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Human Metabolome Database Version 2.5

 

Showing metabocard for Mannose 6-phosphate (HMDB01078)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-18 00:48:41
Accession Number HMDB01078
Secondary Accession Numbers Not Available
Common Name Mannose 6-phosphate
Description Mannose-6-phosphate is a potent competitive inhibitor of pinocytosis of human platelet beta-glucuronidase and it is a necessary component of the recognition marker on the enzyme for pinocytosis by human fibroblasts as well (PMID 908752).
Synonyms
  1. D-Mannose 6-phosphate
  2. Man-6-p
  3. Mannose 6-phosphate
  4. Mannose 6-phosphic acid
  5. Mannose-6-phosphate
  6. alpha-D-mannose-6-P
  7. alpha-D-mannose-6-phosphate
  8. delta-Mannose 6-phosphate
  9. alpha-delta-mannose-6-P
  10. alpha-delta-mannose-6-phosphate
Chemical IUPAC Name [(2R,3R,4S,5S)-3,4,5,6-tetrahydroxyoxan-2-yl]methoxyphosphonic acid
Chemical Formula C6H13O9P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Sugar Phosphates
Sub Class
  • Monosaccharide phosphates
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • secondary alcohol
  • 1,2-diol
  • phosphoric acid ester
  • heterocyclic compound
Biofunction
  • Component of Fructose and mannose metabolism
Application
Source
  • Endogenous
Average Molecular Weight 260.136
Monoisotopic Molecular Weight 260.029724
Isomeric SMILES O[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H](O)[C@@H]1O
Canonical SMILES OC1OC(COP(O)(O)=O)C(O)C(O)C1O
KEGG Compound ID C00275 Link Image
BioCyc ID MANNOSE-6P Link Image
BiGG ID 34471 Link Image
Wikipedia Link Mannose 6-phosphate Link Image
NuGOwiki Link HMDB01078 Link Image
Metagene Link HMDB01078 Link Image
METLIN ID 5987 Link Image
PubChem Compound 65127 Link Image
PubChem Substance 207092 Link Image
ChEBI ID 17369 Link Image
CAS Registry Number 3672-15-9
InChI Identifier InChI=1/C6H13O9P/c7-3-2(1-14-16(11,12)13)15-6(10)5(9)4(3)8/h2-10H,1H2,(H2,11,12,13)/t2-,3-,4+,5+,6-/m1/s1
Synthesis Reference Pascual, C.; Herrera, L. Use of permeabilized yeast cells as a system of enzyme immobilization. Its use for the preparation of mannose 6-phosphate. Folia Microbiologica (Prague, Czech Republic) (1981), 26(2), 103-6.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 31.400002 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.06 [Predicted by ALOGPS]; -3.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
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 (Predicted from LogP)
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts
Intestine
Liver
Spleen
Testes
Concentrations (Normal) Not Available
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
General References
  1. Beljaars L, Molema G, Weert B, Bonnema H, Olinga P, Groothuis GM, Meijer DK, Poelstra K: Albumin modified with mannose 6-phosphate: A potential carrier for selective delivery of antifibrotic drugs to rat and human hepatic stellate cells. Hepatology. 1999 May;29(5):1486-93. [PubMed Link Image]
  2. van der Ploeg AT, van der Kraaij AM, Willemsen R, Kroos MA, Loonen MC, Koster JF, Reuser AJ: Rat heart perfusion as model system for enzyme replacement therapy in glycogenosis type II. Pediatr Res. 1990 Oct;28(4):344-7. [PubMed Link Image]
  3. 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]
  4. Yatziv S, Barfi G, Newburg DS: Lysosomal hydrolases in blood-derived macrophages of patients with I-cell disease. J Lab Clin Med. 1986 Oct;108(4):365-8. [PubMed Link Image]
  5. Tiede S, Muschol N, Reutter G, Cantz M, Ullrich K, Braulke T: Missense mutations in N-acetylglucosamine-1-phosphotransferase alpha/beta subunit gene in a patient with mucolipidosis III and a mild clinical phenotype. Am J Med Genet A. 2005 Sep 1;137(3):235-40. [PubMed Link Image]
  6. Puolakkainen M, Kuo CC, Campbell LA: Chlamydia pneumoniae uses the mannose 6-phosphate/insulin-like growth factor 2 receptor for infection of endothelial cells. Infect Immun. 2005 Aug;73(8):4620-5. [PubMed Link Image]
  7. Holtta-Vuori M, Maatta J, Ullrich O, Kuismanen E, Ikonen E: Mobilization of late-endosomal cholesterol is inhibited by Rab guanine nucleotide dissociation inhibitor. Curr Biol. 2000 Jan 27;10(2):95-8. [PubMed Link Image]
  8. Harper J, Burns JL, Foulstone EJ, Pignatelli M, Zaina S, Hassan AB: Soluble IGF2 receptor rescues Apc(Min/+) intestinal adenoma progression induced by Igf2 loss of imprinting. Cancer Res. 2006 Feb 15;66(4):1940-8. [PubMed Link Image]
  9. Saris JJ, Derkx FH, De Bruin RJ, Dekkers DH, Lamers JM, Saxena PR, Schalekamp MA, Jan Danser AH: High-affinity prorenin binding to cardiac man-6-P/IGF-II receptors precedes proteolytic activation to renin. Am J Physiol Heart Circ Physiol. 2001 Apr;280(4):H1706-15. [PubMed Link Image]
  10. Bird CH, Sun J, Ung K, Karambalis D, Whisstock JC, Trapani JA, Bird PI: Cationic sites on granzyme B contribute to cytotoxicity by promoting its uptake into target cells. Mol Cell Biol. 2005 Sep;25(17):7854-67. [PubMed Link Image]
  11. Adrian JE, Poelstra K, Scherphof GL, Molema G, Meijer DK, Reker-Smit C, Morselt HW, Kamps JA: Interaction of targeted liposomes with primary cultured hepatic stellate cells: Involvement of multiple receptor systems. J Hepatol. 2006 Mar;44(3):560-7. Epub 2005 Oct 19. [PubMed Link Image]
  12. Ullrich K, Basner R, Gieselmann V, Von Figura K: Recognition of human urine alpha-N-acetylglucosaminidase by rat hepatocytes. Involvement of receptors specific for galactose, mannose 6-phosphate and mannose. Biochem J. 1979 May 15;180(2):413-9. [PubMed Link Image]
  13. Davis JA, Wu XH, Wang L, DeRossi C, Westphal V, Wu R, Alton G, Srikrishna G, Freeze HH: Molecular cloning, gene organization, and expression of mouse Mpi encoding phosphomannose isomerase. Glycobiology. 2002 Jul;12(7):435-42. [PubMed Link Image]
  14. Kaplan A, Fischer D, Achord D, Sly W: Phosphohexosyl recognition is a general characteristic of pinocytosis of lysosomal glycosidases by human fibroblasts. J Clin Invest. 1977 Nov;60(5):1088-93. [PubMed Link Image]
  15. Lobel P, Dahms NM, Breitmeyer J, Chirgwin JM, Kornfeld S: Cloning of the bovine 215-kDa cation-independent mannose 6-phosphate receptor. Proc Natl Acad Sci U S A. 1987 Apr;84(8):2233-7. [PubMed Link Image]
  16. Maguchi S, Taniguchi N, Makita A: Elevated activity and increased mannose-6-phosphate in the carbohydrate moiety of cathepsin D from human hepatoma. Cancer Res. 1988 Jan 15;48(2):362-7. [PubMed Link Image]
  17. Sleat DE, Wang Y, Sohar I, Lackland H, Li Y, Li H, Zheng H, Lobel P: Identification and validation of mannose 6-phosphate glycoproteins in human plasma reveal a wide range of lysosomal and non-lysosomal proteins. Mol Cell Proteomics. 2006 Oct;5(10):1942-56. Epub 2006 May 17. [PubMed Link Image]
  18. Sleat DE, Sohar I, Lackland H, Majercak J, Lobel P: Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including lysosomal enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis. J Biol Chem. 1996 Aug 9;271(32):19191-8. [PubMed Link Image]
  19. Wikipedia Link Image
Metabolic Enzymes
  1. Glucokinase
  2. Hexokinase-3
  3. Hexokinase-2
  4. Hexokinase-1
  5. Phosphomannomutase 1
  6. Mannose-6-phosphate receptor-binding protein 1
  7. Cation-dependent mannose-6-phosphate receptor precursor
  8. Cation-independent mannose-6-phosphate receptor precursor
  9. Phosphoglucomutase-2
  10. cDNA FLJ76937, highly similar to Homo sapiens mannose phosphate isomerase
  11. cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
  12. cDNA FLJ75943, highly similar to Homo sapiens phosphomannomutase 1 (PMM1), mRNA (Phosphomannomutase 1, isoform CRA_a)
  13. cDNA FLJ78512, highly similar to Homo sapiens phosphomannomutase 2 (PMM2), mRNA (Phosphomannomutase 2, isoform CRA_b)
  14. Phosphofurin acidic cluster sorting protein 1
  15. Sortilin
  16. Kinesin-like protein KIF13A
  17. WD repeat domain phosphoinositide-interacting protein 1
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 6931
Enzyme 5 Name Phosphomannomutase 1
Enzyme 5 Synonyms
  1. PMM 1
  2. PMMH-22
Enzyme 5 Gene Name PMM1
Enzyme 5 Protein Sequence >Phosphomannomutase 1
MAVTAQAARRKERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIA
EQLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLR
LPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLR
FSRGGMISFDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSV
VSPQDTVQRCREIFFPETAHEA
Enzyme 5 Number of Residues 262
Enzyme 5 Molecular Weight 29747
Enzyme 5 Theoretical pI 5.47
Enzyme 5 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
  • phosphomannomutase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • hexose metabolism
  • mannose biosynthesis
  • mannose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions
Enzyme 5 Pathways
Enzyme 5 Reactions
  • alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1655855 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q92871 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PMM1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >789 bp
ATGGCAGTCACCGCCCAGGCAGCCCGCAGAAGGGAGCGCGTCCTCTGCCTGTTTGACGTG
GACGGGACCCTCACGCCGGCTCGCCAGAAAATTGACCCTGAGGTGGCCGCCTTCCTGCAG
AAGCTACGAAGTAGAGTGCAGATCGGTGTGGTGGGCGGCTCTGACTACTGTAAGATCGCT
GAGCAGCTGGGTGACGGGGATGAAGTCATTGAGAAGTTTGATTATGTGTTTGCCGAGAAC
GGGACGGTGCAGTATAAGCACGGACGACTGCTCTCCAAGCAGACCATCCAGAACCACCTG
GGGGAGGAGCTGCTGCAGGACTTGATCAACTTCTGCCTCAGCTACATGGCCCTGCTCAGG
CTGCCCAAGAAGCGTGGAACCTTCATCGAGTTCCGGAATGGCATGCTGAACATCTCGCCC
ATCGGCCGGAGCTGCACCCTGGAGGAGAGGATCGAGTTCTCCGAACTGGACAAGAAAGAG
AAGATCCGGGAGAAGTTCGTGGAAGACCTGAAAACAGAGTTTGCTGGCAAAGGGCTGAGG
TTCTCTCGAGGAGGCATGATCAGCTTTGACGTCTTCCCCGAGGGCTGGGACAAGCGCTAC
TGCCTGGATAGCCTGGACCAGGACAGCTTCGACACCATCCACTTCTTTGGGAACGAGACT
AGCCCTGGTGGGAACGACTTTGAGATCTTTGCCGACCCCCGGACTGTTGGCCACAGCGTG
GTGTCTCCTCAGGACACGGTGCAGCGATGCCGGGAGATTTTCTTCCCAGAGACAGCTCAT
GAGGCGTGA
Enzyme 5 GenBank Gene ID U62526 Link Image
Enzyme 5 GeneCard ID PMM1 Link Image
Enzyme 5 GenAtlas ID PMM1 Link Image
Enzyme 5 HGNC ID HGNC:9114 Link Image
Enzyme 5 Chromosome Location 22
Enzyme 5 Locus 22q13.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Matthijs G, Schollen E, Pirard M, Budarf ML, Van Schaftingen E, Cassiman JJ: PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is localized on chromosome 22q13. Genomics. 1997 Feb 15;40(1):41-7. [PubMed Link Image]
  2. Wada Y, Sakamoto M: Isolation of the human phosphomannomutase gene (PMM1) and assignment to chromosome 22q13. Genomics. 1997 Feb 1;39(3):416-7. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 7102
Enzyme 6 Name Mannose-6-phosphate receptor-binding protein 1
Enzyme 6 Synonyms
  1. Cargo selection protein TIP47
  2. 47 kDa mannose 6-phosphate receptor-binding protein
  3. 47 kDa MPR-binding protein
  4. Placental protein 17
  5. PP17
Enzyme 6 Gene Name M6PRBP1
Enzyme 6 Protein Sequence >Mannose-6-phosphate receptor-binding protein 1
MSADGAEADGSTQVTVEEPVQQPSVVDRVASMPLISSTCDMVSAAYASTKESYPHIKTVC
DAAEKGVRTLTAAAVSGAQPILSKLEPQIASASEYAHRGLDKLEENLPILQQPTEKVLAD
TKELVSSKVSGAQEMVSSAKDTVATQLSEAVDATRGAVQSGVDKTKSVVTGGVQSVMGSR
LGQMVLSGVDTVLGKSEEWADNHLPLTDAELARIATSLDGFDVASVQQQRQEQSYFVRLG
SLSERLRQHAYEHSLGKLRATKQRAQEALLQLSQALSLMETVKQGVDQKLVEGQEKLHQM
WLSWNQKQLQGPEKEPPKPEQVESRALTMFRDIAQQLQATCTSLGSSIQGLPTNVKDQVQ
QARRQVEDLQATFSSIHSFQDLSSSILAQSRERVASAREALDHMVEYVAQNTPVTWLVGP
FAPGITEKAPEEKK
Enzyme 6 Number of Residues 434
Enzyme 6 Molecular Weight 47047
Enzyme 6 Theoretical pI 5.11
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 3095186 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O60664 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name M6PBP_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1305 bp
ATGTCTGCCGACGGGGCAGAGGCTGATGGCAGCACCCAGGTGACAGTGGAAGAACCGGTA
CAGCAGCCCAGTGTGGTGGACCGTGTGGCCAGCATGCCTCTGATCAGCTCCACCTGCGAC
ATGGTGTCCGCAGCCTATGCCTCCACCAAGGAGAGCTACCCGCACGTCAAGACTGTCTGC
GACGCAGCAGAGAAGGGAGTGAGGACCCTCACGGCGGCTGCTGTCAGCGGGGCTCAGCCG
ATCCTCTCCAAGCTGGAGCCCCAGATTGCATCAGCCAGCGAATACGCCCACAGGGGGCTG
GACAAGTTGGAGGAGAACCTCCCCATCCTGCAGCAGCCCACGGAGAAGGTCCTGGCGGAC
ACCAAGGAGCTTGTGTCGTCTAAGGTGTCGGGGGCCCAAGAGATGGTGTCTAGCGCCAAG
GACACGGTGGCCACCCAATTGTCGGAGGCGGTGGACGCGACCCGCGGTGCTGTGCAGAGC
GGCGTGGACAAGACAAAGTCCGTAGTGACCGGCGGCGTCCAATCAGTCATGGGCTCCCGC
TTGGGCCAGATGGTGCTGAGTGGGGTCGACACGGTGCTGGGGAAGTCGGAGGAGTGGGCG
GACAACCACCTGCCCCTTACGGATGCCGAACTGGCCCGCATCGCCACATCCCTGGATGGC
TTCGACGTCGCGTCCGTGCAGCAGCAGCGGCAGGAACAGAGCTACTTCGTACGTCTGGGC
TCCCTGTCGGAGAGGCTGCGGCAGCACGCCTATGAGCACTCGCTGGGCAAGCTTCGAGCC
ACCAAGCAGAGGGCACAGGAGGCTCTGCTGCAGCTGTCGCAGGCCCTAAGCCTGATGGAA
ACTGTCAAGCAAGGCGTTGATCAGAAGCTGGTGGAAGGCCAGGAGAAGCTGCACCAGATG
TGGCTCAGCTGGAACCAGAAGCAGCTCCAGGGCCCCGAGAAGGAGCCGCCCAAGCCAGAG
CAGGTCGAGTCCCGGGCGCTCACCATGTTCCGGGACATTGCCCAGCAACTGCAGGCCACC
TGTACCTCCCTGGGGTCCAGCATTCAGGGCCTCCCCACCAATGTGAAGGACCAGGTGCAG
CAGGCCCGCCGCCAGGTGGAGGACCTCCAGGCCACGTTTTCCAGCATCCACTCCTTCCAG
GACCTGTCCAGCAGCATTCTGGCCCAGAGCCGTGAGCGTGTCGCCAGCGCCCGCGAGGCC
CTGGACCACATGGTGGAATATGTGGCCCAGAACACACCTGTCACGTGGCTCGTGGGACCC
TTTGCCCCTGGAATCACTGAGAAAGCCCCGGAGGAGAAGAAATAG
Enzyme 6 GenBank Gene ID AF057140 Link Image
Enzyme 6 GeneCard ID M6PRBP1 Link Image
Enzyme 6 GenAtlas ID M6PRBP1 Link Image
Enzyme 6 HGNC ID HGNC:16893 Link Image
Enzyme 6 Chromosome Location 19
Enzyme 6 Locus 19p13.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Diaz E, Pfeffer SR: TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking. Cell. 1998 May 1;93(3):433-43. [PubMed Link Image]
  2. Than NG, Sumegi B, Than GN, Kispal G, Bohn H: Cloning and sequence analysis of cDNAs encoding human placental tissue protein 17 (PP17) variants. Eur J Biochem. 1998 Dec 1;258(2):752-7. [PubMed Link Image]
  3. Than NG, Sumegi B, Than GN, Kispal G, Bohn H: Cloning and sequencing of human oncodevelopmental soluble placental tissue protein 17 (PP17): homology with adipophilin and the mouse adipose differentiation-related protein. Tumour Biol. 1999 Jul-Aug;20(4):184-92. [PubMed Link Image]
  4. Bohn H, Kraus W, Winckler W: Purification and characterization of two new soluble placental tissue proteins (PP13 and PP17). Oncodev Biol Med. 1983;4(5):343-50. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 7104
Enzyme 7 Name Cation-dependent mannose-6-phosphate receptor precursor
Enzyme 7 Synonyms
  1. CD Man-6-P receptor
  2. CD-MPR
  3. 46 kDa mannose 6-phosphate receptor
  4. MPR 46
Enzyme 7 Gene Name M6PR
Enzyme 7 Protein Sequence >Cation-dependent mannose-6-phosphate receptor precursor
MFPFYSCWRTGLLLLLLAVAVRESWQTEEKTCDLVGEKGKESEKELALVKRLKPLFNKSF
ESTVGQGSDTYIYIFRVCREAGNHTSGAGLVQINKSNGKETVVGRLNETHIFNGSNWIML
IYKGGDEYDNHCGKEQRRAVVMISCNRHTLADNFNPVSEERGKVQDCFYLFEMDSSLACS
PEISHLSVGSILLVTFASLVAVYVVGGFLYQRLVVGAKGMEQFPHLAFWQDLGNLVADGC
DFVCRSKPRNVPAAYRGVGDDQLGEESEERDDHLLPM
Enzyme 7 Number of Residues 277
Enzyme 7 Molecular Weight 30994
Enzyme 7 Theoretical pI 5.64
Enzyme 7 GO Classification
Function
  • binding
  • carbohydrate binding
  • carbohydrate transporter activity
  • hexose transporter activity
  • mannose binding
  • mannose transporter activity
  • monosaccharide binding
  • monosaccharide transporter activity
  • sugar binding
  • sugar transporter activity
  • transporter activity
Process
  • carbohydrate transport
  • cellular physiological process
  • hexose transport
  • mannose transport
  • monosaccharide transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intracellular membrane-bound organelle
  • intrinsic to membrane
  • lytic vacuole
  • membrane
  • membrane-bound organelle
  • organelle
  • vacuole
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6- phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-26
Enzyme 7 Transmembrane Regions
  • 186-210
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 307147 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P20645 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name MPRD_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >834 bp
ATGTTCCCTTTCTACAGCTGCTGGAGGACTGGACTGCTACTACTACTCCTGGCTGTGGCA
GTGAGAGAATCCTGGCAGACAGAAGAAAAAACTTGCGACTTGGTAGGAGAAAAGGGTAAA
GAGTCAGAGAAAGAGTTGGCTCTAGTGAAGAGGCTGAAACCACTGTTTAATAAAAGCTTT
GAGAGCACTGTGGGCCAGGGTTCAGACACATACATCTACATCTTCAGGGTGTGCCGGGAA
GCTGGCAACCACACTTCTGGGGCAGGCCTGGTGCAAATCAACAAAAGTAATGGGAAGGAG
ACAGTGGTAGGGAGACTCAACGAGACTCACATCTTCAACGGAAGTAATTGGATCATGCTG
ATCTATAAAGGGGGTGATGAATATGACAACCACTGTGGCAAGGAGCAGCGTCGTGCAGTG
GTGATGATCTCCTGCAATCGACACACCCTAGCGGACAATTTTAACCCTGTGTCTGAGGAG
CGTGGCAAAGTCCAAGATTGTTTCTACCTCTTTGAGATGGATAGCAGCCTGGCCTGTTCA
CCAGAGATCTCCCACCTCAGTGTGGGTTCCATCTTACTTGTCACGTTTGCATCACTGGTT
GCTGTTTATGTTGTTGGGGGGTTCCTATACCAGCGACTGGTAGTGGGAGCCAAAGGAATG
GAGCAGTTTCCCCACTTAGCCTTCTGGCAGGATCTTGGCAACCTGGTAGCAGATGGCTGT
GACTTTGTCTGCCGTTCTAAACCTCGAAATGTGCCTGCAGCATATCGTGGTGTGGGGGAT
GACCAGCTGGGGGAGGAGTCAGAAGAAAGGGATGACCATTTATTACCAATGTAG
Enzyme 7 GenBank Gene ID M16985 Link Image
Enzyme 7 GeneCard ID M6PR Link Image
Enzyme 7 GenAtlas ID M6PR Link Image
Enzyme 7 HGNC ID HGNC:6752 Link Image
Enzyme 7 Chromosome Location 12
Enzyme 7 Locus 12p13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Pohlmann R, Nagel G, Schmidt B, Stein M, Lorkowski G, Krentler C, Cully J, Meyer HE, Grzeschik KH, Mersmann G, et al.: Cloning of a cDNA encoding the human cation-dependent mannose 6-phosphate-specific receptor. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5575-9. [PubMed Link Image]
  2. Klier HJ, von Figura K, Pohlmann R: Isolation and analysis of the human 46-kDa mannose 6-phosphate receptor gene. Eur J Biochem. 1991 Apr 10;197(1):23-8. [PubMed Link Image]
  3. Puertollano R, Aguilar RC, Gorshkova I, Crouch RJ, Bonifacino JS: Sorting of mannose 6-phosphate receptors mediated by the GGAs. Science. 2001 Jun 1;292(5522):1712-6. [PubMed Link Image]
  4. Doray B, Bruns K, Ghosh P, Kornfeld S: Interaction of the cation-dependent mannose 6-phosphate receptor with GGA proteins. J Biol Chem. 2002 May 24;277(21):18477-82. Epub 2002 Mar 8. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 7105
Enzyme 8 Name Cation-independent mannose-6-phosphate receptor precursor
Enzyme 8 Synonyms
  1. CI Man-6-P receptor
  2. CI-MPR
  3. M6PR
  4. Insulin-like growth factor 2 receptor
  5. Insulin-like growth factor II receptor
  6. IGF-II receptor
  7. M6P/IGF2 receptor
  8. M6P/IGF2R
  9. 300 kDa mannose 6-phosphate receptor
  10. MPR 300
  11. MPR300
  12. CD222 antigen
Enzyme 8 Gene Name IGF2R
Enzyme 8 Protein Sequence >Cation-independent mannose-6-phosphate receptor precursor
MGAAAGRSPHLGPAPARRPQRSLLLLQLLLLVAAPGSTQAQAAPFPELCSYTWEAVDTKN
NVLYKINICGSVDIVQCGPSSAVCMHDLKTRTYHSVGDSVLRSATRSLLEFNTTVSCDQQ
GTNHRVQSSIAFLCGKTLGTPEFVTATECVHYFEWRTTAACKKDIFKANKEVPCYVFDEE
LRKHDLNPLIKLSGAYLVDDSDPDTSLFINVCRDIDTLRDPGSQLRACPPGTAACLVRGH
QAFDVGQPRDGLKLVRKDRLVLSYVREEAGKLDFCDGHSPAVTITFVCPSERREGTIPKL
TAKSNCRYEIEWITEYACHRDYLESKTCSLSGEQQDVSIDLTPLAQSGGSSYISDGKEYL
FYLNVCGETEIQFCNKKQAAVCQVKKSDTSQVKAAGRYHNQTLRYSDGDLTLIYFGGDEC
SSGFQRMSVINFECNKTAGNDGKGTPVFTGEVDCTYFFTWDTEYACVKEKEDLLCGATDG
KKRYDLSALVRHAEPEQNWEAVDGSQTETEKKHFFINICHRVLQEGKARGCPEDAAVCAV
DKNGSKNLGKFISSPMKEKGNIQLSYSDGDDCGHGKKIKTNITLVCKPGDLESAPVLRTS
GEGGCFYEFEWHTAAACVLSKTEGENCTVFDSQAGFSFDLSPLTKKNGAYKVETKKYDFY
INVCGPVSVSPCQPDSGACQVAKSDEKTWNLGLSNAKLSYYDGMIQLNYRGGTPYNNERH
TPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPEEPLECVVTDPSTLEQYDL
SSLAKSEGGLGGNWYAMDNSGEHVTWRKYYINVCRPLNPVPGCNRYASACQMKYEKDQGS
FTEVVSISNLGMAKTGPVVEDSGSLLLEYVNGSACTTSDGRQTTYTTRIHLVCSRGRLNS
HPIFSLNWECVVSFLWNTEAACPIQTTTDTDQACSIRDPNSGFVFNLNPLNSSQGYNVSG
IGKIFMFNVCGTMPVCGTILGKPASGCEAETQTEELKNWKPARPVGIEKSLQLSTEGFIT
LTYKGPLSAKGTADAFIVRFVCNDDVYSGPLKFLHQDIDSGQGIRNTYFEFETALACVPS
PVDCQVTDLAGNEYDLTGLSTVRKPWTAVDTSVDGRKRTFYLSVCNPLPYIPGCQGSAVG
SCLVSEGNSWNLGVVQMSPQAAANGSLSIMYVNGDKCGNQRFSTRITFECAQISGSPAFQ
LQDGCEYVFIWRTVEACPVVRVEGDNCEVKDPRHGNLYDLKPLGLNDTIVSAGEYTYYFR
VCGKLSSDVCPTSDKSKVVSSCQEKREPQGFHKVAGLLTQKLTYENGLLKMNFTGGDTCH
KVYQRSTAIFFYCDRGTQRPVFLKETSDCSYLFEWRTQYACPPFDLTECSFKDGAGNSFD
LSSLSRYSDNWEAITGTGDPEHYLINVCKSLAPQAGTEPCPPEAAACLLGGSKPVNLGRV
RDGPQWRDGIIVLKYVDGDLCPDGIRKKSTTIRFTCSESQVNSRPMFISAVEDCEYTFAW
PTATACPMKSNEHDDCQVTNPSTGHLFDLSSLSGRAGFTAAYSEKGLVYMSICGENENCP
PGVGACFGQTRISVGKANKRLRYVDQVLQLVYKDGSPCPSKSGLSYKSVISFVCRPEAGP
TNRPMLISLDKQTCTLFFSWHTPLACEQATECSVRNGSSIVDLSPLIHRTGGYEAYDESE
DDASDTNPDFYINICQPLNPMHGVPCPAGAAVCKVPIDGPPIDIGRVAGPPILNPIANEI
YLNFESSTPCLADKHFNYTSLIAFHCKRGVSMGTPKLLRTSECDFVFEWETPVVCPDEVR
MDGCTLTDEQLLYSFNLSSLSTSTFKVTRDSRTYSVGVCTFAVGPEQGGCKDGGVCLLSG
TKGASFGRLQSMKLDYRHQDEAVVLSYVNGDRCPPETDDGVPCVFPFIFNGKSYEECIIE
SRAKLWCSTTADYDRDHEWGFCRHSNSYRTSSIIFKCDEDEDIGRPQVFSEVRGCDVTFE
WKTKVVCPPKKLECKFVQKHKTYDLRLLSSLTGSWSLVHNGVSYYINLCQKIYKGPLGCS
ERASICRRTTTGDVQVLGLVHTQKLGVIGDKVVVTYSKGYPCGGNKTASSVIELTCTKTV
GRPAFKRFDIDSCTYYFSWDSRAACAVKPQEVQMVNGTITNPINGKSFSLGDIYFKLFRA
SGDMRTNGDNYLYEIQLSSITSSRNPACSGANICQVKPNDQHFSRKVGTSDKTKYYLQDG
DLDVVFASSSKCGKDKTKSVSSTIFFHCDPLVEDGIPEFSHETADCQYLFSWYTSAVCPL
GVGFDSENPGDDGQMHKGLSERSQAVGAVLSLLLVALTCCLLALLLYKKERRETVISKLT
TCCRRSSNVSYKYSKVNKEEETDENETEWLMEEIQLPPPRQGKEGQENGHITTKSVKALS
SLHGDDQDSEDEVLTIPEVKVHSGRGAGAESSHPVRNAQSNALQEREDDRVGLVRGEKAR
KGKSSSAQQKTVSSTKLVSFHDDSDEDLLHI
Enzyme 8 Number of Residues 2491
Enzyme 8 Molecular Weight 274277
Enzyme 8 Theoretical pI 5.71
Enzyme 8 GO Classification
Function
  • receptor activity
  • signal transducer activity
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • intracellular membrane-bound organelle
  • lysosome
  • lytic vacuole
  • membrane
  • membrane-bound organelle
  • organelle
  • vacuole
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6- phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-40
Enzyme 8 Transmembrane Regions
  • 2305-2327
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 33055 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P11717 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name MPRI_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >7476 bp
ATGGGGGCCGCCGCCGGCCGGAGCCCCCACCTGGGGCCCGCGCCCGCCCGCCGCCCGCAG
CGCTCTCTGCTCCTGCTGCAGCTGCTGCTGCTCGTCGCTGCCCCGGGGTCCACGCAGGCC
CAGGCCGCCCCGTTCCCCGAGCTGTGCAGTTATACATGGGAAGCTGTTGATACCAAAAAT
AATGTACTTTATAAAATCAACATCTGTGGAAGTGTGGATATTGTCCAGTGCGGGCCATCA
AGTGCTGTTTGTATGCACGACTTGAAGACACGCACTTATCATTCAGTGGGTGACTCTGTT
TTGAGAAGTGCAACCAGATCTCTCCTGGAATTCAACACAACAGTGAGCTGTGACCAGCAA
GGCACAAATCACAGAGTCCAGAGCAGCATTGCCTTCCTGTGTGGGAAAACCCTGGGAACT
CCTGAATTTGTAACTGCAACAGAATGTGTGCACTACTTTGAGTGGAGGACCACTGCAGCC
TGCAAGAAAGACATATTTAAAGCAAATAAGGAGGTGCCATGCTATGTGTTTGATGAAGAG
TTGAGGAAGCATGATCTCAATCCTCTGATCAAGCTTAGTGGTGCCTACTTGGTGGATGAC
TCCGATCCGGACACTTCTCTATTCATCAATGTTTGTAGAGACATAGACACACTACGAGAC
CCAGGTTCACAGCTGCGGGCCTGTCCCCCCGGCACTGCCGCCTGCCTGGTAAGAGGACAC
CAGGCGTTTGATGTTGGCCAGCCCCGGGACGGACTGAAGCTGGTGCGCAAGGACAGGCTT
GTCCTGAGTTACGTGAGGGAAGAGGCAGGAAAGCTAGACTTTTGTGATGGTCACAGCCCT
GCGGTGACTATTACATTTGTTTGCCCGTCGGAGCGGAGAGAGGGCACCATTCCCAAACTC
ACAGCTAAATCCAACTGCCGCTATGAAATTGAGTGGATTACTGAGTATGCCTGCCACAGA
GATTACCTGGAAAGTAAAACTTGTTCTCTGAGCGGCGAGCAGCAGGATGTCTCCATAGAC
CTCACACCACTTGCCCAGAGCGGAGGTTCATCCTATATTTCAGATGGAAAAGAATATTTG
TTTTATTTGAATGTCTGTGGAGAAACTGAAATACAGTTCTGTAATAAAAAACAAGCTGCA
GTTTGCCAAGTGAAAAAGAGCGATACCTCTCAAGTCAAAGCAGCAGGAAGATACCACAAT
CAGACCCTCCGATATTCGGATGGAGACCTCACCTTGATATATTTTGGAGGTGATGAATGC
AGCTCAGGGTTTCAGCGGATGAGCGTCATAAACTTTGAGTGCAATAAAACCGCAGGTAAC
GATGGGAAAGGAACTCCTGTATTCACAGGGGAGGTTGACTGCACCTACTTCTTCACATGG
GACACGGAATACGCCTGTGTTAAGGAGAAGGAAGACCTCCTCTGCGGTGCCACCGACGGG
AAGAAGCGCTATGACCTGTCCGCGCTGGTCCGCCATGCAGAACCAGAGCAGAATTGGGAA
GCTGTGGATGGCAGTCAGACGGAAACAGAGAAGAAGCATTTTTTCATTAATATTTGTCAC
AGAGTGCTGCAGGAAGGCAAGGCACGAGGGTGTCCCGAGGACGCGGCAGTGTGTGCAGTG
GATAAAAATGGAAGTAAAAATCTGGGAAAATTTATTTCCTCTCCCATGAAAGAGAAAGGA
AACATTCAACTCTCTTATTCAGATGGTGATGATTGTGGTCATGGCAAGAAAATTAAAACT
AATATCACACTTGTATGCAAGCCAGGTGATCTGGAAAGTGCACCAGTGTTGAGAACTTCT
GGGGAAGGCGGTTGCTTTTATGAGTTTGAGTGGCGCACAGCTGCGGCCTGTGTGCTGTCT
AAGACAGAAGGGGAGAACTGCACGGTCTTTGACTCCCAGGCAGGGTTTTCTTTTGACTTA
TCACCTCTCACAAAGAAAAATGGTGCCTATAAAGTTGAGACAAAGAAGTATGACTTTTAT
ATAAATGTGTGTGGCCCGGTGTCTGTGAGCCCCTGTCAGCCAGACTCAGGAGCCTGCCAG
GTGGCAAAAAGTGATGAGAAGACTTGGAACTTGGGTCTGAGTAATGCGAAGCTTTCATAT
TATGATGGGATGATCCAACTGAACTACAGAGGCGGCACACCCTATAACAATGAAAGACAC
ACACCGAGAGCTACGCTCATCACCTTTCTCTGTGATCGAGACGCGGGAGTGGGCTTCCCT
GAATATCAGGAAGAGGATAACTCCACCTACAACTTCCGGTGGTACACCAGCTATGCCTGC
CCGGAGGAGCCCCTGGAATGCGTAGTGACCGACCCCTCCACGCTGGAGCAGTACGACCTC
TCCAGTCTGGCAAAATCTGAAGGTGGCCTTGGAGGAAACTGGTATGCCATGGACAACTCA
GGGGAACATGTCACGTGGAGGAAATACTACATTAACGTGTGTCGGCCTCTGAATCCAGTG
CCGGGCTGCAACCGATATGCATCGGCTTGCCAGATGAAGTATGAAAAAGATCAGGGCTCC
TTCACTGAAGTGGTTTCCATCAGTAACTTGGGAATGGCAAAGACCGGCCCGGTGGTTGAG
GACAGCGGCAGCCTCCTTCTGGAATACGTGAATGGGTCGGCCTGCACCACCAGCGATGGC
AGACAGACCACATATACCACGAGGATCCATCTCGTCTGCTCCAGGGGCAGGCTGAACAGC
CACCCCATCTTTTCTCTCAACTGGGAGTGTGTGGTCAGTTTCCTGTGGAACACAGAGGCT
GCCTGTCCCATTCAGACAACGACGGATACAGACCAGGCTTGCTCTATAAGGGATCCCAAC
AGTGGATTTGTGTTTAATCTTAATCCGCTAAACAGTTCGCAAGGATATAACGTCTCTGGC
ATTGGGAAGATTTTTATGTTTAATGTCTGCGGCACAATGCCTGTCTGTGGGACCATCCTG
GGAAAACCTGCTTCTGGCTGTGAGGCAGAAACCCAAACTGAAGAGCTCAAGAATTGGAAG
CCAGCAAGGCCAGTCGGAATTGAGAAAAGCCTCCAGCTGTCCACAGAGGGCTTCATCACT
CTGACCTACAAAGGGCCTCTCTCTGCCAAAGGTACCGCTGATGCTTTTATCGTCCGCTTT
GTTTGCAATGATGATGTTTACTCAGGGCCCCTCAAATTCCTGCATCAAGATATCGACTCT
GGGCAAGGGATCCGAAACACTTACTTTGAGTTTGAAACCGCGTTGGCCTGTGTTCCTTCT
CCAGTGGACTGCCAAGTCACCGACCTGGCTGGAAATGAGTACGACCTGACTGGCCTAAGC
ACAGTCAGGAAACCTTGGACGGCTGTTGACACCTCTGTCGATGGGAGAAAGAGGACTTTC
TATTTGAGCGTTTGCAATCCTCTCCCTTACATTCCTGGATGCCAGGGCAGCGCAGTGGGG
TCTTGCTTAGTGTCAGAAGGCAATAGCTGGAATCTGGGTGTGGTGCAGATGAGTCCCCAA
GCCGCGGCGAATGGATCTTTGAGCATCATGTATGTCAACGGTGACAAGTGTGGGAACCAG
CGCTTCTCCACCAGGATCACGTTTGAGTGTGCTCAGATATCGGGCTCACCAGCATTTCAG
CTTCAGGATGGTTGTGAGTACGTGTTTATCTGGAGAACTGTGGAAGCCTGTCCCGTTGTC
AGAGTGGAAGGGGACAACTGTGAGGTGAAAGACCCAAGGCATGGCAACTTGTATGACCTG
AAGCCCCTGGGCCTCAACGACACCATCGTGAGCGCTGGCGAATACACTTATTACTTCCGG
GTCTGTGGGAAGCTTTCCTCAGACGTCTGCCCCACAAGTGACAAGTCCAAGGTGGTCTCC
TCATGTCAGGAAAAGCGGGAACCGCAGGGATTTCACAAAGTGGCAGGTCTCCTGACTCAG
AAGCTAACTTATGAAAATGGCTTGTTAAAAATGAACTTCACGGGGGGGGACACTTGCCAT
AAGGTTTATCAGCGCTCCACAGCCATCTTCTTCTACTGTGACCGCGGCACCCAGCGGCCA
GTATTTCTAAAGGAGACTTCAGATTGTTCCTACTTGTTTGAGTGGCGAACGCAGTATGCC
TGCCCACCTTTCGATCTGACTGAATGTTCATTCAAAGATGGGGCTGGCAACTCCTTCGAC
CTCTCGTCCCTGTCAAGGTACAGTGACAACTGGGAAGCCATCACTGGGACGGGGGACCCG
GAGCACTACCTCATCAATGTCTGCAAGTCTCTGGCCCCGCAGGCTGGCACTGAGCCGTGC
CCTCCAGAAGCAGCCGCGTGTCTGCTGGGTGGCTCCAAGCCCGTGAACCTCGGCAGGGTA
AGGGACGGACCTCAGTGGAGAGATGGCATAATTGTCCTGAAATACGTTGATGGCGACTTA
TGTCCAGATGGGATTCGGAAAAAGTCAACCACCATCCGATTCACCTGCAGCGAGAGCCAA
GTGAACTCCAGGCCCATGTTCATCAGCGCCGTGGAGGACTGTGAGTACACCTTTGCCTGG
CCCACAGCCACAGCCTGTCCCATGAAGAGCAACGAGCATGATGACTGCCAGGTCACCAAC
CCAAGCACAGGACACCTGTTTGATCTGAGCTCCTTAAGTGGCAGGGCGGGATTCACAGCT
GCTTACAGCGAGAAGGGGTTGGTTTACATGAGCATCTGTGGGGAGAATGAAAACTGCCCT
CCTGGCGTGGGGGCCTGCTTTGGACAGACCAGGATTAGCGTGGGCAAGGCCAACAAGAGG
CTGAGATACGTGGACCAGGTCCTGCAGCTGGTGTACAAGGATGGGTCCCCTTGTCCCTCC
AAATCCGGCCTGAGCTATAAGAGTGTGATCAGTTTCGTGTGCAGGCCTGAGGCCGGGCCA
ACCAATAGGCCCATGCTCATCTCCCTGGACAAGCAGACATGCACTCTCTTCTTCTCCTGG
CACACGCCGCTGGCCTGCGAGCAAGCGACCGAATGTTCCGTGAGGAATGGAAGCTCTATT
GTTGACTTGTCTCCCCTTATTCATCGCACTGGTGGTTATGAGGCTTATGATGAGAGTGAG
GATGATGCCTCCGATACCAACCCTGATTTCTACATCAATATTTGTCAGCCACTAAATCCC
ATGCACGCAGTGCCCTGTCCTGCCGGAGCCGCTGTGTGCAAAGTTCCTATTGATGGTCCC
CCCATAGATATCGGCCGGGTAGCAGGACCACCAATACTCAATCCAATAGCAAATGAGATT
TACTTGAATTTTGAAAGCAGTACTCCTTGCTTAGCGGACAAGCATTTCAACTACACCTCG
CTCATCGCGTTTCACTGTAAGAGAGGTGTGAGCATGGGAACGCCTAAGCTGTTAAGGACC
AGCGAGTGCGACTTTGTGTTCGAATGGGAGACTCCTGTCGTCTGTCCTGATGAAGTGAGG
ATGGATGGCTGTACCCTGACAGATGAGCAGCTCCTCTACAGCTTCAACTTGTCCAGCCTT
TCCACGAGCACCTTTAAGGTGACTCGCGACTCGCGCACCTACAGCGTTGGGGTGTGCACC
TTTGCAGTCGGGCCAGAACAAGGAGGCTGTAAGGACGGAGGAGTCTGTCTGCTCTCAGGC
ACCAAGGGGGCATCCTTTGGACGGCTGCAATCAATGAAACTGGATTACAGGCACCAGGAT
GAAGCGGTCGTTTTAAGTTACGTGAATGGTGATCGTTGCCCTCCAGAAACCGATGACGGC
GTCCCCTGTGTCTTCCCCTTCATATTCAATGGGAAGAGCTACGAGGAGTGCATCATAGAG
AGCAGGGCGAAGCTGTGGTGTAGCACAACTGCGGACTACGACAGAGACCACGAGTGGGGC
TTCTGCAGACACTCAAACAGCTACCGGACATCCAGCATCATATTTAAGTGTGATGAAGAT
GAGGACATTGGGAGGCCACAAGTCTTCAGTGAAGTGCGTGGGTGTGATGTGACATTTGAG
TGGAAAACAAAAGTTGTCTGCCCTCCAAAGAAGTTGGAGTGCAAATTCGTCCAGAAACAC
AAAACCTACGACCTGCGGCTGCTCTCCTCTCTCACCGGGTCCTGGTCCCTGGTCCACAAC
GGAGTCTCGTACTATATAAATCTGTGCCAGAAAATATATAAAGGGCCCCTGGGCTGCTCT
GAAAGGGCCAGCATTTGCAGAAGGACCACAACTGGTGACGTCCAGGTCCTGGGACTCGTT
CACACGCAGAAGCTGGGTGTCATAGGTGACAAAGTTGTTGTCACGTACTCCAAAGGTTAT
CCGTGTGGTGGAAATAAGACCGCATCCTCCGTGATAGAATTGACCTGTACAAAGACGGTG
GGCAGACCTGCATTCAAGAGGTTTGATATCGACAGCTGCACTTACTACTTCAGCTGGGAC
TCCCGGGCTGCCTGCGCCGTGAAGCCTCAGGAGGTGCAGATGGTGAATGGGACCATCACC
AACCCTATAAATGGCAAGAGCTTCAGCCTCGGAGATATTTATTTTAAGCTGTTCAGAGCC
TCTGGGGACATGAGGACCAATGGGGACAACTACCTGTATGAGATCCAACTTTCCTCCATC
ACAAGCTCCAGAAACCCGGCGTGCTCTGGAGCCAACATATGCCAGGTGAAGCCCAACGAT
CAGCACTTCAGTCGGAAAGTTGGAACCTCTGACAAGACCAAGTACTACCTTCAAGACGGC
GATCTCGATGTCGTGTTTGCCTCTTCCTCTAAGTGCGGAAAGGATAAGACCAAGTCTGTT
TCTTCCACCATCTTCTTCCACTGTGACCCTCTGGTGGAGGACGGGATCCCCGAGTTCAGT
CACGAGACTGCCGACTGCCAGTACCTCTTCTCTTGGTACACCTCAGCCGTGTGTCCTCTG
GGGGTGGGCTTTGACAGCGAGAATCCCGGGGACGACGGGCAGATGCACAAGGGGCTGTCA
GAACGGAGCCAGGCAGTCGGCGCGGTGCTCAGCCTGCTGCTGGTGGCGCTCACCTGCTGC
CTGCTGGCCCTGTTGCTCTACAAGAAGGAGAGGAGGGAAACAGTGATAAGTAAGCTGACC
ACTTGCTGTAGGAGAAGTTCCAACGTGTCCTACAAATACTCAAAGGTGAATAAGGAAGAA
GAGACAGATGAGAATGAAACAGAGTGGCTGATGGAAGAGATCCAGCTGCCTCCTCCACGG
CAGGGAAAGGAAGGGCAGGAGAACGGCCATATTACCACCAAGTCAGTGAAAGCCCTCAGC
TCCCTGCATGGGGATGACCAGGACAGTGAGGATGAGGTTCTGACCATCCCAGAGGTGAAA
GTTCACTCGGGCAGGGGAGCTGGGGCAGAGAGCTCCCACCCAGTGAGAAACGCACAGAGC
AATGCCCTTCAGGAGCGTGAGGACGATAGGGTGGGGCTGGTCAGGGGTGAGAAGGCGAGG
AAAGGGAAGTCCAGCTCTGCACAGCAGAAGACAGTGAGCTCCACCAAGCTGGTGTCCTTC
CATGACGACAGCGACGAGGACCTCTTACACATCTGA
Enzyme 8 GenBank Gene ID Y00285 Link Image
Enzyme 8 GeneCard ID IGF2R Link Image
Enzyme 8 GenAtlas ID IGF2R Link Image
Enzyme 8 HGNC ID HGNC:5467 Link Image
Enzyme 8 Chromosome Location 6
Enzyme 8 Locus 6q26
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Morgan DO, Edman JC, Standring DN, Fried VA, Smith MC, Roth RA, Rutter WJ: Insulin-like growth factor II receptor as a multifunctional binding protein. Nature. 1987 Sep 24-30;329(6137):301-7. [PubMed Link Image]
  2. Oshima A, Nolan CM, Kyle JW, Grubb JH, Sly WS: The human cation-independent mannose 6-phosphate receptor. Cloning and sequence of the full-length cDNA and expression of functional receptor in COS cells. J Biol Chem. 1988 Feb 15;263(5):2553-62. [PubMed Link Image]
  3. Killian JK, Jirtle RL: Genomic structure of the human M6P/IGF2 receptor. Mamm Genome. 1999 Jan;10(1):74-7. [PubMed Link Image]
  4. 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]
  5. Puertollano R, Aguilar RC, Gorshkova I, Crouch RJ, Bonifacino JS: Sorting of mannose 6-phosphate receptors mediated by the GGAs. Science. 2001 Jun 1;292(5522):1712-6. [PubMed Link Image]
  6. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 9329
Enzyme 9 Name Phosphoglucomutase-2
Enzyme 9 Synonyms
  1. Glucose phosphomutase 2
  2. PGM 2
Enzyme 9 Gene Name PGM2
Enzyme 9 Protein Sequence >Phosphoglucomutase-2
MAAPEGSGLGEDARLDQETAQWLRWDKNSLTLEAVKRLIAEGNKEELRKCFGARMEFGTA
GLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFSDLKQKGIVISFDARAHPSSGGSSRRF
ARLAATTFISQGIPVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDN
GAQIISPHDKGISQAIEENLEPWPQAWDDSLIDSSPLLHNPSASINNDYFEDLKKYCFHR
SVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKYPNPEEGK
GVLTLSFALADKTKARIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWK
EKNQDRSALKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLIDQGKTVL
FAFEEAIGYMCCPFVLDKDGVSAAVISAELASFLATKNLSLSQQLKAIYVEYGYHITKAS
YFICHDQETIKKLFENLRNYDGKNNYPKACGKFEISAIRDLTTGYDDSQPDKKAVLPTSK
SSQMITFTFANGGVATMRTSGTEPKIKYYAELCAPPGNSDPEQLKKELNELVSAIEEHFF
QPQKYNLQPKAD
Enzyme 9 Number of Residues 612
Enzyme 9 Molecular Weight 68284
Enzyme 9 Theoretical pI Not Available
Enzyme 9 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 9 General Function Carbohydrate transport and metabolism
Enzyme 9 Specific Function This enzyme participates in both the breakdown and synthesis of glucose
Enzyme 9 Pathways
Enzyme 9 Reactions
  • D-Glucose 1-phosphate <==> D-Glucose 6-phosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 12052930 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q96G03 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PGM2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AL136705 Link Image
Enzyme 9 GeneCard ID Not Available
Enzyme 9 GenAtlas ID PGM2 Link Image
Enzyme 9 HGNC ID HGNC:8906 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  2. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 13036
Enzyme 10 Name cDNA FLJ76937, highly similar to Homo sapiens mannose phosphate isomerase
Enzyme 10 Synonyms
  1. MPI, mRNA
  2. Mannose phosphate isomerase, isoform CRA_b
Enzyme 10 Gene Name MPI
Enzyme 10 Protein Sequence >cDNA FLJ76937, highly similar to Homo sapiens mannose phosphate isomerase
MAAPRVFPLSCAVQQYAWGKMGSNSEVARLLASSDPLAQIAEDKPYAELWMGTHPRGDAK
ILDNRISQKTLSQWIAENQDSLGSKVKDTFNGNLPFLFKVLSVETPLSIQAHPNKELAEK
LHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPVEEIVTFLKKVPEFQFLIGDEAATHLK
QTMSHDSQAVASSLQSCFSHLMKSEKKVVVEQLNLLVKRISQQAAAGNNMEDIFGELLLQ
LHQQYPGDIGCFAIYFLNLLTLKPGEAMFLEANVPHAYLKGDCVECMACSDNTVRAGLTP
KFIDVPTLCEMLSYTPSSSKDRLFLPTRSQEDPYLSIYDPPVPDFTIMKTEVPGSVTEYK
VLALDSASILLMVQGTVIASTPTTQTPIPLQRGGVLFIGANESVSLKLTEPKDLLIFRAC
CLL
Enzyme 10 Number of Residues 423
Enzyme 10 Molecular Weight 46656
Enzyme 10 Theoretical pI 5.81
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function Not Available
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 158258180 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID A8K8K9 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name A8K8K9_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AK292374 Link Image
Enzyme 10 GeneCard ID A8K8K9 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 15209
Enzyme 11 Name cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name Not Available
Enzyme 11 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 11 Number of Residues 917
Enzyme 11 Molecular Weight 102388
Enzyme 11 Theoretical pI 6.70
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function Not Available
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 158257456 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID A8K7J7 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name A8K7J7_HUMAN Link Image
Enzyme 11 PDB ID 1HKB Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 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 11 GenBank Gene ID AK292012 Link Image
Enzyme 11 GeneCard ID A8K7J7 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs Not Available
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 15878
Enzyme 12 Name cDNA FLJ75943, highly similar to Homo sapiens phosphomannomutase 1 (PMM1), mRNA (Phosphomannomutase 1, isoform CRA_a)
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name PMM1
Enzyme 12 Protein Sequence >cDNA FLJ75943, highly similar to Homo sapiens phosphomannomutase 1 (PMM1), mRNA (Phosphomannomutase 1, isoform CRA_a)
MAVTAQAARRKERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIA
EQLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLR
LPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLR
FSRGGMISFDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSV
VSPQDTVQRCREIFFPETAHEA
Enzyme 12 Number of Residues 262
Enzyme 12 Molecular Weight 29747
Enzyme 12 Theoretical pI 5.47
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function Not Available
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID A8K003 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name A8K003_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 AK289368 Link Image
Enzyme 12 GeneCard ID A8K003 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location 22
Enzyme 12 Locus 22q13.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 15879
Enzyme 13 Name cDNA FLJ78512, highly similar to Homo sapiens phosphomannomutase 2 (PMM2), mRNA (Phosphomannomutase 2, isoform CRA_b)
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name PMM2
Enzyme 13 Protein Sequence >cDNA FLJ78512, highly similar to Homo sapiens phosphomannomutase 2 (PMM2), mRNA (Phosphomannomutase 2, isoform CRA_b)
MAAPGPALCLFDVDGTLTAPRQKITKEMDDFLQKLRQKIKIGVVGGSDFEKVQEQLGNDV
VEKYDYVFPENGLVAYKDGKLLCRQNIQSHLGEALIQDLINYCLSYIAKIKLPKKRGTFI
EFRNGMLNVSPIGRSCSQEERIEFYELDKKENIRQKFVADLRKEFAGKGLTFSIGGQISF
DVFPDGWDKRYCLRHVENDGYKTIYFFGDKTMPGGNDHEIFTDPRTMGYSVTAPEDTRRI
CELLFS
Enzyme 13 Number of Residues 246
Enzyme 13 Molecular Weight 28082
Enzyme 13 Theoretical pI 6.76
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 Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID A8K672 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name A8K672_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID AK291537 Link Image
Enzyme 13 GeneCard ID A8K672 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location 16
Enzyme 13 Locus 16p13.3-p13.2
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 17019
Enzyme 14 Name Phosphofurin acidic cluster sorting protein 1
Enzyme 14 Synonyms
  1. PACS-1
Enzyme 14 Gene Name PACS1
Enzyme 14 Protein Sequence >Phosphofurin acidic cluster sorting protein 1
MAERGGAGGGPGGAGGGSGQRGSGVAQSPQQPPPQQQQQQPPQQPTPPKLAQATSSSSST
SAAAASSSSSSTSTSMAVAVASGSAPPGGPGPGRTPAPVQMNLYATWEVDRSSSSCVPRL
FSLTLKKLVMLKEMDKDLNSVVIAVKLQGSKRILRSNEIVLPASGLVETELQLTFSLQYP
HFLKRDANKLQIMLQRRKRYKNRTILGYKTLAVGLINMAEVMQHPNEGALVLGLHSNVKD
VSVPVAEIKIYSLSSQPIDHEGIKSKLSDRSPDIDNYSEEEEESFSSEQEGSDDPLHGQD
LFYEDEDLRKVKKTRRKLTSTSAITRQPNIKQKFVALLKRFKVSDEVGFGLEHVSREQIR
EVEEDLDELYDSLEMYNPSDSGPEMEETESILSTPKPKLKPFFEGMSQSSSQTEIGSLNS
KGSLGKDTTSPMELAALEKIKSTWIKNQDDSLTETDTLEITDQDMFGDASTSLVVPEKVK
TPMKSSKTDLQGSASPSKVEGVHTPRQKRSTPLKERQLSKPLSERTNSSDSERSPDLGHS
TQIPRKVVYDQLNQILVSDAALPENVILVNTTDWQGQYVAELLQDQRKPVVCTCSTVEVQ
AVLSALLTRIQRYCNCNSSMPRPVKVAAVGGQSYLSSILRFFVKSLANKTSDWLGYMRFL
IIPLGSHPVAKYLGSVDSKYSSSFLDSGWRDLFSRSEPPVSEQLDVAGRVMQYVNGAATT
HQLPVAEAMLTCRHKFPDEDSYQKFIPFIGVVKVGLVEDSPSTAGDGDDSPVVSLTVPST
SPPSSSGLSRDATATPPSSPSMSSALAIVGSPNSPYGDVIGLQVDYWLGHPGERRREGDK
RDASSKNTLKSVFRSVQVSRLPHSGEAQLSGTMAMTVVTKEKNKKVPTIFLSKKPREKEV
DSKSQVIEGISRLICSAKQQQTMLRVSIDGVEWSDIKFFQLAAQWPTHVKHFPVGLFSGS
KAT
Enzyme 14 Number of Residues 963
Enzyme 14 Molecular Weight 104899
Enzyme 14 Theoretical pI 7.86
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin- coated membrane pits. Involved in HIV-1 nef-mediated removal of MHC-I from the cell surface to the TGN
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function Not Available
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID Q6VY07 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PACS1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AY320283 Link Image
Enzyme 14 GeneCard ID Q6VY07 Link Image
Enzyme 14 GenAtlas ID PACS1 Link Image
Enzyme 14 HGNC ID HGNC:30032 Link Image
Enzyme 14 Chromosome Location 11
Enzyme 14 Locus 11q13.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed Link Image]
  2. Crump CM, Xiang Y, Thomas L, Gu F, Austin C, Tooze SA, Thomas G: PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic. EMBO J. 2001 May 1;20(9):2191-201. [PubMed Link Image]
  3. Piguet V, Wan L, Borel C, Mangasarian A, Demaurex N, Thomas G, Trono D: HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes. Nat Cell Biol. 2000 Mar;2(3):163-7. [PubMed Link Image]
  4. Blagoveshchenskaya AD, Thomas L, Feliciangeli SF, Hung CH, Thomas G: HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway. Cell. 2002 Dec 13;111(6):853-66. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 17020
Enzyme 15 Name Sortilin
Enzyme 15 Synonyms
  1. Neurotensin receptor 3
  2. NTR3
  3. NT3
  4. Glycoprotein 95
  5. Gp95
  6. 100 kDa NT receptor
Enzyme 15 Gene Name SORT1
Enzyme 15 Protein Sequence >Sortilin
MERPWGAADGLSRWPHGLGLLLLLQLLPPSTLSQDRLDAPPPPAAPLPRWSGPIGVSWGL
RAAAAGGAFPRGGRWRRSAPGEDEECGRVRDFVAKLANNTHQHVFDDLRGSVSLSWVGDS
TGVILVLTTFHVPLVIMTFGQSKLYRSEDYGKNFKDITDLINNTFIRTEFGMAIGPENSG
KVVLTAEVSGGSRGGRIFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLW
VSKNFGGKWEEIHKAVCLAKWGSDNTIFFTTYANGSCKADLGALELWRTSDLGKSFKTIG
VKIYSFGLGGRFLFASVMADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDM
VFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYITSVLS
EDNSIQTMITFDQGGRWTHLRKPENSECDATAKNKNECSLHIHASYSISQKLNVPMAPLS
EPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWTKMLEGPHYYTILDSGGIIVAIEHS
SRPINVIKFSTDEGQCWQTYTFTRDPIYFTGLASEPGARSMNISIWGFTESFLTSQWVSY
TIDFKDILERNCEEKDYTIWLAHSTDPEDYEDGCILGYKEQFLRLRKSSVCQNGRDYVVT
KQPSICLCSLEDFLCDFGYYRPENDSKCVEQPELKGHDLEFCLYGREEHLTTNGYRKIPG
DKCQGGVNPVREVKDLKKKCTSNFLSPEKQNSKSNSVPIILAIVGLMLVTVVAGVLIVKK
YVCGGRFLVHRYSVLQQHAEANGVDGVDALDTASHTNKSGYHDDSDEDLLE
Enzyme 15 Number of Residues 831
Enzyme 15 Molecular Weight 92068
Enzyme 15 Theoretical pI 5.51
Enzyme 15 GO Classification
Function
  • protein transporter activity
  • transporter activity
Process
  • cellular physiological process
  • intracellular protein transport
  • physiological process
  • protein transport
  • transport
Component
  • cell
  • membrane
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-33
Enzyme 15 Transmembrane Regions
  • 756-778
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID Q99523 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name SORT_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID X98248 Link Image
Enzyme 15 GeneCard ID Q99523 Link Image
Enzyme 15 GenAtlas ID SORT1 Link Image
Enzyme 15 HGNC ID HGNC:11186 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Petersen CM, Nielsen MS, Nykjaer A, Jacobsen L, Tommerup N, Rasmussen HH, Roigaard H, Gliemann J, Madsen P, Moestrup SK: Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography. J Biol Chem. 1997 Feb 7;272(6):3599-605. [PubMed Link Image]
  2. Mazella J, Zsurger N, Navarro V, Chabry J, Kaghad M, Caput D, Ferrara P, Vita N, Gully D, Maffrand JP, Vincent JP: The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor. J Biol Chem. 1998 Oct 9;273(41):26273-6. [PubMed Link Image]
  3. Munck Petersen C, Nielsen MS, Jacobsen C, Tauris J, Jacobsen L, Gliemann J, Moestrup SK, Madsen P: Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding. EMBO J. 1999 Feb 1;18(3):595-604. [PubMed Link Image]
  4. Tauris J, Ellgaard L, Jacobsen C, Nielsen MS, Madsen P, Thogersen HC, Gliemann J, Petersen CM, Moestrup SK: The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin. FEBS Lett. 1998 Jun 5;429(1):27-30. [PubMed Link Image]
  5. Nielsen MS, Jacobsen C, Olivecrona G, Gliemann J, Petersen CM: Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. J Biol Chem. 1999 Mar 26;274(13):8832-6. [PubMed Link Image]
  6. Nielsen MS, Madsen P, Christensen EI, Nykjaer A, Gliemann J, Kasper D, Pohlmann R, Petersen CM: The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein. EMBO J. 2001 May 1;20(9):2180-90. [PubMed Link Image]
  7. Takatsu H, Katoh Y, Shiba Y, Nakayama K: Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J Biol Chem. 2001 Jul 27;276(30):28541-5. Epub 2001 Jun 4. [PubMed Link Image]
  8. Navarro V, Vincent JP, Mazella J: Shedding of the luminal domain of the neurotensin receptor-3/sortilin in the HT29 cell line. Biochem Biophys Res Commun. 2002 Nov 15;298(5):760-4. [PubMed Link Image]
  9. Shiba T, Takatsu H, Nogi T, Matsugaki N, Kawasaki M, Igarashi N, Suzuki M, Kato R, Earnest T, Nakayama K, Wakatsuki S: Structural basis for recognition of acidic-cluster dileucine sequence by GGA1. Nature. 2002 Feb 21;415(6874):937-41. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 17021
Enzyme 16 Name Kinesin-like protein KIF13A
Enzyme 16 Synonyms
  1. Kinesin-like protein RBKIN
Enzyme 16 Gene Name KIF13A
Enzyme 16 Protein Sequence >Kinesin-like protein KIF13A
MSDTKVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPPSNTKQGERKPPKVFAFDYC
FWSMDESNTTKYAGQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLG
LIPRLCCALFKRISLEQNESQTFKVEVSYMEIYNEKVRDLLDPKGSRQSLKVREHKVLGP
YVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGN
SGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGKGKSK
FVPYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNE
DPNAKVIRELREEVEKLREQLSQAEAMKAPELKEKLEESEKLIKELTVTWEEKLRKTEEI
AQERQRQLESMGISLEMSGIKVGDDKCYLVNLNADPALNELLVYYLKDHTRVGADTSQDI
QLFGIGIQPQHCEIDIASDGDVTLTPKENARSCVNGTLVCSTTQLWHGDRILWGNNHFFR
INLPKRKRRDWLKDFEKETGPPEHDLDAASEASSEPDYNYEFAQMEVIMKTLNSNDPVQN
VVQVLEKQYLEEKRSALEEQRLMYERELEQLRQQLSPDRQPQSSGPDRLAYSSQTAQQKV
TQWAEERDELFRQSLAKLREQLVKANTLVREANFLAEEMSKLTDYQVTLQIPAANLSANR
KRGAIVSEPAIQVRRKGKSTQVWTIEKLENKLIDMRDLYQEWKEKVPEAKRLYGKRGDPF
YEAQENHNLIGVANVFLECLFCDVKLQYAVPIISQQGEVAGRLHVEVMRVTGAVPERVVE
DDSSENSSESGSLEVVDSSGEIIHRVKKLTCRVKIKEATGLPLNLSNFVFCQYTFWDQCE
STVAAPVVDPEVPSPQSKDAQYTVTFSHCKDYVVNVTEEFLEFISDGALAIEVWGHRCAG
NGSSIWEVDSLHAKTRTLHDRWNEVTRRIEMWISILELNELGEYAAVELHQAKDVNTGGI
FQLRQGHSRRVQVTVKPVQHSGTLPLMVEAILSVSIGCVTARSTKLQRGLDSYQRDDEDG
DDMDSYQEEDLNCVRERWSDALIKRREYLDEQIKKVSNKTEKTEDDVEREAQLVEQWVGL
TEERNAVLVPAPGSGIPGAPADWIPPPGMETHIPVLFLDLNADDLSANEQLVGPHASGVN
SILPKEHGSQFFYLPIIKHSDDEVSATASWDSSVHDSVHLNRVTPQNERIYLIVKTTVQL
SHPAAMELVLRKRIAANIYNKQSFTQSLKRRISLKNIFYSCGVTYEIVSNIPKATEEIED
RETLALLAARSENEGTSDGETYIEKYTRGVLQVENILSLERLRQAVTVKEALSTKARHIR
RSLSTPNVHNVSSSRPDLSGFDEDDKGWPENQLDMSDYSSSYQDVACYGTLPRDSPRRNK
EGCTSETPHALTVSPFKAFSPQPPKFFKPLMPVKEEHKKRIALEARPLLSQESMPPPQAH
NPGCIVPSGSNGSSMPVEHNSKREKKIDSEEEENELEAINRKLISSQPYVPVEFADFSVY
NASLENREWFSSKVDLSNSRVLEKEVSRSPTTSSITSGYFSHSASNATLSDMVVPSSDSS
DQLAIQTKDADSTEHSTPSLVHDFRPSSNKELTEVEKGLVKDKIIVVPLKENSALAKGSP
SSQSIPEKNSKSLCRTGSCSELDACPSKISQPARGFCPREVTVEHTTNILEDHSFTEFMG
VSEGKDFDGLTDSSAGELSSRRSLPNKTGGKTVSDGLHHPSQLHSKLENDQVIIPEAAFW
VLCCQ
Enzyme 16 Number of Residues 1805
Enzyme 16 Molecular Weight 202310
Enzyme 16 Theoretical pI 5.31
Enzyme 16 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • microtubule motor activity
  • motor activity
  • nucleotide binding
  • purine nucleotide binding
Process
  • cell organization and biogenesis
  • cellular physiological process
  • cytoskeleton organization and biogenesis
  • microtubule-based movement
  • microtubule-based process
  • organelle organization and biogenesis
  • physiological process
Component
  • microtubule associated complex
  • protein complex
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Plus end-directed microtubule-dependent motor protein involved in mannose-6-phosphate receptor (M6PR) transport to the plasma membrane
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID Q9H1H9 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name KI13A_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID AJ291578 Link Image
Enzyme 16 GeneCard ID Q9H1H9 Link Image
Enzyme 16 GenAtlas ID KIF13A Link Image
Enzyme 16 HGNC ID HGNC:14566 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 17022
Enzyme 17 Name WD repeat domain phosphoinositide-interacting protein 1
Enzyme 17 Synonyms
  1. WIPI-1
  2. WD40 repeat protein interacting with phosphoinositides of 49 kDa
  3. WIPI 49 kDa
  4. Atg18 protein homolog
Enzyme 17 Gene Name WIPI1
Enzyme 17 Protein Sequence >WD repeat domain phosphoinositide-interacting protein 1
MEAEAADAPPGGVESALSCFSFNQDCTSLATGTKAGYKLFSLSSVEQLDQVHGSNEIPDV
YIVERLFSSSLVVVVSHTKPRQMNVYHFKKGTEICNYSYSSNILSIRLNRQRLLVCLEES
IYIHNIKDMKLLKTLLDIPANPTGLCALSINHSNSYLAYPGSLTSGEIVLYDGNSLKTVC
TIAAHEGTLAAITFNASGSKLASASEKGTVIRVFSVPDGQKLYEFRRGMKRYVTISSLVF
SMDSQFLCASSNTETVHIFKLEQVTNSRPEEPSTWSGYMGKMFMAATNYLPTQVSDMMHQ
DRAFATARLNFSGQRNICTLSTIQKLPRLLVASSSGHLYMYNLDPQDGGECVLIKTHSLL
GSGTTEENKENDLRPSLPQSYAATVARPSASSASTVPGYSEDGGALRGEVIPEHEFATGP
VCLDDENEFPPIILCRGNQKGKTKQS
Enzyme 17 Number of Residues 446
Enzyme 17 Molecular Weight 48674
Enzyme 17 Theoretical pI 6.58
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function May play a role in autophagy. May regulate the trafficking of proteins involved in the mannose-6-phosphate receptor (MPR) recycling pathway
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function Not Available
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein Not Available
Enzyme 17 UniProtKB/Swiss-Prot ID Q5MNZ9 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name WIPI1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID AY691424 Link Image
Enzyme 17 GeneCard ID Q5MNZ9 Link Image
Enzyme 17 GenAtlas ID WIPI1 Link Image
Enzyme 17 HGNC ID HGNC:25471 Link Image
Enzyme 17 Chromosome Location 17
Enzyme 17 Locus 17q24.2
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
Enzyme 17 Metabolite References Not Available