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Human Metabolome Database Version 2.5

 

Showing metabocard for Chitin (HMDB03362)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-12 20:21:29
Update Date 2011-01-21 10:15:51
Accession Number HMDB03362
Secondary Accession Numbers Not Available
Common Name Chitin
Description Chitin is an unusual substance as it is a naturally occurring polymer. Its breakdown is conducted by bacteria which have receptors to simple sugars from the decomposition of chitin. If chitin is detected they then produce enzymes to digest the chitin by reducing it to simple sugars and ammonia. Chitin (IPA: [Kaitin]) is one of the main components in the cell walls of fungi, the exoskeletons of insects and other arthropods, and in some other animals. It is a polysaccharide; it is constructed from units of acetylglucosamine (more completely, N-acetyl-D-glucos-2-amine). These are linked together in beta-1,4 fashion (in a similar manner to the glucose units which form cellulose). In effect chitin may be described as cellulose with one hydroxyl group on each monomer replaced by an acetylamine group. This allows for increased hydrogen bonding between adjacent polymers, giving the polymer increased strength. A linear polysaccharide of beta-1->4 linked units of acetylglucosamine. It is the second most abundant biopolymer on earth, found especially in insects and fungi. When deacetylated it is called chitosan.
Synonyms
  1. Poly 2-Acetamido-2-deoxy-D-glucose
  2. [1,4-(N-Acetyl-beta-D-glucosaminyl)]n
  3. [1,4-(N-Acetyl-beta-D-glucosaminyl)]n+1
  4. beta-1,4-Poly-N-acetyl-D-glucosamine
  5. Poly 2-Acetamido-2-deoxy-delta-glucose
  6. [1,4-(N-Acetyl-beta-delta-glucosaminyl)]n
  7. [1,4-(N-Acetyl-beta-delta-glucosaminyl)]n+1
  8. beta-1,4-Poly-N-acetyl-delta-glucosamine
Chemical IUPAC Name N-[(2R,4R,5S)-5-[[(2R,4S,5S)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]methoxymethyl]-2-[[(3S,4R,6R)-5-acetamido-4,6-dihydroxy-2-(hydroxymethyl)oxan-3-yl]methoxymethyl]-4-hydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide
Chemical Formula C28H49N3O16
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Polysaccharides
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • dialkyl ether
  • secondary carboxylic acid amide
  • heterocyclic compound
Biofunction
  • Component of Aminosugars metabolism
Application
Source
  • Endogenous
Average Molecular Weight 683.699
Monoisotopic Molecular Weight 683.311279
Isomeric SMILES CC(=O)NC1[C@H](O)OC(CO)[C@@H](COC[C@@H]2OC(CO)[C@@H](COC[C@@H]3OC(CO)[C@@H](O)[C@H](O)C3NC(C)=O)[C@H](O)C2NC(C)=O)[C@@H]1O
Canonical SMILES CC(=O)NC1C(O)OC(CO)C(COCC2OC(CO)C(COCC3OC(CO)C(O)C(O)C3NC(C)=O)C(O)C2NC(C)=O)C1O
KEGG Compound ID C00461 Link Image
BioCyc ID 14-N-ACETYL-BETA-D-GLUCOSAMINYLN1 Link Image
BiGG ID 2242111 Link Image
Wikipedia Link Chitin Link Image
NuGOwiki Link HMDB03362 Link Image
Metagene Link HMDB03362 Link Image
METLIN ID 6903 Link Image
PubChem Compound 453624 Link Image
PubChem Substance 599272 Link Image
ChEBI ID 17029 Link Image
CAS Registry Number 1398-61-4
InChI Identifier InChI=1/C28H49N3O16/c1-11(35)29-21-19(9-44-8-15-17(5-33)47-28(42)23(25(15)39)31-13(3)37)45-16(4-32)14(24(21)38)7-43-10-20-22(30-12(2)36)27(41)26(40)18(6-34)46-20/h14-28,32-34,38-42H,4-10H2,1-3H3,(H,29,35)(H,30,36)(H,31,37)/t14-,15-,16?,17?,18?,19+,20+,21?,22?,23?,24+,25+,26-,27-,28-/m1/s1
Synthesis Reference Kurita, Keisuke; Koyama, Yoshiyuki; Nishimura, Shinichiro; Kamiya, Mami. Facile preparation of water-soluble chitin from chitosan. Chemistry Letters (1989), (9), 1597-8.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 31.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -3.03 [Predicted by ALOGPS]; -5.5 [Predicted by PubChem via XLOGP]; -2.83 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts
Intestine
Spleen
Testes
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
Glutamate Metabolism SMP00072 Link Image map00250 Link Image
General References
  1. Nakajima M, Atsumi K, Kifune K, Miura K, Kanamaru H: Chitin is an effective material for sutures. Jpn J Surg. 1986 Nov;16(6):418-24. [PubMed Link Image]
  2. Soule JB, Halverson AL, Becker RB, Pistole MC, Orenstein JM: A patient with acquired immunodeficiency syndrome and untreated Encephalitozoon (Septata) intestinalis microsporidiosis leading to small bowel perforation. Response to albendazole. Arch Pathol Lab Med. 1997 Aug;121(8):880-7. [PubMed Link Image]
  3. Gheri G, Sgambati E, Thyrion GD, Vichi D, Orlandini GE: The oligosaccharidic content of the glycoconjugates of the prepubertal descended and undescended testis: lectin histochemical study. Ital J Anat Embryol. 2004 Apr-Jun;109(2):69-84. [PubMed Link Image]
  4. Hatcher VB, Schwarzmann GO, Jeanloz RW, McArthur JW: Changes in the sialic acid concentration in the major cervical glycoprotein from the bonnet monkey (Macaca radiata) during a hormonally induced cycle. Fertil Steril. 1977 Jun;28(6):682-8. [PubMed Link Image]
  5. Piskun RP, Pentiuk AA, Serkova VK, Polesia TL, Savitskaia EA: [Enterosorbents in the treatment of atherosclerosis] Eksp Klin Farmakol. 1998 Mar-Apr;61(2):69-74. [PubMed Link Image]
  6. Kawashita M, Nakao M, Minoda M, Kim HM, Beppu T, Miyamoto T, Kokubo T, Nakamura T: Apatite-forming ability of carboxyl group-containing polymer gels in a simulated body fluid. Biomaterials. 2003 Jun;24(14):2477-84. [PubMed Link Image]
  7. Howling GI, Dettmar PW, Goddard PA, Hampson FC, Dornish M, Wood EJ: The effect of chitin and chitosan on the proliferation of human skin fibroblasts and keratinocytes in vitro. Biomaterials. 2001 Nov;22(22):2959-66. [PubMed Link Image]
  8. Vasstrand EN, Jensen HB: Affinity chromatography of human saliva lysozyme and effect of pH and ionic strength on lytic activity. Scand J Dent Res. 1980 Jun;88(3):219-28. [PubMed Link Image]
  9. Collard CD, Montalto MC, Reenstra WR, Buras JA, Stahl GL: Endothelial oxidative stress activates the lectin complement pathway: role of cytokeratin 1. Am J Pathol. 2001 Sep;159(3):1045-54. [PubMed Link Image]
  10. Shibuya N, Nakamura K, Ogoshi K, Ohta T, Hori Y, Kodama K, Yamamoto M: Modification of mutagenic activities of pro-mutagens by glyco-ursodeoxycholic acid in the Ames assay. Tohoku J Exp Med. 1999 Sep;189(1):1-9. [PubMed Link Image]
  11. Ishihara C, Yoshimatsu K, Tsuji M, Arikawa J, Saiki I, Tokura S, Azuma I: Anti-viral activity of sulfated chitin derivatives against Friend murine leukaemia and herpes simplex type-1 viruses. Vaccine. 1993;11(6):670-4. [PubMed Link Image]
  12. Zampini M, Pruzzo C, Bondre VP, Tarsi R, Cosmo M, Bacciaglia A, Chhabra A, Srivastava R, Srivastava BS: Vibrio cholerae persistence in aquatic environments and colonization of intestinal cells: involvement of a common adhesion mechanism. FEMS Microbiol Lett. 2005 Mar 15;244(2):267-73. [PubMed Link Image]
  13. Xu Y, Olman V, Xu D: Clustering gene expression data using a graph-theoretic approach: an application of minimum spanning trees. Bioinformatics. 2002 Apr;18(4):536-45. [PubMed Link Image]
  14. Sharaev PN, Strelkov NS, Sannikova AA, Zvorykin IA, Men'shikova NN, Sakhabutdinova EP, Gabdrakhmanova NK: [The method for detection of urinary lysozyme] Klin Lab Diagn. 2001 Apr;(4):52-3. [PubMed Link Image]
  15. Farnia P, Mohammadi F, Zarifi Z, Tabatabee DJ, Ganavi J, Ghazisaeedi K, Farnia PK, Gheydi M, Bahadori M, Masjedi MR, Velayati AA: Improving sensitivity of direct microscopy for detection of acid-fast bacilli in sputum: use of chitin in mucus digestion. J Clin Microbiol. 2002 Feb;40(2):508-11. [PubMed Link Image]
  16. Sano H, Matsukubo T, Shibasaki K, Itoi H, Takaesu Y: Inhibition of adsorption of oral streptococci to saliva treated hydroxyapatite by chitin derivatives. Bull Tokyo Dent Coll. 1991 Feb;32(1):9-17. [PubMed Link Image]
  17. Johnson SM, Pappagianis D: The coccidioidal complement fixation and immunodiffusion-complement fixation antigen is a chitinase. Infect Immun. 1992 Jul;60(7):2588-92. [PubMed Link Image]
  18. Wikipedia Link Image
Metabolic Enzymes
  1. N-acetyl-D-glucosamine kinase
  2. Acidic mammalian chitinase
  3. Chitotriosidase-1
  4. Chitinase family protein 3
  5. Chitinase family protein V2
  6. Chitinase family protein V1
  7. cDNA FLJ76132, highly similar to Homo sapiens chitinase, acidic (CHIA), mRNA
  8. CHIA protein
  9. Chitinase, acidic
  10. Chitinase, acidic
Enzyme 1 [top]
Enzyme 1 ID 6316
Enzyme 1 Name N-acetyl-D-glucosamine kinase
Enzyme 1 Synonyms
  1. N-acetylglucosamine kinase
  2. GlcNAc kinase
Enzyme 1 Gene Name NAGK
Enzyme 1 Protein Sequence >N-acetyl-D-glucosamine kinase
MAAIYGGVEGGGTRSEVLLVSEDGKILAEADGLSTNHWLIGTDKCVERINEMVNRAKRKA
GVDPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYLSESYLITTDAAGSIATATPDGG
VVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHD
IGYVKQAMFHYFQVPDRLGILTHLYRDFDKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGE
MLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTQGREIQAQNFFS
SFTLMKLRHSSALGGASLGARHIGHLLPMDYSANAIAFYSYTFS
Enzyme 1 Number of Residues 344
Enzyme 1 Molecular Weight 37375.3
Enzyme 1 Theoretical pI 6.18
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Carbohydrate transport and metabolism
Enzyme 1 Specific Function Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Also has ManNAc kinase activity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate [RN:R01201]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 6491737 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9UJ70 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name NAGK_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1035 bp
ATGGCCGCGATCTATGGGGGTGTAGAGGGGGGAGGCACACGATCCGAGGTCCTTTTAGTC
TCAGAGGATGGGAAGATCCTGGCAGAAGCAGATGGACTGAGCACAAACCACTGGCTGATC
GGGACAGACAAGTGTGTGGAGAGGATCAATGAGATGGTGAACAGGGCCAAACGGAAAGCA
GGGGTGGATCCTCTGGTACCGCTGCGAATTTTGGGCCTATCTCTGAGCGGTGGGGACCAG
GAGGACGCGGGGAGGATCCTGATCGAGGAGCTGAGGGACCGATTTCCCTACCTGAGTGAA
AGCTACTTAATCACCACCGATGCCGCCGGCTCCATCGCCACAGCTACACCGGATGGTGGG
ATTGTGCTCATATCTGGAACAGGCTCCAACTGCAGGCTCATCAACCCTGATGGCTCCGAG
AGTGGCTGCGGCGGCTGGGGCCATATGATGGGTGATGAGGGTTCAGCCTACTGGATCGCA
CACCAAGCAGTGAAAATAGTGTTTGACTCCATTGACAACCTAGAGGCGGCTCCTCATGAT
ATCGGCTACGTCAAACAGGCCATGTTCCACTATTTCCAGGTGCCAGATCGGCTAGGGATA
CTCACTCACCTGTATAGGGACTTTGATAAATGCAGGTTTGCTGGGTTTTGCCGGAAAATT
GCAGAAGGTGCTCAGCAGGGAGACCCCCTTTCCCGCTATATCTTCAGGAAGGCTGGGGAG
ATGCTGGGCAGACACATCGTAGCAGTGTTGCCCGAGATTGACCCGGTCTTGTTCCAGGGC
AAGATTGGACTCCCCATCCTGTGCGTGGGCTCTGTGTGGAAGAGCTGGGAGCTGCTGAAG
GAAGGTTTTCTTTTGGCGCTGACCCAGGGCAGAGAGATCCAGGCTCAGAACTTCTTCTCC
AGCTTCACCCTGATGAAGCTGAGGCACTCCTCCGCTCTGGGTGGGGCCAGCCTAGGGGCC
AGGCACATCGGGCACCTCCTCCCCATGGACTATAGCGCCAATGCCATTGCCTTCTATTCC
TACACCTTTTCCTAG
Enzyme 1 GenBank Gene ID AJ242910 Link Image
Enzyme 1 GeneCard ID NAGK Link Image
Enzyme 1 GenAtlas ID NAGK Link Image
Enzyme 1 HGNC ID HGNC:17174 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Hinderlich S, Berger M, Schwarzkopf M, Effertz K, Reutter W: Molecular cloning and characterization of murine and human N-acetylglucosamine kinase. Eur J Biochem. 2000 Jun;267(11):3301-8. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ: Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics. 2002 Jun;2(6):642-8. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  9. Weihofen WA, Berger M, Chen H, Saenger W, Hinderlich S: Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation. J Mol Biol. 2006 Dec 1;364(3):388-99. Epub 2006 Sep 3. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6317
Enzyme 2 Name Acidic mammalian chitinase
Enzyme 2 Synonyms
  1. AMCase
  2. Lung-specific protein TSA1902
Enzyme 2 Gene Name CHIA
Enzyme 2 Protein Sequence >Acidic mammalian chitinase
MTKLILLTGLVLILNLQLGSAYQLTCYFTNWAQYRPGLGRFMPDNIDPCLCTHLIYAFAG
RQNNEITTIEWNDVTLYQAFNGLKNKNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFI
TSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMV
TAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAY
LNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGI
WAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVW
AIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSS
GGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
Enzyme 2 Number of Residues 476
Enzyme 2 Molecular Weight 52270.4
Enzyme 2 Theoretical pI 5.63
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chitin binding
  • chitinase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • pattern binding
  • polysaccharide binding
Process
  • aminoglycan catabolic process
  • aminoglycan metabolic process
  • carbohydrate metabolic process
  • chitin catabolic process
  • chitin metabolic process
  • metabolic process
  • polysaccharide catabolic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 2 General Function Involved in chitin binding
Enzyme 2 Specific Function Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding
Enzyme 2 Pathways
Enzyme 2 Reactions
  • Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins ALL_REAC (other) R01206 R02334 R06081(G) R06082(G) INHIBITOR Allosamidine [CPD:C05346]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-21
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 133893286 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BZP6 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CHIA_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1431 bp
ATGACAAAGCTTATTCTCCTCACAGGTCTTGTCCTTATACTGAATTTGCAGCTCGGCTCT
GCCTACCAGCTGACATGCTACTTCACCAACTGGGCCCAGTACCGGCCAGGCCTGGGGCGC
TTCATGCCTGACAACATCGACCCCTGCCTCTGTACCCACCTGATCTACGCCTTTGCTGGG
AGGCAGAACAACGAGATCACCACCATCGAATGGAATGATGTGACTCTCTACCAAGCTTTC
AATGGCCTGAAAAATAAGAACAGCCAGCTGAAAACTCTCCTGGCCATTGGAGGCTGGAAC
TTCGGGACTGCCCCTTTCACTGCCATGGTTTCTACTCCTGAGAACCGCCAGACTTTCATC
ACCTCAGTCATCAAATTCCTGCGCCAGTATGAGTTTGACGGGCTGGACTTTGACTGGGAG
TACCCTGGCTCTCGTGGGAGCCCTCCTCAGGACAAGCATCTCTTCACTGTCCTGGTGCAG
GAAATGCGTGAAGCTTTTGAGCAGGAGGCCAAGCAGATCAACAAGCCCAGGCTGATGGTC
ACTGCTGCAGTAGCTGCTGGCATCTCCAATATCCAGTCTGGCTATGAGATCCCCCAACTG
TCACAGTACCTGGACTACATCCATGTCATGACCTACGACCTCCATGGCTCCTGGGAGGGC
TACACTGGAGAGAACAGCCCCCTCTACAAATACCCGACTGACACCGGCAGCAACGCCTAC
CTCAATGTGGATTATGTCATGAACTACTGGAAGGACAATGGAGCACCAGCTGAGAAGCTC
ATCGTTGGATTCCCTACCTATGGACACAACTTCATCCTGAGCAACCCCTCCAACACTGGA
ATTGGTGCCCCCACCTCTGGTGCTGGTCCTGCTGGGCCCTATGCCAAGGAGTCTGGGATC
TGGGCTTACTACGAGATCTGTACCTTCCTGAAAAATGGAGCCACTCAGGGATGGGATGCC
CCTCAGGAAGTGCCTTATGCCTATCAGGGCAATGTGTGGGTTGGCTATGACAACATCAAG
AGCTTCGATATTAAGGCTCAATGGCTTAAGCACAACAAATTTGGAGGCGCCATGGTCTGG
GCCATTGATCTGGATGACTTCACTGGCACTTTCTGCAACCAGGGCAAGTTTCCCCTAATC
TCCACCCTGAAGAAGGCCCTCGGCCTGCAGAGTGCAAGTTGCACGGCTCCAGCTCAGCCC
ATTGAGCCAATAACTGCTGCTCCCAGTGGCAGCGGGAACGGGAGCGGGAGTAGCAGCTCT
GGAGGCAGCTCGGGAGGCAGTGGATTCTGTGCTGTCAGAGCCAACGGCCTCTACCCCGTG
GCAAATAACAGAAATGCCTTCTGGCACTGCGTGAATGGAGTCACGTACCAGCAGAACTGC
CAGGCCGGGCTTGTCTTCGACACCAGCTGTGATTGCTGCAACTGGGCATAA
Enzyme 2 GenBank Gene ID NM_201653.2 Link Image
Enzyme 2 GeneCard ID CHIA Link Image
Enzyme 2 GenAtlas ID CHIA Link Image
Enzyme 2 HGNC ID HGNC:17432 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p13.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Saito A, Ozaki K, Fujiwara T, Nakamura Y, Tanigami A: Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member. Gene. 1999 Nov 1;239(2):325-31. [PubMed Link Image]
  2. Boot RG, Blommaart EF, Swart E, Ghauharali-van der Vlugt K, Bijl N, Moe C, Place A, Aerts JM: Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. J Biol Chem. 2001 Mar 2;276(9):6770-8. Epub 2000 Nov 20. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Zhu Z, Zheng T, Homer RJ, Kim YK, Chen NY, Cohn L, Hamid Q, Elias JA: Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation. Science. 2004 Jun 11;304(5677):1678-82. [PubMed Link Image]
  6. Hartl D, He CH, Koller B, Da Silva CA, Homer R, Lee CG, Elias JA: Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells. J Biol Chem. 2008 Nov 28;283(48):33472-82. Epub 2008 Sep 29. [PubMed Link Image]
  7. Hartl D, He CH, Koller B, Da Silva CA, Kobayashi Y, Lee CG, Flavell RA, Elias JA: Acidic mammalian chitinase regulates epithelial cell apoptosis via a chitinolytic-independent mechanism. J Immunol. 2009 Apr 15;182(8):5098-106. [PubMed Link Image]
  8. Olland AM, Strand J, Presman E, Czerwinski R, Joseph-McCarthy D, Krykbaev R, Schlingmann G, Chopra R, Lin L, Fleming M, Kriz R, Stahl M, Somers W, Fitz L, Mosyak L: Triad of polar residues implicated in pH specificity of acidic mammalian chitinase. Protein Sci. 2009 Mar;18(3):569-78. [PubMed Link Image]
  9. Seibold MA, Reese TA, Choudhry S, Salam MT, Beckman K, Eng C, Atakilit A, Meade K, Lenoir M, Watson HG, Thyne S, Kumar R, Weiss KB, Grammer LC, Avila P, Schleimer RP, Fahy JV, Rodriguez-Santana J, Rodriguez-Cintron W, Boot RG, Sheppard D, Gilliland FD, Locksley RM, Burchard EG: Differential enzymatic activity of common haplotypic versions of the human acidic Mammalian chitinase protein. J Biol Chem. 2009 Jul 17;284(29):19650-8. Epub 2009 May 12. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6319
Enzyme 3 Name Chitotriosidase-1
Enzyme 3 Synonyms
  1. Chitinase-1
Enzyme 3 Gene Name CHIT1
Enzyme 3 Protein Sequence >Chitotriosidase-1
MVRSVAWAGFMVLLMIPWGSAAKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAG
MTNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFV
NSAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLL
SAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAAS
LNVDAAVQQWLQKGTPASKLILGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGM
LAYYEVCSWKGATKQRIQDQKVPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWAL
DLDDFAGFSCNQGRYPLIQTLRQELSLPYLPSGTPELEVPKPGQPSEPEHGPSPGQDTFC
QGKADGLYPNPRERSSFYSCAAGRLFQQSCPTGLVFSNSCKCCTWN
Enzyme 3 Number of Residues 466
Enzyme 3 Molecular Weight 51681.0
Enzyme 3 Theoretical pI 6.96
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chitin binding
  • chitinase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • pattern binding
  • polysaccharide binding
Process
  • aminoglycan catabolic process
  • aminoglycan metabolic process
  • carbohydrate metabolic process
  • chitin catabolic process
  • chitin metabolic process
  • metabolic process
  • polysaccharide catabolic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 3 General Function Involved in chitin binding
Enzyme 3 Specific Function Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity
Enzyme 3 Pathways
Enzyme 3 Reactions
  • Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins ALL_REAC (other) R01206 R02334 R06081(G) R06082(G) INHIBITOR Allosamidine [CPD:C05346]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-21
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID Q13231 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CHIT1_HUMAN Link Image
Enzyme 3 PDB ID 1WB0 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1401 bp
ATGGTGCGGTCTGTGGCCTGGGCAGGTTTCATGGTCCTGCTGATGATCCCATGGGGCTCT
GCTGCAAAACTGGTCTGCTACTTCACCAACTGGGCCCAGTACAGACAGGGGGAGGCTCGC
TTCCTGCCCAAGGACTTGGACCCCAGCCTTTGCACCCACCTCATCTACGCCTTCGCTGGC
ATGACCAACCACCAGCTGAGCACCACTGAGTGGAATGACGAGACTCTCTACCAGGAGTTC
AATGGCCTGAAGAAGATGAATCCCAAGCTGAAGACCCTGTTAGCCATCGGAGGCTGGAAT
TTCGGCACTCAGAAGTTCACAGATATGGTAGCCACGGCCAACAACCGTCAGACCTTTGTC
AACTCGGCCATCAGGTTTCTGCGCAAATACAGCTTTGACGGCCTTGACCTTGACTGGGAG
TACCCAGGAAGCCAGGGGAGCCCTGCCGTAGACAAGGAGCGCTTCACAACCCTGGTACAG
GACTTGGCCAATGCCTTCCAGCAGGAAGCCCAGACCTCAGGGAAGGAACGCCTTCTTCTG
AGTGCAGCGGTTCCAGCTGGGCAGACCTATGTGGATGCTGGATACGAGGTGGACAAAATC
GCCCAGAACCTGGATTTTGTCAACCTTATGGCCTACGACTTCCATGGCTCTTGGGAGAAG
GTCACGGGACATAACAGCCCCCTCTACAAGAGGCAAGAAGAGAGTGGTGCAGCAGCCAGC
CTCAACGTGGATGCTGCTGTGCAACAGTGGCTGCAGAAGGGGACCCCTGCCAGCAAGCTG
ATCCTTGGCATGCCTACCTACGGACGCTCCTTCACACTGGCCTCCTCATCAGACACCAGA
GTGGGGGCCCCAGCCACAGGGTCTGGCACTCCAGGCCCCTTCACCAAGGAAGGAGGGATG
CTGGCCTACTATGAAGTCTGCTCCTGGAAGGGGGCCACCAAACAGAGAATCCAGGATCAG
AAGGTGCCCTACATCTTCCGGGACAACCAGTGGGTGGGCTTTGATGATGTGGAGAGCTTC
AAAACCAAGGTCAGCTATCTGAAGCAGAAGGGACTGGGCGGGGCCATGGTCTGGGCACTG
GACTTAGATGACTTTGCCGGCTTCTCCTGCAACCAGGGCCGATACCCCCTCATCCAGACG
CTACGGCAGGAACTGAGTCTTCCATACTTGCCTTCAGGCACCCCAGAGCTTGAAGTTCCA
AAACCAGGTCAGCCCTCTGAACCTGAGCATGGCCCCAGCCCTGGACAAGACACGTTCTGC
CAGGGCAAAGCTGATGGGCTCTATCCCAATCCTCGGGAACGGTCCAGCTTCTACAGCTGT
GCAGCGGGGCGGCTGTTCCAGCAAAGCTGCCCGACAGGCCTGGTGTTCAGCAACTCCTGC
AAATGCTGCACCTGGAATTGA
Enzyme 3 GenBank Gene ID U29615 Link Image
Enzyme 3 GeneCard ID CHIT1 Link Image
Enzyme 3 GenAtlas ID CHIT1 Link Image
Enzyme 3 HGNC ID HGNC:1936 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1q31-q32
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Boot RG, Renkema GH, Strijland A, van Zonneveld AJ, Aerts JM: Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages. J Biol Chem. 1995 Nov 3;270(44):26252-6. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Renkema GH, Boot RG, Muijsers AO, Donker-Koopman WE, Aerts JM: Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins. J Biol Chem. 1995 Feb 3;270(5):2198-202. [PubMed Link Image]
  4. Boot RG, Renkema GH, Verhoek M, Strijland A, Bliek J, de Meulemeester TM, Mannens MM, Aerts JM: The human chitotriosidase gene. Nature of inherited enzyme deficiency. J Biol Chem. 1998 Oct 2;273(40):25680-5. [PubMed Link Image]
  5. Fusetti F, von Moeller H, Houston D, Rozeboom HJ, Dijkstra BW, Boot RG, Aerts JM, van Aalten DM: Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins. J Biol Chem. 2002 Jul 12;277(28):25537-44. Epub 2002 Apr 17. [PubMed Link Image]
  6. Rao FV, Houston DR, Boot RG, Aerts JM, Sakuda S, van Aalten DM: Crystal structures of allosamidin derivatives in complex with human macrophage chitinase. J Biol Chem. 2003 May 30;278(22):20110-6. Epub 2003 Mar 14. [PubMed Link Image]
  7. Rao FV, Houston DR, Boot RG, Aerts JM, Hodkinson M, Adams DJ, Shiomi K, Omura S, van Aalten DM: Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases. Chem Biol. 2005 Jan;12(1):65-76. [PubMed Link Image]
  8. Bussink AP, Verhoek M, Vreede J, Ghauharali-van der Vlugt K, Donker-Koopman WE, Sprenger RR, Hollak CE, Aerts JM, Boot RG: Common G102S polymorphism in chitotriosidase differentially affects activity towards 4-methylumbelliferyl substrates. FEBS J. 2009 Oct;276(19):5678-88. Epub 2009 Sep 2. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 16921
Enzyme 4 Name Chitinase family protein 3
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name Not Available
Enzyme 4 Protein Sequence >Chitinase family protein 3
ETSSSVHEQVADSGAQAVAFQSGGESSIVWSCPYTEFAARNSQLKTLLAIGGWNFGTAPF
TAMVSTPENRQTFITSVIRFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAF
EQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENS
PLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTS
GAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKA
QWLKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITA
APSGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVF
DTSCDCCNWA
Enzyme 4 Number of Residues 430
Enzyme 4 Molecular Weight 46615.5
Enzyme 4 Theoretical pI 4.81
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chitin binding
  • chitinase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • pattern binding
  • polysaccharide binding
Process
  • aminoglycan catabolic process
  • aminoglycan metabolic process
  • carbohydrate metabolic process
  • chitin catabolic process
  • chitin metabolic process
  • metabolic process
  • polysaccharide catabolic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 4 General Function Involved in chitin binding
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 61741895 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q2VT96 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q2VT96_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1293 bp
GAAACCTCCTCGTCTGTGCACGAACAGGTGGCCGACTCTGGAGCCCAGGCTGTTGCTTTC
CAGTCTGGTGGTGAATCCTCCATAGTCTGGTCTTGTCCTTATACTGAATTTGCAGCTCGG
AACAGCCAGCTGAAAACTCTCCTGGCCATTGGAGGCTGGAACTTCGGGACTGCCCCTTTC
ACTGCCATGGTTTCTACTCCTGAGAACCGCCAGACTTTCATCACCTCAGTCATCAGATTC
CTGCGCCAGTATGAGTTTGACGGGCTGGACTTTGACTGGGAGTACCCTGGCTCTCGTGGG
AGCCCTCCTCAGGACAAGCATCTCTTCACTGTCCTGGTGCAGGAAATGCGTGAAGCTTTT
GAGCAGGAGGCCAAGCAGATCAACAAGCCCAGGCTGATGGTCACTGCTGCAGTAGCTGCT
GGCATCTCCAATATCCAGTCTGGCTATGAGATCCCCCAACTGTCACAGTACCTGGACTAC
ATCCATGTCATGACCTACGACCTCCATGGCTCCTGGGAGGGCTACACTGGAGAGAACAGC
CCCCTCTACAAATACCCGACTGACACCGGCAGCAACGCCTACCTCAATGTGGATTATGTC
ATGAACTACTGGAAGGACAATGGAGCACCAGCTGAGAAGCTCATCGTTGGATTCCCTACC
TATGGACACAACTTCATCCTGAGCAACCCCTCCAACACTGGAATTGGTGCCCCCACCTCT
GGTGCTGGTCCTGCTGGGCCCTATGCCAAGGAGTCTGGGATCTGGGCTTACTACGAGATC
TGTACCTTCCTGAAAAATGGAGCCACTCAGGGATGGGATGCCCCTCAGGAAGTGCCTTAT
GCCTATCAGGGCAATGTGTGGGTTGGCTATGACAACATCAAGAGCTTCGATATTAAGGCT
CAATGGCTTAAGCACAACAAATTTGGAGGCGCCATGGTCTGGGCCATTGATCTGGATGAC
TTCACTGGCACTTTCTGCAACCAGGGCAAGTTTCCCCTAATCTCCACCCTGAAGAAGGCC
CTCGGCCTGCAGAGTGCAAGTTGCACGGCTCCAGCTCAGCCCATTGAGCCAATAACTGCT
GCTCCCAGTGGCAGCGGGAACGGGAGCGGGAGTAGCAGCTCTGGAGGCAGCTCAGGAGGC
AGTGGATTCTGTGCTGTCAGAGCCAACGGCCTCTACCCCGTGGCAAATAACAGAAATGCC
TTCTGGCACTGCGTGAATGGAGTCACGTACCAGCAGAACTGCCAGGCCGGGCTTGTCTTC
GACACCAGCTGTGATTGCTGCAACTGGGCATAA
Enzyme 4 GenBank Gene ID AY825504 Link Image
Enzyme 4 GeneCard ID Not Available
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID HGNC:17432 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs Not Available
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16922
Enzyme 5 Name Chitinase family protein V2
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name Not Available
Enzyme 5 Protein Sequence >Chitinase family protein V2
MREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGY
TGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGI
GAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNVKS
FDIKAQWLKHNKSGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPI
EPITAAPSGSGNGSGSSSSGGSSGGSGFCAGRANGLYPVASNRNAFWHCVNGVTYQQNCQ
AGLVFDTSCDCCNWA
Enzyme 5 Number of Residues 315
Enzyme 5 Molecular Weight 33762.3
Enzyme 5 Theoretical pI 5.26
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chitin binding
  • chitinase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • pattern binding
  • polysaccharide binding
Process
  • aminoglycan catabolic process
  • aminoglycan metabolic process
  • carbohydrate metabolic process
  • chitin catabolic process
  • chitin metabolic process
  • metabolic process
  • polysaccharide catabolic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 5 General Function Involved in chitin binding
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 62361795 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q1M0P3 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q1M0P3_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >948 bp
ATGCGTGAAGCTTTTGAGCAGGAGGCCAAGCAGATCAACAAGCCCAGGCTGATGGTCACT
GCTGCAGTAGCTGCTGGCATCTCCAATATCCAGTCTGGCTATGAGATCCCCCAACTGTCA
CAGTACCTGGACTACATCCATGTCATGACCTACGACCTCCATGGCTCCTGGGAGGGCTAC
ACTGGAGAGAACAGCCCCCTCTACAAATACCCGACTGACACCGGCAGCAACGCCTACCTC
AATGTGGATTATGTCATGAACTACTGGAAGGACAATGGAGCACCAGCTGAGAAGCTCATC
GTTGGATTCCCTACCTATGGACACAACTTCATCCTGAGCAACCCCTCCAACACTGGAATT
GGTGCCCCCACCTCTGGTGCTGGTCCTGCTGGGCCCTATGCCAAGGAGTCTGGGATCTGG
GCTTACTACGAGATCTGTACCTTCCTGAAAAATGGAGCCACTCAGGGATGGGATGCCCCT
CAGGAAGTGCCTTATGCCTATCAGGGCAATGTGTGGGTTGGCTATGACAACGTCAAGAGC
TTCGATATTAAGGCTCAATGGCTTAAGCACAACAAATCTGGAGGCGCCATGGTCTGGGCC
ATTGATCTGGATGACTTCACTGGCACTTTCTGCAACCAGGGCAAGTTTCCCCTAATCTCC
ACCCTGAAGAAGGCCCTCGGCCTGCAGAGTGCAAGTTGCACGGCTCCAGCTCAGCCCATT
GAGCCAATAACTGCTGCTCCCAGTGGCAGCGGGAACGGGAGCGGGAGTAGCAGCTCTGGA
GGCAGCTCGGGAGGCAGTGGATTCTGTGCTGGCAGAGCCAACGGCCTCTACCCCGTGGCA
AGTAACAGAAATGCCTTCTGGCACTGCGTGAATGGAGTCACGTACCAGCAGAACTGCCAG
GCCGGGCTTGTCTTCGACACCAGCTGTGATTGCTGCAACTGGGCATAA
Enzyme 5 GenBank Gene ID AY911311 Link Image
Enzyme 5 GeneCard ID Not Available
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID HGNC:17432 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs Not Available
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16923
Enzyme 6 Name Chitinase family protein V1
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name Not Available
Enzyme 6 Protein Sequence >Chitinase family protein V1
MREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYVHVMTYDLHGSWEGY
TGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGI
GAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWAGYDNVKS
FDIKAQWLKHNKSGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPI
EPITAAPSGSGNGSGSSSSGGSSGGSGFCAGRANGLYPVANNRNAFWHCVNGVTYQQNCQ
AGLVFDTSCDCCNWA
Enzyme 6 Number of Residues 315
Enzyme 6 Molecular Weight 33747.3
Enzyme 6 Theoretical pI 5.26
Enzyme 6 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chitin binding
  • chitinase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • pattern binding
  • polysaccharide binding
Process
  • aminoglycan catabolic process
  • aminoglycan metabolic process
  • carbohydrate metabolic process
  • chitin catabolic process
  • chitin metabolic process
  • metabolic process
  • polysaccharide catabolic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 6 General Function Involved in chitin binding
Enzyme 6 Specific Function Not Available
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 62361793 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q1M0P4 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q1M0P4_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >948 bp
ATGCGTGAAGCTTTTGAGCAGGAGGCCAAGCAGATCAACAAGCCCAGGCTGATGGTCACT
GCTGCAGTAGCTGCTGGCATCTCCAATATCCAGTCTGGCTATGAGATCCCCCAACTGTCA
CAGTACCTGGACTACGTCCATGTCATGACCTACGACCTCCATGGCTCCTGGGAGGGCTAC
ACTGGAGAGAACAGCCCCCTCTACAAATACCCGACTGACACCGGCAGCAACGCCTACCTC
AATGTGGATTATGTCATGAACTACTGGAAGGACAATGGAGCACCAGCTGAGAAGCTCATC
GTTGGATTCCCTACCTATGGACACAACTTCATCCTGAGCAACCCCTCCAACACTGGAATT
GGTGCCCCCACCTCTGGTGCTGGTCCTGCTGGGCCCTATGCCAAGGAGTCTGGGATCTGG
GCTTACTACGAGATCTGTACCTTCCTGAAAAATGGAGCCACTCAGGGATGGGATGCCCCT
CAGGAAGTGCCTTATGCCTATCAGGGCAATGTATGGGCTGGCTATGACAACGTCAAGAGC
TTCGATATTAAGGCTCAATGGCTTAAGCACAACAAATCTGGAGGCGCCATGGTCTGGGCC
ATTGATCTGGATGACTTCACTGGCACTTTCTGCAACCAGGGCAAGTTTCCCCTAATCTCC
ACCCTGAAGAAGGCCCTCGGCTTGCAGAGTGCAAGTTGCACGGCTCCAGCTCAGCCCATT
GAGCCAATAACTGCTGCTCCCAGTGGCAGCGGGAACGGGAGCGGGAGTAGCAGCTCTGGA
GGCAGCTCGGGAGGCAGTGGATTCTGTGCTGGCAGAGCCAACGGCCTCTACCCCGTGGCA
AATAACAGAAATGCCTTCTGGCACTGCGTGAATGGAGTCACGTACCAGCAGAACTGCCAG
GCCGGGCTTGTCTTCGACACCAGCTGTGATTGCTGCAACTGGGCATAA
Enzyme 6 GenBank Gene ID AY911310 Link Image
Enzyme 6 GeneCard ID Not Available
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID HGNC:17432 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs Not Available
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 17158
Enzyme 7 Name cDNA FLJ76132, highly similar to Homo sapiens chitinase, acidic (CHIA), mRNA
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name Not Available
Enzyme 7 Protein Sequence >cDNA FLJ76132, highly similar to Homo sapiens chitinase, acidic (CHIA), mRNA
MVSTPENRQTSITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQ
EAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPL
YKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGA
GPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQW
LKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAP
SGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDT
SCDCCNWA
Enzyme 7 Number of Residues 368
Enzyme 7 Molecular Weight 40078.4
Enzyme 7 Theoretical pI 4.97
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chitin binding
  • chitinase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • pattern binding
  • polysaccharide binding
Process
  • aminoglycan catabolic process
  • aminoglycan metabolic process
  • carbohydrate metabolic process
  • chitin catabolic process
  • chitin metabolic process
  • metabolic process
  • polysaccharide catabolic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 7 General Function Involved in chitin binding
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 158254840 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID A8K3T7 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name A8K3T7_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1107 bp
ATGGTTTCTACTCCTGAGAACCGCCAGACTTCCATCACCTCAGTCATCAAATTCCTGCGC
CAGTATGAGTTTGACGGGCTGGACTTTGACTGGGAGTACCCTGGCTCTCGTGGGAGCCCT
CCTCAGGACAAGCATCTCTTCACTGTCCTGGTGCAGGAAATGCGTGAAGCTTTTGAGCAG
GAGGCCAAGCAGATCAACAAGCCCAGGCTGATGGTCACTGCTGCAGTAGCTGCTGGCATC
TCCAATATCCAGTCTGGCTATGAGATCCCCCAACTGTCACAGTACCTGGACTACATCCAT
GTCATGACCTACGACCTCCATGGCTCCTGGGAGGGCTACACTGGAGAGAACAGCCCCCTC
TACAAATACCCGACTGACACCGGCAGCAACGCCTACCTCAATGTGGATTATGTCATGAAC
TACTGGAAGGACAATGGAGCACCAGCTGAGAAGCTCATCGTTGGATTCCCTACCTATGGA
CACAACTTCATCCTGAGCAACCCCTCCAACACTGGAATTGGTGCCCCCACCTCTGGTGCT
GGTCCTGCTGGGCCCTATGCCAAGGAGTCTGGGATCTGGGCTTACTACGAGATCTGTACC
TTCCTGAAAAATGGAGCCACTCAGGGATGGGATGCCCCTCAGGAAGTGCCTTATGCCTAT
CAGGGCAATGTGTGGGTTGGCTATGACAACATCAAGAGCTTCGATATTAAGGCTCAATGG
CTTAAGCACAACAAATTTGGAGGCGCCATGGTCTGGGCCATTGATCTGGATGACTTCACT
GGCACTTTCTGCAACCAGGGCAAGTTTCCCCTAATCTCCACCCTGAAGAAGGCCCTCGGC
CTGCAGAGTGCAAGTTGCACGGCTCCAGCTCAGCCCATTGAGCCAATAACTGCTGCTCCC
AGTGGCAGCGGGAACGGGAGCGGGAGTAGCAGCTCTGGAGGCAGCTCGGGAGGCAGTGGA
TTCTGTGCTGTCAGAGCCAACGGCCTCTACCCCGTGGCAAATAACAGAAATGCCTTCTGG
CACTGCGTGAATGGAGTCACGTACCAGCAGAACTGCCAGGCCGGGCTTGTCTTCGACACC
AGCTGTGATTGCTGCAACTGGGCATAA
Enzyme 7 GenBank Gene ID AK290702 Link Image
Enzyme 7 GeneCard ID Not Available
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID HGNC:17432 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs Not Available
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 17159
Enzyme 8 Name CHIA protein
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name CHIA
Enzyme 8 Protein Sequence >CHIA protein
KAYSPHRSCPYTEFAARNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFITSVIRFLRQ
YEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGIS
NIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNY
WKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTF
LKNGATQGWDAPQEVPYAYQGNVWVGYDNVKSFDIKAQWLKHNKSGGAMVWAIDLDDFTG
TFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGF
CAGRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
Enzyme 8 Number of Residues 407
Enzyme 8 Molecular Weight 44306.1
Enzyme 8 Theoretical pI 5.90
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chitin binding
  • chitinase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • pattern binding
  • polysaccharide binding
Process
  • aminoglycan catabolic process
  • aminoglycan metabolic process
  • carbohydrate metabolic process
  • chitin catabolic process
  • chitin metabolic process
  • metabolic process
  • polysaccharide catabolic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 8 General Function Involved in chitin binding
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 146218445 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID A5D6V7 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name A5D6V7_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1225 bp
CAAAGCTTATTCTCCTCACAGGTCTTGTCCTTATACTGAATTTGCAGCTCGGAACAGCCA
GCTGAAAACTCTCCTGGCCATTGGAGGCTGGAACTTCGGGACTGCCCCTTTCACTGCCAT
GGTTTCTACTCCTGAGAACCGCCAGACTTTCATCACCTCAGTCATCAGATTCCTGCGCCA
GTATGAGTTTGACGGGCTGGACTTTGACTGGGAGTACCCTGGCTCTCGTGGGAGCCCTCC
TCAGGACAAGCATCTCTTCACTGTCCTGGTGCAGGAAATGCGTGAAGCTTTTGAGCAGGA
GGCCAAGCAGATCAACAAGCCCAGGCTGATGGTCACTGCTGCAGTAGCTGCTGGCATCTC
CAATATCCAGTCTGGCTATGAGATCCCCCAACTGTCACAGTACCTGGACTACATCCATGT
CATGACCTACGACCTCCATGGCTCCTGGGAGGGCTACACTGGAGAGAACAGCCCCCTCTA
CAAATACCCGACTGACACCGGCAGCAACGCCTACCTCAATGTGGATTATGTCATGAACTA
CTGGAAGGACAATGGAGCACCAGCTGAGAAGCTCATCGTTGGATTCCCTACCTATGGACA
CAACTTCATCCTGAGCAACCCCTCCAACACTGGAATTGGTGCCCCCACCTCTGGTGCTGG
TCCTGCTGGGCCCTATGCCAAGGAGTCTGGGATCTGGGCTTACTACGAGATCTGTACCTT
CCTGAAAAATGGAGCCACTCAGGGATGGGATGCCCCTCAGGAAGTGCCTTATGCCTATCA
GGGCAATGTGTGGGTTGGCTATGACAACGTCAAGAGCTTCGATATTAAGGCTCAATGGCT
TAAGCACAACAAATCTGGAGGCGCCATGGTCTGGGCCATTGATCTGGATGACTTCACTGG
CACTTTCTGCAACCAGGGCAAGTTTCCCCTAATCTCCACCCTGAAGAAGGCCCTCGGCCT
GCAGAGTGCAAGTTGCACGGCTCCAGCTCAGCCCATTGAGCCAATAACTGCTGCTCCCAG
TGGCAGCGGGAACGGGAGCGGGAGTAGCAGCTCTGGAGGCAGCTCGGGAGGCAGTGGATT
CTGTGCTGGCAGAGCCAACGGCCTCTACCCCGTGGCAAATAACAGAAATGCCTTCTGGCA
CTGCGTGAATGGAGTCACGTACCAGCAGAACTGCCAGGCCGGGCTTGTCTTCGACACCAG
CTGTGATTGCTGCAACTGGGCATAA
Enzyme 8 GenBank Gene ID BC139901 Link Image
Enzyme 8 GeneCard ID CHIA Link Image
Enzyme 8 GenAtlas ID CHIA Link Image
Enzyme 8 HGNC ID HGNC:17432 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1p13.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 17160
Enzyme 9 Name Chitinase, acidic
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name CHIA
Enzyme 9 Protein Sequence >Chitinase, acidic
YSPHRSCPYTEFAARNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFITSVIKFLRQYE
FDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGISNI
QSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNYWK
DNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLK
NGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTF
CNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGFCA
VRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
Enzyme 9 Number of Residues 405
Enzyme 9 Molecular Weight 44195.0
Enzyme 9 Theoretical pI 5.61
Enzyme 9 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chitin binding
  • chitinase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • pattern binding
  • polysaccharide binding
Process
  • aminoglycan catabolic process
  • aminoglycan metabolic process
  • carbohydrate metabolic process
  • chitin catabolic process
  • chitin metabolic process
  • metabolic process
  • polysaccharide catabolic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 9 General Function Involved in chitin binding
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 56205873 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q5VUV3 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q5VUV3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1220 bp
AGAACCTAGACACTACGTCTTGTCCTTATACTGAATTTGCAGCTCGGAACAGCCAGCTGA
AAACTCTCCTGGCCATTGGAGGCTGGAACTTCGGGACTGCCCCTTTCACTGCCATGGTTT
CTACTCCTGAGAACCGCCAGACTTTCATCACCTCAGTCATCAAATTCCTGCGCCAGTATG
AGTTTGACGGGCTGGACTTTGACTGGGAGTACCCTGGCTCTCGTGGGAGCCCTCCTCAGG
ACAAGCATCTCTTCACTGTCCTGGTGCAGGAAATGCGTGAAGCTTTTGAGCAGGAGGCCA
AGCAGATCAACAAGCCCAGGCTGATGGTCACTGCTGCAGTAGCTGCTGGCATCTCCAATA
TCCAGTCTGGCTATGAGATCCCCCAACTGTCACAGTACCTGGACTACATCCATGTCATGA
CCTACGACCTCCATGGCTCCTGGGAGGGCTACACTGGAGAGAACAGCCCCCTCTACAAAT
ACCCGACTGACACCGGCAGCAACGCCTACCTCAATGTGGATTATGTCATGAACTACTGGA
AGGACAATGGAGCACCAGCTGAGAAGCTCATCGTTGGATTCCCTACCTATGGACACAACT
TCATCCTGAGCAACCCCTCCAACACTGGAATTGGTGCCCCCACCTCTGGTGCTGGTCCTG
CTGGGCCCTATGCCAAGGAGTCTGGGATCTGGGCTTACTACGAGATCTGTACCTTCCTGA
AAAATGGAGCCACTCAGGGATGGGATGCCCCTCAGGAAGTGCCTTATGCCTATCAGGGCA
ATGTGTGGGTTGGCTATGACAACATCAAGAGCTTCGATATTAAGGCTCAATGGCTTAAGC
ACAACAAATTTGGAGGCGCCATGGTCTGGGCCATTGATCTGGATGACTTCACTGGCACTT
TCTGCAACCAGGGCAAGTTTCCCCTAATCTCCACCCTGAAGAAGGCCCTCGGCCTGCAGA
GTGCAAGTTGCACGGCTCCAGCTCAGCCCATTGAGCCAATAACTGCTGCTCCCAGTGGCA
GCGGGAACGGGAGCGGGAGTAGCAGCTCTGGAGGCAGCTCGGGAGGCAGTGGATTCTGTG
CTGTCAGAGCCAACGGCCTCTACCCCGTGGCAAATAACAGAAATGCCTTCTGGCACTGCG
TGAATGGAGTCACGTACCAGCAGAACTGCCAGGCCGGGCTTGTCTTCGACACCAGCTGTG
ATTGCTGCAACTGGGCATAA
Enzyme 9 GenBank Gene ID AL356387 Link Image
Enzyme 9 GeneCard ID CHIA Link Image
Enzyme 9 GenAtlas ID CHIA Link Image
Enzyme 9 HGNC ID HGNC:17432 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1p13.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 17161
Enzyme 10 Name Chitinase, acidic
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name CHIA
Enzyme 10 Protein Sequence >Chitinase, acidic
ETSSSVHEQVADSGAQAVAFQSGGESSIVWNSQLKTLLAIGGWNFGTAPFTAMVSTPENR
QTFITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKP
RLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTG
SNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAK
ESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGG
AMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSG
SSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
Enzyme 10 Number of Residues 420
Enzyme 10 Molecular Weight 45461.2
Enzyme 10 Theoretical pI 4.79
Enzyme 10 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chitin binding
  • chitinase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • pattern binding
  • polysaccharide binding
Process
  • aminoglycan catabolic process
  • aminoglycan metabolic process
  • carbohydrate metabolic process
  • chitin catabolic process
  • chitin metabolic process
  • metabolic process
  • polysaccharide catabolic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 10 General Function Involved in chitin binding
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 56205871 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q5VUV5 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name Q5VUV5_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1263 bp
GATAGTCAAAAACAATATTGGGGGAGAGAGAGGTAGGTGGGTGATAACCTCCAACCAGAG
CTTCCCAAGGAGATATCACTGTGTCCTTAGAACAGCCAGCTGAAAACTCTCCTGGCCATT
GGAGGCTGGAACTTCGGGACTGCCCCTTTCACTGCCATGGTTTCTACTCCTGAGAACCGC
CAGACTTTCATCACCTCAGTCATCAAATTCCTGCGCCAGTATGAGTTTGACGGGCTGGAC
TTTGACTGGGAGTACCCTGGCTCTCGTGGGAGCCCTCCTCAGGACAAGCATCTCTTCACT
GTCCTGGTGCAGGAAATGCGTGAAGCTTTTGAGCAGGAGGCCAAGCAGATCAACAAGCCC
AGGCTGATGGTCACTGCTGCAGTAGCTGCTGGCATCTCCAATATCCAGTCTGGCTATGAG
ATCCCCCAACTGTCACAGTACCTGGACTACATCCATGTCATGACCTACGACCTCCATGGC
TCCTGGGAGGGCTACACTGGAGAGAACAGCCCCCTCTACAAATACCCGACTGACACCGGC
AGCAACGCCTACCTCAATGTGGATTATGTCATGAACTACTGGAAGGACAATGGAGCACCA
GCTGAGAAGCTCATCGTTGGATTCCCTACCTATGGACACAACTTCATCCTGAGCAACCCC
TCCAACACTGGAATTGGTGCCCCCACCTCTGGTGCTGGTCCTGCTGGGCCCTATGCCAAG
GAGTCTGGGATCTGGGCTTACTACGAGATCTGTACCTTCCTGAAAAATGGAGCCACTCAG
GGATGGGATGCCCCTCAGGAAGTGCCTTATGCCTATCAGGGCAATGTGTGGGTTGGCTAT
GACAACATCAAGAGCTTCGATATTAAGGCTCAATGGCTTAAGCACAACAAATTTGGAGGC
GCCATGGTCTGGGCCATTGATCTGGATGACTTCACTGGCACTTTCTGCAACCAGGGCAAG
TTTCCCCTAATCTCCACCCTGAAGAAGGCCCTCGGCCTGCAGAGTGCAAGTTGCACGGCT
CCAGCTCAGCCCATTGAGCCAATAACTGCTGCTCCCAGTGGCAGCGGGAACGGGAGCGGG
AGTAGCAGCTCTGGAGGCAGCTCGGGAGGCAGTGGATTCTGTGCTGTCAGAGCCAACGGC
CTCTACCCCGTGGCAAATAACAGAAATGCCTTCTGGCACTGCGTGAATGGAGTCACGTAC
CAGCAGAACTGCCAGGCCGGGCTTGTCTTCGACACCAGCTGTGATTGCTGCAACTGGGCA
TAA
Enzyme 10 GenBank Gene ID AL356387 Link Image
Enzyme 10 GeneCard ID CHIA Link Image
Enzyme 10 GenAtlas ID CHIA Link Image
Enzyme 10 HGNC ID HGNC:17432 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p13.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available