|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5855 |
| Enzyme 1 Name |
Asparagine synthetase [glutamine-hydrolyzing] |
| Enzyme 1 Synonyms |
- Cell cycle control protein TS11
- Glutamine-dependent asparagine synthetase
|
| Enzyme 1 Gene Name |
ASNS |
| Enzyme 1 Protein Sequence |
>Asparagine synthetase [glutamine-hydrolyzing]
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGV
FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFN
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPK
WINATDPSARTLTHYKSAVKA
|
| Enzyme 1 Number of Residues |
561 |
| Enzyme 1 Molecular Weight |
64369.4 |
| Enzyme 1 Theoretical pI |
6.85 |
| Enzyme 1 GO Classification |
| Function |
- asparagine synthase (glutamine-hydrolyzing) activity
- asparagine synthase (glutamine-hydrolyzing) activity
- carbon-nitrogen ligase activity, with glutamine as amido-N-donor
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| Process |
- asparagine biosynthetic process
- asparagine metabolic process
- aspartate 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 asparagine synthase (glutamine-hydrolyzing) activity |
| Enzyme 1 Specific Function |
ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- (1) ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate [RN:R00578]
- (2) (1a) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
- (3) (1b) ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine [RN:R00483]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
179100  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P08243  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ASNS_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1686 bp
ATGTGTGGCATTTGGGCGCTGTTTGGCAGTGATGATTGCCTTTCTGTTCAGTGTCTGAGT
GCTATGAAGATTGCACACAGAGGTCCAGATGCATTCCGTTTTGAGAATGTCAATGGATAC
ACCAACTGCTGCTTTGGATTTCACCGGTTGGCGGTAGTTGACCCGCTGTTTGGAATGCAG
CCAATTCGAGTGAAGAAATATCCGTATTTGTGGCTCTGTTACAATGGTGAAATCTACAAC
CATAAGAAGATGCAACAGCATTTTGAATTTGAATACCAGACCAAAGTGGATGGTGAGATA
ATCCTTCATCTTTATGACAAAGGAGGAATTGAGCAAACAATTTGTATGTTGGATGGTGTG
TTTGCATTTGTTTTACTGGATACTGCCAATAAGAAAGTGTTCCTGGGTAGAGATACATAT
GGAGTCAGACCTTTGTTTAAAGCAATGACAGAAGATGGATTTTTGGCTGTATGTTCAGAA
GCTAAAGGTCTTGTTACATTGAAGCACTCCGCGACTCCCTTTTTAAAAGTGGAGCCTTTT
CTTCCTGGACACTATGAAGTTTTGGATTTAAAGCCAAATGGCAAAGTTGCATCCGTGGAA
ATGGTTAAATATCATCACTGTCGGGATGTACCCCTGCACGCCCTCTATGACAATGTGGAG
AAACTCTTTCCAGGTTTTGAGATAGAAACTGTGAAGAACAACCTCAGGATCCTTTTTAAT
AATGCTGTAAAGAAACGTTTGATGACAGACAGAAGGATTGGCTGCCTTTTATCAGGGGGC
TTGGACTCCAGCTTGGTTGCTGCCACTCTGTTGAAGCAGCTGAAAGAAGCCCAAGTACAG
TATCCTCTCCAGACATTTGCAATTGGCATGGAAGACAGCCCCGATTTACTGGCTGCTAGA
AAGGTGGCAGATCATATTGGAAGTGAACATTATGAAGTCCTTTTTAACTCTGAGGAAGGC
ATTCAGGCTCTGGATGAAGTCATATTTTCCTTGGAAACTTATGACATTACAACAGTTCGT
GCTTCAGTAGGTATGTATTTAATTTCCAAGTATATTCGGAAGAACACAGATAGCGTGGTG
ATCTTCTCTGGAGAAGGATCAGATGAACTTACGCAGGGTTACATATATTTTCACAAGGCT
CCTTCTCCTGAAAAAGCCGAGGAGGAGAGTGAGAGGCTTCTGAGGGAACTCTATTTGTTT
GATGTTCTCCGCGCAGATCGAACTACTGCTGCCCATGGTCTTGAACTGAGAGTCCCATTT
CTAGATCATCGATTTTTTTCCTATTACTTGTCTCTGCCACCAGAAATGAGAATTCCAAAG
AATGGGATAGAAAAACATCTCCTGAGAGAGACGTTTGAGGATTCCAATCTGATACCCAAA
GAGATTCTCTGGCGACCAAAAGAAGCCTTCAGTGATGGAATAACTTCAGTTAAGAATTCC
TGGTTTAAGATTTTACAGGAATACGTTGAACATCAGGTTGATGATGCAATGATGGCAAAT
GCAGCCCAGAAATTTCCCTTCAATACTCCTAAAACCAAAGAAGGATATTACTACCGTCAA
GTCTTTGAACGCCATTACCCAGGCCGGGCTGACTGGCTGAGCCATTACTGGATGCCCAAG
TGGATCAATGCCACTGACCCTTCTGCCCGCACGCTGACCCACTACAAGTCAGCTGTCAAA
GCTTAG
|
| Enzyme 1 GenBank Gene ID |
M27396  |
| Enzyme 1 GeneCard ID |
ASNS  |
| Enzyme 1 GenAtlas ID |
ASNS  |
| Enzyme 1 HGNC ID |
HGNC:753  |
| Enzyme 1 Chromosome Location |
7 |
| Enzyme 1 Locus |
7q21.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Andrulis IL, Chen J, Ray PN: Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol. 1987 Jul;7(7):2435-43. [PubMed
]
- Zhang YP, Lambert MA, Cairney AE, Wills D, Ray PN, Andrulis IL: Molecular structure of the human asparagine synthetase gene. Genomics. 1989 Apr;4(3):259-65. [PubMed
]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [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
]
- Greco A, Ittmann M, Basilico C: Molecular cloning of a gene that is necessary for G1 progression in mammalian cells. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1565-9. [PubMed
]
- Greco A, Gong SS, Ittmann M, Basilico C: Organization and expression of the cell cycle gene, ts11, that encodes asparagine synthetase. Mol Cell Biol. 1989 Jun;9(6):2350-9. [PubMed
]
- Van Heeke G, Schuster SM: Expression of human asparagine synthetase in Escherichia coli. J Biol Chem. 1989 Apr 5;264(10):5503-9. [PubMed
]
- Van Heeke G, Schuster SM: The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. J Biol Chem. 1989 Nov 25;264(33):19475-7. [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
]
- 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 |
5883 |
| Enzyme 2 Name |
Asparaginyl-tRNA synthetase, cytoplasmic |
| Enzyme 2 Synonyms |
- Asparagine--tRNA ligase
- AsnRS
|
| Enzyme 2 Gene Name |
NARS |
| Enzyme 2 Protein Sequence |
>Asparaginyl-tRNA synthetase, cytoplasmic
MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISK
SQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGAL
EGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVA
VYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGE
NMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSS
QLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCD
VVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIP
EAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIF
DSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP
RFVQRCTP
|
| Enzyme 2 Number of Residues |
548 |
| Enzyme 2 Molecular Weight |
62942.4 |
| Enzyme 2 Theoretical pI |
6.17 |
| Enzyme 2 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- asparagine-tRNA ligase activity
- aspartate-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- asparaginyl-tRNA aminoacylation
- aspartyl-tRNA aminoacylation
- 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
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 2 General Function |
Involved in nucleotide binding |
| Enzyme 2 Specific Function |
ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn) |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn [RN:R03648]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
2764505  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
O43776  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
SYNC_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1647 bp
ATGGTGCTAGCAGAGCTGTACGTCTCTGACCGAGAGGGAAGCGATGCCACGGGAGATGGA
ACCAAGGAGAAACCATTTAAAACAGGTCTAAAGGCTTTGATGACAGTAGGGAAAGAACCA
TTTCCTACCATTTACGTAGATTCACAAAAAGAAAATGAGAGGTGGAATGTTATTTCTAAA
TCACAGTTGAAGAACATTAAAAAGATGTGGCATAGGGAACAAATGAAGAGTGAATCCCGG
GAAAAGAAAGAGGCAGAAGATAGTTTACGAAGAGAAAAGAACCTGGAAGAAGCAAAGAAG
ATTACCATTAAAAATGATCCAAGTCTCCCAGAGCCAAAATGTGTGAAGATTGGTGCGTTA
GAAGGATATAGAGGCCAAAGAGTAAAGGTGTTTGGCTGGGTCCACAGGCTGCGCAGGCAA
GGAAAGAATTTAATGTTTCTGGTGTTGCGAGATGGTACAGGTTATCTTCAGTGTGTCTTG
GCGGATGAGTTGTGTCAGTGCTACAATGGAGTTCTCTTGTCCACGGAGAGCAGTGTTGCA
GTGTATGGAATGCTAAATCTTACCCCAAAGGGCAAGCAGGCTCCAGGTGGCCATGAGCTG
AGTTGTGACTTCTGGGAACTAATTGGGTTGGCCCCTGCTGGAGGAGCTGACAACCTGATC
AATGAGGAGTCTGACGTTGATGTCCAGCTCAACAACAGACACATGATGATCCGAGGAGAA
AACATGTCCAAAATCCTAAAAGCACGATCCATGGTCACCAGGTGCTTTAGAGATCACTTC
TTTGATAGGGGGTACTATGAAGTTACTCCTCCAACATTAGTGCAAACACAAGTAGAAGGT
GGTGCCACACTCTTCAAGCTTGACTATTTTGGGGAAGAGGCATTTTTGACTCAATCCTCT
CAGTTGTACTTGGAGACCTGCCTCCCAGCCCTGGGAGATGTTTTTTGTATTGCTCAGTCA
TACCGGGCAGAGCAGTCCAGAACACGAAGGCACCTGGCTGAGTACACTCACGTGGAAGCT
GAGTGTCCTTTCCTGACTTTTGACGACCTCCTGAACCGGTTGGAGGACTTGGTTTGTGAT
GTGGTAGATCGAATATTGAAGTCACCTGCAGGGAGCATAGTGCATGAGCTCAACCCGAAC
TTTCAGCCCCCCAAACGGCCTTTCAAACGGATGAACTATTCAGATGCTATCGTTTGGCTA
AAAGAACATGATGTAAAGAAAGAAGATGGAACTTTCTATGAATTTGGAGAAGATATCCCA
GAAGCTCCTGAGAGACTGATGACAGACACCATTAATGAACCAATCTTGCTGTGTCGATTT
CCTGTGGAGATCAAGTCCTTCTACATGCAGCGATGTCCTGAGGATTCCCGTCTTACTGAA
TCTGTCGACGTGTTGATGCCCAATGTTGGTGAGATTGTGGGAGGCTCAATGCGTATCTTT
GATAGTGAAGAAATACTGGCAGGTTATAAAAGGGAAGGGATTGACCCCACTCCCTATTAC
TGGTATACGGATCAGAGAAAATACGGTACATGTCCCCATGGAGGATATGGCTTGGGCTTG
GAACGATTCTTAACGTGGATTCTGAATAGGTATCACATCCGAGACGTGTGCTTATACCCT
CGATTTGTCCAGCGTTGCACGCCATAA
|
| Enzyme 2 GenBank Gene ID |
AJ000334  |
| Enzyme 2 GeneCard ID |
NARS  |
| Enzyme 2 GenAtlas ID |
NARS  |
| Enzyme 2 HGNC ID |
HGNC:7643  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
18q21.31 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Beaulande M, Tarbouriech N, Hartlein M: Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen. Nucleic Acids Res. 1998 Jan 15;26(2):521-4. [PubMed
]
- Shiba K, Motegi H, Yoshida M, Noda T: Human asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family. Nucleic Acids Res. 1998 Nov 15;26(22):5045-51. [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
]
- Xu G, Shin SB, Jaffrey SR: Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19310-5. Epub 2009 Nov 5. [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
]
- 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6885 |
| Enzyme 3 Name |
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 |
| Enzyme 3 Synonyms |
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit
- Ribophorin I
- RPN-I
- Ribophorin-1
|
| Enzyme 3 Gene Name |
RPN1 |
| Enzyme 3 Protein Sequence |
>Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
MEAPAAGLFLLLLLGTWAPAPGSASSEAPPLINEDVKRTVDLSSHLAKVTAEVVLAHLGG
GSTSRATSFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVA
LDPGAKISVIVETVYTHVLHPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASR
NVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWG
NIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNV
STSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVF
DEQVIDSLTVKIILPEGAKNIEIDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQH
IQDIVVHYTFNKVLMLQEPLLVVAAFYILFFTVIIYVRLDFSITKDPAAEARMKVACITE
QVLTLVNKRIGLYRHFDETVNRYKQSRDISTLNSGKKSLETEHKALTSEIALLQSRLKTE
GSDLCDRVSEMQKLDAQVKELVLKSAVEAERLVAGKLKKDTYIENEKLISGKRQELVTKI
DHILDAL
|
| Enzyme 3 Number of Residues |
607 |
| Enzyme 3 Molecular Weight |
68568.8 |
| Enzyme 3 Theoretical pI |
6.34 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- dolichyl-diphosphooligosaccharide-protein glycotransferase activity
- oligosaccharyl transferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum
- integral to membrane
- intracellular membrane-bounded organelle
- intrinsic to membrane
- membrane part
- membrane-bounded organelle
- organelle
|
|
| Enzyme 3 General Function |
Involved in dolichyl-diphosphooligosaccharide-protein glycotransferase activity |
| Enzyme 3 Specific Function |
Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
36053  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P04843  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
RPN1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1824 bp
ATGGAGGCGCCAGCCGCCGGCTTGTTTCTGCTCCTGTTGCTTGGGACTTGGGCCCCGGCG
CCGGGCAGCGCCTCCTCCGAGGCACCGCCGCTGATCAATGAGGACGTGAAGCGCACAGTG
GACCTAAGCAGCCACCTGGCTAAGGTGACGGCCGAGGTGGTCCTGGCGCACCTGGGCGGC
GGCTCCACGTCCCGAGCTACCTCTTTCCTGCTGGCTTTGGAGCCTGAGCTCGAGGCCCGG
CTGGCGCACCTGGGCGTGCAGGTAAAGGGAGAAGATGAGGAAGAGAACAATTTGGAAGTA
CGTGAAACCAAAATTAAGGGTAAAAGTGGGAGATTCTTCACAGTCAAGCTCCCAGTTGCT
CTTGATCCTGGGGCCAAGATTTCAGTCATTGTGGAAACAGTCTACACCCATGTGCTTCAT
CCATATCCAACCCAGATCACCCAGTCAGAGAAACAGTTTGTGGTGTTTGAGGGGAACCAT
TATTTCTACTCTCCCTATCCAACGAAGACACAAACCATGCGTGTGAAGCTTGCCTCTCGA
AATGTGGAGAGCTACACCAAGCTGGGGAACCCCACGCGCTCTGAGGACCTACTGGATTAT
GGGCCTTTCAGAGATGTGCCTGCCTATAGTCAGGATACTTTTAAAGTACATTATGAGAAC
AACAGCCCTTTCCTGACCATCACCAGCATGACCCGAGTCATTGAAGTCTCTCACTGGGGT
AATATTGCTGTGGAAGAAAATGTGGACTTAAAGCACACAGGAGCTGTGCTTAAGGGGCCT
TTCTCACGCTATGATTACCAGAGACAGCCAGATAGTGGAATATCCTCCATCCGTTCTTTT
AAGACCATCCTTCCTGCTGCTGCCCAGGATGTTTATTACCGGGATGAGATTGGCAATGTT
TCTACCAGCCACCTCCTTATTTTGGATGACTCTGTAGAGATGGAAATCCGGCCTCGCTTC
CCTCTCTTTGGCGGGTGGAAGACCCATTACATCGTTGGCTACAACCTCCCAAGCTATGAG
TACCTCTATAATTTGGGTGACCAGTATGCACTGAAGATGAGGTTTGTGGACCATGTGTTT
GATGAACAAGTGATAGATTCTCTGACTGTGAAGATCATCCTGCCTGAAGGAGCCAAGAAC
ATTGAAATTGATAGTCCCTATGAAATCAGCCGTGCCCCAGATGAGCTGCACTACACCTAT
CTGGATACATTTGGCCGCCCTGTGATTGTTGCCTACAAGAAAAATCTGGTAGAACAGCAC
ATTCAGGACATTGTGGTCCACTACACGTTCAACAAGGTGCTCATGCTGCAGGAGCCCCTG
CTGGTGGTGGCGGCCTTCTACATCCTGTTCTTCACCGTTATCATCTATGTTCGGCTGGAC
TTCTCCATCACCAAGGATCCAGCCGCAGAAGCCAGGATGAAGGTAGCCTGCATCACAGAG
CAGGTCTTGACCCTGGTCAACAAGAGAATAGGCCTTTACCGTCACTTTGACGAGACCGTC
AATAGGTACAAGCAATCCCGGGACATCTCCACCCTCAACAGTGGCAAGAAGAGCCTGGAG
ACTGAACACAAGGCCTTGACCAGTGAGATTGCACTGCTGCAGTCCAGGCTGAAGACAGAG
GGCTCTGATCTGTGCGACAGAGTGAGCGAAATGCAGAAGCTGGATGCACAGGTCAAGGAG
CTGGTGCTGAAGTCGGCGGTGGAGGCTGAGCGCCTGGTGGCTGGCAAGCTCAAGAAAGAC
ACGTACATTGAGAATGAGAAGCTCATCTCAGGAAAGCGCCAGGAGCTGGTCACCAAGATC
GACCACATCCTGGATGCCCTGTAG
|
| Enzyme 3 GenBank Gene ID |
Y00281  |
| Enzyme 3 GeneCard ID |
RPN1  |
| Enzyme 3 GenAtlas ID |
RPN1  |
| Enzyme 3 HGNC ID |
HGNC:10381  |
| Enzyme 3 Chromosome Location |
3 |
| Enzyme 3 Locus |
3q21.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Crimaudo C, Hortsch M, Gausepohl H, Meyer DI: Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins. EMBO J. 1987 Jan;6(1):75-82. [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
]
- 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
]
- 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
]
- Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. [PubMed
]
- Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed
]
- Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [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
]
- 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
]
- 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 |
6887 |
| Enzyme 4 Name |
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit |
| Enzyme 4 Synonyms |
- DDOST 48 kDa subunit
- Oligosaccharyl transferase 48 kDa subunit
|
| Enzyme 4 Gene Name |
DDOST |
| Enzyme 4 Protein Sequence |
>Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
MGYFRCARAGSFGRRRKMEPSTAARAWALFWLLLPLLGAVCASGPRTLVLLDNLNVRETH
SLFFRSLKDRGFELTFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFI
DGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDLGQHTLIVADTENL
LKAPTIVGKSSLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKN
TLLIAGLQARNNARVIFSGSLDFFSDSFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVF
KEEGVLRVGPVSHHRVGETAPPNAYTVTDLVEYSIVIQQLSNGKWVPFDGDDIQLEFVRI
DPFVRTFLKKKGGKYSVQFKLPDVYGVFQFKVDYNRLGYTHLYSSTQVSVRPLQHTQYER
FIPSAYPYYASAFSMMLGLFIFSIVFLHMKEKEKSD
|
| Enzyme 4 Number of Residues |
456 |
| Enzyme 4 Molecular Weight |
50800.3 |
| Enzyme 4 Theoretical pI |
6.52 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- dolichyl-diphosphooligosaccharide-protein glycotransferase activity
- oligosaccharyl transferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid N-linked glycosylation
- protein amino acid N-linked glycosylation via asparagine
- protein amino acid glycosylation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- membrane
- organelle membrane
|
|
| Enzyme 4 General Function |
Involved in dolichyl-diphosphooligosaccharide-protein glycotransferase activity |
| Enzyme 4 Specific Function |
Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
20070197  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P39656  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
OST48_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1371 bp
ATGGGGTACTTCCGGTGTGCAGGTGCTGGGTCCTTCGGCAGGAGGAGGAAGATGGAGCCC
AGCACCGCGGCCCGGGCTTGGGCCCTCTTTTGGTTGCTGCTGCCCTTGCTTGGCGCGGTT
TGCGCCAGCGGACCCCGCACCTTAGTGCTGCTGGACAACCTCAACGTGCGGGAGACTCAT
TCGCTTTTCTTCCGGAGCCTGAAGGACCGGGGCTTTGAGCTCACATTCAAGACCGCTGAT
GACCCCAGCCTGTCTCTCATAAAGTATGGGGAATTCCTCTATGACAATCTCATCATTTTC
TCCCCTTCGGTAGAAGATTTTGGAGGCAACATCAACGTGGAGACCATCAGTGCCTTTATT
GACGGCGGAGGCAGTGTGCTGGTAGCTGCCAGCTCCGACATTGGTGACCCTCTTCGAGAG
CTGGGCAGTGAGTGCGGGATTGAGTTTGACGAGGAGAAAACGGCTGTCATTGACCATCAC
AACTATGACATCTCAGACCTTGGCCAGCATACGCTCATCGTGGCTGACACTGAGAACCTG
CTGAAGGCCCCAACCATCGTTGGGAAATCATCTCTAAATCCCATCCTCTTTCGAGGTGTT
GGGATGGTGGCCGATCCTGATAACCCTTTGGTGCTGGACATCCTGACGGGCTCTTCCACC
TCTTACTCCTTCTTCCCGGACAAGCCTATCACCCAGTATCCACATGCGGTGGGGAAGAAC
ACCCTCCTCATTGCTGGGCTCCAGGCCAGGAACAATGCCCGCGTCATCTTCAGCGGCTCC
CTCGACTTCTTCAGCGACTCCTTCTTCAACTCAGCAGTGCAGAAGGCGGCGCCCGGCTCC
CAGAGGTATTCCCAGACAGGCAACTATGAACTAGCTGTGGCCCTCTCCCGCTGGGTGTTC
AAGGAGGAGGGTGTCCTCCGTGTGGGGCCTGTGTCCCATCATCGGGTGGGCGAGACAGCC
CCACCCAATGCCTACACTGTCACTGACCTAGTGGAGTATAGCATCGTGATCCAGCAGCTC
TCAAATGGCAAATGGGTCCCCTTTGATGGCGATGACATTCAGCTGGAGTTTGTCCGCATT
GATCCTTTTGTGAGGACCTTCCTGAAGAAGAAAGGTGGCAAATACAGTGTTCAGTTCAAG
TTGCCCGACGTGTATGGTGTATTCCAGTTTAAAGTGGATTACAACCGGCTAGGCTACACA
CACCTGTACTCTTCCACTCAGGTATCCGTGCGGCCACTCCAGCACACGCAGTATGAGCGC
TTCATCCCCTCGGCCTACCCCTACTACGCCAGCGCCTTCTCCATGATGCTGGGGCTCTTC
ATCTTCAGCATCGTCTTCTTGCACATGAAGGAGAAGGAGAAGTCCGACTGA
|
| Enzyme 4 GenBank Gene ID |
NM_005216.4  |
| Enzyme 4 GeneCard ID |
DDOST  |
| Enzyme 4 GenAtlas ID |
DDOST  |
| Enzyme 4 HGNC ID |
HGNC:2728  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1p36.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Yamagata T, Tsuru T, Momoi MY, Suwa K, Nozaki Y, Mukasa T, Ohashi H, Fukushima Y, Momoi T: Genome organization of human 48-kDa oligosaccharyltransferase (DDOST). Genomics. 1997 Nov 1;45(3):535-40. [PubMed
]
- Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [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
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6888 |
| Enzyme 5 Name |
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 |
| Enzyme 5 Synonyms |
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit
- RIBIIR
- Ribophorin II
- RPN-II
- Ribophorin-2
|
| Enzyme 5 Gene Name |
RPN2 |
| Enzyme 5 Protein Sequence |
>Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
MAPPGSSTVFLLALTIIASTWALTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSS
LGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDS
SVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSI
VEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAI
FSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPL
TQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIA
NTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQL
VDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYT
LYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTV
VSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIIFHLGHAAMLGLMYVYWTQLNMF
QTLKYLAILGSVTFLAGNRMLAQQAVKRTAH
|
| Enzyme 5 Number of Residues |
631 |
| Enzyme 5 Molecular Weight |
69283.3 |
| Enzyme 5 Theoretical pI |
5.46 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- dolichyl-diphosphooligosaccharide-protein glycotransferase activity
- oligosaccharyl transferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid N-linked glycosylation
- protein amino acid N-linked glycosylation via asparagine
- protein amino acid glycosylation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- macromolecular complex
- membrane
- oligosaccharyltransferase complex
- organelle membrane
- protein complex
|
|
| Enzyme 5 General Function |
Involved in dolichyl-diphosphooligosaccharide-protein glycotransferase activity |
| Enzyme 5 Specific Function |
Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
5834424  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P04844  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
RPN2_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1896 bp
ATGGCGCCGCCGGGTTCAAGCACTGTCTTCCTGTTGGCCCTGACAATCATAGCCAGCACC
TGGGCTCTGACGCCCACTCACTACCTCACCAAGCATGACGTGGAGAGACTAAAAGCCTCG
CTGGATCGCCCTTTCACAAATTTGGAATCTGCCTTCTACTCCATCGTGGGACTCAGCAGC
CTTGGTGCTCAGGTGCCAGATGCAAAGAAAGCATGTACCTACATCAGATCTAACCTTGAT
CCCAGCAATGTGGATTCCCTCTTCTACGCTGCCCAGGCCAGCCAGGCCCTCTCAGGATGT
GAGATCTCTATTTCAAATGAGACCAAAGATCTGCTTCTGGCAGCTGTCAGTGAGGACTCA
TCAGTTACCCAGATCTACCATGCAGTTGCAGCTCTAAGTGGCTTTGGCCTTCCCTTGGCA
TCCCAAGAAGCACTCAGTGCCCTTACTGCTCGTCTCAGCAAGGAGGAGACTGTGCTGGCA
ACAGTCCAGGCTCTGCAGACAGCATCCCACCTGTCCCAGCAGGCTGACCTGAGGAGCATC
GTGGAGGAGATTGAGGACCTTGTTGCTCGCCTGGATGAACTCGGGGGCGTGTATCTCCAG
TTTGAAGAAGGACTGGAAACAACAGCGTTATTTGTGGCTGCCACCTACAAGCTCATGGAT
CATGTGGGGACTGAGCCATCCATTAAGGAGGATCAGGTCATCCAGCTGATGAACGCGATC
TTCAGCAAGAAGAACTTTGAGTCCCTCTCCGAAGCCTTCAGCGTGGCCTCTGCAGCTGCT
GTGCTCTCGCATAATCGCTACCACGTGCCAGTTGTGGTTGTGCCTGAGGGCTCTGCTTCC
GACACTCATGAACAGGCTATCTTGCGGTTGCAAGTCACCAATGTTCTGTCTCAGCCTCTG
ACTCAGGCCACTGTTAAACTAGAACATGCTAAATCTGTTGCTTCCAGAGCCACTGTCCTC
CAGAAGACATCCTTCACCCCTGTAGGGGATGTTTTTGAACTAAATTTCATGAACGTCAAA
TTTTCCAGTGGTTATTATGACTTCCTTGTCGAAGTTGAAGGTGACAACCGGTATATTGCA
AATACCGTAGAGCTCAGAGTCAAGATCTCCACTGAAGTTGGCATCACAAATGTTGATCTT
TCCACCGTGGATAAGGATCAGAGCATTGCACCCAAAACTACCCGGGTGACATACCCAGCC
AAAGCCAAGGGCACATTCATCGCAGACAGCCACCAGAACTTCGCCTTGTTCTTCCAGCTG
GTAGATGTGAACACTGGTGCTGAACTCACTCCTCACCAGACATTTGTCCGACTCCATAAC
CAGAAGACTGGCCAGGAAGTGGTGTTTGTTGCCGAGCCAGACAACAAGAACGTGTACAAG
TTTGAACTGGATACCTCTGAAAGAAAGATTGAATTTGACTCTGCCTCTGGCACCTACACT
CTCTACTTAATCATTGGAGATGCCACTTTGAAGAACCCAATCCTCTGGAATGTGGCTGAT
GTGGTCATCAAGTTCCCTGAGGAAGAAGCTCCCTCGACTGTCTTGTCCCAGAACCTTTTC
ACTCCAAAACAGGAAATTCAGCACCTGTTCCGCGAGCCTGAGAAGAGGCCCCCCACCGTG
GTGTCCAATACATTCACTGCCCTGATCCTCTCGCCGTTGCTTCTGCTCTTCGCTCTGTGG
ATCCGGATTGGTGCCAATGTCTCCAACTTCACTTTTGCTCCTAGCACGATTATATTTCAC
CTGGGACATGCTGCTATGCTGGGACTCATGTATGTCTACTGGACTCAGCTCAACATGTTC
CAGACCTTGAAGTACCTGGCCATCTTGGGCAGTGTGACGTTTCTGGCTGGCAATCGGATG
CTGGCCCAGCAGGCAGTCAAGAGAACAGCACATTAG
|
| Enzyme 5 GenBank Gene ID |
AJ237734  |
| Enzyme 5 GeneCard ID |
RPN2  |
| Enzyme 5 GenAtlas ID |
RPN2  |
| Enzyme 5 HGNC ID |
HGNC:10382  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
20q12-q13.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Crimaudo C, Hortsch M, Gausepohl H, Meyer DI: Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins. EMBO J. 1987 Jan;6(1):75-82. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed
]
- Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [PubMed
]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [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
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
7373 |
| Enzyme 6 Name |
Neutral amino acid transporter B(0) |
| Enzyme 6 Synonyms |
- ATB(0)
- Baboon M7 virus receptor
- RD114/simian type D retrovirus receptor
- Sodium-dependent neutral amino acid transporter type 2
- Solute carrier family 1 member 5
|
| Enzyme 6 Gene Name |
SLC1A5 |
| Enzyme 6 Protein Sequence |
>Neutral amino acid transporter B(0)
MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGSRDQVRRCLRANLLVLLTVV
AVVAGVALGLGVSGAGGALALGPERLSAFVFPGELLLRLLRMIILPLVVCSLIGGAASLD
PGALGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINASVGAAGSAENAPSKEV
LDSFLDLARNIFPSNLVSAAFRSYSTTYEERNITGTRVKVPVGQEVEGMNILGLVVFAIV
FGVALRKLGPEGELLIRFFNSFNEATMVLVSWIMWYAPVGIMFLVAGKIVEMEDVGLLFA
RLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLM
MKCVEENNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLSQQSLDFVKIITILVT
ATASSVGAAGIPAGGVLTLAIILEAVNLPVDHISLILAVDWLVDRSCTVLNVEGDALGAG
LLQNYVDRTESRSTEPELIQVKSELPLDPLPVPTEEGNPLLKHYRGPAGDATVASEKESV
M
|
| Enzyme 6 Number of Residues |
541 |
| Enzyme 6 Molecular Weight |
56597.6 |
| Enzyme 6 Theoretical pI |
5.14 |
| Enzyme 6 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 6 General Function |
Involved in sodium:dicarboxylate symporter activity |
| Enzyme 6 Specific Function |
Has a broad substrate specificity, a preference for zwitterionic amino acids, and a sodium-dependence. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated amino acids, anionic amino acids, and cationic amino acids. Act as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
- 53-73
99-119
133-153
225-245
266-286
306-326
336-356
377-397
399-419
426-446
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
4191556  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q15758  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
AAAT_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1626 bp
ATGGTGGCCGATCCTCCTCGAGACTCCAAGGGGCTCGCAGCGGCGGAGCCCACCGCCAAC
GGGGGCCTGGCGCTGGCCTCCATCGAGGACCAAGGCGCGGCAGCAGGCGGCTACTGCGGT
TCCCGGGACCAGGTGCGCCGCTGCCTTCGAGCCAACCTGCTTGTGCTGCTGACAGTGGTG
GCCGTGGTGGCCGGCGTGGCGCTGGGACTGGGGGTGTCGGGGGCCGGGGGTGCGCTGGCG
TTGGGCCCGGAGCGCTTGAGCGCCTTCGTCTTCCCGGGCGAGCTGCTGCTGCGTCTGCTG
CGGATGATCATCTTGCCGCTGGTGGTGTGCAGCTTGATAGGCGGCGCCGCCAGCCTGGAC
CCCGGCGCGCTCGGCCGTCTGGGCGCCTGGGCGCTGCTCTTTTTCCTGGTCACCACGCTG
CTGGCGTCGGCGCTCGGAGTGGGCTTGGCGCTGGCTCTGCAGCCGGGCGCCGCCTCCGCC
GCCATCAACGCCTCCGTGGGAGCCGCGGGCAGTGCCGAAAATGCCCCCAGCAAGGAGGTG
CTCGATTCGTTCCTGGATCTTGCGAGAAATATCTTCCCTTCCAACCTGGTGTCAGCAGCC
TTTCGCTCATACTCTACCACCTATGAAGAGAGGAATATCACCGGAACCAGGGTGAAGGTG
CCCGTGGGGCAGGAGGTGGAGGGGATGAACATCCTGGGCTTGGTAGTGTTTGCCATCGTC
TTTGGTGTGGCGCTGCGGAAGCTGGGGCCTGAAGGGGAGCTGCTTATCCGCTTCTTCAAC
TCCTTCAATGAGGCCACCATGGTTCTGGTCTCCTGGATCATGTGGTACGCCCCTGTGGGC
ATCATGTTCCTGGTGGCTGGCAAGATCGTGGAGATGGAGGATGTGGGTTTACTCTTTGCC
CGCCTTGGCAAGTACATTCTGTGCTGCCTGCTGGGTCACGCCATCCATGGGCTCCTGGTA
CTGCCCCTCATCTACTTCCTCTTCACCCGCAAAAACCCCTACCGCTTCCTGTGGGGCATC
GTGACGCCGCTGGCCACTGCCTTTGGGACCTCTTCCAGTTCCGCCACGCTGCCGCTGATG
ATGAAGTGCGTGGAGGAGAATAATGGCGTGGCCAAGCACATCAGCCGTTTCATCCTGCCC
ATCGGCGCCACCGTCAACATGGACGGTGCCGCGCTCTTCCAGTGCGTGGCCGCAGTGTTC
ATTGCACAGCTCAGCCAGCAGTCCTTGGACTTCGTAAAGATCATCACCATCCTGGTCACG
GCCACAGCGTCCAGCGTGGGGGCAGCGGGCATCCCTGCTGGAGGTGTCCTCACTCTGGCC
ATCATCCTCGAAGCAGTCAACCTCCCGGTCGACCATGTCTCCTTGATCCTGGCTGTGGGC
TGGCTAGCCGACCGGTCCTGTACCGTCCTCAATGTAGAAGGTGACGCTCTGGGGGCAGGA
CTCCTCCAAAATTACGTGGACCGTACGGAGTCGAGAAGCACAGAGCCTGAGTTGATACAA
GTGAAGAGTGAGCTGCCCCTGGGTCCGCTGCCAGTCCCCACTGAGGAAGGAAACCCCCTC
CTCAAACACTATCGGGGGCCCGCAGGGGATGCCACGGTCGCCTCTGAGAAGGAATCAGTC
ATGTAA
|
| Enzyme 6 GenBank Gene ID |
AF102826  |
| Enzyme 6 GeneCard ID |
SLC1A5  |
| Enzyme 6 GenAtlas ID |
SLC1A5  |
| Enzyme 6 HGNC ID |
HGNC:10943  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
19q13.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Kekuda R, Prasad PD, Fei YJ, Torres-Zamorano V, Sinha S, Yang-Feng TL, Leibach FH, Ganapathy V: Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line. J Biol Chem. 1996 Aug 2;271(31):18657-61. [PubMed
]
- Rasko JE, Battini JL, Gottschalk RJ, Mazo I, Miller AD: The RD114/simian type D retrovirus receptor is a neutral amino acid transporter. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2129-34. [PubMed
]
- Tailor CS, Nouri A, Zhao Y, Takeuchi Y, Kabat D: A sodium-dependent neutral-amino-acid transporter mediates infections of feline and baboon endogenous retroviruses and simian type D retroviruses. J Virol. 1999 May;73(5):4470-4. [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
]
- Tailor CS, Marin M, Nouri A, Kavanaugh MP, Kabat D: Truncated forms of the dual function human ASCT2 neutral amino acid transporter/retroviral receptor are translationally initiated at multiple alternative CUG and GUG codons. J Biol Chem. 2001 Jul 20;276(29):27221-30. Epub 2001 May 11. [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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
8287 |
| Enzyme 7 Name |
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A |
| Enzyme 7 Synonyms |
- Oligosaccharyl transferase subunit STT3A
- STT3-A
- B5
- Integral membrane protein 1
- Transmembrane protein TMC
|
| Enzyme 7 Gene Name |
STT3A |
| Enzyme 7 Protein Sequence |
>Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
MTKFGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFL
AEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLA
PLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTY
YMWIKAVKTGSICWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAY
CTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFR
SVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSY
YFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGI
GVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTS
EAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTI
LVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMV
RIGGSTDTGKHIKENDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGF
DRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT
|
| Enzyme 7 Number of Residues |
705 |
| Enzyme 7 Molecular Weight |
80528.8 |
| Enzyme 7 Theoretical pI |
8.17 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- oligosaccharyl transferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
|
|
| Enzyme 7 General Function |
Involved in oligosaccharyl transferase activity |
| Enzyme 7 Specific Function |
Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3A seems to be involved in complex substrate specificity |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
- 18-38
115-135
170-190
209-229
236-259
301-321
360-380
384-404
406-426
454-474
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
158261103  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P46977  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
STT3A_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2118 bp
ATGACTAAGTTTGGATTTTTGCGATTGTCCTATGAGAAGCAGGACACACTTTTGAAGCTT
CTCATTCTGTCAATGGCTGCTGTATTATCCTTCTCCACTCGTCTGTTTGCTGTCCTGAGA
TTTGAAAGTGTTATCCATGAGTTTGATCCGTACTTTAATTATCGGACTACCAGGTTCCTG
GCTGAGGAGGGGTTTTATAAATTCCATAACTGGTTTGATGACCGAGCCTGGTACCCTTTG
GGACGAATCATTGGAGGAACAATTTACCCAGGTTTAATGATCACCTCTGCTGCAATCTAC
CATGTACTCCATTTTTTCCACATCACCATCGACATTCGGAATGTCTGTGTGTTCCTGGCC
CCTCTCTTCTCCTCCTTCACCACCATCGTCACGTACCACCTTACCAAAGAGCTCAAGGAT
GCAGGGGCTGGGCTTCTTGCTGCTGCCATGATTGCTGTAGTTCCTGGATATATCTCCCGA
TCTGTGGCTGGCTCCTATGATAATGAAGGGATTGCCATCTTTTGCATGCTACTCACCTAC
TACATGTGGATCAAGGCAGTAAAGACTGGTTCCATCTGTTGGGCAGCTAAGTGTGCCCTT
GCTTATTTCTACATGGTCTCGTCATGGGGAGGTTATGTGTTCCTGATCAACTTAATTCCT
CTCCACGTCCTCGTGCTGATGCTCACAGGCCGTTTCTCTCACCGGATCTATGTGGCCTAC
TGTACTGTTTACTGCCTGGGCACTATACTTTCTATGCAGATCTCCTTTGTGGGTTTCCAG
CCTGTCCTTTCATCAGAGCACATGGCAGCCTTTGGGGTCTTTGGTCTCTGCCAGATCCAT
GCCTTTGTGGATTACCTGCGCAGCAAGTTGAATCCACAACAATTTGAAGTTCTTTTCCGG
AGCGTCATCTCTCTGGTAGGCTTTGTCCTTCTCACCGTGGGAGCTCTCCTCATGCTGACA
GGAAAAATATCTCCCTGGACGGGGCGTTTCTACTCACTGCTGGATCCCTCTTATGCTAAG
AACAACATCCCCATCATTGCTTCTGTGTCTGAGCATCAGCCCACAACCTGGTCCTCATAC
TATTTTGACCTGCAGCTCCTCGTCTTCATGTTTCCAGTTGGCCTCTATTACTGCTTTAGC
AACCTGTCTGATGCCCGGATTTTTATCATCATGTATGGTGTGACCAGCATGTACTTTTCA
GCTGTAATGGTGCGTCTAATGCTAGTGTTGGCACCTGTTATGTGCATTCTCTCTGGCATT
GGAGTCTCCCAGGTGCTGTCCACATACATGAAGAATCTGGACATAAGTCGTCCAGACAAG
AAGAGCAAGAAGCAACAGGATTCCACCTACCCTATTAAGAATGAAGTGGCAAGTGGGATG
ATACTGGTCATGGCTTTCTTTCTCATCACCTACACCTTTCATTCAACCTGGGTGACCAGT
GAGGCCTACTCTTCTCCGTCCATTGTACTATCTGCCCGTGGTGGGGATGGCAGTAGGATC
ATATTTGATGACTTCCGAGAAGCATATTATTGGCTTCGTCATAATACTCCAGAGGATGCG
AAGGTCATGTCCTGGTGGGATTATGGCTATCAGATTACAGCTATGGCAAACCGAACAATT
TTAGTGGACAATAACACATGGAATAATACCCATATTTCTCGAGTAGGGCAGGCAATGGCG
TCCACAGAGGAAAAAGCCTATGAGATCATGAGGGAGCTCGATGTCAGCTATGTGCTGGTC
ATTTTTGGAGGCCTCACTGGGTATTCCTCTGATGATATCAACAAGTTTCTTTGGATGGTC
CGGATTGGAGGGAGCACAGATACAGGCAAACATATCAAGGAGAATGACTATTATACTCCA
ACTGGGGAGTTCCGTGTGGACCGTGAAGGTTCTCCAGTGCTGCTCAACTGCCTCATGTAC
AAGATGTGTTACTATCGCTTTGGACAGGTTTACACAGAAGCCAAGCGTCCTCCAGGCTTT
GACCGTGTCCGAAATGCTGAGATTGGGAATAAAGACTTTGAGCTTGATGTCCTGGAGGAA
GCATATACCACAGAACATTGGCTGGTCAGGATATACAAGGTAAAGGACCTGGATAATCGA
GGCTTGTCAAGGACATAA
|
| Enzyme 7 GenBank Gene ID |
AK290040  |
| Enzyme 7 GeneCard ID |
STT3A  |
| Enzyme 7 GenAtlas ID |
STT3A  |
| Enzyme 7 HGNC ID |
HGNC:6172  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
11q23.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Hong G, Deleersnijder W, Kozak CA, Van Marck E, Tylzanowski P, Merregaert J: Molecular cloning of a highly conserved mouse and human integral membrane protein (Itm1) and genetic mapping to mouse chromosome 9. Genomics. 1996 Feb 1;31(3):295-300. [PubMed
]
- Lissy NA, Bellacosa A, Sonoda G, Miller PD, Jhanwar SC, Testa JR: Isolation, characterization, and mapping to human chromosome 11q24-25 of a cDNA encoding a highly conserved putative transmembrane protein, TMC. Biochim Biophys Acta. 1996 May 2;1306(2-3):137-41. [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
]
- Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed
]
- Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
8562 |
| Enzyme 8 Name |
Sodium-coupled neutral amino acid transporter 3 |
| Enzyme 8 Synonyms |
- N-system amino acid transporter 1
- Na(+)-coupled neutral amino acid transporter 3
- Solute carrier family 38 member 3
- System N amino acid transporter 1
|
| Enzyme 8 Gene Name |
SLC38A3 |
| Enzyme 8 Protein Sequence |
>Sodium-coupled neutral amino acid transporter 3
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
|
| Enzyme 8 Number of Residues |
504 |
| Enzyme 8 Molecular Weight |
55772.4 |
| Enzyme 8 Theoretical pI |
8.01 |
| Enzyme 8 GO Classification |
Not Available |
| Enzyme 8 General Function |
Amino acid transport and metabolism |
| Enzyme 8 Specific Function |
Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
- 83-103
106-126
144-164
187-207
213-233
324-344
366-386
408-428
431-451
471-491
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
5870893  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q99624  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
S38A3_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1515 bp
ATGGAGGCGCCTTTGCAGACAGAGATGGTGGAGCTGGTGCCCAATGGCAAACACTCAGAG
GGGCTGCTCCCGGTCATCACCCCCATGGCAGGCAACCAGAGGGTCGAGGACCCTGCACGG
AGCTGTATGGAGGGCAAGAGCTTCCTACAGAAAAGTCCCAGCAAGGAGCCACACTTCACT
GACTTCGAGGGGAAGACATCATTCGGGATGTCAGTGTTCAACCTCAGCAATGCCATCATG
GGCAGCGGCATCCTGGGACTCGCCTATGCCATGGCCAATACGGGCATTATCCTTTTCCTG
TTCCTGTTGACAGCTGTCGCCTTGCTCTCCAGCTACTCCATCCACCTGCTACTCAAGTCC
TCAGGGGTCGTGGGCATCCGTGCCTATGAGCAGCTGGGCTACCGTGCCTTTGGGACCCCA
GGAAAGCTGGCAGCAGCCCTGGCCATCACGCTCCAGAACATCGGAGCCATGTCCAGCTAC
CTGTACATCATCAAGTCTGAGCTGCCACTTGTCATACAGACCTTCCTGAACCTGGAGGAG
AAAACCTCGGACTGGTACATGAACGGGAACTACCTGGTAATCCTTGTCTCTGTCACCATC
ATTCTGCCCCTGGCACTGATGCGGCAGCTTGGCTACCTGGGCTACTCCAGCGGCTTCTCT
CTTAGCTGCATGGTGTTCTTCCTAATTGCAGTCATCTACAAAAAGTTCCACGTGCCCTGC
CCACTGCCCCCCAACTTCAACAACACCACAGGCAACTTCAGCCACGTGGAGATCGTGAAG
GAGAAGGTGCAGCTGCAGGTCGAGCCTGAGGCTTCAGCCTTCTGCACTCCCAGCTACTTC
ACGCTCAACTCACAGACAGCATACACCATCCCCATCATGGCCTTCGCCTTCGTCTGCCAC
CCCGAGGTGCTGCCCATCTATACTGAGCTCAAGGACCCCTCCAAGAAGAAGATGCAGCAC
ATCTCCAACCTGTCCATCGCTGTCATGTACATCATGTACTTCCTGGCTGCCCTCTTCGGC
TACCTCACCTTCTACAACGGGGTGGAGTCGGAGCTGCTGCACACCTACAGCAAGGTGGAC
CCGTTTGACGTCCTGATCCTGTGTGTGCGCGTGGCCGTGCTGACAGCAGTCACGCTCACA
GTGCCCATCGTTCTGTTCCCGGTGCGCCGCGCCATCCAGCAGATGCTGTTTCCAAACCAG
GAGTTCAGCTGGCTGCGGCATGTGCTTATTGCCGTTGGCCTGCTCACTTGTATCAACCTG
CTGGTCATCTTTGCCCCCAACATCCTGGGCATCTTTGGGGTCATCGGTGCCACATCTGCC
CCATTCCTCATCTTCATCTTCCCTGCCATCTTCTACTTCCGAATCATGCCCACGGAGAAG
GAGCCTGCAAGATCCACCCCCAAAATCCTGGCCCTGTGTTTTGCTATGCTTGGCTTCTTG
CTGATGACCATGAGCTTGAGCTTCATCATCATTGACTGGGCCTCAGGGACCAGCCGGCAT
GGAGGAAACCACTAG
|
| Enzyme 8 GenBank Gene ID |
NM_006841.4  |
| Enzyme 8 GeneCard ID |
SLC38A3  |
| Enzyme 8 GenAtlas ID |
SLC38A3  |
| Enzyme 8 HGNC ID |
HGNC:18044  |
| Enzyme 8 Chromosome Location |
3 |
| Enzyme 8 Locus |
3p21.3 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Fei YJ, Sugawara M, Nakanishi T, Huang W, Wang H, Prasad PD, Leibach FH, Ganapathy V: Primary structure, genomic organization, and functional and electrogenic characteristics of human system N 1, a Na+- and H+-coupled glutamine transporter. J Biol Chem. 2000 Aug 4;275(31):23707-17. [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
]
- 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
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, 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, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [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
]
- Lerman MI, Minna JD: The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium. Cancer Res. 2000 Nov 1;60(21):6116-33. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
8843 |
| Enzyme 9 Name |
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 |
| Enzyme 9 Synonyms |
- Oligosaccharyl transferase subunit DAD1
- Defender against cell death 1
- DAD-1
|
| Enzyme 9 Gene Name |
DAD1 |
| Enzyme 9 Protein Sequence |
>Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
MSASVVSVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGF
ISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG
|
| Enzyme 9 Number of Residues |
113 |
| Enzyme 9 Molecular Weight |
12496.5 |
| Enzyme 9 Theoretical pI |
7.17 |
| Enzyme 9 GO Classification |
Not Available |
| Enzyme 9 General Function |
Involved in dolichyl-diphosphooligosaccharide-protein g |
| Enzyme 9 Specific Function |
Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
29501770  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P61803  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
DAD1_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>342 bp
ATGTCGGCGTCGGTAGTGTCTGTCATTTCGCGGTTCTTAGAAGAGTACTTGAGCTCCACT
CCGCAGCGTCTGAAGTTGCTGGACGCGTACCTGCTGTATATACTGCTGACCGGGGCGCTG
CAGTTCGGTTACTGTCTCCTCGTGGGGACCTTCCCCTTCAACTCTTTTCTCTCGGGCTTC
ATCTCTTGTGTGGGGAGTTTCATCCTAGCGGTTTGCCTGAGAATACAGATCAACCCACAG
AACAAAGCGGATTTCCAAGGCATCTCCCCAGAGCGAGCCTTTGCTGATTTTCTCTTTGCC
AGCACCATCCTGCACCTTGTTGTCATGAACTTTGTTGGCTGA
|
| Enzyme 9 GenBank Gene ID |
AY259117  |
| Enzyme 9 GeneCard ID |
DAD1  |
| Enzyme 9 GenAtlas ID |
DAD1  |
| Enzyme 9 HGNC ID |
HGNC:2664  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
14q11.2 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Nakashima T, Sekiguchi T, Kuraoka A, Fukushima K, Shibata Y, Komiyama S, Nishimoto T: Molecular cloning of a human cDNA encoding a novel protein, DAD1, whose defect causes apoptotic cell death in hamster BHK21 cells. Mol Cell Biol. 1993 Oct;13(10):6367-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
8930 |
| Enzyme 10 Name |
L-asparaginase |
| Enzyme 10 Synonyms |
- Asparaginase-like protein 1
- L-asparagine amidohydrolase
|
| Enzyme 10 Gene Name |
ASRGL1 |
| Enzyme 10 Protein Sequence |
>L-asparaginase
MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPE
FNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQ
GAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNV
AYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQ
GKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPD
DTTITDLP
|
| Enzyme 10 Number of Residues |
308 |
| Enzyme 10 Molecular Weight |
32054.3 |
| Enzyme 10 Theoretical pI |
6.17 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in hydrolase activity |
| Enzyme 10 Specific Function |
Acts in asparagine catabolism. May be involved in astroglial production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- L-asparagine + H2O = L-aspartate + NH3 [RN:R00485]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
20799290  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q7L266  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
ASGL1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>927 bp
ATGAATCCCATCGTAGTGGTCCACGGCGGCGGAGCCGGTCCCATCTCCAAGGATCGGAAG
GAGCGAGTGCACCAGGGCATGGTCAGAGCCGCCACCGTGGGCTACGGCATCCTCCGGGAG
GGCGGGAGCGCCGTGGATGCCGTAGAGGGAGCTGTCGTCGCCCTGGAAGACGATCCCGAG
TTCAACGCAGGTTGTGGGTCTGTCTTGAACACAAATGGTGAGGTTGAAATGGATGCTAGT
ATCATGGATGGAAAAGACCTGTCTGCAGGAGCAGTGTCCGCAGTCCAGTGTATAGCAAAT
CCCATTAAACTTGCTCGGCTTGTCATGGAAAAGACACCTCATTGCTTTCTGACTGACCAA
GGCGCAGCGCAGTTTGCAGCAGCTATGGGGGTTCCAGAGATTCCTGGAGAAAAACTGGTG
ACAGAGAGAAACAAAAAGCGCCTGGAAAAAGAGAAGCATGAAAAAGGTGCTCAGAAAACA
GATTGTCAAAAAAACTTGGGAACCGTGGGTGCTGTTGCCTTGGACTGCAAAGGGAATGTA
ACCTACGCAACCTCCACAGGCGGTATCGTTAATAAAATGGTCGGCCGCGTTGGGGACTCA
CCGTGTCTAGGAGCTGGAGGTTATGCCGACAATGACATCGGAGCCGTCTCAACCACAGGG
CATGGGGAAAGCATCCTGAAGGTGAACCTGGCTAGACTCACCCTGTTCCACATAGAACAA
GGAAAGACGGTAGAAGAGGCTGCGGACCTATCGTTGGGTTATATGAAGTCAAGGGTTAAA
GGTTTAGGTGGCCTCATCGTGGTTAGCAAAACAGGAGACTGGGTGGCAAAGTGGACCTCC
ACCTCCATGCCCTGGGCAGCCGCCAAGGACGGCAAGCTGCACTTTGGAATTGATCCTGAC
GATACTACTATCACCGACCTTCCCTAA
|
| Enzyme 10 GenBank Gene ID |
AF411076  |
| Enzyme 10 GeneCard ID |
ASRGL1  |
| Enzyme 10 GenAtlas ID |
ASRGL1  |
| Enzyme 10 HGNC ID |
HGNC:16448  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
11q12.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Bush LA, Herr JC, Wolkowicz M, Sherman NE, Shore A, Flickinger CJ: A novel asparaginase-like protein is a sperm autoantigen in rats. Mol Reprod Dev. 2002 Jun;62(2):233-47. [PubMed
]
- Evtimova V, Zeillinger R, Kaul S, Weidle UH: Identification of CRASH, a gene deregulated in gynecological tumors. Int J Oncol. 2004 Jan;24(1):33-41. [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
]
- 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 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
12876 |
| Enzyme 11 Name |
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B |
| Enzyme 11 Synonyms |
- Oligosaccharyl transferase subunit STT3B
- STT3-B
- Source of immunodominant MHC-associated peptides homolog
|
| Enzyme 11 Gene Name |
STT3B |
| Enzyme 11 Protein Sequence |
>Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
MAEPSAPESKHKSSLNSSPWSGLMALGNSRHGHHGPGAQCAHKAAGGAAPPKPAPAGLSG
GLSQPAGWQSLLSFTILFLAWLAGFSSRLFAVIRFESIIHEFDPWFNYRSTHHLASHGFY
EFLNWFDERAWYPLGRIVGGTVYPGLMITAGLIHWILNTLNITVHIRDVCVFLAPTFSGL
TSISTFLLTRELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWVKS
VKTGSVFWTMCCCLSYFYMVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIAYSTFYIV
GLILSMQIPFVGFQPIRTSEHMAAAGVFALLQAYAFLQYLRDRLTKQEFQTLFFLGVSLA
AGAVFLSVIYLTYTGYIAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWVSFFFDLHI
LVCTFPAGLWFCIKNINDERVFVALYAISAVYFAGVMVRLMLTLTPVVCMLSAIAFSNVF
EHYLGDDMKRENPPVEDSSDEDDKRNQGNLYDKAGKVRKHATEQEKTEEGLGPNIKSIVT
MLMLMLLMMFAVHCTWVTSNAYSSPSVVLASYNHDGTRNILDDFREAYFWLRQNTDEHAR
VMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNETAAYKIMRTLDVDYVLVI
FGGVIGYSGDDINKFLWMVRIAEGEHPKDIRESDYFTPQGEFRVDKAGSPTLLNCLMYKM
SYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRET
LDHKPRVTNIFPKQKYLSKKTTKRKRGYIKNKLVFKKGKKISKKTV
|
| Enzyme 11 Number of Residues |
826 |
| Enzyme 11 Molecular Weight |
93673.5 |
| Enzyme 11 Theoretical pI |
9.17 |
| Enzyme 11 GO Classification |
| Function |
- catalytic activity
- oligosaccharyl transferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
|
|
| Enzyme 11 General Function |
Involved in oligosaccharyl transferase activity |
| Enzyme 11 Specific Function |
Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3B seems to be involved in complex substrate specificity |
| Enzyme 11 Pathways |
- Glycan structures - biosynthesis 1 (map01030
)
- N-Glycan biosynthesis (map00510
)
|
| Enzyme 11 Reactions |
- dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
- 65-85
137-157
169-189
192-212
243-259
263-283
292-312
320-340
351-371
411-431
441-461
464-484
538-558
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
30578410  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q8TCJ2  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
STT3B_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>2481 bp
ATGGCGGAGCCCTCGGCCCCGGAGAGCAAGCACAAGTCGTCCCTCAACTCGTCCCCGTGG
AGTGGCCTCATGGCCCTGGGAAACAGCCGGCACGGCCACCACGGGCCCGGGGCCCAGTGC
GCGCACAAGGCGGCGGGCGGCGCGGCGCCGCCGAAGCCGGCCCCGGCGGGGCTGTCCGGG
GGGCTGTCGCAGCCGGCTGGGTGGCAGTCGCTTCTCTCCTTCACCATCCTCTTCCTGGCC
TGGCTTGCCGGCTTCAGCTCGCGCCTCTTCGCCGTCATCCGCTTCGAAAGCATCATCCAC
GAGTTCGACCCGTGGTTTAACTATAGATCAACACATCATCTTGCATCTCATGGGTTCTAT
GAATTTTTAAATTGGTTTGATGAAAGAGCATGGTATCCACTAGGAAGAATAGTAGGTGGT
ACTGTTTACCCAGGGTTGATGATAACCGCTGGCCTTATTCATTGGATTTTAAATACATTG
AACATAACTGTTCACATAAGAGACGTATGTGTGTTCCTTGCACCAACTTTTAGCGGCCTT
ACATCTATATCTACTTTCCTGCTTACAAGAGAACTTTGGAACCAAGGAGCAGGACTTTTA
GCTGCTTGTTTTATTGCTATTGTACCAGGCTACATATCTCGGTCAGTAGCTGGATCCTTT
GATAATGAAGGCATTGCTATTTTTGCACTTCAGTTCACATACTATTTATGGGTAAAATCT
GTAAAAACTGGGTCAGTTTTTTGGACAATGTGCTGCTGCTTATCCTATTTCTATATGGTC
TCTGCTTGGGGTGGTTATGTATTTATCATCAATCTTATTCCACTGCATGTATTTGTGTTG
TTACTGATGCAGAGATACAGCAAAAGAGTCTACATAGCATATAGCACTTTCTACATTGTG
GGTTTAATATTATCAATGCAGATACCTTTTGTGGGATTCCAGCCAATCAGAACAAGTGAA
CACATGGCAGCTGCAGGTGTCTTTGCATTGCTGCAAGCTTATGCTTTCTTGCAGTATCTG
AGAGACCGATTAACAAAACAAGAGTTCCAGACCCTTTTCTTTTTGGGTGTATCACTAGCT
GCAGGTGCTGTGTTCCTTAGTGTCATCTATTTGACTTATACAGGTTACATTGCACCATGG
AGTGGCAGGTTTTATTCATTGTGGGATACTGGGTATGCAAAAATACACATTCCAATTATT
GCATCAGTGTCTGAGCATCAACCTACGACTTGGGTGTCTTTCTTCTTTGATCTACATATT
CTTGTATGTACCTTCCCAGCAGGCCTTTGGTTCTGCATCAAAAATATCAACGATGAAAGA
GTATTTGTTGCTCTATATGCAATCAGTGCTGTCTACTTTGCTGGAGTGATGGTGCGACTG
ATGTTGACTTTGACTCCAGTCGTGTGTATGCTGTCTGCAATTGCCTTTTCAAATGTTTTT
GAGCACTATTTGGGGGATGACATGAAAAGGGAAAATCCACCTGTGGAGGACAGCAGTGAT
GAGGATGACAAAAGAAACCAAGGAAATTTGTATGATAAGGCAGGTAAAGTGAGGAAACAT
GCAACTGAACAGGAAAAAACTGAAGAGGGATTAGGCCCTAATATAAAAAGCATTGTCACC
ATGTTGATGCTGATGCTATTGATGATGTTTGCTGTCCACTGTACCTGGGTCACAAGCAAT
GCCTACTCTAGTCCAAGTGTAGTCCTGGCCTCATACAATCATGATGGCACCAGGAATATC
TTAGATGATTTTAGAGAAGCTTACTTTTGGCTAAGGCAAAATACAGATGAACATGCACGA
GTAATGTCTTGGTGGGATTATGGCTATCAGATAGCTGGAATGGCTAATAGAACTACGTTG
GTGGATAATAACACCTGGAATAACAGCCACATAGCACTGGTGGGAAAAGCTATGTCTTCT
AATGAAACAGCAGCCTATAAAATCATGAGGACTCTAGATGTAGATTATGTTTTGGTTATT
TTTGGAGGGGTTATTGGCTATTCTGGTGATGATATCAACAAATTTCTCTGGATGGTTAGG
ATAGCTGAAGGAGAACATCCCAAAGACATTCGGGAAAGTGACTATTTTACCCCACAGGGA
GAATTCCGTGTAGACAAAGCAGGATCCCCTACTTTGTTGAATTGCCTTATGTATAAAATG
TCATACTACAGATTTGGAGAAATGCAGCTGGATTTTCGTACACCCCCAGGTTTTGACCGA
ACACGTAATGCTGAGATTGGAAATAAGGACATTAAATTCAAACATTTGGAAGAAGCCTTT
ACATCAGAACACTGGCTTGTTAGGATATATAAAGTAAAAGCACCTGATAACAGGGAGACA
TTAGATCACAAACCTCGAGTCACCAACATTTTCCCAAAACAGAAGTATTTGTCAAAGAAG
ACTACCAAAAGGAAGCGTGGCTACATTAAAAATAAGCTGGTTTTTAAGAAAGGCAAGAAA
ATATCTAAGAAGACTGTTTAA
|
| Enzyme 11 GenBank Gene ID |
NM_178862.1  |
| Enzyme 11 GeneCard ID |
STT3B  |
| Enzyme 11 GenAtlas ID |
STT3B  |
| Enzyme 11 HGNC ID |
HGNC:30611  |
| Enzyme 11 Chromosome Location |
3 |
| Enzyme 11 Locus |
3p23 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- McBride K, Baron C, Picard S, Martin S, Boismenu D, Bell A, Bergeron J, Perreault C: The model B6(dom1) minor histocompatibility antigen is encoded by a mouse homolog of the yeast STT3 gene. Immunogenetics. 2002 Nov;54(8):562-9. Epub 2002 Oct 2. [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
]
- Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed
]
- Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [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
]
- 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
]
- 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
]
- 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
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [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
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
12921 |
| Enzyme 12 Name |
60 kDa lysophospholipase |
| Enzyme 12 Synonyms |
- L-asparaginase
- L-asparagine amidohydrolase
- Platelet-activating factor acetylhydrolase
- PAF acetylhydrolase
|
| Enzyme 12 Gene Name |
ASPG |
| Enzyme 12 Protein Sequence |
>60 kDa lysophospholipase
MARAVGPERRLLAVYTGGTIGMRSELGVLVPGTGLAAILRTLPMFHDEEHARARGLSEDT
LVLPPASRNQRILYTVLECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMA
FAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQL
FRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSMEQDVGL
LRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCL
QGAVTTDYAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGLSLDVRKELLTKDLRGEM
TPPSVEERRPSLQGNTLGGGVSWLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQAL
VELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHP
GVIGLLREAGASLSTQELEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHV
AEAAGNLAVVAFLQSLEGAVGAQAPCP
|
| Enzyme 12 Number of Residues |
567 |
| Enzyme 12 Molecular Weight |
60287.7 |
| Enzyme 12 Theoretical pI |
5.59 |
| Enzyme 12 GO Classification |
| Function |
- asparaginase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in asparaginase activity |
| Enzyme 12 Specific Function |
Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
- L-asparagine + H2O = L-aspartate + NH3 [RN:R00485]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
122937331  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q86U10  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
LPP60_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1740 bp
ATGGCGCGCGCGGTGGGGCCCGAGCGGAGGCTGCTGGCCGTCTACACCGGCGGCACCATT
GGCATGCGGAGTGAGCTCGGCGTGCTTGTGCCCGGGACGGGCCTGGCTGCCATCCTGAGG
ACACTGCCCATGTTCCATGACGAGGAGCACGCCCGAGCCCGCGGCCTCTCTGAGGACACC
CTGGTGCTACCCCCGGCCAGCCGCAACCAGAGGATTCTCTACACCGTGCTGGAGTGCCAG
CCCCTCTTCGACTCCAGTGACATGACCATCGCTGAGTGGGTTTGCCTTGCCCAGACCATC
AAGAGGCACTACGAGCAGTACCACGGCTTTGTGGTCATCCACGGCACCGACACCATGGCC
TTTGCTGCCTCGATGCTGTCCTTCATGCTGGAGAACCTGCAGAAGACTGTCATCCTCACT
GGGGCCCAGGTGCCCATCCATGCCCTGTGGAGCGACGGCCGTGAGAACCTGCTGGGGGCA
CTGCTCATGGCTGGCCAGTATGTGATCCCAGAGGTCTGCCTTTTCTTCCAGAATCAGCTG
TTTCGGGGCAACCGGGCAACCAAGGTAGACGCTCGGAGGTTCGCAGCTTTCTGCTCCCCG
AACCTGCTGCCTCTGGCCACAGTGGGTGCTGACATCACAATCAACAGGGAGCTGGTGCGG
AAGGTGGACGGGAAGGCTGGGCTGGTGGTGCACAGCAGCATGGAGCAGGACGTGGGCCTG
CTGCGCCTCTACCCTGGGATCCCTGCCGCCCTGGTTCGGGCCTTCTTGCAGCCTCCCCTG
AAGGGCGTGGTCATGGAGACCTTCGGTTCAGGGAACGGACCCACCAAGCCCGACCTGCTG
CAGGAGCTGCGGGTGGCCACCGAGCGCGGCCTGGTCATCGTCAACTGTACCCACTGCCTC
CAGGGGGCTGTGACCACAGACTATGCAGCTGGCATGGCCATGGCGGGAGCCGGCGTCATC
TCAGGCTTCGACATGACATCGGAGGCCGCCCTGGCCAAGCTATCGTATGTGCTGGGCCAG
CCAGGGCTGAGCCTGGATGTCAGGAAGGAGCTGCTGACCAAGGACCTTCGGGGGGAGATG
ACGCCACCCTCGGTGGAAGAGCGCCGGCCCTCACTGCAGGGCAACACGCTGGGCGGTGGG
GTCTCCTGGCTCCTCAGTCTGAGCGGCAGCCAGGAGGCAGATGCCCTGCGGAATGCCCTG
GTGCCCAGCCTGGCCTGTGCTGCTGCCCACGCCGGTGACGTGGAGGCGCTGCAGGCGCTT
GTGGAGCTGGGCAGTGACCTGGGCCTGGTGGACTTTAACGGCCAAACCCCACTGCACGCG
GCCGCCCGGGGAGGCCACACAGAGGCAGTCACCATGCTGCTGCAGAGAGGTGTGGACGTG
AACACCCGGGACACGGATGGCTTCAGCCCGCTGCTGCTGGCCGTGCGGGGCAGGCATCCG
GGTGTCATTGGGTTGCTGCGGGAAGCCGGGGCCTCCCTGTCCACCCAGGAGCTGGAGGAA
GCAGGGACGGAGCTGTGCAGGCTGGCATACAGGGCCGACCTCGAAGGCCTGCAGGTGTGG
TGGCAGGCAGGGGCTGACCTGGGGCAGCCGGGCTATGACGGGCACAGCGCCCTGCACGTC
GCAGAGGCAGCCGGGAACCTGGCAGTGGTGGCCTTTCTACAGAGCCTGGAGGGTGCGGTT
GGTGCCCAGGCCCCATGCCCAGAGCCCTCATGTTTTCAGGAAGTGCTGCCTGGTGTCTAA
|
| Enzyme 12 GenBank Gene ID |
NM_001080464  |
| Enzyme 12 GeneCard ID |
ASPG  |
| Enzyme 12 GenAtlas ID |
ASPG  |
| Enzyme 12 HGNC ID |
HGNC:20123  |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
14q32.33 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [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 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
15083 |
| Enzyme 13 Name |
Probable asparaginyl-tRNA synthetase, mitochondrial |
| Enzyme 13 Synonyms |
- Asparagine--tRNA ligase
- AsnRS
|
| Enzyme 13 Gene Name |
NARS2 |
| Enzyme 13 Protein Sequence |
>Probable asparaginyl-tRNA synthetase, mitochondrial
MLGVRCLLRSVRFCSSAPFPKHKPSAKLSVRDALGAQNASGERIKIQGWIRSVRSQKEVL
FLHVNDGSSLESLQVVADSGLDSRELNFGSSVEVQGQLIKSPSKRQNVELKAEKIKVIGN
CDAKDFPIKYKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHT
PIITSNDSEGAGELFQLEPSGKLKVPEENFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGP
TFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELCHK
FIAPGQKDRLEHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCG
NIPVFVINYPLTLKPFYMRDNEDGPQHTVAAVDLLVPGVGELFGGGLREERYHFLEERLA
RSGLTEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPHSCLL
|
| Enzyme 13 Number of Residues |
477 |
| Enzyme 13 Molecular Weight |
54089.6 |
| Enzyme 13 Theoretical pI |
7.26 |
| Enzyme 13 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- asparagine-tRNA ligase activity
- aspartate-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- asparaginyl-tRNA aminoacylation
- aspartyl-tRNA aminoacylation
- 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
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 13 General Function |
Involved in nucleotide binding |
| Enzyme 13 Specific Function |
ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn) |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
- ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn [RN:R03648]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
39644781  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q96I59  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
SYNM_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1434 bp
ATGCTGGGGGTCCGCTGCCTGCTGCGGTCCGTGCGCTTCTGTTCCTCCGCCCCCTTCCCC
AAGCACAAACCTTCAGCCAAACTGAGCGTGCGGGACGCTCTCGGGGCTCAGAACGCGAGT
GGGGAGCGCATTAAGATCCAGGGATGGATTCGTTCTGTCCGATCCCAGAAGGAAGTCTTG
TTCCTGCATGTAAATGATGGGTCATCTTTGGAAAGCCTTCAGGTTGTTGCAGATTCAGGC
CTTGACAGTAGAGAATTAACTTTTGGGAGTTCTGTGGAAGTACAAGGGCAGCTGATAAAA
AGTCCATCCAAAAGGCAAAATGTGGAACTGAAGGCAGAAAAAATTAAAGTTATTGGAAAT
TGTGATGCCAAGGATTTCCCCATCAAATATAAAGAGAGGCATCCTCTGGAGTACCTGCGA
CAATATCCTCACTTTAGGTGTAGGACTAACGTTCTGGGTTCTATATTGAGGATTCGCAGT
GAAGCGACAGCTGCTATTCATTCTTTCTTTAAGGACAGTGGCTTTGTACATATTCATACT
CCAATAATCACATCCAATGACTCTGAGGGAGCTGGAGAACTTTTTCAACTTGAACCTTCA
GGCAAACTTAAGGTACCTGAGGAGAATTTCTTCAATGTTCCTGCTTTCTTAACTGTCTCA
GGACAACTTCATCTAGAAGTGATGTCAGGAGCTTTTACTCAAGTGTTTACCTTTGGTCCG
ACCTTCCGAGCTGAAAATTCTCAGAGCCGGAGGCACCTGGCAGAGTTTTATATGATAGAA
GCAGAGATTTCTTTTGTTGACAGCCTTCAAGATCTTATGCAGGTTATAGAGGAACTGTTC
AAGGCTACAACAATGATGGTTCTCTCAAAATGTCCTGAAGATGTTGAACTCTGTCACAAA
TTCATAGCACCTGGCCAAAAGGACAGATTAGAACATATGCTAAAAAACAACTTTTTAATC
ATTTCTTATACTGAAGCAGTGGAGATCTTAAAGCAAGCATCCCAGAACTTCACCTTTACC
CCAGAGTGGGGTGCTGACCTACGGACTGAACATGAAAAGTACCTGGTGAAGCACTGTGGC
AACATACCTGTCTTCGTTATTAATTATCCATTAACACTCAAGCCTTTCTACATGAGGGAT
AATGAAGATGGCCCTCAGCACACGGTTGCTGCTGTTGATCTTCTGGTTCCTGGAGTTGGG
GAACTCTTTGGAGGAGGCCTCAGAGAAGAACGATACCATTTCTTAGAGGAGCGCTTAGCC
AGATCGGGACTTACAGAAGTCTACCAATGGTATCTGGACCTTCGTCGATTTGGATCTGTG
CCACATGGAGGTTTTGGGATGGGATTTGAACGCTACCTGCAGTGCATCTTGGGTGTTGAC
AATATCAAAGATGTTATCCCTTTCCCAAGGTTTCCTCATTCATGCCTTTTATAG
|
| Enzyme 13 GenBank Gene ID |
BC007800  |
| Enzyme 13 GeneCard ID |
NARS2  |
| Enzyme 13 GenAtlas ID |
NARS2  |
| Enzyme 13 HGNC ID |
HGNC:26274  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
11q14.1 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- 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
]
- 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
]
- 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 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
16462 |
| Enzyme 14 Name |
cDNA FLJ34575 fis, clone KIDNE2008362, highly similar to Homo sapiens asparaginase like 1 (ASRGL1), mRNA |
| Enzyme 14 Synonyms |
- SubName: Asparaginase like 1, isoform CRA_a
- SubName: cDNA, FLJ93550, highly similar to Homo sapiens asparaginase like 1 (ASRGL1), mRNA
|
| Enzyme 14 Gene Name |
ASRGL1 |
| Enzyme 14 Protein Sequence |
>cDNA FLJ34575 fis, clone KIDNE2008362, highly similar to Homo sapiens asparaginase like 1 (ASRGL1), mRNA
MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPE
FNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQ
GAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNV
AYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQ
GKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPD
DTTITDLP
|
| Enzyme 14 Number of Residues |
308 |
| Enzyme 14 Molecular Weight |
32055 |
| Enzyme 14 Theoretical pI |
6.17 |
| Enzyme 14 GO Classification |
| Function |
- asparaginase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- cellular protein metabolism
- glycoprotein catabolism
- glycoprotein metabolism
- macromolecule metabolism
- metabolism
- physiological process
- protein metabolism
|
| Component |
| — |
|
| Enzyme 14 General Function |
Amino acid transport and metabolism |
| Enzyme 14 Specific Function |
Not Available |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
B2R7Q0  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
B2R7Q0_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
Not Available |
| Enzyme 14 GenBank Gene ID |
AK313069  |
| Enzyme 14 GeneCard ID |
B2R7Q0  |
| Enzyme 14 GenAtlas ID |
Not Available |
| Enzyme 14 HGNC ID |
Not Available |
| Enzyme 14 Chromosome Location |
11 |
| Enzyme 14 Locus |
11q12.3 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
Not Available |
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
17098 |
| Enzyme 15 Name |
Solute carrier family 38, member 3, isoform CRA_b |
| Enzyme 15 Synonyms |
- SubName: cDNA, FLJ94006, Homo sapiens solute carrier family 38, member 3 (SLC38A3), mRNA
|
| Enzyme 15 Gene Name |
SLC38A3 |
| Enzyme 15 Protein Sequence |
>Solute carrier family 38, member 3, isoform CRA_b
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
|
| Enzyme 15 Number of Residues |
504 |
| Enzyme 15 Molecular Weight |
55774 |
| Enzyme 15 Theoretical pI |
8.01 |
| Enzyme 15 GO Classification |
Not Available |
| Enzyme 15 General Function |
Amino acid transport and metabolism |
| Enzyme 15 Specific Function |
Not Available |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
Not Available |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
B2R8Q0  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
B2R8Q0_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
Not Available |
| Enzyme 15 GenBank Gene ID |
AK313461  |
| Enzyme 15 GeneCard ID |
B2R8Q0  |
| Enzyme 15 GenAtlas ID |
Not Available |
| Enzyme 15 HGNC ID |
Not Available |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
Not Available |
| Enzyme 15 Metabolite References |
Not Available |