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Bovine Metabolome Database



Showing metabocard for L-Asparagine (BMDB00168)

Legend: metabolite field enzyme field

Version 1.0
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:44
Accession Number BMDB00168
Common Name L-Asparagine
Description Asparagine (Asn) is one of the 20 most common natural amino acids on Earth. It has carboxamide as the side chain's functional group. It is considered a non-essential amino acid. Asparagine is not an essential amino acid, which means that it can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet. The precursor to asparagine is oxaloacetate. Oxaloacetate is converted to aspartate using a transaminase enzyme. The enzyme transfers the amino group from glutamate to oxaloacetate producing alpha-ketoglutarate and aspartate. The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. In the asparagine synthetase reaction, ATP is used to activate aspartate, forming beta-aspartyl-AMP. glutamine donates an ammonium group which reacts with beta-aspartyl-AMP to form asparagine and free AMP. Since the asparagine side chain can make efficient hydrogen bond interactions with the peptide backbone, asparagines are often found near the beginning and end of alpha-helices, and in turn motifs in beta sheets. Its role can be thought as "capping" the hydrogen bond interactions which would otherwise need to be satisfied by the polypeptide backbone. glutamines have an extra methylene group, have more conformational entropy and thus are less useful in this regard. Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains. A reaction between asparagine and reducing sugars or reactive carbonyls produces acrylamide (acrylic amide) in food when heated to sufficient temperature, i.e. baking. These occur primarily in baked goods such as french fries, potato chips, and roasted coffee. Asparagine was first isolated in 1806 from asparagus juice, in which it is abundant--hence its name--becoming the first amino acid to be isolated. The smell observed in the urine of some individuals after their consumption of asparagus is attributed to a byproduct of the metabolic breakdown of asparagine, asparagine-amino-succinic-acid monoamide. (However, some scientists disagree and implicate other substances in the smell, especially methanethiol). (http://en.wikipedia.org/wiki/Asparagine)
Synonyms
  1. (-)-Asparagine
  2. (S)-2,4-Diamino-4-oxobutanoate
  3. (S)-2,4-Diamino-4-oxobutanoic acid
  4. (S)-Asparagine
  5. 2-Aminosuccinamate
  6. 2-Aminosuccinamic acid
  7. Agedoite
  8. Altheine
  9. Asn
  10. Asparagine
  11. Asparagine acid
  12. Asparamide
  13. Aspartamate
  14. Aspartamic acid
  15. Aspartic acid amide
  16. Aspartic acid b-amide
  17. Aspartic acid beta amide
  18. B2,4-(S)-diamino-4-oxo-utanoate
  19. B2,4-(S)-diamino-4-oxo-utanoic acid
  20. Crystal VI
  21. L-2,4-Diamino-4-oxobutanoate
  22. L-2,4-Diamino-4-oxobutanoic acid
  23. L-Aspartamine
  24. L-b-Asparagine
  25. L-beta-Asparagine
  26. a-Aminosuccinamate
  27. a-Aminosuccinamic acid
  28. alpha Amminosuccinamate
  29. alpha Amminosuccinamic acid
  30. alpha-Aminosuccinamate
  31. alpha-Aminosuccinamic acid
  32. l-Asparagine
Chemical IUPAC Name 2,4-diamino-4-oxo-butanoic acid
Chemical Formula C4H8N2O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian_Metabolite
Species
  • primary amine; primary aliphatic amine (alkylamine); carboxylic acid; primary carboxylic acid amide; alpha-aminoacid
Biofunction
  • Essential amino acid; Component of Alanine and aspartate metabolism; Component of Aminoacyl-tRNA biosynthesis; Component of Nitrogen metabolism
Application
Source
  • Endogenous
Average Molecular Weight 132.118
Monoisotopic Molecular Weight 132.053497
Isomeric SMILES N[C@@H](CC(N)=O)C(O)=O
Canonical SMILES NC(CC(N)=O)C(O)=O
KEGG Compound ID C00152 Link Image
BioCyc ID ASN Link Image
BiGG ID 34055 Link Image
Wikipedia Link Asn Link Image
METLIN ID 14 Link Image
PubChem Compound 6267 Link Image
PubChem Substance 3452 Link Image
ChEBI ID 17196 Link Image
CAS Registry Number 70-47-3
InChI Identifier InChI=1/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1
Synthesis Reference Wang, Fangda. Preparation of L-b-asparagine. Faming Zhuanli Shenqing Gongkai Shuomingshu (2005), 8 pp.
Melting Point (Experimental) 234-235 oC
Experimental Water Solubility 29.4 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 168.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -3.82 [CHMELIK,J ET AL. (1991)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.36 [Predicted by ALOGPS]; -4.4 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1POK Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
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Experimental 13C NMR Spectrum Download Spectrum
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Experimental 13C HSQC Spectrum Download Spectrum
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Predicted 1H NMR Spectrum Show Image
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Predicted 13C NMR Spectrum Show Image
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Mass Spectrum
Low Energy
Download File
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Medium Energy
Download File
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High Energy
Download File
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Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
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Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 25.6 uM
Age N/A
Sex Both
Condition Normal
Comments Not Available
References
Biofluid Breast_Milk
Value 2.275 +/- 0.05 uM
Age N/A
Sex N/A
Condition Normal
Comments 2% milk
References
Biofluid Breast_Milk
Value 2.2175 +/- 0.10 uM
Age N/A
Sex N/A
Condition Normal
Comments 1% milk
References
Biofluid Breast_Milk
Value 4 +/- 0.33 uM
Age N/A
Sex N/A
Condition Normal
Comments Skim milk
References
Biofluid Breast_Milk
Value 3.6 +/- 0.174 uM
Age N/A
Sex N/A
Condition Normal
Comments 3.25% milk
References
Concentrations (Abnormal) Not Available
Pathway Names
  • Alanine and aspartate metabolism
  • Nitrogen Metabolism
  • Transcription Translation
HMDB Pathways
Name Alanine and aspartate metabolism
Image Show Link Image
Name Nitrogen Metabolism
Image Show Link Image
Name Transcription Translation
Image Show Link Image
KEGG Pathways
Name Alanine and aspartate metabolism
Image Show Link Image
Name Nitrogen Metabolism
Image Show Link Image
SimCell Pathways
Name Alanine and aspartate metabolism
Image Show Link Image
Graph Show Link Image
SBML Download (XML) Link Image
Name Nitrogen Metabolism
Image Show Link Image
Graph
SBML
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Asparagine synthetase [glutamine-hydrolyzing]
  2. L-asparaginase
  3. Asparaginyl-tRNA synthetase, cytoplasmic
  4. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
  5. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
  6. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
  7. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
  8. Sodium-coupled neutral amino acid transporter 5
Enzyme 1 [top]
Enzyme 1 ID 563
Enzyme 1 Name Asparagine synthetase [glutamine-hydrolyzing]
Enzyme 1 Synonyms
  1. Glutamine-dependent asparagine synthetase
Enzyme 1 Gene Name ASNS
Enzyme 1 Protein Sequence >Asparagine synthetase [glutamine-hydrolyzing]
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDQLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKLQHHFEFEYQTKVDGEIILHLYDKGGIEQTVCMLDGV
FAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVNLKHSMTPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKHHHCRDEPLHALYDGVEKLFPGFEIETVKSNLRILFD
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVANHIGSEHHEVLFNSEEGIQVLDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPDMRVPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFRILQDYIEHQVDDAAMASAAQKFPINTPKTKEGYYYRQIFENHYPGRADWLPHYWMPR
WTNATDPSARTLTHYKAAAKA
Enzyme 1 Number of Residues 561
Enzyme 1 Molecular Weight 64219.1
Enzyme 1 Theoretical pI 6.77
Enzyme 1 GO Classification
Function
Process
Component
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate
Enzyme 1 Pathways
  • Amino-acid biosynthesis
  • L-asparagine biosynthesis
  • L- asparagine from L-aspartate (L-Gln route):step 1/1
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 94534952 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q1LZA3 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ASNS_BOVIN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1686 bp
ATGTGTGGCATTTGGGCGCTCTTTGGCAGCGATGACTGCCTTTCTGTTCAGTGTCTGAGT
GCTATGAAGATTGCACACAGGGGTCCGGATGCATTCCGTTTTGAAAATGTTAATGGGTAC
ACCAATTGCTGCTTTGGATTTCACCGGTTGGCGGTAGTTGACCAGCTGTTTGGAATGCAG
CCAATTCGAGTGAAGAAATATCCTTACTTGTGGCTCTGTTACAACGGTGAAATCTACAAC
CACAAGAAGCTGCAACACCATTTTGAATTTGAATACCAGACCAAAGTGGATGGTGAAATA
ATCCTTCATCTTTATGACAAAGGAGGAATTGAACAAACAGTTTGTATGTTGGATGGAGTA
TTTGCATTTATTTTACTGGATACTGCCAATAAGAAAGTGTTCTTGGGCAGAGATACCTAT
GGAGTGAGACCTTTGTTTAAAGCCATGACAGAAGATGGATTTTTGGCCGTGTGTTCAGAA
GCTAAAGGACTGGTTAACTTGAAGCACTCCATGACTCCTTTTTTAAAAGTGGAGCCTTTT
CTGCCAGGACATTATGAAGTTTTGGACCTAAAGCCAAATGGCAAAGTGGCGTCGGTGGAA
ATGGTGAAGCACCATCACTGTAGAGACGAGCCTCTGCATGCCCTGTATGACGGCGTGGAG
AAACTCTTCCCAGGTTTTGAGATAGAAACTGTGAAGAGCAACCTCCGGATTCTTTTTGAC
AATGCCGTTAAGAAACGTTTGATGACGGACAGAAGGATTGGCTGCCTTTTATCAGGTGGC
TTGGATTCCAGTTTGGTTGCTGCCACTCTGTTGAAGCAGCTAAAAGAGGCCCAAGTTCAG
TACCCTCTCCAGACATTTGCGATTGGCATGGAAGACAGTCCCGATTTACTAGCTGCTAGA
AAGGTGGCAAATCATATTGGGAGCGAACACCATGAAGTCCTCTTTAACTCTGAGGAAGGC
ATTCAGGTCCTGGATGAAGTCATATTTTCCTTGGAAACTTATGATATTACAACAGTCCGT
GCTTCAGTAGGTATGTACTTAATTTCTAAGTACATTCGGAAGAACACAGATAGCGTGGTG
ATCTTCTCTGGAGAAGGTTCAGATGAACTTACGCAGGGTTATATATATTTTCACAAGGCT
CCTTCCCCGGAGAAAGCTGAGGAGGAGAGTGAGCGGCTTCTAAGGGAACTCTACTTGTTT
GATGTTCTCCGAGCAGATCGAACTACTGCAGCCCATGGCCTTGAATTGAGAGTCCCTTTC
TTGGATCATCGCTTTTCTTCCTACTACTTGTCTCTGCCACCAGATATGAGAGTTCCCAAG
AATGGGATAGAAAAGCATCTCCTGAGAGAGACATTTGAGGACTCCAATCTGATACCTAAA
GAGATTCTCTGGCGACCAAAAGAAGCCTTCAGTGATGGAATAACCTCAGTTAAAAATTCC
TGGTTTAGGATTTTACAGGACTATATTGAACATCAGGTTGATGATGCAGCGATGGCAAGC
GCAGCCCAGAAATTTCCCATCAATACCCCCAAAACAAAAGAAGGCTATTACTACCGTCAG
ATCTTTGAAAACCACTACCCAGGCCGTGCCGACTGGCTGCCCCATTACTGGATGCCCAGG
TGGACCAACGCCACGGACCCTTCTGCCCGCACTCTGACCCATTACAAGGCCGCTGCCAAA
GCTTAG
Enzyme 1 GenBank Gene ID BC116123 Link Image
Enzyme 1 GeneCard ID ASNS Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Chromosome:7
Enzyme 1 Locus 7q21.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References Not Available
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 565
Enzyme 2 Name L-asparaginase
Enzyme 2 Synonyms
  1. L-asparagine amidohydrolase
  2. Asparaginase-like protein 1
Enzyme 2 Gene Name ASRGL1
Enzyme 2 Protein Sequence >L-asparaginase
MNPVVVVHGGGASNISKDRKERVRQGILRAATVGYNILKQGGSAVDAVEGAVTVLEDDPD
FNAGCGSVLNENGEVEMDASIMNGKDLSAGAVSAVRCIANPIKLARLVMDKTPHCFLTDQ
GAARFAAANGIPTIPGQQLVTERSRKRLEKEKLEKDAQKPDCQKNLGTVGAVALDCQGNL
AYATSTGGIVNKMPGRVGDTPCVGSGGYADNDIGAVSTTGHGESILKVNLARLALFHVEQ
GKSLEEAANASLGHMKSKVKGVGGIIMVNKAGEWAVKWTSTSMPWAAAKDGKLHSGIDFG
DTSIIDLS
Enzyme 2 Number of Residues 308
Enzyme 2 Molecular Weight 32050.2
Enzyme 2 Theoretical pI 7.47
Enzyme 2 GO Classification
Function
Process
Component
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 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 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 81673606 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q32LE5 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ASGL1_BOVIN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >927 bp
ATGAACCCCGTCGTCGTGGTCCACGGTGGCGGAGCCAGCAATATCTCCAAAGACCGGAAA
GAGCGGGTGCGCCAGGGCATCCTCAGAGCCGCCACCGTGGGTTACAACATCCTCAAGCAG
GGAGGGAGCGCCGTTGACGCGGTGGAAGGAGCCGTGACAGTGCTGGAAGACGATCCCGAC
TTCAACGCAGGTTGTGGATCTGTCTTGAACGAAAACGGGGAGGTTGAAATGGATGCCAGT
ATCATGAATGGGAAAGACCTGTCTGCAGGGGCGGTGTCTGCAGTCCGCTGTATCGCAAAT
CCCATTAAACTTGCACGGCTTGTTATGGACAAGACACCTCACTGCTTTCTGACTGACCAA
GGTGCAGCAAGATTTGCAGCAGCCAATGGGATTCCAACAATTCCTGGACAACAGCTGGTA
ACAGAAAGAAGCAGAAAACGCCTGGAAAAAGAAAAGCTTGAAAAAGATGCTCAGAAACCA
GACTGTCAGAAAAACTTGGGGACTGTGGGTGCTGTTGCCTTGGACTGCCAAGGAAACCTG
GCTTATGCAACCTCAACAGGGGGCATCGTCAACAAGATGCCGGGCCGCGTCGGGGACACG
CCGTGTGTAGGATCTGGAGGTTACGCTGACAATGACATCGGAGCTGTCTCAACGACAGGG
CACGGTGAGAGCATCCTGAAGGTGAATCTGGCCAGACTCGCGCTCTTCCACGTTGAACAG
GGAAAATCACTAGAAGAAGCTGCCAACGCATCACTGGGTCATATGAAGTCAAAGGTCAAG
GGCGTAGGTGGTATCATCATGGTCAACAAAGCAGGAGAGTGGGCGGTGAAGTGGACCTCC
ACATCCATGCCCTGGGCAGCGGCAAAGGATGGCAAGCTGCACTCGGGAATTGACTTCGGC
GACACGAGCATCATTGACCTGTCCTAA
Enzyme 2 GenBank Gene ID BC109621 Link Image
Enzyme 2 GeneCard ID ASRGL1 Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Chromosome:1
Enzyme 2 Locus 11q12.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 840
Enzyme 3 Name Asparaginyl-tRNA synthetase, cytoplasmic
Enzyme 3 Synonyms
  1. Asparagine--tRNA ligase
  2. AsnRS
Enzyme 3 Gene Name NARS
Enzyme 3 Protein Sequence >Asparaginyl-tRNA synthetase, cytoplasmic
MSLEVVRAAAGMVLAELYVSDREGNDVTGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQ
KENERWDVISKSQMKNIRKLWHREQMKSESREKKEAEDNLRREKNLEEAKKITIKNDPSL
PEPKCVKIRELKGYRGQRIKVFGWVHRLRRQGKNLMFLVLRDGTGFLQCVLSDDLCQCYN
GVVLSTESSVAVYGVLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQ
LNNRHMMIRGENMSKILKARSVITRCFRDHFFDRGYHEITPPTLVQTQVEGGATLFKLDY
FGEEAYLTQSSQLYLETCIPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFEE
LLNRLEDLVCDVVDRVLKSPAGNIVRDLNPNFKPPKRPFKRMNYSDAIVWLKEHNIKKED
GTFYEFGEDIPEAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNV
GEIVGGSMRIWDNEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILD
RYHIRDVCLYPRFVQRCKP
Enzyme 3 Number of Residues 559
Enzyme 3 Molecular Weight 64398.2
Enzyme 3 Theoretical pI 6.73
Enzyme 3 GO Classification
Function
Process
Component
Enzyme 3 General Function Translation, ribosomal structure and biogenesis
Enzyme 3 Specific Function ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 86823811 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q2KJG3 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SYNC_BOVIN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1680 bp
ATGTCCTTGGAGGTGGTCAGGGCGGCCGCAGGGATGGTGCTCGCAGAACTGTATGTCTCC
GACCGAGAGGGAAATGATGTTACTGGTGATGGAACCAAGGAGAAACCTTTTAAAACAGGC
CTTAAGGCTTTGATGACAGTTGGAAAAGAACCCTTTCCTACCATTTACGTAGATTCACAA
AAAGAAAATGAGAGGTGGGATGTTATTTCTAAGTCCCAGATGAAGAACATTAGGAAGCTG
TGGCACAGGGAGCAGATGAAGAGTGAGTCCCGGGAGAAGAAAGAGGCAGAAGACAATTTG
CGAAGAGAGAAGAACCTGGAAGAAGCAAAGAAGATTACCATTAAAAATGACCCAAGTCTT
CCAGAGCCGAAATGTGTGAAGATTCGGGAACTAAAAGGATACAGAGGCCAAAGGATAAAG
GTGTTTGGCTGGGTCCACAGGCTGCGTAGGCAAGGAAAGAATTTAATGTTTCTGGTGTTG
CGGGACGGTACGGGTTTTCTCCAGTGTGTCCTGTCAGATGATCTGTGTCAGTGTTACAAT
GGCGTTGTCTTGTCCACTGAGAGCAGTGTTGCAGTGTATGGAGTGCTGAATCTTACCCCA
AAGGGCAAGCAGGCTCCGGGGGGCCACGAGCTGAGCTGCGACTTCTGGGAGCTGATCGGG
TTGGCCCCCGCCGGAGGTGCTGACAACTTGATCAACGAGGAGTCCGACGTGGACGTCCAG
CTCAACAACAGACACATGATGATCCGCGGGGAGAACATGTCCAAAATCCTGAAGGCGCGC
TCCGTCATCACCAGGTGCTTCAGAGACCACTTCTTCGACAGGGGGTACCACGAAATCACT
CCTCCAACGTTGGTGCAAACACAGGTGGAAGGCGGCGCCACGCTCTTCAAGCTCGACTAT
TTTGGGGAAGAGGCGTATCTGACGCAGTCCTCTCAGCTCTACCTGGAGACCTGCATTCCA
GCTCTGGGGGACGTCTTTTGCATCGCACAGTCATACAGGGCAGAACAGTCCAGAACACGA
AGGCACCTGGCTGAATACACTCACGTGGAAGCCGAGTGTCCTTTCCTGACCTTCGAGGAG
CTCCTGAACCGCCTGGAGGACTTGGTGTGTGACGTGGTTGATAGAGTCCTGAAATCACCC
GCAGGAAACATAGTGCGCGACCTCAACCCGAATTTTAAGCCCCCTAAACGGCCTTTCAAA
CGGATGAACTATTCAGATGCGATTGTGTGGCTGAAAGAACACAATATAAAGAAAGAAGAC
GGAACTTTCTATGAATTTGGAGAGGACATCCCGGAAGCTCCAGAGAGACTGATGACGGAC
ACCATCAACGAGCCCATCTTGCTGTGTCGCTTTCCCGTGGAGATCAAGTCCTTCTACATG
CAGCGCTGTCCCGAGGACCCCCGGCTCACCGAATCTGTCGACGTGTTGATGCCCAATGTT
GGTGAGATCGTGGGTGGCTCCATGCGTATCTGGGATAATGAAGAGATCCTGGCAGGTTAC
AAAAGAGAAGGGATTGATCCCACTCCCTATTACTGGTACACGGATCAGAGAAAATATGGC
ACGTGTCCACATGGCGGCTATGGCCTGGGCTTGGAACGATTCTTAACCTGGATTCTGGAC
AGATACCACATCCGAGATGTGTGTTTGTACCCTCGGTTTGTCCAGCGCTGCAAGCCATGA
Enzyme 3 GenBank Gene ID BC105358 Link Image
Enzyme 3 GeneCard ID NARS Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Chromosome:1
Enzyme 3 Locus 18q21.2-q21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 841
Enzyme 4 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
Enzyme 4 Synonyms
  1. Oligosaccharyl transferase subunit DAD1
  2. Defender against cell death 1
  3. DAD-1
Enzyme 4 Gene Name DAD1
Enzyme 4 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
MSASVLSVISRFLEEYLSATPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGF
ISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG
Enzyme 4 Number of Residues 113
Enzyme 4 Molecular Weight 12494.6
Enzyme 4 Theoretical pI 7.17
Enzyme 4 GO Classification
Function
Process
Component
Enzyme 4 General Function Involved in dolichyl-diphosphooligosaccharide-protein g
Enzyme 4 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 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 31-51 53-73
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 59858361 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q5E9C2 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DAD1_BOVIN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >342 bp
ATGTCGGCGTCTGTGTTGTCGGTCATCTCGCGGTTTTTAGAAGAGTATTTGAGCGCCACA
CCTCAGCGTTTGAAGTTGTTGGACGCGTACCTCCTGTATATACTGCTGACTGGAGCGCTG
CAATTCGGTTATTGTCTCCTCGTGGGGACCTTCCCCTTCAACTCCTTCCTCTCGGGCTTC
ATCTCTTGTGTGGGGAGCTTCATCCTAGCGGTTTGTCTGAGAATACAGATCAACCCACAA
AACAAGGCGGATTTCCAAGGCATCTCCCCAGAGCGAGCCTTTGCTGATTTTCTCTTTGCC
AGCACCATCCTTCACCTTGTCGTCATGAACTTCGTTGGCTGA
Enzyme 4 GenBank Gene ID BT020998 Link Image
Enzyme 4 GeneCard ID DAD1 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Chromosome:1
Enzyme 4 Locus 14q11-q12
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 842
Enzyme 5 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Enzyme 5 Synonyms
  1. Oligosaccharyl transferase 48 kDa subunit
  2. DDOST 48 kDa subunit
Enzyme 5 Gene Name DDOST
Enzyme 5 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
MATRAARVWSGWWLLLLPLLGLAGASGPRTLVLLDNLNLRETHSLFFRSLKDRGFVLTFK
TADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFIDGGGSVLVAASSDIGDP
LRELGSECGIEFDEEKTAVIDHHNYDVSDLGQHTLIVADTENLLKAPTIVGKSSLNPILF
RGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVIF
SGSLDFFSDAFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVFKEEGVLRVGPVSHHRVG
ETAPPNAYTVTDLVEYSIVIEQLSDGKWVPFDGDDIQLEFVRIDPFVRTFLKRKGGKYSV
QFKLPDVYGVFQFKVDYNRLGYTHLYSSTQVSVRPLQHTQYERFIPSAYPYYASAFSMML
GLFIFSVVFLHMKEKEKSD
Enzyme 5 Number of Residues 439
Enzyme 5 Molecular Weight 48791.0
Enzyme 5 Theoretical pI 5.61
Enzyme 5 GO Classification
Function
Process
Component
Enzyme 5 General Function Involved in dolichyl-diphosphooligosaccharide-protein g
Enzyme 5 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 5 Pathways
  • Protein modification
  • protein glycosylation
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-26
Enzyme 5 Transmembrane Regions
  • 410-430
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 151555878 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A6QPY0 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name OST48_BOVIN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1320 bp
ATGGCGACCCGCGCGGCCCGTGTGTGGTCCGGCTGGTGGCTGCTGCTGCTGCCTTTGCTT
GGCCTGGCCGGCGCCAGCGGTCCCCGCACCTTGGTACTGCTGGACAACCTCAACCTCCGG
GAGACGCATTCGCTTTTCTTCCGGAGCCTGAAGGATCGCGGCTTTGTACTCACATTCAAG
ACCGCAGATGACCCCAGCCTGTCCCTCATTAAGTACGGGGAGTTTCTTTATGACAATCTC
ATCATTTTCTCCCCTTCGGTAGAAGATTTTGGAGGAAATATCAACGTGGAGACCATCAGT
GCCTTTATCGACGGTGGAGGCAGTGTCCTGGTGGCTGCCGGCTCAGACATCGGCGACCCT
CTCCGAGAGCTGGGCAGTGAGTGTGGGATTGAGTTCGACGAGGAGAAAACAGCTGTCATC
GATCATCACAACTATGACGTCTCAGACCTTGGCCAGCACACGCTCATCGTGGCCGACACA
GAGAACCTGCTGAAGGCCCCCACCATCGTTGGGAAATCATCTCTGAATCCCATCCTCTTT
CGGGGCGTGGGTATGGTGGCCGACCCTGACAATCCTTTGGTGCTGGACATCCTGACGGGC
TCTTCCACCTCTTACTCCTTCTTCCCGGATAAACCCATCACCCAGTACCCGCACGCCGTG
GGGAAGAACACCCTTCTCATCGCGGGGCTGCAGGCCCGGAACAACGCCCGGGTCATCTTC
AGCGGCTCCCTTGACTTCTTCAGCGATGCCTTCTTCAACTCAGCGGTGCAGAAGGCTGCA
CCCGGCTCCCAGAGGTATTCCCAGACTGGCAACTACGAGCTGGCTGTGGCCCTTTCCCGC
TGGGTGTTCAAGGAGGAGGGGGTCCTCCGGGTGGGGCCCGTGTCCCATCATCGGGTGGGC
GAGACAGCGCCACCCAACGCCTACACCGTCACTGACCTAGTGGAATACAGCATCGTCATT
GAACAGCTCTCAGATGGAAAGTGGGTCCCATTTGATGGCGATGACATTCAGCTGGAGTTT
GTCCGCATCGATCCTTTTGTGAGGACCTTCTTGAAGAGGAAAGGTGGCAAATACAGCGTC
CAGTTCAAGTTGCCTGATGTGTACGGTGTGTTCCAGTTCAAAGTGGATTACAACCGGCTA
GGCTACACGCACCTGTACTCCTCCACTCAGGTGTCCGTGCGGCCGCTGCAGCACACGCAG
TACGAGCGCTTCATCCCCTCGGCCTACCCCTACTACGCCAGCGCCTTCTCCATGATGCTC
GGGCTCTTCATCTTCAGCGTCGTCTTCCTGCACATGAAGGAGAAGGAGAAGTCCGACTGA
Enzyme 5 GenBank Gene ID BC149546 Link Image
Enzyme 5 GeneCard ID DDOST Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Chromosome:1
Enzyme 5 Locus 1p36.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 843
Enzyme 6 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
Enzyme 6 Synonyms
  1. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit
  2. Ribophorin-2
  3. Ribophorin II
  4. RPN-II
Enzyme 6 Gene Name RPN2
Enzyme 6 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
MALPGSSTVFLLALTIIASTQALTPTHYLTKHDVERLKASLDRPFTSLESAFYSIVGLSS
LGAQVPDVKKACTFIKSNLDPSNVDSLFYAAQSSQALSGCEISISNETKDLLLAAVSEDS
SVAQIYHAVAALSGFGLPLASQEALGALTARLSKEETVLATVQALQTASYLSQQADLRSI
VEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAI
FSKKNFESLSEAFSVASAAAALSENRYHVPVVVVPEGSPSYTQEQAILRLQVTNVLSQPL
TQATVKLEHAKSVASRATVLQKTSFTLIGDVFELNFMNVKFSSGYYDFSVKVEGDNRYIA
NTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQL
VDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDSKNVYKFELDTSERKLEFDSASGTYT
LYLIIGDATLKNPILWNVADVVIRFPEDDVPSTVLSKNIFTPKQEIQHLFREPEKRPPTV
VSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIVFHLGHAAMLGLMYVYWTQLNMF
QTLKYLAILGSVTFLAGNRMLAQQAIKRTAH
Enzyme 6 Number of Residues 631
Enzyme 6 Molecular Weight 69213.4
Enzyme 6 Theoretical pI 5.49
Enzyme 6 GO Classification
Function
Process
Component
Enzyme 6 General Function Involved in dolichyl-diphosphooligosaccharide-protein g
Enzyme 6 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 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-22
Enzyme 6 Transmembrane Regions
  • 541-561 572-592 597-617
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 146231756 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q3SZI6 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name RPN2_BOVIN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1896 bp
ATGGCGCTGCCGGGTTCAAGCACTGTCTTCCTGTTGGCCCTGACAATCATAGCCAGCACC
CAGGCTTTGACGCCTACTCACTACCTCACCAAGCATGACGTGGAGAGACTGAAAGCCTCT
CTGGACCGCCCTTTCACAAGTTTGGAGTCTGCTTTCTACTCCATCGTGGGACTCAGCAGC
CTTGGTGCCCAGGTGCCAGATGTAAAGAAAGCGTGCACCTTCATTAAATCAAACCTTGAT
CCCAGCAACGTGGATTCCCTTTTCTACGCCGCTCAGTCCAGCCAGGCCCTCTCAGGGTGT
GAGATCTCTATTTCAAATGAGACCAAAGACCTGCTACTGGCAGCTGTGAGCGAAGACTCT
TCGGTGGCCCAGATCTACCATGCAGTGGCAGCCCTCAGTGGCTTTGGCCTCCCCTTGGCT
TCCCAGGAAGCGCTCGGTGCCCTTACTGCCCGTCTCAGCAAGGAGGAGACCGTGCTAGCA
ACAGTCCAGGCTCTACAGACGGCCTCCTACCTGTCCCAGCAGGCTGACCTGAGAAGCATC
GTGGAGGAGATTGAGGACCTTGTTGCTCGCCTGGATGAACTGGGAGGTGTGTATCTCCAG
TTTGAAGAAGGACTGGAAACGACGGCATTGTTTGTGGCTGCCACCTACAAGCTTATGGAC
CATGTGGGGACGGAGCCATCCATTAAGGAGGATCAGGTCATCCAGCTCATGAACGCCATC
TTCAGCAAGAAGAACTTTGAGTCACTCTCTGAAGCCTTCAGTGTGGCCTCTGCTGCCGCT
GCGCTCTCTGAGAATCGCTACCATGTGCCCGTTGTGGTTGTGCCCGAGGGCTCTCCTTCC
TACACTCAGGAACAGGCTATCCTGCGGTTGCAGGTCACCAACGTTCTGTCCCAGCCTTTG
ACTCAGGCTACTGTTAAACTAGAACATGCGAAATCTGTTGCTTCCAGAGCTACAGTCCTT
CAGAAGACATCATTCACCCTCATCGGGGATGTTTTTGAGCTAAACTTCATGAATGTCAAA
TTTTCCAGTGGTTATTATGACTTCTCTGTCAAAGTTGAAGGTGACAACCGTTACATTGCA
AATACTGTAGAGCTCAGAGTCAAGATTTCCACTGAAGTTGGCATCACAAATGTCGATCTC
TCCACTGTGGATAAGGATCAGAGCATCGCCCCCAAAACAACACGGGTGACCTACCCAGCC
AAAGCCAAGGGCACATTCATTGCGGACAGCCACCAGAACTTTGCCTTATTCTTCCAGCTG
GTAGATGTGAACACTGGCGCTGAACTCACCCCTCACCAGACATTTGTCCGACTCCACAAC
CAGAAGACTGGCCAGGAAGTGGTGTTTGTTGCAGAGCCGGACAGCAAGAATGTGTACAAG
TTTGAACTGGACACCTCCGAGAGAAAGCTCGAATTTGACTCTGCATCTGGCACCTACACA
CTCTACTTGATCATCGGAGATGCAACTTTGAAGAACCCAATCCTGTGGAATGTGGCTGAT
GTGGTCATCAGGTTCCCTGAAGATGATGTTCCGTCAACTGTCCTGTCCAAGAACATTTTC
ACCCCCAAACAGGAAATTCAGCACCTGTTCCGCGAGCCTGAGAAGAGGCCCCCCACAGTG
GTGTCCAATACATTCACCGCGCTGATCCTCTCGCCCCTGCTCCTGCTCTTTGCTCTGTGG
ATCCGGATTGGTGCCAATGTCTCCAACTTCACTTTTGCTCCCAGCACAATTGTCTTTCAC
CTGGGACATGCTGCTATGCTGGGGCTCATGTATGTCTACTGGACACAACTCAACATGTTC
CAGACCCTGAAGTACCTGGCCATCTTAGGCAGCGTGACGTTTCTGGCTGGCAATCGGATG
CTGGCTCAGCAGGCAATCAAGAGAACAGCACATTAG
Enzyme 6 GenBank Gene ID BT030513 Link Image
Enzyme 6 GeneCard ID RPN2 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Chromosome:2
Enzyme 6 Locus 20q12-q13.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 844
Enzyme 7 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
Enzyme 7 Synonyms
  1. Oligosaccharyl transferase subunit STT3A
  2. STT3-A
Enzyme 7 Gene Name STT3A
Enzyme 7 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
MTKLGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFL
AEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLA
PLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTY
YMWIKAVKTGSIYWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAY
CTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFR
SVISLVGFVLLTIGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSY
YFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGI
GVSQVLSTYMKNLDISRQDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTS
EAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTI
LVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMV
RIGGSTDTGKHIKEHDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPLGY
DRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT
Enzyme 7 Number of Residues 705
Enzyme 7 Molecular Weight 80655.0
Enzyme 7 Theoretical pI 8.21
Enzyme 7 GO Classification
Function
Process
Component
Enzyme 7 General Function Involved in dolichyl-diphosphooligosaccharide-protein g
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 Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
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 86823970 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q2KJI2 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name STT3A_BOVIN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2118 bp
ATGACCAAGCTGGGATTTTTGCGGTTGTCCTATGAGAAGCAGGACACACTTCTGAAGCTT
CTGATTCTGTCGATGGCTGCTGTGTTATCATTCTCCACTCGTCTCTTTGCTGTCTTGAGA
TTTGAAAGTGTCATCCATGAATTTGATCCGTACTTTAATTATCGCACCACCCGGTTCCTG
GCTGAGGAGGGATTTTATAAATTCCATAACTGGTTTGATGACCGGGCCTGGTACCCCTTG
GGACGAATCATTGGAGGAACAATTTACCCAGGCTTAATGATCACTTCTGCTGCAATCTAC
CATGTCCTCCATTTTTTCCACATCACCATCGACATTCGGAATGTCTGTGTGTTCCTGGCC
CCTCTCTTCTCTTCCTTCACTACCATCGTCACGTACCACCTTACCAAAGAGCTCAAGGAT
GCAGGAGCTGGGCTTCTTGCTGCCGCCATGATTGCTGTGGTTCCTGGCTATATCTCCCGG
TCTGTGGCTGGCTCCTATGATAATGAAGGGATTGCCATCTTTTGCATGCTGCTTACCTAT
TACATGTGGATCAAAGCAGTCAAGACTGGTTCCATCTACTGGGCAGCAAAGTGTGCCCTT
GCTTACTTCTACATGGTCTCTTCCTGGGGAGGTTATGTGTTCTTGATCAACTTGATCCCT
CTTCATGTACTAGTGCTGATGCTCACGGGACGTTTCTCGCACCGGATCTACGTGGCGTAC
TGTACTGTCTACTGCCTGGGCACCATTCTTTCCATGCAGATCTCCTTTGTGGGTTTCCAG
CCCGTCCTTTCATCAGAGCACATGGCAGCCTTTGGGGTGTTTGGTCTCTGCCAGATTCAT
GCCTTTGTGGATTATCTACGCAGCAAGTTGAATCCACAGCAATTTGAAGTTCTTTTCCGA
AGTGTCATCTCCCTAGTGGGCTTTGTCCTTCTCACCATTGGAGCTCTCCTCATGCTGACA
GGAAAAATATCTCCCTGGACGGGGCGTTTCTACTCACTGTTGGACCCTTCCTATGCTAAG
AACAACATCCCCATCATCGCCTCCGTGTCTGAGCATCAGCCTACGACCTGGTCCTCGTAC
TATTTCGACCTACAGCTTCTTGTCTTCATGTTTCCAGTTGGTCTCTATTACTGCTTTAGC
AACCTGTCTGATGCCCGGATTTTCATCATCATGTATGGTGTGACCAGCATGTACTTTTCA
GCTGTAATGGTGCGTCTGATGCTGGTGTTGGCGCCTGTTATGTGCATTCTTTCTGGCATT
GGAGTCTCTCAGGTGCTGTCCACTTACATGAAGAATTTGGACATAAGTCGACAAGACAAG
AAGAGCAAGAAACAGCAGGATTCTACTTACCCTATTAAGAATGAAGTGGCAAGTGGCATG
ATACTGGTCATGGCTTTCTTTCTCATTACCTACACCTTCCACTCGACCTGGGTGACCAGT
GAGGCCTACTCTTCTCCCTCCATTGTGCTGTCTGCTCGTGGTGGAGATGGCAGTAGGATC
ATTTTTGATGATTTTCGAGAAGCGTACTATTGGCTTCGTCACAATACTCCAGAGGATGCG
AAGGTCATGTCATGGTGGGATTATGGCTACCAGATTACAGCTATGGCGAATCGGACAATT
TTAGTGGATAATAACACGTGGAATAATACCCATATATCTCGAGTAGGGCAGGCAATGGCA
TCCACAGAAGAAAAAGCCTATGAGATCATGAGGGAGCTTGATGTCAGCTATGTGCTGGTC
ATTTTTGGAGGCCTCACTGGGTATTCTTCAGATGACATCAACAAATTTCTGTGGATGGTC
CGGATTGGAGGGAGCACAGATACAGGGAAACACATCAAGGAGCACGATTATTATACTCCA
ACTGGGGAGTTTCGTGTGGACCGTGAGGGCTCTCCAGTGCTGCTCAACTGCCTTATGTAC
AAGATGTGTTACTACCGATTTGGACAGGTTTACACAGAAGCCAAGCGTCCACTAGGCTAT
GACCGTGTCCGGAATGCTGAGATTGGGAATAAAGACTTCGAGCTTGATGTCCTAGAAGAA
GCATACACCACAGAACATTGGCTGGTCAGGATATACAAGGTGAAGGACCTGGATAATCGA
GGCTTGTCAAGAACATAA
Enzyme 7 GenBank Gene ID BC105328 Link Image
Enzyme 7 GeneCard ID STT3A Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Chromosome:1
Enzyme 7 Locus 11q23.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 2092
Enzyme 8 Name Sodium-coupled neutral amino acid transporter 5
Enzyme 8 Synonyms
  1. System N transporter 2
  2. Solute carrier family 38 member 5
Enzyme 8 Gene Name SLC38A5
Enzyme 8 Protein Sequence >Sodium-coupled neutral amino acid transporter 5
MAISSAEGMELQDPKMNGALPGNAVEQEHEGFLPSHSPSPGRKPAQFMDFEGKTSFGMSV
FNLSNAIMGSGILGLAYAMAHTGILLFLALLLCIALLSSYSIHLLLTCAGVVGIRAYEQL
GQRALGPAGKVVVAAVICLHNVGAMSSYLFIIKSELPLVIATFLDMDPEGDWFLKGNLLI
IIVSVLIILPLALMRHLGYLGYTSGLSLTCMLFFLISVIYKKFQLGCTVGHNGTAVESKS
SPSLPIHGLNTSCEAQMFTADSQMFYTVPIMAFAFVCHPEVLPIYTELCRPSKRRMQAVA
NVSIGAMFCMYGLTATFGYLTFYSSVEAEMLHMYSQHDLLILCVRLAVLLAVTLTVPVVL
FPIRRALQQLLFPSKAFSWPRHVAIALILLVLVNVLVICVPTIRDIFGVIGSTSAPSLIF
ILPSIFYLRIVPSEVEPLYSWPKIQALCFGVLGVLFMAISLGFMFANWATGQSHVSGH
Enzyme 8 Number of Residues 478
Enzyme 8 Molecular Weight 51957.3
Enzyme 8 Theoretical pI 7.51
Enzyme 8 GO Classification
Function
Process
Component
Enzyme 8 General Function Amino acid transport and metabolism
Enzyme 8 Specific Function Functions as a sodium-dependent amino acid transporter which countertransport protons. Mediates the saturable, pH- sensitive, and electrogenic cotransport of several neutral amino acids including glycine, asparagine, alanine, serine, glutamine and histidine with sodium
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 58-80 94-114 132-152 173-193 199-219 264-284 302-322 341-361 383-403 406-426 446-466
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 59858047 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q5E9S9 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name S38A5_BOVIN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1437 bp
ATGGCCATCTCGTCTGCTGAGGGGATGGAACTGCAGGATCCAAAGATGAACGGAGCCCTC
CCTGGGAATGCTGTGGAGCAGGAGCATGAGGGCTTCCTGCCTAGCCATAGTCCTTCTCCT
GGGAGGAAACCGGCCCAGTTCATGGATTTCGAGGGGAAGACATCGTTTGGAATGTCAGTG
TTCAACCTCAGCAACGCCATCATGGGCAGCGGCATCCTGGGGCTGGCCTATGCCATGGCC
CACACGGGGATCCTCCTCTTCCTGGCTTTGTTGCTGTGCATCGCTCTTCTGTCTTCGTAC
TCCATCCATCTCCTGCTGACCTGTGCTGGTGTTGTAGGCATCCGAGCCTATGAACAGCTG
GGACAGAGGGCGCTGGGGCCTGCGGGGAAAGTAGTGGTGGCGGCGGTCATCTGTCTGCAC
AATGTTGGGGCCATGTCCAGTTACCTGTTCATCATCAAATCCGAACTTCCCCTGGTTATC
GCCACTTTCCTGGACATGGACCCTGAGGGGGACTGGTTCTTGAAGGGAAACCTCCTTATC
ATCATTGTCAGTGTTTTAATCATCCTGCCACTGGCCCTCATGAGACACTTGGGCTACCTG
GGGTATACCAGTGGTCTCTCTCTGACCTGTATGCTGTTTTTCCTCATTTCGGTCATCTAT
AAGAAGTTCCAGCTTGGCTGCACTGTAGGCCACAATGGAACAGCAGTGGAGAGCAAGAGC
TCCCCAAGCCTTCCCATCCATGGGCTCAACACAAGCTGTGAGGCCCAGATGTTCACAGCT
GACTCACAGATGTTCTACACAGTGCCCATTATGGCTTTTGCCTTTGTCTGCCACCCTGAA
GTGCTGCCCATCTACACAGAACTCTGCCGGCCCTCCAAGCGCAGAATGCAGGCTGTGGCC
AACGTGTCCATTGGGGCCATGTTCTGCATGTATGGGCTCACGGCGACCTTTGGATACCTC
ACCTTCTACAGCAGCGTGGAGGCGGAGATGCTGCACATGTACAGCCAGCATGACCTGCTC
ATCCTCTGTGTGCGTCTAGCGGTGCTGCTCGCTGTGACTCTCACGGTGCCAGTTGTGCTG
TTCCCTATCCGCCGGGCTCTGCAGCAGCTACTTTTTCCAAGCAAGGCCTTCAGCTGGCCA
CGCCATGTGGCCATAGCACTGATCCTGCTTGTCTTGGTCAATGTTCTTGTCATCTGTGTG
CCAACCATCCGGGATATCTTTGGGGTTATCGGGTCTACCTCAGCCCCCAGCCTCATTTTC
ATCCTTCCCAGCATCTTCTACCTCCGCATTGTGCCCTCTGAGGTGGAGCCCCTCTACTCC
TGGCCCAAGATCCAGGCTCTGTGTTTTGGTGTCTTGGGGGTCCTCTTCATGGCGATCAGC
CTAGGTTTCATGTTTGCCAACTGGGCCACAGGCCAGAGCCATGTATCTGGACACTGA
Enzyme 8 GenBank Gene ID BT020841 Link Image
Enzyme 8 GeneCard ID SLC38A5 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Xp11.23
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available