|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6316 |
| Enzyme 1 Name |
N-acetyl-D-glucosamine kinase |
| Enzyme 1 Synonyms |
- N-acetylglucosamine kinase
- 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 |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
6491737  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9UJ70  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
NAGK_HUMAN  |
| 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  |
| Enzyme 1 GeneCard ID |
NAGK  |
| Enzyme 1 GenAtlas ID |
NAGK  |
| Enzyme 1 HGNC ID |
HGNC:17174  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2p13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6317 |
| Enzyme 2 Name |
Acidic mammalian chitinase |
| Enzyme 2 Synonyms |
- AMCase
- 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 |
|
|
| 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 |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
133893286  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9BZP6  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
CHIA_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
CHIA  |
| Enzyme 2 GenAtlas ID |
CHIA  |
| Enzyme 2 HGNC ID |
HGNC:17432  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p13.2 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6319 |
| Enzyme 3 Name |
Chitotriosidase-1 |
| Enzyme 3 Synonyms |
- 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 |
|
|
| 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 |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q13231  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
CHIT1_HUMAN  |
| Enzyme 3 PDB ID |
1WB0  |
| 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  |
| Enzyme 3 GeneCard ID |
CHIT1  |
| Enzyme 3 GenAtlas ID |
CHIT1  |
| Enzyme 3 HGNC ID |
HGNC:1936  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1q31-q32 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
|
| 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 |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
61741895  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q2VT96  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
Q2VT96_HUMAN  |
| 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  |
| Enzyme 4 GeneCard ID |
Not Available |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
HGNC:17432  |
| 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 |
|
|
| 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 |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
62361795  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q1M0P3  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
Q1M0P3_HUMAN  |
| 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  |
| Enzyme 5 GeneCard ID |
Not Available |
| Enzyme 5 GenAtlas ID |
Not Available |
| Enzyme 5 HGNC ID |
HGNC:17432  |
| 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 |
|
|
| 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 |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
62361793  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q1M0P4  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
Q1M0P4_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
Not Available |
| Enzyme 6 GenAtlas ID |
Not Available |
| Enzyme 6 HGNC ID |
HGNC:17432  |
| 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 |
|
|
| 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 |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
158254840  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
A8K3T7  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
A8K3T7_HUMAN  |
| 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  |
| Enzyme 7 GeneCard ID |
Not Available |
| Enzyme 7 GenAtlas ID |
Not Available |
| Enzyme 7 HGNC ID |
HGNC:17432  |
| 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 |
|
|
| 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 |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
146218445  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
A5D6V7  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
A5D6V7_HUMAN  |
| 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  |
| Enzyme 8 GeneCard ID |
CHIA  |
| Enzyme 8 GenAtlas ID |
CHIA  |
| Enzyme 8 HGNC ID |
HGNC:17432  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
1p13.2 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- 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
]
|
| 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 |
|
|
| 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 |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
56205873  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q5VUV3  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
Q5VUV3_HUMAN  |
| 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  |
| Enzyme 9 GeneCard ID |
CHIA  |
| Enzyme 9 GenAtlas ID |
CHIA  |
| Enzyme 9 HGNC ID |
HGNC:17432  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1p13.2 |
| Enzyme 9 SNPs |
SNPJam Report  |
| 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 |
|
|
| 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 |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
56205871  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q5VUV5  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
Q5VUV5_HUMAN  |
| 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  |
| Enzyme 10 GeneCard ID |
CHIA  |
| Enzyme 10 GenAtlas ID |
CHIA  |
| Enzyme 10 HGNC ID |
HGNC:17432  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
1p13.2 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
Not Available |
| Enzyme 10 Metabolite References |
Not Available |