TGGGTGAATGGCACAGATCTTGAACTACTGAAGGAACTACAGCAGGTCAGAGAACAGATG
GAGGAGGAGCAGAAAGCAATGAGAGAAATCCTTGGGAAAAACACAACGGAACCTACTAAG
AAGAGTGAGAAGCAGTTAGAGTGTTTGCTAACACACTGCATTAAGGTGCCAATGCTTGTC
CTGGACCCAGCCCTGCCAGCCAACATCACCCTGAAGGACCTGCCATCTCTTTATCCTTCT
TTTCATTCTGCCAGTGACATTTTCAATGTTGCAAAACCAAAAAACCCTTCTACCAATGTC
TCAGTTGTTGTTTTTGACAGTACTAAGGATGTTGAAGATGCCCACTCTGGACTGCTTAAA
GGAAATAGCAGACAGACAGTATGGAGGGGCTACTTGACAACAGATAAAGAAGTCCCTGGA
TTAGTGCTAATGCAAGATTTGGCTTTCCTGAGTGGATTTCCACCAACATTCAAGGAAACA
AATCAACTAAAAACAAAATTGCCAGAAAATCTTTCCTCTAAAGTCAAACTGTTGCAGTTG
TATTCAGAGGCCAGTGTAGCGCTTCTAAAACTGAATAACCCCAAGGATTTTCAAGAATTG
AATAAGCAAACTAAGAAGAACATGACCATTGATGGAAAAGAACTGACCATAAGTCCTGCA
TATTTATTATGGGATCTGAGCGCCATCAGCCAGTCTAAGCAGGATGAAGACATCTCTGCC
AGTCGTTTTGAAGATAACGAAGAACTGAGGTACTCATTGCGATCTATCGAGAGGCATGCA
CCATGGGTTCGGAATATTTTCATTGTCACCAACGGGCAGATTCCATCCTGGCTGAACCTT
GACAATCCTCGAGTGACAATAGTAACACACCAGGATGTTTTTCGAAATTTGAGCCACTTG
CCTACCTTTAGTTCACCTGCTATTGAAAGTCACATTCATCGCATCGAAGGGCTGTCCCAG
AAGTTTATTTACCTAAATGATGATGTCATGTTTGGGAAGGATGTCTGGCCAGATGATTTT
TACAGTCACTCCAAAGGCCAGAAGGTTTATTTGACATGGCCTGTGCCAAACTGTGCCGAG
GGCTGCCCAGGTTCCTGGATTAAGGATGGCTATTGTGACAAGGCTTGTAATAATTCAGCC
TGCGATTGGGATGGTGGGGATTGCTCTGGAAACAGTGGAGGGAGTCGCTATATTGCAGGA
GGTGGAGGTACTGGGAGTATTGGAGTTGGACAGCCCTGGCAGTTTGGTGGAGGAATAAAC
AGTGTCTCTTACTGTAATCAGGGATGTGCGAATTCCTGGCTCGCTGATAAGTTCTGTGAC
CAAGCATGCAATGTCTTGTCCTGTGGGTTTGATGCTGGCGACTGTGGGCAAGATCATTTT
CATGAATTGTATAAAGTGATCCTTCTCCCAAACCAGACTCACTATATTATTCCAAAAGGT
GAATGCCTGCCTTATTTCAGCTTTGCAGAAGTAGCCAAAAGAGGAGTTGAAGGTGCCTAT
AGTGACAATCCAATAATTCGACATGCTTCTATTGCCAACAAGTGGAAAACCATCCACCTC
ATAATGCACAGTGGAATGAATGCCACCACAATACATTTTAATCTCACGTTTCAAAATACA
AACGATGAAGAGTTCAAAATGCAGATAACAGTGGAGGTGGACACAAGGGAGGGACCAAAA
CTGAATTCTACAGCCCAGAAGGGTTACGAAAATTTAGTTAGTCCCATAACACTTCTTCCA
GAGGCGGAAATCCTTTTTGAGGATATTCCCAAAGAAAAACGCTTCCCGAAGTTTAAGAGA
CATGATGTTAACTCAACAAGGAGAGCCCAGGAAGAGGTGAAAATTCCCCTGGTAAATATT
TCACTCCTTCCAAAAGACGCCCAGTTGAGTCTCAATACCTTGGATTTGCAACTGGAACAT
GGAGACATCACTTTGAAAGGATACAATTTGTCCAAGTCAGCCTTGCTGAGATCATTTCTG
ATGAACTCACAGCATGCTAAAATAAAAAATCAAGCTATAATAACAGATGAAACAAATGAC
AGTTTGGTGGCTCCACAGGAAAAACAGGTTCATAAAAGCATCTTGCCAAACAGCTTAGGA
GTGTCTGAAAGATTGCAGAGGTTGACTTTTCCTGCAGTGAGTGTAAAAGTGAATGGTCAT
GACCAGGGTCAGAATCCACCCCTGGACTTGGAGACCACAGCAAGATTTAGAGTGGAAACT
CACACCCAAAAAACCATAGGCGGAAATGTGACAAAAGAAAAGCCCCCATCTCTGATTGTT
CCACTGGAAAGCCAGATGACAAAAGAAAAGAAAATCACAGGGAAAGAAAAAGAGAACAGT
AGAATGGAGGAAAATGCTGAAAATCACATAGGCGTTACTGAAGTGTTACTTGGAAGAAAG
CTGCAGCATTACACAGATAGTTACTTGGGCTTTTTGCCATGGGAGAAAAAAAAGTATTTC
CAAGATCTTCTCGACGAAGAAGAGTCATTGAAGACACAATTGGCATACTTCACTGATAGC
AAAAATACTGGGAGGCAACTAAAAGATACATTTGCAGATTCCCTCAGATATGTAAATAAA
ATTCTAAATAGCAAGTTTGGATTCACATCGCGGAAAGTCCCTGCTCACATGCCTCACATG
ATTGACCGGATTGTTATGCAAGAACTGCAAGATATGTTCCCTGAAGAATTTGACAAGACG
TCATTTCACAAAGTGCGCCATTCTGAGGATATGCAGTTTGCCTTCTCTTATTTTTATTAT
CTCATGAGTGCAGTGCAGCCACTGAATATATCTCAAGTCTTTGATGAAGTTGATACAGAT
CAATCTGGTGTCTTGTCTGACAGAGAAATCCGAACACTGGCTACCAGAATTCACGAACTG
CCGTTAAGTTTGCAGGATTTGACAGGTCTGGAACACATGCTAATAAATTGCTCAAAAATG
CTTCCTGCTGATATCACGCAGCTAAATAATATTCCACCAACTCAGGAATCCTACTATGAT
CCCAACCTGCCACCGGTCACTAAAAGTCTAGTAACAAACTGTAAACCAGTAACTGACAAA
ATCCACAAAGCATATAAGGACAAAAACAAATATAGGTTTGAAATCATGGGAGAAGAAGAA
ATCGCTTTTAAAATGATTCGTACCAACGTTTCTCATGTGGTTGGCCAGTTGGATGACATA
AGAAAAAACCCTAGGAAGTTTGTTTGCCTGAATGACAACATTGACCACAATCATAAAGAT
GCTCAGACAGTGAAGGCTGTTCTCAGGGACTTCTATGAATCCATGTTCCCCATACCTTCC
CAATTTGAACTGCCAAGAGAGTATCGAAACCGTTTCCTTCATATGCATGAGCTGCAGGAA
TGGAGGGCTTATCGAGACAAATTGAAGTTTTGGACCCATTGTGTACTAGCAACATTGATT
ATGTTTACTATATTCTCATTTTTTGCTGAGCAGTTAATTGCACTTAAGCGGAAGATATTT
CCCAGAAGGAGGATACACAAAGAAGCTAGTCCCAATCGAATCAGAGTATAG
Enzyme 14 GenBank Gene ID AM085438 Link Image
Enzyme 14 GeneCard ID Q3T906 Link Image
Enzyme 14 GenAtlas ID GNPTAB Link Image
Enzyme 14 HGNC ID HGNC:29670 Link Image
Enzyme 14 Chromosome Location 12
Enzyme 14 Locus 12q23.2
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed Link Image]
  2. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available