|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6092 |
| Enzyme 1 Name |
Hydroxyacylglutathione hydrolase, mitochondrial |
| Enzyme 1 Synonyms |
- Glyoxalase II
- Glx II
|
| Enzyme 1 Gene Name |
HAGH |
| Enzyme 1 Protein Sequence |
>Hydroxyacylglutathione hydrolase, mitochondrial
MVVGRGLLGRRSLAALGAACARRGLGPALLGVFCHTDLRKNLTVDEGTMKVEVLPALTDN
YMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESG
LKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFT
GDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAA
IREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREK
DQFKMPRD
|
| Enzyme 1 Number of Residues |
308 |
| Enzyme 1 Molecular Weight |
33805.6 |
| Enzyme 1 Theoretical pI |
8.23 |
| Enzyme 1 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- hydroxyacylglutathione hydrolase activity
- ion binding
- metal ion binding
- thiolester hydrolase activity
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in hydrolase activity |
| Enzyme 1 Specific Function |
Thiolesterase that catalyzes the hydrolysis of S-D- lactoyl-glutathione to form glutathione and D-lactic acid |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate [RN:R04090]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
94538322  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q16775  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
GLO2_HUMAN  |
| Enzyme 1 PDB ID |
1QH3  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>927 bp
ATGGTGGTGGGCCGAGGGCTGCTCGGCCGCCGCAGCCTCGCCGCGCTGGGAGCCGCCTGC
GCCCGCCGAGGCCTCGGTCCAGCCCTGCTGGGAGTTTTCTGCCACACAGATTTGCGGAAG
AACCTGACCGTGGACGAGGGCACCATGAAGGTAGAGGTGCTGCCTGCCCTGACCGACAAC
TACATGTACCTGGTCATTGATGATGAGACCAAGGAGGCTGCCATTGTGGATCCGGTGCAG
CCCCAGAAGGTCGTGGACGCGGCGAGAAAGCACGGGGTGAAACTGACCACAGTGCTCACC
ACCCACCACCACTGGGACCATGCTGGCGGGAATGAGAAACTGGTCAAGCTGGAGTCGGGA
CTGAAGGTGTACGGGGGTGACGACCGTATCGGGGCCCTGACTCACAAGATCACTCACCTG
TCCACACTGCAGGTGGGGTCTCTGAACGTCAAGTGCCTGGCGACCCCGTGCCACACTTCA
GGACACATTTGTTACTTCGTGAGCAAGCCCGGAGGCTCGGAGCCCCCTGCCGTGTTCACA
GGTGACACCTTGTTTGTGGCTGGCTGCGGGAAGTTCTATGAAGGGACTGCGGATGAGATG
TGTAAAGCTCTGCTGGAGGTCTTGGGCCGGCTCCCCCCGGACACAAGAGTCTACTGTGGC
CACGAGTACACCATCAACAACCTCAAGTTTGCACGCCACGTGGAGCCCGGCAATGCCGCC
ATCCGGGAGAAGCTGGCCTGGGCCAAGGAGAAGTACAGCATCGGGGAGCCCACAGTGCCA
TCCACCCTGGCAGAGGAGTTTACCTACAACCCCTTCATGAGAGTGAGGGAGAAGACGGTG
CAGCAGCACGCAGGTGAGACGGACCCGGTGACCACCATGCGGGCCGTGCGCAGGGAGAAG
GACCAGTTCAAGATGCCCCGGGACTGA
|
| Enzyme 1 GenBank Gene ID |
NM_005326.4  |
| Enzyme 1 GeneCard ID |
HAGH  |
| Enzyme 1 GenAtlas ID |
HAGH  |
| Enzyme 1 HGNC ID |
HGNC:4805  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
16p13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [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
]
- Ridderstrom M, Saccucci F, Hellman U, Bergman T, Principato G, Mannervik B: Molecular cloning, heterologous expression, and characterization of human glyoxalase II. J Biol Chem. 1996 Jan 5;271(1):319-23. [PubMed
]
- Cordell PA, Futers TS, Grant PJ, Pease RJ: The Human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II. J Biol Chem. 2004 Jul 2;279(27):28653-61. Epub 2004 Apr 26. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Cameron AD, Ridderstrom M, Olin B, Mannervik B: Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure. 1999 Sep 15;7(9):1067-78. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
9170 |
| Enzyme 2 Name |
Probable D-lactate dehydrogenase, mitochondrial |
| Enzyme 2 Synonyms |
- DLD
- Lactate dehydrogenase D
|
| Enzyme 2 Gene Name |
LDHD |
| Enzyme 2 Protein Sequence |
>Probable D-lactate dehydrogenase, mitochondrial
MARLLRSATWELFPWRGYCSQKAKGELCRDFVEALKAVVGGSHVSTAAVVREQHGRDESV
HRCEPPDAVVWPQNVEQVSRLAALCYRQGVPIIPFGTGTGLEGGVCAVQGGVCVNLTHMD
RILELNQEDFSVVVEPGVTRKALNAHLRDSGLWFPVDPGADASLCGMAATGASGTNAVRY
GTMRDNVLNLEVVLPDGRLLHTAGRGRHFRFGFWPEIPHHTAWYSPCVSLGRRKSAAGYN
LTGLFVGSEGTLGLITATTLRLHPAPEATVAATCAFPSVQAAVDSTVHILQAAVPVARIE
FLDEVMMDACNRYSKLNCLVAPTLFLEFHGSQQALEEQLQRTEEIVQQNGASDFSWAKEA
EERSRLWTARHNAWYAALATRPGCKGYSTDVCVPISRLPEIVVQTKEDLNASGLTGSIVG
HVGDGNFHCILLVNPDDAEELGRVKAFAEQLGRRALALHGTCTGEHGIGMGKRQLLQEEV
GAVGVETMRQLKAVLDPQGLMNPGKVL
|
| Enzyme 2 Number of Residues |
507 |
| Enzyme 2 Molecular Weight |
54870.2 |
| Enzyme 2 Theoretical pI |
6.65 |
| Enzyme 2 GO Classification |
| Function |
- FAD or FADH2 binding
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- purine nucleoside binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in catalytic activity |
| Enzyme 2 Specific Function |
(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c [RN:R00197]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
37595754  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q86WU2  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
LDHD_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1524 bp
ATGGCCCGACTGCTCAGGTCTGCAACCTGGGAGCTGTTCCCCTGGAGGGGCTACTGCTCC
CAGAAGGCAAAGGGAGAGCTCTGCAGGGACTTCGTAGAGGCTCTGAAGGCCGTGGTGGGC
GGCTCCCACGTGTCCACTGCCGCGGTGGTCCGAGAGCAGCACGGGCGCGATGAGTCGGTG
CACAGGTGCGAACCTCCTGATGCTGTGGTGTGGCCCCAGAACGTGGAGCAGGTCAGCCGG
CTGGCAGCCCTGTGCTATCGCCAAGGTGTGCCCATCATCCCATTCGGCACCGGCACCGGG
CTTGAGGGTGGCGTCTGTGCTGTGCAGGGCGGCGTCTGCGTTAACCTGACGCATATGGAC
CGAATCCTGGAGCTGAACCAGGAGGACTTCTCTGTGGTGGTGGAGCCAGGTGTCACCCGC
AAAGCCCTCAACGCCCACCTGCGGGACAGCGGCCTCTGGTTTCCCGTGGACCCAGGCGCG
GACGCCTCTCTCTGTGGCATGGCGGCCACCGGGGCGTCGGGGACCAACGCGGTCCGCTAC
GGCACCATGCGGGACAACGTGCTCAACCTGGAGGTGGTGCTGCCCGACGGGCGGCTGCTG
CACACGGCGGGCCGAGGCCGGCATTTCCGCTTCGGCTTCTGGCCAGAAATCCCTCATCAC
ACAGCCTGGTACTCACCTTGTGTGTCCCTGGGACGTAGGAAGAGTGCAGCCGGCTACAAC
CTCACGGGGCTCTTCGTGGGCTCCGAGGGGACGCTGGGCCTCATCACAGCCACCACCCTG
CGCCTGCACCCTGCCCCTGAGGCCACAGTGGCCGCCACGTGTGCGTTCCCCAGTGTCCAG
GCTGCTGTGGACAGCACTGTACACATCCTCCAGGCTGCAGTGCCCGTAGCCCGCATTGAG
TTCCTGGATGAAGTCATGATGGATGCCTGCAACAGGTACAGCAAGCTGAATTGCTTAGTG
GCGCCCACACTCTTCCTGGAGTTCCATGGCTCCCAGCAGGCACTGGAGGAGCAGCTGCAG
CGCACAGAGGAGATAGTCCAGCAGAACGGAGCCTCTGACTTCTCCTGGGCCAAGGAGGCC
GAGGAGCGCAGCCGGCTTTGGACAGCACGGCACAATGCCTGGTACGCAGCCCTGGCCACG
CGGCCAGGCTGCAAGGGCTACTCCACGGATGTGTGTGTGCCCATCTCCCGGCTGCCGGAG
ATCGTGGTGCAGACCAAGGAGGATCTGAATGCCTCAGGACTCACAGGAAGCATTGTCGGG
CATGTGGGTGACGGCAACTTCCACTGCATCCTGCTGGTCAACCCTGATGACGCCGAGGAA
CTGGGCAGGGTCAAGGCTTTTGCAGAACAGCTGGGCAGGCGGGCACTGGCTCTCCACGGA
ACGTGCACGGGGGAGCATGGCATCGGAATGGGCAAGCGGCAGCTGCTGCAGGAGGAGGTG
GGCGCCGTGGGCGTGGAGACCATGCGGCAGCTCAAGGCCGTGCTAGACCCCCAAGGCCTC
ATGAATCCAGGCAAAGTGCTGTGA
|
| Enzyme 2 GenBank Gene ID |
NM_153486.2  |
| Enzyme 2 GeneCard ID |
LDHD  |
| Enzyme 2 GenAtlas ID |
LDHD  |
| Enzyme 2 HGNC ID |
HGNC:19708  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
16q23.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Flick MJ, Konieczny SF: Identification of putative mammalian D-lactate dehydrogenase enzymes. Biochem Biophys Res Commun. 2002 Jul 26;295(4):910-6. [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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
11578 |
| Enzyme 3 Name |
Hydroxyacylglutathione hydrolase-like protein |
| Enzyme 3 Synonyms |
Not Available |
| Enzyme 3 Gene Name |
HAGHL |
| Enzyme 3 Protein Sequence |
>Hydroxyacylglutathione hydrolase-like protein
MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHA
RGNPELARLRPGLAVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLW
EDDCPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTLPPETKVFCGHEHTLSNLE
FAQKVEPCNDHVRAKLSWAKARPLSRRGKRVGGEGTGFGVGGALRQGLMVTGACGHSRRG
MRMTCPLCRRLWARSASTTPSCGWREYGCCPGASTVTWTLRKASGDCVLG
|
| Enzyme 3 Number of Residues |
290 |
| Enzyme 3 Molecular Weight |
31557.1 |
| Enzyme 3 Theoretical pI |
8.27 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in hydrolase activity |
| Enzyme 3 Specific Function |
Hydrolase acting on ester bonds (Potential) |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
46361987  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q6PII5  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
HAGHL_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>873 bp
ATGAAGGTCAAGGTCATCCCCGTGCTCGAGGACAACTACATGTACCTGGTCATCGAGGAG
CTCACGCGCGAGGCGGTGGCCGTGGACGTGGCTGTGCCCAAGAGGCTGCTGGAGATCGTG
GGCCGGGAGGGGGTGTCTCTGACCGCTGTGCTGACCACCCACCATCACTGGGACCACGCG
CGGGGAAACCCGGAGCTGGCGCGGCTTCGTCCCGGGCTGGCGGTGCTGGGCGCGGACGAG
CGCATCTTCTCGCTGACGCGCAGGCTGGCGCACGGCGAGGAGCTGCGGTTCGGGGCCATC
CACGTGCGTTGCCTCCTGACGCCCGGCCACACCGCCGGCCACATGAGCTACTTCCTGTGG
GAGGACGATTGCCCGGACCCACCCGCCCTGTTCTCGGGCGACGCGCTGTCGGTGGCCGGC
TGCGGCTCGTGCCTGGAGGGCAGCGCCCAGCAGATGTACCAGAGCCTGGCCGAGCTGGGT
ACCCTGCCCCCCGAGACGAAGGTGTTCTGCGGCCACGAGCACACGCTTAGCAACCTGGAG
TTTGCCCAGAAAGTGGAGCCCTGCAACGACCACGTGAGAGCCAAGCTGTCCTGGGCTAAG
GCACGGCCCCTTTCCCGCCGCGGCAAGAGGGTGGGGGGGGAGGGAACAGGCTTCGGGGTG
GGGGGGGCTCTCAGACAAGGCCTAATGGTGACCGGGGCCTGTGGTCACTCCAGAAGAGGG
ATGAGGATGACGTGCCCACTGTGCCGTCGACTCTGGGCGAGGAGCGCCTCTACAACCCCT
TCCTGCGGGTGGCGTGAGTATGGCTGTTGTCCCGGGGCCTCCACCGTTACGTGGACCCTT
AGGAAGGCATCTGGGGACTGCGTGTTGGGCTGA
|
| Enzyme 3 GenBank Gene ID |
NM_207112.1  |
| Enzyme 3 GeneCard ID |
HAGHL  |
| Enzyme 3 GenAtlas ID |
HAGHL  |
| Enzyme 3 HGNC ID |
HGNC:14177  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
16p13.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed
]
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| Enzyme 3 Metabolite References |
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