|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5536 |
| Enzyme 1 Name |
Branched-chain-amino-acid aminotransferase, cytosolic |
| Enzyme 1 Synonyms |
- BCAT(c)
- Protein ECA39
|
| Enzyme 1 Gene Name |
BCAT1 |
| Enzyme 1 Protein Sequence |
>Branched-chain-amino-acid aminotransferase, cytosolic
MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTV
EWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTK
ALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDN
GCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQ
WGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPK
LASRILSKLTDIQYGREESDWTIVLS
|
| Enzyme 1 Number of Residues |
386 |
| Enzyme 1 Molecular Weight |
42965.8 |
| Enzyme 1 Theoretical pI |
4.95 |
| Enzyme 1 GO Classification |
| Function |
- branched-chain-amino-acid transaminase activity
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- branched chain family amino acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in catalytic activity |
| Enzyme 1 Specific Function |
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine |
| Enzyme 1 Pathways |
- Pantothenate and CoA Biosynthesis (map00770
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 1 Reactions |
- L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate [RN:R01090]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
38176287  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P54687  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
BCAT1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1161 bp
ATGAAGGATTGCAGTAACGGATGCTCCGCAGAGTGTACCGGAGAAGGAGGATCAAAAGAG
GTGGTGGGGACTTTTAAGGCTAAAGACCTAATAGTCACACCAGCTACCATTTTAAAGGAA
AAACCAGACCCCAATAATCTGGTTTTTGGAACTGTGTTCACGGATCATATGCTGACGGTG
GAGTGGTCCTCAGAGTTTGGATGGGAGAAACCTCATATCAAGCCTCTTCAGAACCTGTCA
TTGCACCCTGGCTCATCAGCTTTGCACTATGCAGTGGAATTATTTGAAGGATTGAAGGCA
TTTCGAGGAGTAGATAATAAAATTCGACTGTTTCAGCCAAACCTCAACATGGATAGAATG
TATCGCTCTGCTGTGAGGGCAACTCTGCCGGTATTTGACAAAGAAGAGCTCTTAGAGTGT
ATTCAACAGCTTGTGAAATTGGATCAAGAATGGGTCCCATATTCAACATCTGCTAGTCTG
TATATTCGTCCTACATTCATTGGAACTGAGCCTTCTCTTGGAGTCAAGAAGCCTACCAAA
GCCCTGCTCTTTGTACTCTTGAGCCCAGTGGGACCTTATTTTTCAAGTGGAACCTTTAAT
CCAGTGTCCCTGTGGGCCAATCCCAAGTATGTAAGAGCCTGGAAAGGTGGAACTGGGGAC
TGCAAGATGGGAGGGAATTACGGCTCATCTCTTTTTGCCCAATGTGAAGCAGTAGATAAT
GGGTGTCAGCAGGTCCTGTGGCTCTATGGAGAGGACCATCAGATCACTGAAGTGGGAACT
ATGAATCTTTTTCTTTACTGGATAAATGAAGATGGAGAAGAAGAACTGGCAACTCCTCCA
CTAGATGGCATCATTCTTCCAGGAGTGACAAGGCGGTGCATTCTGGACCTGGCACATCAG
TGGGGTGAATTTAAGGTGTCAGAGAGATACCTCACCATGGATGACTTGACAACAGCCCTG
GAGGGGAACAGAGTGAGAGAGATGTTTGGCTCTGGTACAGCCTGTGTTGTTTGCCCAGTT
TCTGATATACTGTACAAAGGCGAGACAATACACATTCCAACTATGGAGAATGGTCCTAAG
CTGGCAAGCCGCATCTTGAGCAAATTAACTGATATCCAGTATGGAAGAGAAGAGAGCGAC
TGGACAATTGTGCTATCCTGA
|
| Enzyme 1 GenBank Gene ID |
NM_005504.6  |
| Enzyme 1 GeneCard ID |
BCAT1  |
| Enzyme 1 GenAtlas ID |
BCAT1  |
| Enzyme 1 HGNC ID |
HGNC:976  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
12p12.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Schuldiner O, Eden A, Ben-Yosef T, Yanuka O, Simchen G, Benvenisty N: ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S cell cycle regulation in yeast. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7143-8. [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
]
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5763 |
| Enzyme 2 Name |
Branched-chain-amino-acid aminotransferase, mitochondrial |
| Enzyme 2 Synonyms |
- BCAT(m)
- Placental protein 18
- PP18
|
| Enzyme 2 Gene Name |
BCAT2 |
| Enzyme 2 Protein Sequence |
>Branched-chain-amino-acid aminotransferase, mitochondrial
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
|
| Enzyme 2 Number of Residues |
392 |
| Enzyme 2 Molecular Weight |
44287.4 |
| Enzyme 2 Theoretical pI |
8.82 |
| Enzyme 2 GO Classification |
| Function |
- branched-chain-amino-acid transaminase activity
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- branched chain family amino acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in catalytic activity |
| Enzyme 2 Specific Function |
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids |
| Enzyme 2 Pathways |
- Pantothenate and CoA Biosynthesis (map00770
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 2 Reactions |
- L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate [RN:R01090]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
13699234  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
O15382  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
BCAT2_HUMAN  |
| Enzyme 2 PDB ID |
1KTA  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1179 bp
ATGGCCGCAGCCGCTCTGGGGCAGATCTGGGCACGAAAGCTTCTCTCTGTCCCTTGGCTT
CTGTGTGGTCCCAGAAGATATGCCTCCTCCAGTTTCAAGGCTGCAGACCTGCAGCTGGAA
ATGACACAGAAGCCTCATAAGAAGCCTGGCCCCGGCGAGCCCCTGGTGTTTGGGAAGACA
TTTACCGACCACATGCTGATGGTGGAATGGAATGACAAGGGCTGGGGCCAGCCCCGAATC
CAGCCCTTCCAGAACCTCACGCTGCACCCAGCCTCCTCCAGCCTCCACTACTCCCTGCAG
CTGTTTGAGGGCATGAAGGCGTTCAAAGGCAAAGACCAGCAGGTGCGCCTCTTCCGCCCC
TGGCTCAACATGGACCGGATGCTGCGCTCAGCCATGCGCCTGTGCCTGCCGAGTTTCGAC
AAGCTGGAGTTGCTGGAGTGCATCCGCCGGCTCATCGAAGTGGACAAGGACTGGGTCCCC
GATGCCGCCGGCACCAGCCTCTATGTGCGGCCTGTGCTCATTGGGAACGAGCCCTCGCTG
GGTGTCAGCCAGCCCACGCGCGCGCTCCTGTTCGTCATTCTCTGCCCAGTGGGTGCCTAC
TTCCCTGGAGGCTCCGTGACCCCGGTCTCCCTCCTGGCCGACCCAGCCTTCATCCGGGCC
TGGGTGGGCGGGGTCGGCAACTACAAGTTAGGTGGGAATTATGGGCCCACCGTGTTAGTG
CAACAGGAGGCACTCAAGCGGGGCTGTGAACAGGTCCTCTGGCTGTATGGGCCCGACCAC
CAGCTCACCGAGGTGGGAACCATGAACATCTTTGTCTACTGGACCCACGAAGATGGGGTG
CTGGAGCTGGTGACGCCCCCGCTGAATGGTGTTATCCTGCCTGGAGTGGTCAGACAGAGT
CTACTGGACATGGCTCAGACCTGGGGTGAGTTCCGGGTGGTGGAGCGCACGATCACCATG
AAGCAGTTGCTGCGGGCCCTGGAGGAGGGCCGCGTGCGGGAAGTCTTTGGCTCGGGCACC
GCTTGCCAGGTCTGCCCAGTGCACCGAATCCTGTACAAAGACAGGAACCTCCACATTCCC
ACCATGGAAAATGGGCCTGAGCTGATCCTCCGCTTCCAGAAGGAGCTGAAGGAGATCCAG
TACGGAATCAGAGCCCACGAGTGGATGTTCCCGGTGTGA
|
| Enzyme 2 GenBank Gene ID |
AF268047  |
| Enzyme 2 GeneCard ID |
BCAT2  |
| Enzyme 2 GenAtlas ID |
BCAT2  |
| Enzyme 2 HGNC ID |
HGNC:977  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
19q13 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Bledsoe RK, Dawson PA, Hutson SM: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Biochim Biophys Acta. 1997 Apr 25;1339(1):9-13. [PubMed
]
- Than NG, Sumegi B, Than GN, Bellyei S, Bohn H: Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant. Placenta. 2001 Feb-Mar;22(2-3):235-43. [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
]
- 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
]
- Eden A, Simchen G, Benvenisty N: Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases. J Biol Chem. 1996 Aug 23;271(34):20242-5. [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
]
- Yennawar N, Dunbar J, Conway M, Hutson S, Farber G: The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):506-15. [PubMed
]
- Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry. 2002 Oct 1;41(39):11592-601. [PubMed
]
- Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. [PubMed
]
- Yennawar NH, Islam MM, Conway M, Wallin R, Hutson SM: Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis. J Biol Chem. 2006 Dec 22;281(51):39660-71. Epub 2006 Oct 18. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5868 |
| Enzyme 3 Name |
Probable leucyl-tRNA synthetase, mitochondrial |
| Enzyme 3 Synonyms |
- Leucine--tRNA ligase
- LeuRS
|
| Enzyme 3 Gene Name |
LARS2 |
| Enzyme 3 Protein Sequence |
>Probable leucyl-tRNA synthetase, mitochondrial
MASVWQRLGFYASLLKRQLNGGPDVIKWERRVIPGCTRSIYSATGKWTKEYTLQTRKDVE
KWWHQRIKEQASKISEADKSKPKFYVLSMFPYPSGKLHMGHVRVYTISDTIARFQKMRGM
QVINPMGWDAFGLPAENAAVERNLHPQSWTQSNIKHMRKQLDRLGLCFSWDREITTCLPD
YYKWTQYLFIKLYEAGLAYQKEALVNWDPVDQTVLANEQVDEHGCSWRSGAKVEQKYLRQ
WFIKTTAYAKAMQDALADLPEWYGIKGMQAHWIGDCVGCHLDFTLKVHGQATGEKLTAYT
ATPEAIYGTSHVAISPSHRLLHGHSSLKEALRMALVPGKDCLTPVMAVNMLTQQEVPVVI
LAKADLEGSLDSKIGIPSTSSEDTILAQTLGLAYSEVIETLPDGTERLSSSAEFTGMTRQ
DAFLALTQKARGKRVGGDVTSDKLKDWLISRQRYWGTPIPIVHCPVCGPTPVPLEDLPVT
LPNIASFTGKGGPPLAMASEWVNCSCPRCKGAAKRETDTMDTFVDSAWYYFRYTDPHNPH
SPFNTAVADYWMPVDLYIGGKEHAVMHLFYARFFSHFCHDQKMVKHREPFHKLLAQGLIK
GQTFRLPSGQYLQREEVDLTGSVPVHAKTKEKLEVTWEKMSKSKHNGVDPEEVVEQYGID
TIRLYILFAAPPEKDILWDVKTDALPGVLRWQQRLWTLTTRFIEARASGKSPQPQLLSNK
EKAEARKLWEYKNSVISQVTTHFTEDFSLNSAISQLMGLSNALSQASQSVILHSPEFEDA
LCALMVMAAPLAPHVTSEIWAGLALVPRKLCAHYTWDASVLLQAWPAVDPEFLQQPEVVQ
MAVLINNKACGKIPVPQQVARDQDKVHEFVLQSELGVRLLQGRSIKKSFLSPRTALINFL
VQD
|
| Enzyme 3 Number of Residues |
903 |
| Enzyme 3 Molecular Weight |
101975.4 |
| Enzyme 3 Theoretical pI |
8.32 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- leucine-tRNA ligase activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- leucyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 3 General Function |
Involved in nucleotide binding |
| Enzyme 3 Specific Function |
ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu) |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu [RN:R03657]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
19683964  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q15031  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
SYLM_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2712 bp
ATGGCTTCTGTTTGGCAGAGATTGGGTTTTTATGCCTCTCTTCTGAAAAGACAGCTAAAT
GGTGGGCCAGATGTCATCAAGTGGGAAAGGAGAGTAATTCCCGGATGTACCAGAAGCATC
TACAGTGCCACGGGAAAGTGGACAAAAGAGTATACATTGCAGACAAGAAAGGATGTTGAG
AAATGGTGGCATCAACGAATAAAAGAACAGGCCTCCAAAATTTCAGAAGCTGATAAATCG
AAGCCAAAATTTTACGTGCTTTCCATGTTCCCTTATCCTTCTGGTAAGCTGCACATGGGC
CATGTGCGTGTCTACACCATCAGCGACACCATAGCACGGTTCCAGAAGATGAGAGGGATG
CAGGTCATCAACCCCATGGGATGGGATGCTTTTGGATTGCCTGCTGAAAATGCCGCAGTC
GAGAGGAATCTACATCCACAAAGTTGGACACAAAGTAATATTAAACACATGAGGAAACAG
CTTGATCGTCTGGGCCTGTGTTTCAGCTGGGATAGGGAAATAACTACGTGTTTGCCAGAT
TACTACAAGTGGACTCAGTATCTCTTTATTAAACTGTATGAGGCTGGGCTGGCCTATCAA
AAGGAGGCCCTGGTTAACTGGGACCCAGTGGATCAAACAGTGCTTGCCAATGAGCAGGTG
GATGAACATGGCTGTTCATGGCGTTCTGGAGCAAAGGTGGAACAGAAGTACCTCAGACAA
TGGTTTATTAAGACAACCGCTTATGCAAAGGCCATGCAGGACGCGTTGGCAGACCTTCCA
GAATGGTATGGAATAAAAGGCATGCAAGCCCACTGGATTGGGGACTGTGTGGGCTGCCAC
CTGGACTTCACATTAAAGGTTCATGGGCAAGCCACGGGCGAAAAGCTGACTGCCTATACG
GCCACCCCTGAAGCCATTTATGGCACCTCCCACGTGGCCATCTCGCCCAGCCACAGACTC
CTACATGGGCACAGCTCTCTGAAGGAAGCCTTGAGGATGGCCCTTGTCCCTGGCAAAGAT
TGCCTCACGCCTGTAATGGCTGTGAACATGCTCACCCAGCAGGAGGTCCCTGTCGTTATT
TTGGCCAAAGCTGACTTGGAAGGCTCTCTGGATTCAAAAATAGGAATTCCCAGTACTAGC
TCAGAGGACACCATCTTAGCCCAAACCCTGGGCCTGGCCTACTCTGAAGTCATTGAAACT
TTGCCAGATGGCACAGAGAGACTGAGCAGCTCTGCTGAGTTCACAGGTATGACCCGGCAG
GATGCTTTTCTAGCCCTGACTCAGAAAGCCCGGGGGAAGAGAGTGGGTGGAGACGTGACA
AGTGATAAACTGAAAGACTGGCTGATTTCACGGCAGCGGTACTGGGGCACACCAATCCCC
ATTGTCCACTGCCCAGTCTGTGGCCCCACACCTGTGCCCCTGGAGGACTTGCCTGTGACC
CTGCCCAACATCGCATCTTTCACTGGCAAGGGAGGCCCCCCACTGGCCATGGCTTCAGAG
TGGGTGAACTGCTCCTGCCCAAGGTGCAAGGGAGCAGCCAAGAGAGAGACAGACACGATG
GATACCTTTGTTGATTCTGCTTGGTACTACTTCAGATACACTGACCCTCATAATCCACAC
AGCCCTTTTAACACAGCAGTGGCCGATTACTGGATGCCTGTGGATTTGTACATTGGAGGG
AAAGAACATGCCGTCATGCACTTGTTCTATGCAAGATTCTTTAGTCATTTTTGCCATGAT
CAAAAAATGGTTAAACATAGGGAGCCTTTTCATAAGCTGCTGGCCCAAGGCCTTATCAAG
GGGCAGACATTCCGCCTACCATCTGGACAGTATCTACAGAGAGAGGAAGTGGATCTCACA
GGTTCCGTTCCTGTTCATGCAAAAACGAAAGAGAAGTTAGAGGTGACGTGGGAGAAGATG
AGTAAGTCCAAACACAACGGGGTGGACCCAGAGGAAGTTGTGGAGCAGTATGGGATCGAC
ACGATTCGGCTCTACATCCTTTTTGCTGCCCCTCCTGAGAAGGATATCTTGTGGGATGTG
AAAACTGATGCTCTCCCTGGGGTGCTGAGATGGCAACAACGACTGTGGACCTTGACAACT
CGGTTTATTGAGGCCAGGGCTTCTGGGAAGTCTCCCCAGCCTCAGCTGCTGAGTAACAAG
GAGAAAGCCGAGGCCAGGAAGCTCTGGGAGTACAAGAACTCCGTCATCTCTCAGGTGACC
ACCCATTTCACAGAGGACTTCTCACTGAATTCTGCAATTTCTCAGCTGATGGGACTCAGC
AATGCCCTCTCGCAAGCCTCTCAGAGCGTCATTCTCCACAGCCCCGAGTTTGAGGATGCT
TTGTGTGCCCTGATGGTGATGGCTGCTCCACTGGCCCCTCATGTAACCTCAGAGATCTGG
GCAGGCCTGGCGCTGGTGCCGAGGAAGCTCTGTGCCCACTACACTTGGGATGCCAGTGTG
CTGCTCCAGGCATGGCCTGCTGTGGACCCGGAGTTCCTGCAGCAGCCTGAGGTTGTCCAG
ATGGCAGTTCTGATCAACAATAAAGCTTGTGGCAAAATTCCTGTGCCCCAACAAGTTGCC
CGGGACCAGGACAAAGTCCACGAATTTGTTCTTCAAAGCGAGCTGGGTGTCAGGCTTTTG
CAAGGACGAAGCATCAAGAAGTCCTTCCTTTCCCCGAGAACTGCCCTCATCAACTTCCTG
GTGCAAGATTGA
|
| Enzyme 3 GenBank Gene ID |
BC025989  |
| Enzyme 3 GeneCard ID |
LARS2  |
| Enzyme 3 GenAtlas ID |
LARS2  |
| Enzyme 3 HGNC ID |
HGNC:17095  |
| Enzyme 3 Chromosome Location |
3 |
| Enzyme 3 Locus |
3p21.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5920 |
| Enzyme 4 Name |
Leucyl-tRNA synthetase, cytoplasmic |
| Enzyme 4 Synonyms |
- Leucine--tRNA ligase
- LeuRS
|
| Enzyme 4 Gene Name |
LARS |
| Enzyme 4 Protein Sequence |
>Leucyl-tRNA synthetase, cytoplasmic
MAERKGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMNGRLH
LGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPDE
EEEEEETSVKTEDIIIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHW
LDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIY
SPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMF
GQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGA
SLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRD
DMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVD
GFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWK
KQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIY
MAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQ
EFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKWPTAVRANGHLLLNSEKMSKS
TGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVAN
WDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAV
EGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVNEVLIHSSQ
YLMEVTHDLRLRLKNYMMPAKGKKTDKQPLQKPSHCTIYVAKNYPPWQHTTLSVLRKHFE
ANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVL
MENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGKPLNVFRIEPGVSVSLVNPQPSNGH
FSTKIEIRQGDNCDSIIRRLMKMNRGIKDLSKVKLMRFDDPLLGPRRVPVLGKEYTEKTP
ISEHAVFNVDLMSKKIHLTENGIRVDIGDTIIYLVH
|
| Enzyme 4 Number of Residues |
1176 |
| Enzyme 4 Molecular Weight |
134465.2 |
| Enzyme 4 Theoretical pI |
7.31 |
| Enzyme 4 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- leucine-tRNA ligase activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- leucyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 4 General Function |
Involved in nucleotide binding |
| Enzyme 4 Specific Function |
Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction:the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Exhibits a post-transfer editing activity to hydrolyze mischarged tRNAs |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu [RN:R03657]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
108773810  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9P2J5  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SYLC_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>3531 bp
ATGGCGGAAAGAAAAGGAACAGCCAAAGTGGACTTTTTGAAGAAGATTGAGAAAGAAATC
CAACAGAAATGGGATACTGAGAGAGTGTTTGAGGTCAATGCATCTAATTTAGAGAAACAG
ACCAGCAAGGGCAAGTATTTTGTAACCTTCCCATATCCATATATGAATGGACGCCTTCAT
TTGGGACACACGTTTTCTTTATCCAAATGTGAGTTTGCTGTAGGGTACCAGCGATTGAAA
GGAAAATGTTGTCTGTTTCCCTTTGGCCTGCACTGTACTGGAATGCCTATTAAGGCATGT
GCTGATAAGTTGAAAAGAGAAATAGAGCTGTATGGTTGCCCCCCTGATTTTCCAGATGAA
GAAGAGGAAGAGGAAGAAACCAGTGTTAAAACAGAAGATATAATAATTAAGGATAAAGCT
AAAGGAAAAAAGAGTAAAGCTGCTGCTAAAGCTGGATCTTCTAAATACCAGTGGGGCATT
ATGAAATCCCTTGGCCTGTCTGATGAAGAGATAGTAAAATTTTCTGAAGCAGAACATTGG
CTTGATTATTTCCCGCCACTGGCTATTCAGGATTTAAAAAGAATGGGTTTGAAGGTAGAC
TGGCGTCGTTCCTTCATCACCACTGATGTTAATCCTTACTATGATTCATTTGTCAGATGG
CAATTTTTAACATTAAGAGAAAGAAACAAAATTAAATTTGGGAAGCGGTATACAATTTAC
TCTCCGAAAGATGGACAGCCTTGCATGGATCATGATAGACAAACTGGAGAGGGTGTTGGA
CCTCAGGAATATACTTTACTCAAATTGAAGGTGCTTGAGCCATACCCATCTAAATTAAGT
GGCCTGAAAGGTAAAAATATTTTCTTGGTGGCTGCTACTCTCAGACCTGAGACCATGTTT
GGGCAGACAAATTGTTGGGTTCGTCCTGATATGAAGTACATTGGATTTGAGACGGTGAAT
GGTGATATATTCATCTGTACCCAAAAAGCAGCCAGGAATATGTCATACCAGGGCTTTACC
AAAGACAATGGCGTGGTGCCTGTTGTTAAGGAATTAATGGGGGAGGAAATTCTTGGTGCA
TCACTTTCTGCACCTTTAACATCATACAAGGTGATCTATGTTCTCCCAATGCTAACTATT
AAGGAGGATAAAGGCACTGGTGTGGTTACAAGTGTTCCTTCCGACTCCCCTGATGATATT
GCTGCCCTCAGAGACTTGAAGAAAAAGCAAGCCTTACGAGCAAAATATGGAATTAGAGAT
GACATGGTCTTGCCATTTGAGCCGGTGCCAGTCATTGAAATCCCAGGTTTTGGAAATCTT
TCTGCTGTAACCATTTGTGATGAGTTGAAAATTCAGAGCCAGAATGACCGGGAAAAACTT
GCAGAAGCAAAGGAGAAGATATATCTAAAAGGATTTTATGAGGGTATCATGTTGGTGGAT
GGATTTAAAGGACAGAAGGTTCAAGATGTAAAGAAGACTATTCAGAAAAAGATGATTGAC
GCTGGAGATGCACTTATTTACATGGAACCAGAGAAACAAGTGATGTCCAGGTCGTCAGAT
GAATGTGTTGTGGCTCTGTGTGACCAGTGGTACTTGGATTATGGAGAAGAGAATTGGAAG
AAACAGACATCTCAGTGCTTGAAGAACCTGGAAACATTCTGTGAGGAGACCAGGAGGAAT
TTTGAAGCCACCTTAGGTTGGCTACAAGAACATGCTTGCTCAAGAACTTATGGTCTAGGC
ACTCACCTGCCTTGGGATGAGCAGTGGCTGATTGAATCACTTTCTGACTCCACTATTTAC
ATGGCATTTTACACAGTTGCACACCTATTGCAGGGGGGTAACTTGCATGGACAGGCAGAG
TCTCCGCTGGGCATTAGACCGCAACAGATGACCAAGGAAGTTTGGGATTATGTTTTCTTC
AAGGAGGCTCCATTTCCTAAGACTCAGATTGCAAAGGAAAAATTAGATCAGTTAAAGCAG
GAGTTTGAATTCTGGTATCCTGTTGATCTTCGCGTCTCTGGCAAGGATCTTGTTCCAAAT
CATCTTTCATATTACCTTTATAATCATGTGGCTATGTGGCCGGAACAAAGTGACAAATGG
CCTACAGCTGTGAGAGCAAATGGACATCTCCTCCTGAACTCTGAGAAGATGTCAAAATCC
ACAGGCAACTTCCTCACTTTGACCCAAGCTATTGACAAATTTTCAGCAGATGGAATGCGT
TTGGCTCTGGCTGATGCTGGTGACACTGTAGAAGATGCCAACTTTGTGGAAGCCATGGCA
GATGCAGGTATTCTCCGTCTGTACACCTGGGTAGAGTGGGTGAAAGAAATGGTTGCCAAC
TGGGACAGCCTAAGAAGTGGTCCTGCCAGCACTTTCAATGATAGAGTTTTTGCCAGTGAA
TTGAATGCAGGAATTATAAAAACAGATCAAAACTATGAAAAGATGATGTTTAAAGAAGCT
TTGAAAACAGGGTTTTTTGAGTTTCAGGCCGCAAAAGATAAGTACCGTGAATTGGCTGTG
GAAGGGATGCACAGAGAACTTGTGTTCCGGTTTATTGAAGTTCAGACACTTCTCCTCGCT
CCATTCTGTCCACATTTGTGTGAGCACATCTGGACACTCCTGGGAAAGCCTGACTCAATT
ATGAATGCTTCATGGCCTGTGGCAGGTCCTGTTAATGAAGTTTTAATACACTCCTCACAG
TATCTTATGGAAGTAACACATGACCTTAGACTACGACTCAAGAACTATATGATGCCAGCT
AAAGGGAAGAAGACTGACAAACAACCCCTGCAGAAGCCCTCACATTGCACCATCTATGTG
GCAAAGAACTATCCACCTTGGCAACATACCACCCTGTCTGTTCTACGTAAACACTTTGAG
GCCAATAACGGAAAACTGCCTGACAACAAAGTCATTGCTAGTGAACTAGGCAGTATGCCA
GAACTGAAGAAATACATGAAGAAAGTCATGCCATTTGTTGCCATGATTAAGGAAAATCTG
GAGAAGATGGGGCCTCGTATTCTGGATTTGCAATTAGAATTTGATGAAAAGGCTGTGCTT
ATGGAGAATATAGTCTATCTGACTAATTCGCTTGAGCTAGAACACATAGAAGTCAAGTTT
GCCTCCGAAGCAGAAGATAAAATCAGGGAAGACTGCTGTCCTGGGAAACCACTTAATGTT
TTTAGAATAGAACCTGGTGTGTCCGTTTCTCTGGTGAATCCCCAGCCATCCAATGGCCAC
TTCTCAACCAAAATTGAAATCAGGCAAGGAGATAACTGTGATTCCATAATCAGGCGTTTA
ATGAAAATGAATCGAGGAATTAAAGACCTTTCCAAAGTGAAACTGATGAGATTTGATGAT
CCACTGTTGGGGCCTCGACGAGTTCCTGTCCTGGGAAAGGAGTACACCGAGAAGACCCCC
ATTTCTGAGCATGCTGTTTTCAATGTGGACCTCATGAGCAAGAAAATTCATCTGACTGAG
AATGGGATAAGGGTGGATATTGGCGATACAATAATCTATCTGGTTCATTAA
|
| Enzyme 4 GenBank Gene ID |
NM_020117.9  |
| Enzyme 4 GeneCard ID |
LARS  |
| Enzyme 4 GenAtlas ID |
LARS  |
| Enzyme 4 HGNC ID |
HGNC:6512  |
| Enzyme 4 Chromosome Location |
5 |
| Enzyme 4 Locus |
5q32 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [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
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Seiradake E, Mao W, Hernandez V, Baker SJ, Plattner JJ, Alley MR, Cusack S: Crystal structures of the human and fungal cytosolic Leucyl-tRNA synthetase editing domains: A structural basis for the rational design of antifungal benzoxaboroles. J Mol Biol. 2009 Jul 10;390(2):196-207. Epub 2009 May 6. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
7884 |
| Enzyme 5 Name |
Large neutral amino acids transporter small subunit 2 |
| Enzyme 5 Synonyms |
- L-type amino acid transporter 2
- hLAT2
- Solute carrier family 7 member 8
|
| Enzyme 5 Gene Name |
SLC7A8 |
| Enzyme 5 Protein Sequence |
>Large neutral amino acids transporter small subunit 2
MEEGARHRNNTEKKHPGGGESDASPEAGSGGGGVALKKEIGLVSACGIIVGNIIGSGIFV
SPKGVLENAGSVGLALIVWIVTGFITVVGALCYAELGVTIPKSGGDYSYVKDIFGGLAGF
LRLWIAVLVIYPTNQAVIALTFSNYVLQPLFPTCFPPESGLRLLAAICLLLLTWVNCSSV
RWATRVQDIFTAGKLLALALIIIMGIVQICKGEYFWLEPKNAFENFQEPDIGLVALAFLQ
GSFAYGGWNFLNYVTEELVDPYKNLPRAIFISIPLVTFVYVFANVAYVTAMSPQELLASN
AVAVTFGEKLLGVMAWIMPISVALSTFGGVNGSLFTSSRLFFAGAREGHLPSVLAMIHVK
RCTPIPALLFTCISTLLMLVTSDMYTLINYVGFINYLFYGVTVAGQIVLRWKKPDIPRPI
KINLLFPIIYLLFWAFLLVFSLWSEPVVCGIGLAIMLTGVPVYFLGVYWQHKPKCFSDFI
ELLTLVSQKMCVVVYPEVERGSGTEEANEDMEEQQQPMYQPTPTKDKDVAGQPQP
|
| Enzyme 5 Number of Residues |
535 |
| Enzyme 5 Molecular Weight |
58381.1 |
| Enzyme 5 Theoretical pI |
5.75 |
| Enzyme 5 GO Classification |
| Function |
- active transmembrane transporter activity
- amine transmembrane transporter activity
- amino acid transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- amine transport
- amino acid transport
- establishment of localization
- transmembrane transport
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 5 General Function |
Involved in transport |
| Enzyme 5 Specific Function |
Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
- 40-60
72-92
113-133
155-175
189-209
231-251
268-288
310-330
362-382
388-408
424-444
447-467
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
12597192  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9UHI5  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
LAT2_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1608 bp
ATGGAAGAAGGAGCCAGGCACCGAAACAACACCGAAAAGAAACACCCAGGTGGGGGCGAG
TCGGACGCCAGCCCCGAGGCTGGTTCCGGAGGGGGCGGAGTAGCCCTGAAGAAAGAGATC
GGATTGGTCAGTGCCTGTGGTATCATCGTAGGGAACATCATCGGCTCTGGAATCTTTGTC
TCGCCAAAGGGAGTGCTGGAGAATGCTGGTTCTGTGGGCCTTGCTCTCATCGTCTGGATT
GTGACGGGCTTCATCACAGTTGTGGGAGCCCTCTGCTATGCTGAACTCGGGGTCACCATC
CCCAAATCTGGAGGTGACTACTCCTATGTCAAGGACATCTTCGGAGGACTGGCTGGGTTC
CTGAGGCTGTGGATTGCTGTGCTGGTGATCTACCCCACCAACCAGGCTGTCATCGCCCTC
ACCTTCTCCAACTACGTGCTGCAGCCGCTCTTCCCCACCTGCTTCCCCCCAGAGTCTGGC
CTTCGGCTCCTGGCTGCCATCTGCTTATTGCTCCTCACATGGGTCAACTGTTCCAGTGTG
CGGTGGGCCACCCGGGTTCAAGACATCTTCACAGCTGGGAAGCTCCTGGCCTTGGCCCTG
ATTATCATCATGGGGATTGTACAGATATGCAAAGGAGAGTACTTCTGGCTGGAGCCAAAG
AATGCATTTGAGAATTTCCAGGAACCTGACATCGGCCTCGTCGCACTGGCTTTCCTTCAG
GGCTCCTTTGCCTATGGAGGCTGGAACTTTCTGAATTACGTGACTGAGGAGCTTGTTGAT
CCCTACAAGAACCTTCCCAGAGCCATCTTCATCTCCATCCCACTGGTCACATTTGTGTAT
GTCTTTGCCAATGTCGCTTATGTCACTGCAATGTCCCCCCAGGAGCTGCTGGCATCCAAC
GCCGTCGCTGTGACTTTTGGAGAGAAGCTCCTAGGAGTCATGGCCTGGATCATGCCCATT
TCTGTTGCCCTGTCCACATTTGGAGGAGTTAATGGGTCTCTCTTCACCTCCTCTCGGCTG
TTCTTCGCTGGAGCCCGAGAGGGCCACCTTCCCAGTGTGTTGGCCATGATCCACGTGAAG
CGCTGCACCCCAATCCCAGCCCTGCTCTTCACATGCATCTCCACCCTGCTGATGCTGGTC
ACCAGCGACATGTACACACTCATCAACTACGTGGGCTTCATCAACTACCTCTTCTATGGG
GTCACGGTTGCTGGACAGATAGTCCTTCGCTGGAAGAAGCCTGATATCCCCCGCCCCATC
AAGATCAACCTGCTGTTCCCCATCATCTACTTGCTGTTCTGGGCCTTCCTGCTGGTCTTC
AGCCTGTGGTCAGAGCCGGTGGTGTGTGGCATTGGCCTGGCCATCATGCTGACAGGAGTG
CCTGTCTATTTCCTGGGTGTTTACTGGCAACACAAGCCCAAGTGTTTCAGTGACTTCATT
GAGCTGCTAACCCTGGTGAGCCAGAAGATGTGTGTGGTCGTGTACCCCGAGGTGGAGCGG
GGCTCAGGGACAGAGGAGGCTAATGAGGACATGGAGGAGCAGCAGCAGCCCATGTACCAA
CCCACTCCCACGAAGGACAAGGACGTGGCGGGGCAGCCCCAGCCCTGA
|
| Enzyme 5 GenBank Gene ID |
AB037669  |
| Enzyme 5 GeneCard ID |
SLC7A8  |
| Enzyme 5 GenAtlas ID |
SLC7A8  |
| Enzyme 5 HGNC ID |
HGNC:11066  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
14q11.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Pineda M, Fernandez E, Torrents D, Estevez R, Lopez C, Camps M, Lloberas J, Zorzano A, Palacin M: Identification of a membrane protein, LAT-2, that Co-expresses with 4F2 heavy chain, an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids. J Biol Chem. 1999 Jul 9;274(28):19738-44. [PubMed
]
- Rossier G, Meier C, Bauch C, Summa V, Sordat B, Verrey F, Kuhn LC: LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine. J Biol Chem. 1999 Dec 3;274(49):34948-54. [PubMed
]
- Borsani G, Bassi MT, Sperandeo MP, De Grandi A, Buoninconti A, Riboni M, Manzoni M, Incerti B, Pepe A, Andria G, Ballabio A, Sebastio G: SLC7A7, encoding a putative permease-related protein, is mutated in patients with lysinuric protein intolerance. Nat Genet. 1999 Mar;21(3):297-301. [PubMed
]
- Park SY, Kim JK, Kim IJ, Choi BK, Jung KY, Lee S, Park KJ, Chairoungdua A, Kanai Y, Endou H, Kim DK: Reabsorption of neutral amino acids mediated by amino acid transporter LAT2 and TAT1 in the basolateral membrane of proximal tubule. Arch Pharm Res. 2005 Apr;28(4):421-32. [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
]
- 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
]
- Broer A, Friedrich B, Wagner CA, Fillon S, Ganapathy V, Lang F, Broer S: Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires different domains. Biochem J. 2001 May 1;355(Pt 3):725-31. [PubMed
]
- Simmons-Willis TA, Koh AS, Clarkson TW, Ballatori N: Transport of a neurotoxicant by molecular mimicry: the methylmercury-L-cysteine complex is a substrate for human L-type large neutral amino acid transporter (LAT) 1 and LAT2. Biochem J. 2002 Oct 1;367(Pt 1):239-46. [PubMed
]
- Liu X, Charrier L, Gewirtz A, Sitaraman S, Merlin D: CD98 and intracellular adhesion molecule I regulate the activity of amino acid transporter LAT-2 in polarized intestinal epithelia. J Biol Chem. 2003 Jun 27;278(26):23672-7. Epub 2003 Apr 25. [PubMed
]
- Gandhi MD, Pal D, Mitra AK: Identification and functional characterization of a Na(+)-independent large neutral amino acid transporter (LAT2) on ARPE-19 cells. Int J Pharm. 2004 May 4;275(1-2):189-200. [PubMed
]
- Fraga S, Pinho MJ, Soares-da-Silva P: Expression of LAT1 and LAT2 amino acid transporters in human and rat intestinal epithelial cells. Amino Acids. 2005 Nov;29(3):229-33. Epub 2005 Jul 20. [PubMed
]
- Li S, Whorton AR: Identification of stereoselective transporters for S-nitroso-L-cysteine: role of LAT1 and LAT2 in biological activity of S-nitrosothiols. J Biol Chem. 2005 May 20;280(20):20102-10. Epub 2005 Mar 15. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
8627 |
| Enzyme 6 Name |
4F2 cell-surface antigen heavy chain |
| Enzyme 6 Synonyms |
- 4F2hc
- 4F2 heavy chain antigen
- Lymphocyte activation antigen 4F2 large subunit
- CD98 antigen
|
| Enzyme 6 Gene Name |
SLC3A2 |
| Enzyme 6 Protein Sequence |
>4F2 cell-surface antigen heavy chain
MELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLPS
ASQNAEMIETGSDCVTQAGLQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELEP
EKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLSKEELLKVAGSPGWVR
TRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAGN
LAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKKK
SIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSFL
AEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYLSDSGSTGEHTKSLVT
QYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAALP
GQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHGD
FHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLSTQ
PGREEGSPLELERLKLEPHEGLLLRFPYAA
|
| Enzyme 6 Number of Residues |
630 |
| Enzyme 6 Molecular Weight |
67993.3 |
| Enzyme 6 Theoretical pI |
4.63 |
| Enzyme 6 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in catalytic activity |
| Enzyme 6 Specific Function |
Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L- nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier |
| 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 |
65506891  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P08195  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
4F2_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1893 bp
ATGGAGCTACAGCCTCCTGAAGCCTCGATCGCCGTCGTGTCGATTCCGCGCCAGTTGCCT
GGCTCACATTCGGAGGCTGGTGTCCAGGGTCTCAGCGCGGGGGACGACTCAGAGTTGGGG
TCTCACTGTGTTGCCCAGACTGGTCTCGAACTCTTGGCCTCAGGTGATCCTCTTCCCTCA
GCTTCCCAGAATGCCGAGATGATAGAGACGGGGTCTGACTGTGTTACCCAGGCTGGTCTT
CAACTCTTGGCCTCAAGTGATCCTCCTGCCTTAGCTTCCAAGAATGCTGAGGTTACAGGC
ACCATGAGCCAGGACACCGAGGTGGATATGAAGGAGGTGGAGCTGAATGAGTTAGAGCCC
GAGAAGCAGCCGATGAACGCGGCGTCTGGGGCGGCCATGTCCCTGGCGGGAGCCGAGAAG
AATGGTCTGGTGAAGATCAAGGTGGCGGAAGACGAGGCGGAGGCGGCAGCCGCGGCTAAG
TTCACGGGCCTGTCCAAGGAGGAGCTGCTGAAGGTGGCAGGCAGCCCCGGCTGGGTACGC
ACCCGCTGGGCACTGCTGCTGCTCTTCTGGCTCGGCTGGCTCGGCATGCTTGCTGGTGCC
GTGGTCATAATCGTGCGAGCGCCGCGTTGTCGCGAGCTACCGGCGCAGAAGTGGTGGCAC
ACGGGCGCCCTCTACCGCATCGGCGACCTTCAGGCCTTCCAGGGCCACGGCGCGGGCAAC
CTGGCGGGTCTGAAGGGGCGTCTCGATTACCTGAGCTCTCTGAAGGTGAAGGGCCTTGTG
CTGGGTCCAATTCACAAGAACCAGAAGGATGATGTCGCTCAGACTGACTTGCTGCAGATC
GACCCCAATTTTGGCTCCAAGGAAGATTTTGACAGTCTCTTGCAATCGGCTAAAAAAAAG
AGCATCCGTGTCATTCTGGACCTTACTCCCAACTACCGGGGTGAGAACTCGTGGTTCTCC
ACTCAGGTTGACACTGTGGCCACCAAGGTGAAGGATGCTCTGGAGTTTTGGCTGCAAGCT
GGCGTGGATGGGTTCCAGGTTCGGGACATAGAGAATCTGAAGGATGCATCCTCATTCTTG
GCTGAGTGGCAAAATATCACCAAGGGCTTCAGTGAAGACAGGCTCTTGATTGCGGGGACT
AACTCCTCCGACCTTCAGCAGATCCTGAGCCTACTCGAATCCAACAAAGACTTGCTGTTG
ACTAGCTCATACCTGTCTGATTCTGGTTCTACTGGGGAGCATACAAAATCCCTAGTCACA
CAGTATTTGAATGCCACTGGCAATCGCTGGTGCAGCTGGAGTTTGTCTCAGGCAAGGCTC
CTGACTTCCTTCTTGCCGGCTCAACTTCTCCGACTCTACCAGCTGATGCTCTTCACCCTG
CCAGGGACCCCTGTTTTCAGCTACGGGGATGAGATTGGCCTGGATGCAGCTGCCCTTCCT
GGACAGCCTATGGAGGCTCCAGTCATGCTGTGGGATGAGTCCAGCTTCCCTGACATCCCA
GGGGCTGTAAGTGCCAACATGACTGTGAAGGGCCAGAGTGAAGACCCTGGCTCCCTCCTT
TCCTTGTTCCGGCGGCTGAGTGACCAGCGGAGTAAGGAGCGCTCCCTACTGCATGGGGAC
TTCCACGCGTTCTCCGCTGGGCCTGGACTCTTCTCCTATATCCGCCACTGGGACCAGAAT
GAGCGTTTTCTGGTAGTGCTTAACTTTGGGGATGTGGGCCTCTCGGCTGGACTGCAGGCC
TCCGACCTGCCTGCCAGCGCCAGCCTGCCAGCCAAGGCTGACCTCCTGCTCAGCACCCAG
CCAGGCCGTGAGGAGGGCTCCCCTCTTGAGCTGGAACGCCTGAAACTGGAGCCTCACGAA
GGGCTGCTGCTCCGCTTCCCCTACGCGGCCTGA
|
| Enzyme 6 GenBank Gene ID |
NM_002394.5  |
| Enzyme 6 GeneCard ID |
SLC3A2  |
| Enzyme 6 GenAtlas ID |
SLC3A2  |
| Enzyme 6 HGNC ID |
HGNC:11026  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
11q13 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Quackenbush E, Clabby M, Gottesdiener KM, Barbosa J, Jones NH, Strominger JL, Speck S, Leiden JM: Molecular cloning of complementary DNAs encoding the heavy chain of the human 4F2 cell-surface antigen: a type II membrane glycoprotein involved in normal and neoplastic cell growth. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6526-30. [PubMed
]
- Teixeira S, Di Grandi S, Kuhn LC: Primary structure of the human 4F2 antigen heavy chain predicts a transmembrane protein with a cytoplasmic NH2 terminus. J Biol Chem. 1987 Jul 15;262(20):9574-80. [PubMed
]
- Lumadue JA, Glick AB, Ruddle FH: Cloning, sequence analysis, and expression of the large subunit of the human lymphocyte activation antigen 4F2. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9204-8. [PubMed
]
- Gottesdiener KM, Karpinski BA, Lindsten T, Strominger JL, Jones NH, Thompson CB, Leiden JM: Isolation and structural characterization of the human 4F2 heavy-chain gene, an inducible gene involved in T-lymphocyte activation. Mol Cell Biol. 1988 Sep;8(9):3809-19. [PubMed
]
- Yanagida O, Kanai Y, Chairoungdua A, Kim DK, Segawa H, Nii T, Cha SH, Matsuo H, Fukushima J, Fukasawa Y, Tani Y, Taketani Y, Uchino H, Kim JY, Inatomi J, Okayasu I, Miyamoto K, Takeda E, Goya T, Endou H: Human L-type amino acid transporter 1 (LAT1): characterization of function and expression in tumor cell lines. Biochim Biophys Acta. 2001 Oct 1;1514(2):291-302. [PubMed
]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [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
]
- Torrents D, Estevez R, Pineda M, Fernandez E, Lloberas J, Shi YB, Zorzano A, Palacin M: Identification and characterization of a membrane protein (y+L amino acid transporter-1) that associates with 4F2hc to encode the amino acid transport activity y+L. A candidate gene for lysinuric protein intolerance. J Biol Chem. 1998 Dec 4;273(49):32437-45. [PubMed
]
- Mastroberardino L, Spindler B, Pfeiffer R, Skelly PJ, Loffing J, Shoemaker CB, Verrey F: Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family. Nature. 1998 Sep 17;395(6699):288-91. [PubMed
]
- Pfeiffer R, Rossier G, Spindler B, Meier C, Kuhn L, Verrey F: Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family. EMBO J. 1999 Jan 4;18(1):49-57. [PubMed
]
- Broer A, Wagner CA, Lang F, Broer S: The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine efflux in exchange with glutamine. Biochem J. 2000 Aug 1;349 Pt 3:787-95. [PubMed
]
- Broer A, Friedrich B, Wagner CA, Fillon S, Ganapathy V, Lang F, Broer S: Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires different domains. Biochem J. 2001 May 1;355(Pt 3):725-31. [PubMed
]
- Ritchie JW, Taylor PM: Role of the System L permease LAT1 in amino acid and iodothyronine transport in placenta. Biochem J. 2001 Jun 15;356(Pt 3):719-25. [PubMed
]
- Kolesnikova TV, Mannion BA, Berditchevski F, Hemler ME: Beta1 integrins show specific association with CD98 protein in low density membranes. BMC Biochem. 2001;2:10. Epub 2001 Oct 15. [PubMed
]
- Friesema EC, Docter R, Moerings EP, Verrey F, Krenning EP, Hennemann G, Visser TJ: Thyroid hormone transport by the heterodimeric human system L amino acid transporter. Endocrinology. 2001 Oct;142(10):4339-48. [PubMed
]
- Okamoto Y, Sakata M, Ogura K, Yamamoto T, Yamaguchi M, Tasaka K, Kurachi H, Tsurudome M, Murata Y: Expression and regulation of 4F2hc and hLAT1 in human trophoblasts. Am J Physiol Cell Physiol. 2002 Jan;282(1):C196-204. [PubMed
]
- He X, Di Y, Li J, Xie Y, Tang Y, Zhang F, Wei L, Zhang Y, Qin W, Huo K, Li Y, Wan D, Gu J: Molecular cloning and characterization of CT120, a novel membrane-associated gene involved in amino acid transport and glutathione metabolism. Biochem Biophys Res Commun. 2002 Sep 27;297(3):528-36. [PubMed
]
- Simmons-Willis TA, Koh AS, Clarkson TW, Ballatori N: Transport of a neurotoxicant by molecular mimicry: the methylmercury-L-cysteine complex is a substrate for human L-type large neutral amino acid transporter (LAT) 1 and LAT2. Biochem J. 2002 Oct 1;367(Pt 1):239-46. [PubMed
]
- Kim DK, Kanai Y, Choi HW, Tangtrongsup S, Chairoungdua A, Babu E, Tachampa K, Anzai N, Iribe Y, Endou H: Characterization of the system L amino acid transporter in T24 human bladder carcinoma cells. Biochim Biophys Acta. 2002 Sep 20;1565(1):112-21. [PubMed
]
- Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ: Cluster analysis of an extensive human breast cancer cell line protein expression map database. Proteomics. 2002 Feb;2(2):212-23. [PubMed
]
- Arancibia-Garavilla Y, Toledo F, Casanello P, Sobrevia L: Nitric oxide synthesis requires activity of the cationic and neutral amino acid transport system y+L in human umbilical vein endothelium. Exp Physiol. 2003 Nov;88(6):699-710. [PubMed
]
- Liu X, Charrier L, Gewirtz A, Sitaraman S, Merlin D: CD98 and intracellular adhesion molecule I regulate the activity of amino acid transporter LAT-2 in polarized intestinal epithelia. J Biol Chem. 2003 Jun 27;278(26):23672-7. Epub 2003 Apr 25. [PubMed
]
- Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed
]
- Tomi M, Mori M, Tachikawa M, Katayama K, Terasaki T, Hosoya K: L-type amino acid transporter 1-mediated L-leucine transport at the inner blood-retinal barrier. Invest Ophthalmol Vis Sci. 2005 Jul;46(7):2522-30. [PubMed
]
- Li S, Whorton AR: Identification of stereoselective transporters for S-nitroso-L-cysteine: role of LAT1 and LAT2 in biological activity of S-nitrosothiols. J Biol Chem. 2005 May 20;280(20):20102-10. Epub 2005 Mar 15. [PubMed
]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Nawashiro H, Otani N, Shinomiya N, Fukui S, Ooigawa H, Shima K, Matsuo H, Kanai Y, Endou H: L-type amino acid transporter 1 as a potential molecular target in human astrocytic tumors. Int J Cancer. 2006 Aug 1;119(3):484-92. [PubMed
]
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed
]
- Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed
]
- Nguyen HT, Dalmasso G, Yan Y, Obertone TS, Sitaraman SV, Merlin D: Ecto-phosphorylation of CD98 regulates cell-cell interactions. PLoS One. 2008;3(12):e3895. Epub 2008 Dec 9. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [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
]
- Fort J, de la Ballina LR, Burghardt HE, Ferrer-Costa C, Turnay J, Ferrer-Orta C, Uson I, Zorzano A, Fernandez-Recio J, Orozco M, Lizarbe MA, Fita I, Palacin M: The structure of human 4F2hc ectodomain provides a model for homodimerization and electrostatic interaction with plasma membrane. J Biol Chem. 2007 Oct 26;282(43):31444-52. Epub 2007 Aug 26. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
14756 |
| Enzyme 7 Name |
Leucine carboxyl methyltransferase 2 |
| Enzyme 7 Synonyms |
- p21WAF1/CIP1 promoter-interacting protein
- tRNA wybutosine-synthesizing protein 4 homolog
- tRNA yW-synthesizing protein 4 homolog
|
| Enzyme 7 Gene Name |
LCMT2 |
| Enzyme 7 Protein Sequence |
>Leucine carboxyl methyltransferase 2
MGPRSRERRAGAVQNTNDSSALSKRSLAARGYVQDPFAALLVPGAARRAPLIHRGYYVRA
RAVRHCVRAFLEQIGAPQAALRAQILSLGAGFDSLYFRLKTAGRLARAAVWEVDFPDVAR
RKAERIGETPELCALTGPFERGEPASALCFESADYCILGLDLRQLQRVEEALGAAGLDAA
SPTLLLAEAVLTYLEPESAAALIAWAAQRFPNALFVVYEQMRPQDAFGQFMLQHFRQLNS
PLHGLERFPDVEAQRRRFLQAGWTACGAVDMNEFYHCFLPAEERRRVENIEPFDEFEEWH
LKCAHYFILAASRGDTLSHTLVFPSSEAFPRVNPASPSGVFPASVVSSEGQVPNLKRYGH
ASVFLSPDVILSAGGFGEQEGRHCRVSQFHLLSRDCDSEWKGSQIGSCGTGVQWDGRLYH
TMTRLSESRVLVLGGRLSPVSPALGVLQLHFFKSEDNNTEDLKVTITKAGRKDDSTLCCW
RHSTTEVSCQNQEYLFVYGGRSVVEPVLSDWHFLHVGTMAWVRIPVEGEVPEARHSHSAC
TWQGGALIAGGLGASEEPLNSVLFLRPISCGFLWESVDIQPPITPRYSHTAHVLNGKLLL
VGGIWIHSSSFPGVTVINLTTGLSSEYQIDTTYVPWPLMLHNHTSILLPEEQQLLLLGGG
GNCFSFGTYFNPHTVTLDLSSLSAGQ
|
| Enzyme 7 Number of Residues |
686 |
| Enzyme 7 Molecular Weight |
75601.1 |
| Enzyme 7 Theoretical pI |
6.71 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in methyltransferase activity |
| Enzyme 7 Specific Function |
Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. May methylate the carboxyl group of leucine residues to form alpha- leucine ester residues |
| 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 |
25188199  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
O60294  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
LCMT2_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2061 bp
ATGGGCCCCCGGAGCCGTGAGCGTCGGGCAGGCGCGGTACAGAACACCAACGACAGCAGC
GCCCTCAGCAAGCGTTCCCTGGCCGCGCGCGGGTACGTGCAGGACCCCTTTGCCGCGTTG
CTGGTTCCGGGCGCGGCGCGCCGCGCACCGCTCATTCACCGAGGCTACTACGTCCGCGCA
CGCGCCGTGAGGCACTGCGTGCGCGCTTTTTTGGAGCAGATTGGCGCGCCCCAGGCCGCG
CTTCGCGCGCAGATCTTGTCTCTCGGCGCTGGCTTCGACTCGCTCTATTTTCGCTTAAAA
ACCGCGGGCCGCCTGGCCCGGGCTGCAGTCTGGGAGGTGGATTTTCCGGACGTGGCGCGG
CGCAAAGCAGAAAGGATTGGAGAGACGCCAGAGCTGTGCGCGTTAACCGGGCCTTTCGAG
AGGGGGGAGCCCGCGTCCGCGCTGTGCTTTGAGAGCGCAGACTACTGCATCCTGGGTCTG
GACTTGCGGCAGCTCCAGCGAGTGGAGGAGGCCCTGGGCGCCGCGGGGCTCGACGCAGCC
TCACCCACTCTGCTCCTGGCCGAGGCGGTGCTGACCTACCTCGAGCCGGAGAGTGCCGCG
GCCCTCATCGCCTGGGCAGCCCAGCGTTTTCCTAATGCCCTTTTCGTGGTCTATGAGCAG
ATGAGGCCTCAAGACGCCTTTGGCCAGTTCATGCTGCAACATTTTCGGCAGCTAAACTCC
CCCCTGCATGGCCTGGAGCGTTTTCCTGACGTGGAGGCGCAGCGGCGCCGCTTCCTTCAA
GCTGGCTGGACCGCCTGCGGTGCCGTGGACATGAATGAATTCTATCACTGCTTTCTTCCC
GCAGAAGAACGCCGGCGGGTGGAAAATATTGAACCCTTTGACGAATTTGAGGAGTGGCAT
CTGAAGTGCGCCCATTATTTCATTCTGGCAGCTTCTAGGGGAGACACCCTCTCCCACACC
CTAGTGTTTCCATCCTCAGAGGCATTTCCTCGCGTAAATCCTGCTTCGCCTTCAGGGGTA
TTCCCTGCCAGCGTAGTCAGTAGCGAGGGCCAGGTCCCAAACCTGAAGAGATATGGCCAC
GCCTCTGTCTTCTTGAGCCCAGACGTTATTCTCAGTGCAGGAGGATTTGGAGAGCAGGAG
GGGCGGCACTGCCGAGTGAGCCAGTTTCACTTGCTCTCAAGAGATTGTGACTCTGAATGG
AAAGGCAGCCAAATAGGCAGTTGTGGGACTGGAGTTCAGTGGGATGGACGCCTTTATCAC
ACCATGACAAGACTCTCAGAGAGTCGGGTTCTGGTTCTGGGAGGGAGACTGTCCCCAGTA
AGTCCAGCCTTGGGGGTTCTCCAGCTTCATTTTTTTAAGAGTGAGGATAATAACACTGAG
GACCTGAAAGTGACAATAACAAAGGCTGGCCGAAAGGATGATTCCACTTTGTGTTGTTGG
CGGCATTCAACAACAGAAGTGTCCTGTCAGAATCAGGAATATTTGTTTGTGTATGGGGGT
CGAAGCGTGGTGGAACCTGTACTAAGTGACTGGCATTTCCTCCATGTAGGGACAATGGCT
TGGGTCAGGATCCCAGTGGAGGGAGAAGTACCTGAAGCCCGGCATTCTCACAGTGCCTGC
ACTTGGCAAGGGGGAGCCCTTATTGCTGGAGGTCTCGGGGCTTCTGAGGAGCCATTGAAC
TCTGTGCTCTTTCTGAGACCAATCTCTTGTGGATTCCTCTGGGAGTCAGTAGACATCCAG
CCTCCCATTACCCCAAGGTACTCCCACACAGCTCATGTGCTCAATGGAAAGCTGTTACTG
GTTGGAGGGATCTGGATTCATTCCTCCTCATTTCCTGGAGTGACTGTGATCAATTTGACT
ACAGGATTGAGCTCTGAGTATCAGATTGACACAACATATGTGCCATGGCCATTAATGTTA
CACAACCATACTAGTATCCTTCTTCCTGAAGAGCAACAGCTCCTGCTCCTTGGAGGTGGT
GGGAACTGCTTTTCCTTTGGTACCTACTTCAACCCCCATACAGTCACATTAGACCTTTCT
TCCTTAAGTGCTGGGCAGTAA
|
| Enzyme 7 GenBank Gene ID |
NM_014793.3  |
| Enzyme 7 GeneCard ID |
LCMT2  |
| Enzyme 7 GenAtlas ID |
LCMT2  |
| Enzyme 7 HGNC ID |
HGNC:17558  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
15q15.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [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
]
- De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J: Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 1999 Dec 14;38(50):16539-47. [PubMed
]
- Ng CC, Arakawa H, Fukuda S, Kondoh H, Nakamura Y: p53RFP, a p53-inducible RING-finger protein, regulates the stability of p21WAF1. Oncogene. 2003 Jul 10;22(28):4449-58. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
15076 |
| Enzyme 8 Name |
LARS protein (Leucyl-tRNA synthetase, isoform CRA_a) (Leucyl-tRNA synthetase) |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
LARS |
| Enzyme 8 Protein Sequence |
>LARS protein (Leucyl-tRNA synthetase, isoform CRA_a) (Leucyl-tRNA synthetase)
MAERKGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMNGRLH
LGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPDE
EEEEEETSVKTEDIIIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHW
LDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIY
SPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMF
GQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGA
SLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRD
DMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVD
GFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWK
KQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIY
MAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQ
EFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKWPTAVRANGHLLLNSEKMSKS
TGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVAN
WDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAV
EGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVNEVLIHSSQ
YLMEVTHDLRLRLKNYMMPAKGKKTDKQPLQKPSHCTIYVAKNYPPWQHTTLSVLRKHFE
ANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVL
MENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGKPLNVFRIEPGVSVSLVNPQPSNGH
FSTKIEIRQGDNCDSIIRRLMKMNRGIKDLSKVKLMRFDDPLLGPRRVPVLGKEYTEKTP
ISEHAVFNVDLMSKKIHLTENGIRVDIGDTIIYLVH
|
| Enzyme 8 Number of Residues |
1176 |
| Enzyme 8 Molecular Weight |
134468 |
| Enzyme 8 Theoretical pI |
7.31 |
| Enzyme 8 GO Classification |
| Function |
- ATP binding
- RNA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- leucine-tRNA ligase activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
- nucleotide binding
- purine nucleotide binding
- tRNA ligase activity
|
| Process |
- RNA metabolism
- cellular metabolism
- macromolecule biosynthesis
- macromolecule metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- protein biosynthesis
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 8 General Function |
Translation, ribosomal structure and biogenesis |
| 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 |
152013023  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
A7E266  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
A7E266_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>3531 bp
ATGGCGGAAAGAAAAGGAACAGCCAAAGTGGACTTTTTGAAGAAGATTGAGAAAGAAATC
CAACAGAAATGGGATACTGAGAGAGTGTTTGAGGTCAATGCATCTAATTTAGAGAAACAG
ACCAGCAAGGGCAAGTATTTTGTAACCTTCCCATATCCATATATGAATGGACGCCTTCAT
TTGGGACACACGTTTTCTTTATCCAAATGTGAGTTTGCTGTAGGGTACCAGCGATTGAAA
GGAAAATGTTGTCTGTTTCCCTTTGGCCTGCACTGTACTGGAATGCCTATTAAGGCATGT
GCTGATAAGTTGAAAAGAGAAATAGAGCTGTATGGTTGCCCCCCTGATTTTCCAGATGAA
GAAGAGGAAGAGGAAGAAACCAGTGTTAAAACAGAAGATATAATAATTAAGGATAAAGCT
AAAGGAAAAAAGAGTAAAGCTGCTGCTAAAGCTGGATCTTCTAAATACCAGTGGGGCATT
ATGAAATCCCTTGGCCTGTCTGATGAAGAGATAGTAAAATTTTCTGAAGCAGAACATTGG
CTTGATTATTTCCCGCCACTGGCTATTCAGGATTTAAAAAGAATGGGTTTGAAGGTAGAC
TGGCGTCGTTCCTTCATCACCACTGATGTTAATCCTTACTATGATTCATTTGTCAGATGG
CAATTTTTAACATTAAGAGAAAGAAACAAAATTAAATTTGGGAAGCGGTATACAATTTAC
TCTCCGAAAGATGGACAGCCTTGCATGGATCATGATAGACAAACTGGAGAGGGTGTTGGA
CCTCAGGAATATACTTTACTCAAATTGAAGGTGCTTGAGCCATACCCATCTAAATTAAGT
GGCCTGAAAGGTAAAAATATTTTCTTGGTGGCTGCTACTCTCAGACCTGAGACCATGTTT
GGGCAGACAAATTGTTGGGTTCGTCCTGATATGAAGTACATTGGATTTGAGACGGTGAAT
GGTGATATATTCATCTGTACCCAAAAAGCAGCCAGGAATATGTCATACCAGGGCTTTACC
AAAGACAATGGCGTGGTGCCTGTTGTTAAGGAATTAATGGGGGAGGAAATTCTTGGTGCA
TCACTTTCTGCACCTTTAACATCATACAAGGTGATCTATGTTCTCCCAATGCTAACTATT
AAGGAGGATAAAGGCACTGGTGTGGTTACAAGTGTTCCTTCCGACTCCCCTGATGATATT
GCTGCCCTCAGAGACTTGAAGAAAAAGCAAGCCTTACGAGCAAAATATGGAATTAGAGAT
GACATGGTCTTGCCATTTGAGCCGGTGCCAGTCATTGAAATCCCAGGTTTTGGAAATCTT
TCTGCTGTAACCATTTGTGATGAGTTGAAAATTCAGAGCCAGAATGACCGGGAAAAACTT
GCAGAAGCAAAGGAGAAGATATATCTAAAAGGATTTTATGAGGGTATCATGTTGGTGGAT
GGATTTAAAGGACAGAAGGTTCAAGATGTAAAGAAGACTATTCAGAAAAAGATGATTGAC
GCTGGAGATGCACTTATTTACATGGAACCAGAGAAACAAGTGATGTCCAGGTCGTCAGAT
GAATGTGTTGTGGCTCTGTGTGACCAGTGGTACTTGGATTATGGAGAAGAGAATTGGAAG
AAACAGACATCTCAGTGCTTGAAGAACCTGGAAACATTCTGTGAGGAGACCAGGAGGAAT
TTTGAAGCCACCTTAGGTTGGCTACAAGAACATGCTTGCTCAAGAACTTATGGTCTAGGC
ACTCACCTGCCTTGGGATGAGCAGTGGCTGATTGAATCACTTTCTGACTCCACTATTTAC
ATGGCATTTTACACAGTTGCACACCTATTGCAGGGGGGTAACTTGCATGGACAGGCAGAG
TCTCCGCTGGGCATTAGACCGCAACAGATGACCAAGGAAGTTTGGGATTATGTTTTCTTC
AAGGAGGCTCCATTTCCTAAGACTCAGATTGCAAAGGAAAAATTAGATCAGTTAAAGCAG
GAGTTTGAATTCTGGTATCCTGTTGATCTTCGCGTCTCTGGCAAGGATCTTGTTCCAAAT
CATCTTTCATATTACCTTTATAATCATGTGGCTATGTGGCCGGAACAAAGTGACAAATGG
CCTACAGCTGTGAGAGCAAATGGACATCTCCTCCTGAACTCTGAGAAGATGTCAAAATCC
ACAGGCAACTTCCTCACTTTGACCCAAGCTATTGACAAATTTTCAGCAGATGGAATGCGT
TTGGCTCTGGCTGATGCTGGTGACACTGTAGAAGATGCCAACTTTGTGGAAGCCATGGCA
GATGCAGGTATTCTCCGTCTGTACACCTGGGTAGAGTGGGTGAAAGAAATGGTTGCCAAC
TGGGACAGCCTAAGAAGTGGTCCTGCCAGCACTTTCAATGATAGAGTTTTTGCCAGTGAA
TTGAATGCAGGAATTATAAAAACAGATCAAAACTATGAAAAGATGATGTTTAAAGAAGCT
TTGAAAACAGGGTTTTTTGAGTTTCAGGCCGCAAAAGATAAGTACCGTGAATTGGCTGTG
GAAGGGATGCACAGAGAACTTGTGTTCCGGTTTATTGAAGTTCAGACACTTCTCCTCGCT
CCATTCTGTCCACATTTGTGTGAGCACATCTGGACACTCCTGGGAAAGCCTGACTCAATT
ATGAATGCTTCATGGCCTGTGGCAGGTCCTGTTAATGAAGTTTTAATACACTCCTCACAG
TATCTTATGGAAGTAACACATGACCTTAGACTACGACTCAAGAACTATATGATGCCAGCT
AAAGGGAAGAAGACTGACAAACAACCCCTGCAGAAGCCCTCACATTGCACCATCTATGTG
GCAAAGAACTATCCACCTTGGCAACATACCACCCTGTCTGTTCTACGTAAACACTTTGAG
GCCAATAACGGAAAACTGCCTGACAACAAAGTCATTGCTAGTGAACTAGGCAGTATGCCA
GAACTGAAGAAATACATGAAGAAAGTCATGCCATTTGTTGCCATGATTAAGGAAAATCTG
GAGAAGATGGGGCCTCGTATTCTGGATTTGCAATTAGAATTTGATGAAAAGGCTGTGCTT
ATGGAGAATATAGTCTATCTGACTAATTCGCTTGAGCTAGAACACATAGAAGTCAAGTTT
GCCTCCGAAGCAGAAGATAAAATCAGGGAAGACTGCTGTCCTGGGAAACCACTTAATGTT
TTTAGAATAGAACCTGGTGTGTCCGTTTCTCTGGTGAATCCCCAGCCATCCAATGGCCAC
TTCTCAACCAAAATTGAAATCAGGCAAGGAGATAACTGTGATTCCATAATCAGGCGTTTA
ATGAAAATGAATCGAGGAATTAAAGACCTTTCCAAAGTGAAACTGATGAGATTTGATGAT
CCACTGTTGGGGCCTCGACGAGTTCCTGTCCTGGGAAAGGAGTACACCGAGAAGACCCCC
ATTTCTGAGCATGCTGTTTTCAATGTGGACCTCATGAGCAAGAAAATTCATCTGACTGAG
AATGGGATAAGGGTGGATATTGGCGATACAATAATCTATCTGGTTCATTAA
|
| Enzyme 8 GenBank Gene ID |
BC150213  |
| Enzyme 8 GeneCard ID |
A7E266  |
| Enzyme 8 GenAtlas ID |
Not Available |
| Enzyme 8 HGNC ID |
Not Available |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
16424 |
| Enzyme 9 Name |
cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial) |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
BCAT2 |
| Enzyme 9 Protein Sequence |
>cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
|
| Enzyme 9 Number of Residues |
392 |
| Enzyme 9 Molecular Weight |
44288 |
| Enzyme 9 Theoretical pI |
8.82 |
| Enzyme 9 GO Classification |
| Function |
- branched-chain-amino-acid transaminase activity
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- branched chain family amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Amino acid transport and metabolism |
| 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 |
Not Available |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
B2RB87  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
B2RB87_HUMAN  |
| Enzyme 9 PDB ID |
1KTA  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
Not Available |
| Enzyme 9 GenBank Gene ID |
AK314548  |
| Enzyme 9 GeneCard ID |
B2RB87  |
| Enzyme 9 GenAtlas ID |
Not Available |
| Enzyme 9 HGNC ID |
Not Available |
| Enzyme 9 Chromosome Location |
19 |
| Enzyme 9 Locus |
19q13 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
Not Available |
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
16930 |
| Enzyme 10 Name |
Leucine carboxyl methyltransferase 1 |
| Enzyme 10 Synonyms |
- Protein-leucine O-methyltransferase
|
| Enzyme 10 Gene Name |
LCMT1 |
| Enzyme 10 Protein Sequence |
>Leucine carboxyl methyltransferase 1
MATRQRESSITSCCSTSSCDADDEGVRGTCEDASLCKRFAVSIGYWHDPYIQHFVRLSKE
RKAPEINRGYFARVHGVSQLIKAFLRKTECHCQIVNLGAGMDTTFWRLKDEDLLPSKYFE
VDFPMIVTRKLHSIKCKPPLSSPILELHSEDTLQMDGHILDSKRYAVIGADLRDLSELEE
KLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAANSFERAMFINYEQVNMGDRFGQI
MIENLRRRQCDLAGVETCKSLESQKERLLSNGWETASAVDMMELYNRLPRAEVSRIESLE
FLDEMELLEQLMRHYCLCWATKGGNELGLKEITY
|
| Enzyme 10 Number of Residues |
334 |
| Enzyme 10 Molecular Weight |
38378.7 |
| Enzyme 10 Theoretical pI |
5.91 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in methyltransferase activity |
| Enzyme 10 Specific Function |
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues |
| 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 |
74048434  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q9UIC8  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
LCMT1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1005 bp
ATGGCCACTAGGCAGAGGGAATCCTCTATCACCTCCTGCTGTTCCACCTCGAGCTGCGAC
GCAGACGACGAGGGCGTGCGCGGCACCTGCGAAGATGCTTCCCTGTGCAAGAGGTTTGCA
GTAAGCATTGGCTACTGGCATGACCCTTACATACAGCACTTTGTGAGACTGTCTAAAGAG
AGGAAAGCCCCTGAAATCAACAGAGGATATTTTGCTCGAGTCCATGGTGTCAGTCAGCTT
ATAAAGGCATTTCTACGGAAGACAGAATGTCATTGTCAAATTGTCAACCTTGGGGCAGGC
ATGGATACCACCTTCTGGAGATTAAAGGATGAAGATCTTCTCCCAAGTAAATATTTTGAG
GTTGACTTTCCAATGATTGTCACGAGAAAGCTGCACAGTATCAAATGCAAGCCTCCCCTA
TCCAGCCCCATTCTAGAACTGCATTCAGAGGACACACTTCAGATGGATGGACACATACTG
GATTCAAAGAGATATGCCGTTATTGGAGCAGATCTCCGAGACCTGTCTGAACTGGAAGAG
AAGCTAAAGAAATGTAACATGAATACACAATTGCCAACACTCCTGATAGCTGAATGTGTG
CTGGTTTACATGACTCCAGAGCAGTCCGCAAACCTCCTGAAGTGGGCAGCCAACAGTTTT
GAGAGAGCCATGTTCATAAACTACGAACAGGTGAACATGGGTGATCGGTTTGGGCAGATC
ATGATTGAAAACCTGCGGAGACGCCAGTGTGACCTGGCGGGAGTGGAGACCTGCAAGTCA
TTAGAGTCACAGAAAGAACGGCTCCTGTCGAATGGGTGGGAAACAGCATCGGCCGTCGAC
ATGATGGAGTTGTACAACAGGTTACCTCGAGCTGAAGTGAGCAGGATAGAATCACTTGAA
TTCCTGGATGAAATGGAGCTGCTGGAGCAGCTCATGCGGCATTACTGCCTTTGCTGGGCA
ACCAAAGGAGGAAATGAGCTTGGGCTGAAGGAGATAACTTATTAA
|
| Enzyme 10 GenBank Gene ID |
NM_016309.2  |
| Enzyme 10 GeneCard ID |
LCMT1  |
| Enzyme 10 GenAtlas ID |
LCMT1  |
| Enzyme 10 HGNC ID |
HGNC:17557  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
16p12.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J: Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 1999 Dec 14;38(50):16539-47. [PubMed
]
- Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [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
]
- 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
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [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
]
|
| Enzyme 10 Metabolite References |
Not Available |