|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5853 |
| Enzyme 1 Name |
Threonyl-tRNA synthetase, cytoplasmic |
| Enzyme 1 Synonyms |
- Threonine--tRNA ligase
- ThrRS
|
| Enzyme 1 Gene Name |
TARS |
| Enzyme 1 Protein Sequence |
>Threonyl-tRNA synthetase, cytoplasmic
MFEEKASSPSGKMGGEEKPIGAGEEKQKEGGKKKNKEGSGDGGRAELNPWPEYIYTRLEM
YNILKAEHDSILAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIA
KVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIE
NGFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRIL
NEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGI
SFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFI
RSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMF
DHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL
DFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFY
GPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERM
IAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNK
KIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAE
EEF
|
| Enzyme 1 Number of Residues |
723 |
| Enzyme 1 Molecular Weight |
83434.5 |
| Enzyme 1 Theoretical pI |
6.64 |
| Enzyme 1 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- threonine-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- threonyl-tRNA aminoacylation
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 1 General Function |
Involved in nucleotide binding |
| Enzyme 1 Specific Function |
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr) |
| Enzyme 1 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 1 Reactions |
- ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr [RN:R03663]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
158258124  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P26639  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
SYTC_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>2172 bp
ATGTTTGAGGAGAAGGCCAGCAGTCCTTCAGGGAAGATGGGAGGCGAGGAGAAGCCGATT
GGTGCTGGTGAAGAGAAGCAAAAGGAAGGAGGCAAAAAGAAGAACAAAGAAGGATCTGGA
GATGGAGGTCGAGCTGAGTTGAATCCTTGGCCTGAATATATTTACACACGTCTTGAGATG
TATAATATACTAAAAGCAGAACATGATTCCATTCTGGCAGAAAAGGCAGAAAAAGATAGC
AAGCCAATTAAAGTCACTTTGCCTGATGGTAAACAGGTTGATGCGGAATCTTGGAAAACT
ACACCATATCAAATTGCCTGTGGAATTAGTCAAGGCCTGGCCGACAACACCGTTATTGCT
AAAGTAAATAATGTTGTGTGGGACCTGGACCGCCCTCTGGAAGAAGATTGTACCTTGGAG
CTTCTCAAGTTTGAGGATGAGGAAGCTCAGGCAGTGTATTGGCACTCTAGTGCTCACATA
ATGGGTGAAGCCATGGAAAGAGTCTATGGTGGATGTTTATGCTACGGTCCGCCAATAGAA
AATGGATTCTATTATGACATGTACCTCGAAGAAGGGGGTGTGTCTAGCAATGATTTCTCT
TCTCTGGAGGCTTTGTGTAAGAAAATCATTAAAGAAAAACAAGCTTTTGAAAGACTGGAA
GTTAAGAAAGAAACTTTACTGGCAATGTTTAAGTACAACAAGTTCAAATGCCGGATATTG
AATGAAAAGGTGAATACTCCAACTACCACAGTCTATAGATGTGGCCCTTTGATAGATCTC
TGCCGGGGTCCTCATGTTAGACACACGGGCAAAATTAAGGCTTTAAAAATACACAAAAAT
TCCTCCACGTACTGGGAAGGCAAAGCAGATATGGAGACTCTCCAGAGAATTTATGGCATT
TCATTCCCAGATCCTAAAATGTTGAAAGAGTGGGAGAAGTTCCAAGAGGAAGCTAAAAAC
CGAGATCATAGGAAAATTGGCAGGGACCAAGAACTATATTTCTTTCATGAACTCAGCCCT
GGAAGTTGCTTTTTTCTGCCAAAAGGAGCCTACATTTATAATGCACTTATTGAATTCATT
AGGAGCGAATATAGGAAAAGAGGATTCCAGGAGGTAGTCACCCCAAACATCTTCAACAGC
CGACTCTGGATGACCTCGGGCCACTGGCAGCACTACAGCGAGAACATGTTCTCCTTTGAG
GTGGAGAAGGAGCTGTTTGCCCTGAAACCCATGAACTGCCCAGGACACTGCCTTATGTTT
GATCATCGGCCAAGGTCCTGGCGAGAACTGCCTCTGCGGCTAGCTGATTTTGGGGTACTT
CATAGGAACGAGCTGTCTGGAGCACTCACAGGACTCACCCGGGTACGAAGATTCCAACAG
GATGATGCTCACATATTCTGTGCCATGGAGCAGATTGAAGATGAAATAAAAGGTTGTTTG
GATTTTCTACGTACGGTATATAGCGTATTTGGATTTTCTTTTAAACTAAACCTTTCTACT
CGCCCGGAAAAATTCCTTGGAGATATCGAAGTATGGGATCAAGCTGAGAAACAACTTGAA
AACAGTCTGAATGAATTTGGTGAAAAGTGGGAGTTAAACTCTGGAGATGGAGCTTTCTAT
GGCCCAAAGATTGACATACAGATTAAAGATGCGATTGGGCGGTACCACCAGTGTGCAACC
ATCCAGCTGGATTTCCAGTTGCCCATCAGATTTAATCTTACTTATGTAAGCCATGATGGT
GATGATAAGAAAAGGCCAGTGATTGTTCATCGAGCCATCTTGGGATCAGTGGAAAGAATG
ATTGCTATCCTCACAGAAAACTATGGGGGCAAATGGCCCTTTTGGCTGTCCCCTCGCCAG
GTAATGGTAGTTCCAGTGGGACCAACCTGTGATGAATATGCCCAAAAGGTACGACAACAA
TTCCACGATGCCAAATTCATGGCAGACATTGATCTGGATCCAGGCTGTACATTGAATAAA
AAGATTCGAAATGCACAGTTAGCACAGTATAACTTCATTTTAGTTGTTGGTGAAAAAGAG
AAAATCAGTGGCACTGTTAATATCCGCACAAGAGACAATAAGGTCCACGGGGAACGCACC
ATTTCTGAAACTATCGAGCGGCTACAGCAGCTCAAAGAGTTCCGCAGCAAACAGGCAGAA
GAAGAATTTTAA
|
| Enzyme 1 GenBank Gene ID |
AK292346  |
| Enzyme 1 GeneCard ID |
TARS  |
| Enzyme 1 GenAtlas ID |
TARS  |
| Enzyme 1 HGNC ID |
HGNC:11572  |
| Enzyme 1 Chromosome Location |
5 |
| Enzyme 1 Locus |
5p13.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Cruzen ME, Arfin SM: Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes. J Biol Chem. 1991 May 25;266(15):9919-23. [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
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Vasilescu J, Zweitzig DR, Denis NJ, Smith JC, Ethier M, Haines DS, Figeys D: The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells. J Proteome Res. 2007 Jan;6(1):298-305. [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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
8650 |
| Enzyme 2 Name |
Neutral amino acid transporter A |
| Enzyme 2 Synonyms |
- Alanine/serine/cysteine/threonine transporter 1
- ASCT-1
- SATT
- Solute carrier family 1 member 4
|
| Enzyme 2 Gene Name |
SLC1A4 |
| Enzyme 2 Protein Sequence |
>Neutral amino acid transporter A
MEKSNETNGYLDSAQAGPAAGPGAPGTAAGRARRCAGFLRRQALVLLTVSGVLAGAGLGA
ALRGLSLSRTQVTYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASCLGRLGGIAVAY
FGLTTLSASALAVALAFIIKPGSGAQTLQSSDLGLEDSGPPPVPKETVDSFLDLARNLFP
SNLVVAAFRTYATDYKVVTQNSSSGNVTHEKIPIGTEIEGMNILGLVLFALVLGVALKKL
GSEGEDLIRFFNSLNEATMVLVSWIMWYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFA
SILGHVIHGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSSSATLPSMMKCIEENN
GVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVELNAGQIFTILVTATASSVGA
AGVPAGGVLTIAIILEAIGLPTHDLPLILAVDWIVDRTTTVVNVEGDALGAGILHHLNQK
ATKKGEQELAEVKVEAIPNCKSEEETSPLVTHQNPAGPVASAPELESKESVL
|
| Enzyme 2 Number of Residues |
532 |
| Enzyme 2 Molecular Weight |
55722.5 |
| Enzyme 2 Theoretical pI |
6.18 |
| Enzyme 2 GO Classification |
| Function |
- carboxylic acid transmembrane transporter activity
- dicarboxylic acid transmembrane transporter activity
- organic acid transmembrane transporter activity
- sodium:dicarboxylate symporter activity
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- carboxylic acid transport
- dicarboxylic acid transport
- establishment of localization
- organic acid transport
- transport
|
| Component |
|
|
| Enzyme 2 General Function |
Involved in sodium:dicarboxylate symporter activity |
| Enzyme 2 Specific Function |
Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
Not Available |
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
- 42-62
88-108
119-139
217-237
257-277
298-318
328-348
373-393
418-438
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
62822396  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P43007  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
SATT_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1596 bp
ATGGCCCTGGGTGAAGAAAAGGCAGAAGCGGAAGCATCTGAAGACACAAAGGCCCAGTCC
TATGGGAGAGGGAGCTGCAGGGAGCGGGAGCTGGACATCCCAGGGCCCATGAGTGGGGAG
CAGCCCCCACGCCTGGAAGCTGAGGGAGGGCTCATCTCCCCTGTATGGGGGGCAGAAGGG
ATACCTGCCCCTACTTGCTGGATTGGGACTGACCCTGGCGGCCCCTCTAGAGCCCACCAG
CCACAGGCCAGTGATGCCAACAGAGAGCCCGTAGCTGAGAGGTCTGAGCCTGCACTCAGT
GGCCTGCCTCCTGCCACCATGGGGTCTGGAGACCTTCTGCTCTCCGGGGAAAGCCAGGTG
GAGAAGACCAAGCTTTCTTCCTCCGAGGAGTTCCCTCAGACTCTGAGCCTTCCCAGAACA
ACAACTATTTGCTCAGGACATGATGCTGATACCGAAGATGATCCATCCCTAGCAGATTTG
CCCCAGGCACTGGACCTCAGCCAGCAGCCTCACAGCTCAGGTCTCTCTTGCCTGTCACAG
TGGAAGTCCGTGCTGAGCCCAGGTTCCGCAGCTCAGCCTTCCAGCTGCAGCATCTCTGCT
TCCTCCACAGGCAGCAGTCTCCAGGGTCACCAGGAGAGGGCGGAGCCTCGTGGTGGTTCT
CTGGCCAAGGTCTCCTCCTCCCTGGAGCCGGTCGTCCCCCAGGAACCTTCCTCTGTGGTG
GGGCTAGGACCTCGGCCCCAGTGGTCACCACAGCCTGTGTTCTCTGGGGGTGATGCTTCT
GGGCTAGGCAGGAGACGCCTCTCCTTCCAGGCTGAGTACTGGGCCTGTGTGCTGCCAGAT
TCCCTGCCTCCATCACCCGACCGCCACTCCCCTCTCTGGAACCCAAATAAAGAGTATGAA
GATCTGCTTGACTATACTTACCCACTGAGGCCCGGGCCTCAGCTCCCAAAGCACCTTGAT
AGCCGTGTGCCAGCTGACCCTGTCCTGCAGGACTCCGGGGTAGACCTGGATAGCTTCTCT
GTCTCTCCAGCAAGCACCCTCAAATCACCTACTAATGTCTCCCCCAACTGCCCACCAGCA
GAGGCCACTGCCCTGCCATTTTCTGGGCCCAGAGAGCCAAGCCTTAAGCAGTGGCCCTCC
AGAGTACCCCAGAAACAGGGTGGCATGGGCTTGGCATCTTGGAGCCAACTTGCATCTACC
CCCAGAGCCCCAGGCAGTAGGGATGCTCGTTGGGAGCGCAGAGAGCCAGCCCTGAGGGGT
GCGAAGGACCGGCTGACTATAGGCAAGCACCTTGATATGGGCTCTCCCCAGCTAAGGACA
CGGGACAGAGGGTGGCCCTCGCCCAGGCCAGAGAGGGAGAAGAGGACCAGCCAGAGTGCC
CGGCGCCCTACCTGCACAGAGTCTAGGTGGAAATCAGAAGAGGAAGTGGAAAGTGATGAC
GAGTATCTTGCCCTCCCCGCTCGGCTGACACAGACATTTTGCTGTCAGCTGGAAGAGCTG
ATCTGCTGGCTGTATAATGTTGCAGATGTTACTGACCACGGGACTGCAGCCAGGTCCAAT
CTTACAAGTCTCAAGTCTTCTCTGCAGCTTTACCGG
|
| Enzyme 2 GenBank Gene ID |
AC007386  |
| Enzyme 2 GeneCard ID |
SLC1A4  |
| Enzyme 2 GenAtlas ID |
SLC1A4  |
| Enzyme 2 HGNC ID |
HGNC:10942  |
| Enzyme 2 Chromosome Location |
2 |
| Enzyme 2 Locus |
2p15-p13 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Arriza JL, Kavanaugh MP, Fairman WA, Wu YN, Murdoch GH, North RA, Amara SG: Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J Biol Chem. 1993 Jul 25;268(21):15329-32. [PubMed
]
- Shafqat S, Tamarappoo BK, Kilberg MS, Puranam RS, McNamara JO, Guadano-Ferraz A, Fremeau RT Jr: Cloning and expression of a novel Na(+)-dependent neutral amino acid transporter structurally related to mammalian Na+/glutamate cotransporters. J Biol Chem. 1993 Jul 25;268(21):15351-5. [PubMed
]
- Hofmann K, Duker M, Fink T, Lichter P, Stoffel W: Human neutral amino acid transporter ASCT1: structure of the gene (SLC1A4) and localization to chromosome 2p13-p15. Genomics. 1994 Nov 1;24(1):20-6. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
8882 |
| Enzyme 3 Name |
Threonine synthase-like 1 |
| Enzyme 3 Synonyms |
- TSH1
|
| Enzyme 3 Gene Name |
THNSL1 |
| Enzyme 3 Protein Sequence |
>Threonine synthase-like 1
MLHFNRCHHLKKITQKCFSSIHVKTDKHAQRFLSRTFALAELRKSWYSTHSLVGDKNIIL
MGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSVSEKLQDVGNEQFLEEEGKAVL
NFSASGSVISLTGSNPMHDASMWHLKKNGIIVYLDVPLLDLICRLKLMKTDRIVGQNSGT
SMKDLLKFRRQYYKKWYDARVFCESGASPEEVADKVLNAIKRYQDVDSETFISTRHVWPE
DCEQKVSAKFFSEAVIEGLASDGGLFVPAKEFPKLSCGEWKSLVGATYVERAQILLERCI
HPADIPAARLGEMIETAYGENFACSKIAPVRHLSGNQFILELFHGPTGSFKDLSLQLMPH
IFAHCIPPSCNYMILVATSGDTGSAVLNGFSRLNKNDKQRIAVVAFFPENGVSDFQKAQI
IGSQRENGWAVGVESDFDFCQTAIKRIFNDSDFTGFLTVEYGTILSSANSINWGRLLPQV
VYHASAYLDLVSQGFISFGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNHVL
TDFIKTGHYDLRERKLAQTFSPSIDILKSSNLERHLHLMANKDGQLMTELFNRLESQHHF
QIEKALVEKLQQDFVADWCSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQDKTCPV
IISSTAHYSKFAPAIMQALKIKEINETSSSQLYLLGSYNALPPLHEALLERTKQQEKMEY
QVCAADMNVLKSHVEQLVQNQFI
|
| Enzyme 3 Number of Residues |
743 |
| Enzyme 3 Molecular Weight |
83069.5 |
| Enzyme 3 Theoretical pI |
7.13 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- carbon-oxygen lyase activity
- carbon-oxygen lyase activity, acting on phosphates
- catalytic activity
- cofactor binding
- kinase activity
- lyase activity
- nucleoside binding
- purine nucleoside binding
- pyridoxal phosphate binding
- shikimate kinase activity
- threonine synthase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- aspartate family amino acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- threonine biosynthetic process
- threonine metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in catalytic activity |
| Enzyme 3 Specific Function |
Not Available |
| 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 |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q8IYQ7  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
THNS1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2232 bp
ATGCTCCACTTTAACCGATGTCATCATCTGAAAAAGATAACACAGAAATGTTTTTCTAGT
ATACATGTTAAAACGGATAAACATGCACAGCGATTTCTTTCAAGAACCTTTGCACTTGCG
GAATTGAGGAAGTCATGGTATTCAACCCACTCTCTTGTTGGAGACAAAAATATTATCCTG
ATGGGACCTCCTGGTGCTGGGAAAACAACAGTAGGCAGAATAATAGGTCAGAAACTAGGT
TGTTGTGTCATAGATGTGGATGATGATATCCTTGAAAAAACCTGGAATATGAGTGTGTCT
GAAAAATTACAGGATGTTGGTAATGAGCAATTTTTAGAAGAGGAAGGAAAAGCTGTGTTA
AACTTCTCTGCATCTGGAAGTGTGATTTCCCTTACTGGGTCCAATCCAATGCATGATGCT
AGCATGTGGCATCTGAAGAAAAATGGAATAATTGTATACCTGGATGTACCTCTACTAGAT
CTAATTTGTCGTCTAAAATTAATGAAGACAGATAGGATTGTAGGTCAGAATTCTGGAACA
TCTATGAAAGACTTACTTAAATTTAGAAGACAGTATTATAAGAAGTGGTATGATGCTCGT
GTTTTCTGTGAAAGTGGGGCTTCCCCAGAGGAGGTAGCTGACAAAGTGCTGAATGCAATT
AAAAGATACCAAGATGTGGACTCGGAAACATTCATTTCAACAAGACACGTTTGGCCTGAA
GACTGTGAACAGAAGGTTTCAGCAAAATTCTTTAGTGAAGCTGTAATTGAGGGGTTGGCT
TCTGATGGTGGCCTCTTTGTTCCTGCAAAGGAGTTTCCAAAATTAAGCTGCGGGGAGTGG
AAAAGCCTAGTAGGAGCAACCTACGTAGAAAGAGCACAGATACTGTTGGAAAGATGTATC
CATCCTGCAGACATACCTGCTGCCAGGTTGGGAGAAATGATTGAAACTGCTTATGGGGAA
AACTTTGCCTGCTCAAAAATTGCTCCTGTCAGGCACCTTTCAGGCAACCAGTTCATCCTG
GAGTTGTTTCATGGACCAACAGGATCATTTAAAGATTTGTCTTTACAGCTTATGCCTCAT
ATTTTTGCACACTGTATCCCACCAAGTTGCAATTATATGATACTTGTAGCTACTTCAGGA
GACACAGGGAGTGCAGTCTTAAATGGTTTTAGTCGTCTAAATAAGAATGATAAGCAAAGG
ATAGCTGTGGTTGCATTTTTTCCTGAGAATGGAGTAAGTGATTTTCAAAAAGCACAAATA
ATTGGCAGTCAGAGAGAAAATGGATGGGCAGTGGGTGTTGAGTCAGATTTTGATTTTTGC
CAGACAGCTATAAAAAGAATTTTTAATGATTCTGATTTTACTGGCTTTCTTACTGTGGAA
TATGGAACAATCTTAAGTTCGGCTAACTCCATAAACTGGGGCCGACTACTTCCGCAGGTA
GTTTATCATGCTTCCGCATATCTTGATCTTGTTAGTCAAGGATTTATTTCTTTTGGAAGC
CCAGTCGATGTCTGTATTCCCACAGGAAACTTTGGTAACATTTTAGCAGCAGTGTATGCC
AAAATGATGGGAATCCCGATTCGAAAATTTATCTGTGCCTCTAATCAGAACCATGTTTTG
ACTGATTTTATAAAAACAGGACATTATGATCTAAGGGAAAGAAAACTAGCACAAACCTTT
TCACCGTCAATAGATATTCTCAAATCTTCAAACCTAGAACGACATTTACACTTGATGGCT
AATAAAGATGGACAGCTAATGACAGAATTATTTAATCGATTAGAAAGTCAGCATCATTTC
CAGATAGAAAAGGCTCTAGTTGAGAAACTTCAGCAGGATTTTGTAGCTGACTGGTGCTCT
GAGGGAGAGTGCCTAGCAGCTATTAACTCCACCTATAATACTTCAGGGTATATTTTGGAT
CCACACACTGCTGTTGCAAAAGTGGTTGCAGATAGGGTGCAAGACAAAACTTGCCCTGTG
ATTATCTCATCTACAGCCCATTACTCAAAGTTTGCACCTGCTATCATGCAGGCTTTAAAG
ATTAAAGAAATCAATGAGACTTCATCAAGTCAGCTCTATTTGCTGGGTTCATACAATGCA
TTACCTCCACTGCATGAGGCTTTATTAGAGAGAACAAAACAGCAAGAGAAGATGGAGTAC
CAGGTCTGTGCAGCTGATATGAATGTCTTGAAGAGTCATGTGGAACAACTTGTCCAAAAT
CAATTCATATGA
|
| Enzyme 3 GenBank Gene ID |
AK125249  |
| Enzyme 3 GeneCard ID |
THNSL1  |
| Enzyme 3 GenAtlas ID |
THNSL1  |
| Enzyme 3 HGNC ID |
HGNC:26160  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
10p12.1 |
| 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
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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 |
13009 |
| Enzyme 4 Name |
Acetolactate synthase-like protein |
| Enzyme 4 Synonyms |
- IlvB-like protein
|
| Enzyme 4 Gene Name |
ILVBL |
| Enzyme 4 Protein Sequence |
>Acetolactate synthase-like protein
METPAAAAPAGSLFPSFLLLACGTLVAALLGAAHRLGLFYQLLHKVDKASVRHGGENVAA
VLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAV
TAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVR
RVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPYFMVQKEMVPAKPPKGLVGRVVSWY
LENYLANLFAGAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPTS
ADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIVLAGTVCDFRLSY
GRVLSHSSKIIIVNRNREEMLLNSDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVE
ELREADRQKEQTFREKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQ
PRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIP
VMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLSRENEDQVVKV
LHDAQQQCRDGHPVVVNILIGRTDFRDGSIAV
|
| Enzyme 4 Number of Residues |
632 |
| Enzyme 4 Molecular Weight |
67867.2 |
| Enzyme 4 Theoretical pI |
8.22 |
| Enzyme 4 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- magnesium ion binding
- metal ion binding
- thiamin pyrophosphate binding
- transferase activity
- vitamin binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in magnesium ion binding |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
2725625  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
A1L0T0  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
ILVBL_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1899 bp
ATGGAGACCCCCGCGGCCGCCGCCCCCGCTGGGAGCTTATTCCCCTCCTTCCTGCTCCTG
GCCTGCGGGACGCTGGTGGCCGCCTTGCTGGGCGCCGCTCACCGCCTGGGGCTCTTCTAT
CAGCTGCTGCACAAGGTGGACAAGGCAAGCGTCCGGCATGGCGGAGAGAACGTGGCCGCT
GTGCTGAGGGCCCATGGTGTGCGGTTCATCTTCACGCTGGTCGGTGGGCACATTTCCCCG
CTGCTGGTGGCCTGTGAGAAACTGGGCATCCGTGTGGTGGACACACGCCATGAGGTCACG
GCCGTCTTTGCTGCTGATGCTATGGCCCGCCTGTCCGGGACGGTGGGCGTGGCGGCAGTG
ACAGCAGGCCCTGGCCTCACCAACACGGTGACTGCGGTGAAGAATGCTCAGATGGCTCAG
TCCCCAATCCTGCTTCTGGGTGGGGCTGCCAGCACTCTGCTGCAGAACCGGGGTGCGCTC
CAGGCTGTTGATCAGCTGTCCCTTTTCCGGCCACTCTGTAAGTTTTGTGTGTCTGTGCGG
AGGGTGCGGGACATTGTGCCCACCCTGAGGGCCGCGATGGCTGCCGCCCAGTCGGGCACC
CCAGGTCCGGTGTTTGTGGAGCTGCCCGTTGACGTGCTGTACCCCTACTTCATGGTCCAG
AAGGAGATGGTGCCAGCCAAGCCACCCAAGGGCCTCGTGGGCCGAGTGGTCTCCTGGTAT
TTAGAGAATTACCTGGCCAACCTCTTTGCAGGAGCCTGGGAGCCTCAGCCCGAGGGACCG
CTGCCCCTGGACATCCCCCAGGCTTCCCCGCAGCAGGTTCAGCGCTGTGTGGAGATCCTG
AGCCGGGCCAAGAGGCCTCTGATGGTGCTGGGGAGTCAGGCCCTGCTCACCCCAACGTCT
GCCGACAAGCTTCGGGCTGCCGTGGAGACCTTGGGTGTTCCCTGCTTCCTTGGAGGGATG
GCACGGGGGCTGTTAGGCCGCAACCACCCCCTCCACATCCGGGAGAACCGCAGTGCGGCC
CTGAAGAAGGCGGATGTCATTGTCCTAGCAGGAACTGTGTGTGACTTCCGCCTATCCTAT
GGCCGTGTCCTCAGCCACAGCAGCAAGATCATCATCGTCAATCGTAATCGGGAAGAGATG
TTGCTCAACTCAGACATCTTCTGGAAGCCCCAGGAGGCTGTGCAGGGAGATGTGGGTTCC
TTCGTGCTGAAGTTAGTGGAGGGCCTTCAGGGCCAGACCTGGGCCCCAGACTGGGTGGAG
GAGCTGCGGGAAGCCGACCGGCAGAAGGAGCAGACCTTTCGGGAGAAGGCAGCGATGCCT
GTGGCCCAGCACCTGAACCCAGTGCAGGTGCTGCAGCTGGTGGAGGAAACGCTACCTGAC
AACTCAATTCTGGTGGTGGATGGCGGGGACTTCGTGGGCACTGCTGCCCATCTGGTACAG
CCCCGCGGCCCCCTGCGCTGGCTCGATCCTGGGGCCTTTGGGACTCTGGGAGTTGGTGCA
GGATTTGCACTTGGGGCCAAGCTGTGCCGGCCAGATGCTGAGGTCTGGTGCCTGTTTGGG
GACGGAGCTTTTGGCTACAGCCTCATCGAATTTGATACATTCGTCAGACACAAGATCCCA
GTGATGGCCTTGGTAGGGAATGATGCTGGCTGGACACAGATTTCTCGGGAGCAGGTGCCC
TCTCTGGGCAGCAACGTGGCCTGTGGCCTGGCCTACACTGATTATCACAAGGCAGCCATG
GGTCTGGGGGCCCGGGGCTTGCTGCTCTCACGGGAGAACGAGGATCAGGTGGTCAAGGTG
CTGCACGATGCCCAGCAGCAGTGCCGAGACGGCCACCCGGTTGTGGTCAACATCCTCATT
GGGAGGACGGACTTCCGCGATGGCTCCATTGCTGTATAG
|
| Enzyme 4 GenBank Gene ID |
AC003956  |
| Enzyme 4 GeneCard ID |
ILVBL  |
| Enzyme 4 GenAtlas ID |
ILVBL  |
| Enzyme 4 HGNC ID |
HGNC:6041  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
19p13.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Joutel A, Ducros A, Alamowitch S, Cruaud C, Domenga V, Marechal E, Vahedi K, Chabriat H, Bousser MG, Tournier-Lasserve E: A human homolog of bacterial acetolactate synthase genes maps within the CADASIL critical region. Genomics. 1996 Dec 1;38(2):192-8. [PubMed
]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
13056 |
| Enzyme 5 Name |
cDNA FLJ75173, highly similar to Homo sapiens threonyl-tRNA synthetase, mRNA |
| Enzyme 5 Synonyms |
- Threonyl-tRNA synthetase, isoform CRA_b
|
| Enzyme 5 Gene Name |
TARS |
| Enzyme 5 Protein Sequence |
>cDNA FLJ75173, highly similar to Homo sapiens threonyl-tRNA synthetase, mRNA
MFEEKASSPSGKMGGEEKPIGAGEEKQKEGGKKKNKEGSGDGGRAELNPWPEYIYTRLEM
YNILKAEHDSILAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIA
KVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIE
NGFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRIL
NEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGI
SFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFI
RSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMF
DHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL
DFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFY
GPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERM
IAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNK
KIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAE
EEF
|
| Enzyme 5 Number of Residues |
723 |
| Enzyme 5 Molecular Weight |
83436 |
| Enzyme 5 Theoretical pI |
6.64 |
| Enzyme 5 GO Classification |
Not Available |
| Enzyme 5 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
Not Available |
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
158258124  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
A8K8I1  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
A8K8I1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
AK292346  |
| Enzyme 5 GeneCard ID |
A8K8I1  |
| Enzyme 5 GenAtlas ID |
Not Available |
| Enzyme 5 HGNC ID |
Not Available |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
15074 |
| Enzyme 6 Name |
Probable threonyl-tRNA synthetase 2, cytoplasmic |
| Enzyme 6 Synonyms |
- Threonine--tRNA ligase
- ThrRS
- Threonyl-tRNA synthetase-like protein 2
|
| Enzyme 6 Gene Name |
TARSL2 |
| Enzyme 6 Protein Sequence |
>Probable threonyl-tRNA synthetase 2, cytoplasmic
MAAEALAAEAVASRLERQEEDIRWLWSEVERLRDEQLNAPYSCQAEGPCLTREVAQLRAE
NCDLRHRLCSLRLCLAEERSRQATLESAELEAAQEAGAQPPPSQSQDKDMKKKKMKESEA
DSEVKHQPIFIKERLKLFEILKKDHQLLLAIYGKKGDTSNIITVRVADGQTVQGEVWKTT
PYQVAAEISQELAESTVIAKVNGELWDLDRPLEGDSSLELLTFDNEEAQAVYWHSSAHIL
GEAMELYYGGHLCYGPPIENGFYYDMFIEDRAVSSTELSALENICKAIIKEKQPFERLEV
SKEILLEMFKYNKFKCRILNEKVNTATTTVYRCGPLIDLCKGPHVRHTGKIKTIKIFKNS
STYWEGNPEMETLQRIYGISFPDNKMMRDWEKFQEEAKNRDHRKIGKEQELFFFHDLSPG
SCFFLPRGAFIYNTLTDFIREEYHKRDFTEVLSPNMYNSKLWEASGHWQHYSENMFTFEI
EKDTFALKPMNCPGHCLMFAHRPRSWREMPIRFADFGVLHRNELSGTLSGLTRVRRFQQD
DAHIFCTVEQIEEEIKGCLQFLQSVYSTFGFSFQLNLSTRPENFLGEIEMWNEAEKQLQN
SLMDFGEPWKMNPGDGAFYGPKIDIKIKDAIGRYHQCATIQLDFQLPIRFNLTYVSKDGD
DKKRPVIIHRAILGSVERMIAILSENYGGKWPFWLSPRQVMVIPVGPTCEKYALQVSSEF
FEEGFMADVDLDHSCTLNKKIRNAQLAQYNFILVVGEKEKIDNAVNVRTRDNKIHGEILV
TSAIDKLKNLRKTRTLNAEEAF
|
| Enzyme 6 Number of Residues |
802 |
| Enzyme 6 Molecular Weight |
92644.8 |
| Enzyme 6 Theoretical pI |
5.93 |
| Enzyme 6 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- threonine-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- threonyl-tRNA aminoacylation
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 6 General Function |
Involved in nucleotide binding |
| Enzyme 6 Specific Function |
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr) |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
- ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr [RN:R03663]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
38570111  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
A2RTX5  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
SYTC2_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>2409 bp
ATGGCGGCCGAGGCCCTGGCGGCGGAGGCCGTGGCGTCGCGCCTGGAGCGGCAGGAGGAG
GACATCCGCTGGCTGTGGTCGGAGGTCGAGCGCCTGAGGGACGAGCAGCTGAACGCGCCC
TACAGCTGCCAGGCGGAGGGGCCGTGCCTCACGCGGGAGGTGGCGCAGCTCCGGGCCGAG
AACTGCGACCTGCGCCACCGCCTGTGCAGCCTGCGGCTGTGCCTCGCCGAGGAGCGGAGC
CGCCAGGCCACGCTGGAGAGCGCGGAGCTAGAGGCGGCGCAGGAGGCCGGCGCACAGCCT
CCTCCTAGTCAAAGCCAAGACAAGGACATGAAAAAGAAGAAAATGAAGGAAAGCGAGGCT
GACAGCGAGGTGAAGCATCAACCAATTTTCATAAAAGAAAGATTGAAGCTTTTTGAAATA
CTGAAGAAAGACCATCAGCTCTTACTTGCCATTTATGGAAAAAAGGGGGATACAAGCAAC
ATCATCACAGTAAGAGTGGCTGATGGGCAAACAGTGCAAGGGGAAGTCTGGAAAACAACG
CCTTACCAAGTGGCTGCTGAAATTAGTCAGGAACTGGCTGAAAGCACGGTAATAGCCAAA
GTCAATGGTGAACTGTGGGACCTGGACCGCCCATTGGAAGGGGACTCTTCTCTAGAGCTG
CTTACATTTGATAATGAGGAAGCTCAAGCTGTGTACTGGCACTCCAGTGCTCACATTCTT
GGGGAGGCCATGGAGCTTTACTATGGAGGCCACCTGTGCTACGGTCCGCCCATTGAAAAT
GGATTTTATTATGACATGTTCATTGAAGACAGAGCAGTGTCCAGCACAGAATTGTCAGCC
CTGGAGAATATATGTAAAGCCATCATAAAAGAAAAGCAACCTTTTGAAAGACTAGAAGTC
AGCAAGGAAATCCTCCTGGAAATGTTTAAGTACAATAAATTTAAATGCCGCATTCTGAAT
GAGAAAGTTAACACTGCAACTACCACCGTGTACAGGTGCGGTCCATTAATTGACCTTTGC
AAAGGTCCACATGTAAGACACACTGGAAAAATTAAAACCATCAAAATTTTTAAGAATTCC
TCAACATATTGGGAGGGCAATCCGGAAATGGAAACATTGCAGAGGATCTATGGAATATCC
TTTCCTGATAACAAGATGATGAGAGACTGGGAAAAGTTCCAAGAGGAAGCAAAGAACCGA
GATCACAGGAAGATCGGGAAGGAACAAGAACTTTTCTTTTTCCACGATTTGAGTCCTGGA
AGCTGTTTTTTCCTTCCCAGAGGAGCCTTCATTTATAATACGCTTACAGATTTCATACGA
GAGGAATATCACAAACGGGACTTCACGGAGGTGCTCTCTCCCAATATGTACAACAGTAAA
CTCTGGGAAGCCTCAGGCCACTGGCAGCATTACAGCGAGAACATGTTTACCTTTGAGATT
GAAAAGGACACTTTTGCCCTCAAACCCATGAATTGTCCAGGGCACTGTCTAATGTTTGCC
CATCGTCCACGATCTTGGAGGGAAATGCCTATTAGATTTGCTGATTTTGGAGTTCTGCAT
AGAAATGAACTGTCGGGGACTCTCAGCGGCTTGACCAGAGTGAGGCGCTTCCAGCAGGAC
GATGCTCACATTTTTTGCACAGTGGAGCAGATTGAAGAAGAAATAAAGGGGTGTTTGCAG
TTTTTGCAATCTGTTTACTCAACATTTGGCTTCTCCTTTCAATTAAACCTGTCAACAAGG
CCGGAAAACTTCCTAGGAGAGATTGAGATGTGGAATGAGGCTGAGAAGCAACTGCAGAAC
AGCTTGATGGACTTTGGAGAACCGTGGAAAATGAACCCAGGAGATGGAGCATTTTATGGC
CCTAAAATTGACATAAAAATCAAGGATGCTATTGGCAGATACCATCAATGTGCTACAATT
CAGCTGGACTTCCAACTGCCTATTAGATTTAATCTCACATATGTTAGTAAGGATGGGGAT
GATAAGAAGAGACCTGTGATCATTCATCGAGCCATTTTGGGATCAGTGGAAAGAATGATA
GCCATTCTTTCAGAAAACTATGGCGGAAAATGGCCTTTCTGGCTATCTCCTCGTCAGGTG
ATGGTCATCCCTGTGGGGCCAACTTGTGAAAAATATGCACTTCAGGTATCCAGTGAATTT
TTTGAAGAAGGATTTATGGCTGACGTTGACTTGGATCACAGTTGTACACTAAATAAGAAA
ATACGAAATGCACAGCTGGCTCAGTATAATTTTATTTTGGTGGTTGGAGAAAAGGAAAAG
ATAGATAATGCTGTAAACGTGCGAACAAGAGACAACAAAATTCATGGAGAGATTTTAGTA
ACTTCTGCCATTGATAAACTGAAGAATCTCAGGAAGACACGGACACTCAATGCTGAGGAG
GCCTTTTGA
|
| Enzyme 6 GenBank Gene ID |
NM_152334.2  |
| Enzyme 6 GeneCard ID |
TARSL2  |
| Enzyme 6 GenAtlas ID |
TARSL2  |
| Enzyme 6 HGNC ID |
HGNC:24728  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
15q26.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 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
]
- 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
15075 |
| Enzyme 7 Name |
Threonyl-tRNA synthetase, mitochondrial |
| Enzyme 7 Synonyms |
- Threonine--tRNA ligase
- ThrRS
- Threonyl-tRNA synthetase-like 1
|
| Enzyme 7 Gene Name |
TARS2 |
| Enzyme 7 Protein Sequence |
>Threonyl-tRNA synthetase, mitochondrial
MALYQRWRCLRLQGLQACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASMAQKEPRT
IKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFL
TFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEYGFYHDFFLGKERTIRGSELPV
LERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLC
QGPHLRHTGQIGGLKLLSNSSSLWRSSGAPETLQRVSGISFPTTELLRVWEAWREEAELR
DHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTK
LWEQSGHWEHYQEDMFAVQPPGSDRPPSSQSDDSTRHITDTLALKPMNCPAHCLMFAHRP
RSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLR
SVYAVLGFSFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKI
DVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGQAGALERPVLIHRAVLGSVERLLGVLA
ESCGGKWPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDADSGLTLSRRIRRA
QLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTRVPNAEEIF
|
| Enzyme 7 Number of Residues |
718 |
| Enzyme 7 Molecular Weight |
81035.3 |
| Enzyme 7 Theoretical pI |
7.31 |
| Enzyme 7 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- threonine-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- threonyl-tRNA aminoacylation
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 7 General Function |
Involved in nucleotide binding |
| Enzyme 7 Specific Function |
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr) |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr [RN:R03663]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
62897187  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9BW92  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
SYTM_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2157 bp
ATGGCCCTGTATCAGAGGTGGCGGTGTCTCCGGCTCCAAGGTTTACAGGCTTGCAGGCTA
CACACGGCAGTTGTGTCGACCCCTCCACGCTGGTTGGCAGAGCGGCTTGGCCTTTTTGAG
GAGCTGTGGGCTGCTCAGGTAAAGAGATTAGCAAGCATGGCACAGAAGGAACCCCGGACT
ATTAAGATATCACTTCCTGGAGGCCAGAAAATTGATGCTGTGGCATGGAACACAACCCCC
TACCAACTAGCCCGGCAGATCAGTTCAACACTGGCAGATACTGCAGTGGCTGCTCAAGTG
AATGGAGAACCTTATGATCTGGAGCGGCCCTTGGAGACAGATTCTGACCTCAGATTTCTG
ACATTCGATTCCCCAGAGGGGAAAGCAGTGTTCTGGCACTCCAGCACCCATGTCCTGGGG
GCAGCAGCTGAACAATTCCTAGGTGCTGTTCTCTGCAGAGGTCCAAGTACAGAATATGGC
TTTTACCATGATTTCTTCCTGGGAAAGGAGAGGACAATCCGGGGCTCAGAGCTGCCTGTT
TTGGAGCGGATTTGCCAGGAACTTACAGCTGCTGCTCGACCCTTCCGGAGGCTAGAGGCT
TCACGGGATCAGCTTCGCCAGTTGTTCAAGGATAACCCCTTTAAGCTTCACTTGATTGAG
GAGAAAGTGACAGGTCCAACAGCAACAGTATATGGGTGTGGCACATTGGTTGACCTTTGC
CAGGGCCCCCACCTTCGGCATACTGGACAGATTGGAGGACTGAAGCTGCTATCGAACTCA
TCATCCTTATGGAGGTCTTCAGGGCCCCCAGAGACACTGCAGAGAGTGTCAGGGATTTCC
TTCCCCACAACAGAATTGCTGAGGGTCTGGGAAGCATGGAGGGAGGAAGCAGAATTGCGG
GACCACCGGCGCATTGGGAAGGAACAGGAGCTCTTCTTCTTCCATGAACTGAGCCCTGGG
AGCTGCTTCTTCCTGCCACGAGGGACAAGGGTGTATAATGCACTAGTGGCGTTTATCAGG
GCTGAGTATGCCCATCGTGGTTTCTCCGAGGTGAAAACTCCCACACTGTTTTCTACGAAG
CTCTGGGAACAGTCAGGGCACTGGGAGCATTATCAGGAAGACATGTTTGCCGTGCAGCCC
CCAGGCTCTGACAGGCCTCCCAGCTCCCAGAGTGACGATTCTACCAGGCATATCACAGAT
ACACTCGCCCTCAAGCCTATGAACTGCCCTGCACACTGCCTGATGTTCGCCCACCGGCCC
AGATCCTGGCGGGAACTGCCCCTGCGACTAGCTGACTTTGGGGCTCTACACCGGGCCGAA
GCCTCTGGTGGTCTGGGGGGACTGACCCGACTGCGGTGCTTCCAGCAGGATGACGCTCAC
ATCTTCTGTACAACAGATCAGCTGGAAGCAGAGATCCAAAGCTGTCTTGATTTCCTCCGT
TCCGTCTATGCCGTTCTTGGCTTCTCCTTCCGCCTGGCACTGTCCACCCGGCCATCTGGC
TTCCTGGGGGACCCTTGCCTTTGGGACCAGGCCGAACAGGTCCTTAAACAGGCCCTGAAG
GAATTTGGAGAACCCTGGGACCTCAACTCTGGAGATGGTGCCTTCTATGGACCTAAGATT
GACGTGCACCTCCACGATGCCCTGGGCCGGCCACATCAGTGTGGGACAATTCAGCTTGAC
TTCCAACTGCCCCTGAGATTTGACCTCCAGTATAAGGGGCAGGCGGGTGCCCTGGGGCGT
CCAGTCCTCATTCACCGAGCAGTGCTCGGTTCTGTGGAAAGACTGTTGGGAGTGCTGGCA
GAAAGCTGCGGGGGGAAATGGCCACTGTGGCTGTCCCCGTTCCAGGTGGTGGTCATCCCT
GTGGGGAGTGAGCAAGAGGAATACGCCAAAGAGGCACAGCAGAGCCTGCGGGCTGCAGGA
CTGGTCAGTGACCTGGATGCAGACTCTGGACTGACCCTCAGCCGGAGAATCCGCCGGGCC
CAGCTTGCCCACTACAATTTTCAGTTTGTGGTTGGCCAGAAAGAGCAAAGTAAGAGAACA
GTGAACATTCGGACTCGAGATAATCGTCGCCTTGGGGAGTGGGACTTGCCTGAGGCTGTG
CAGCGACTGGTGGAGCTACAGAACACGAGGGTCCCAAATGCCGAAGAAATTTTCTGA
|
| Enzyme 7 GenBank Gene ID |
AK222814  |
| Enzyme 7 GeneCard ID |
TARS2  |
| Enzyme 7 GenAtlas ID |
TARS2  |
| Enzyme 7 HGNC ID |
HGNC:30740  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
1q21.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |