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Bovine Rumen Metabolome Database



Showing metabocard for D-Glucose (RMDB00122)

Legend: metabolite field enzyme field

Version 1.0
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-06 13:21:32
Accession Number RMDB00122
Common Name D-Glucose
Description Glucose is a monosaccharide containing six carbon atoms and an aldehyde group and is therefore referred to as an aldohexose. The glucose molecule can exist in an open-chain (acyclic) and ring (cyclic) form, the latter being the result of an intramolecular reaction between the aldehyde C atom and the C-5 hydroxyl group to form an intramolecular hemiacetal. In water solution both forms are in equilibrium and at pH 7 the cyclic one is the predominant. Glucose is a primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. In animals glucose arises from the breakdown of glycogen in a process known as glycogenolysis. Glucose is synthesized in the liver and kidneys from non-carbohydrate intermediates, such as pyruvate and glycerol, by a process known as gluconeogenesis.
Synonyms
  1. (+)-Glucose
  2. Anhydrous dextrose
  3. CPC hydrate
  4. Cerelose
  5. Cerelose 2001
  6. Clearsweet 95
  7. Clintose L
  8. Corn sugar
  9. D(+)-Glucose
  10. Dextropur
  11. Dextrose
  12. Dextrosol
  13. Glucodin
  14. Glucolin
  15. Glucose
  16. Goldsugar
  17. Grape sugar
  18. Meritose
  19. Roferose ST
  20. Staleydex 111
  21. Staleydex 95M
  22. Tabfine 097(HS)
  23. Vadex
Chemical IUPAC Name (3R,4R,5S,6S)-6-(hydroxymethyl)oxane-2,3,4,5-tetrol
Chemical Formula C6H12O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Monosaccharides
Family
  • Mammalian_Metabolite
Species
  • hemiacetal; primary alcohol; secondary alcohol; 1,2-diol; heterocyclic compound
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 180.156
Monoisotopic Molecular Weight 180.063385
Isomeric SMILES OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O
Canonical SMILES OCC1OC(O)C(O)C(O)C1O
KEGG Compound ID C00031 Link Image
BioCyc ID GLC Link Image
BiGG ID 33582 Link Image
Wikipedia Link Dextrose Link Image
METLIN ID 133 Link Image
PubChem Compound 5793 Link Image
PubChem Substance 833240 Link Image
ChEBI ID 17634 Link Image
CAS Registry Number 50-99-7
InChI Identifier InChI=1/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6u/m1/s1
Synthesis Reference Li, Dalin; Ruan, Yi; Song, Wen; Wang, Yongjun. Improved process for producing glucose. Faming Zhuanli Shenqing Gongkai Shuomingshu (2003), 4 pp
Melting Point (Experimental) 146-150 oC
Experimental Water Solubility 1200.0 mg/mL [MULLIN,JW (1972)] Source: PhysProp
Predicted Water Solubility 782.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -3.24 [SANGSTER (1994)] Source: PhysProp
Predicted LogP/Hydrophobicity -2.57 [Predicted by ALOGPS]; -2.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1A47 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • endoplasmic reticulum
  • Extracellular
  • golgi apparatus
  • lysosome
Biofluid Location
  • Cow_Milk
  • Rumen
Tissue Location
Concentrations (Normal)
Biofluid Rumen
Value 549.4+/- 97.5 uM
Age 4-5 years old
Sex Female (lactating)
Condition Normal (0% barley grain in dry matter (DM) basis)
Breed Holstein-Friesian
Experimental Condition Rumen fluid for the analysis was collected 15-20 minutes before the morning feeding on days 12 and 21 of each experimental period. Cows were fed once daily at 0800.
Comments Not Available
References
  • The rumen metabolome (in preparation)
Biofluid Rumen
Value 490.0 +/- 127.3 uM
Age N/A
Sex Female
Condition Normal
Breed Not Available
Experimental Condition Not Available
Comments Not Available
References
  • Metabolomics reveals unhealthy alterations in rumen metabolism with increased proportion of cereal grain in the diet of dairy cows. Burim N. Ametaj, Qendrim Zebeli, Fozia Saleem, Nikolaos Psychogios, Michael J. Lewis, Suzanna M. Dunn, Jianguo Xia and David S. Wishart Metabolomics 2010;6(4):583-594
Concentrations (Abnormal)
Biofluid Rumen
Value 523 +/- 130 uM
Age 4-5 years old
Sex Female (lactating)
Condition 15% barley grain in dry matter (DM) basis
Breed Holstein-Friesian
Experimental Condition Rumen fluid for the analysis was collected 15-20 minutes before the morning feeding on days 12 and 21 of each experimental period. Cows were fed once daily at 0800.
Comments Not Available
References
  • The rumen metabolome (in preparation)
Biofluid Rumen
Value 996 +/- 334 uM
Age 4-5 years old
Sex Female (lactating)
Condition 30% barley grain in dry matter (DM) basis
Breed Holstein-Friesian
Experimental Condition Rumen fluid for the analysis was collected 15-20 minutes before the morning feeding on days 12 and 21 of each experimental period. Cows were fed once daily at 0800.
Comments Not Available
References
  • The rumen metabolome (in preparation)
Biofluid Rumen
Value 1806 +/- 1305 uM
Age 4-5 years old
Sex Female (lactating)
Condition 45% barley grain in dry matter (DM) basis
Breed Holstein-Friesian
Experimental Condition Rumen fluid for the analysis was collected 15-20 minutes before the morning feeding on days 12 and 21 of each experimental period. Cows were fed once daily at 0800.
Comments Not Available
References
  • The rumen metabolome (in preparation)
Pathway Names Not Available
HMDB Pathways Not Available
KEGG Pathways Not Available
SimCell Pathways Not Available
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Glucosylceramidase
  2. Beta-1,4-galactosyltransferase 1
  3. Hexokinase-1
  4. Kininogen-2
  5. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
  6. Phosphatidylinositol 3-kinase regulatory subunit alpha
  7. AMP-activated protein kinase gamma subunit
  8. RAC-alpha serine/threonine-protein kinase
  9. Kininogen-1
Enzyme 1 [top]
Enzyme 1 ID 131
Enzyme 1 Name Glucosylceramidase
Enzyme 1 Synonyms
  1. Beta-glucocerebrosidase
  2. Acid beta-glucosidase
  3. D-glucosyl-N-acylsphingosine glucohydrolase
Enzyme 1 Gene Name GBA
Enzyme 1 Protein Sequence >Glucosylceramidase
MELSSPSREEYPMPRGRVGIMAASLMGLLLLHTVSWVSGARPCSPKSFGYSSVVCVCNGT
YCDSLDPLTLPDPGTFSRFESTRSGRRMELSLGTIQANRTGTGLLLTLQPDQKFQKVKGF
GGAMTDAAALNILALSPAARNLLLKSYFSEEGIEYNIIRVPMASCDFSIRTYTYDDSPDD
FQLLNFSLPEEDVKLKIPLIHQALELANRSVSLFASPWTSPTWLKTNGAVNGKGTLKGQA
GDLYHKTWARYFVKFLDAYAEHKLRFWAVTAENEPTAGLLTGYPFQCLGFTPEHQRDFIA
RDLGPILANSTHRDVRLLMLDDQRLLLPRWAQVVLADPEAAKYVHGIAVHWYLDFLAPAK
ATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMRYSHSIITNLLYHVVGWTDW
NLALNPEGGPNWVRNFVDSPIIVDIAKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASKK
SDLDTVALLRPDGSAVAVVLNRSSKDVPLTIKDPAVGFMETVSPGYSIHTYLWRRQ
Enzyme 1 Number of Residues 536
Enzyme 1 Molecular Weight 59854.0
Enzyme 1 Theoretical pI 8.08
Enzyme 1 GO Classification
Function
Process
Component
Enzyme 1 General Function Involved in cation binding
Enzyme 1 Specific Function D-glucosyl-N-acylsphingosine + H(2)O = D- glucose + N-acylsphingosine
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-39
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 86438386 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q2KHZ8 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GLCM_BOVIN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1611 bp
ATGGAGCTTTCAAGTCCTTCCAGAGAGGAGTATCCTATGCCTCGGGGCAGAGTAGGAATC
ATGGCTGCCAGCCTCATGGGATTACTTCTACTTCATACAGTGTCGTGGGTATCAGGTGCC
CGCCCCTGCAGCCCTAAAAGCTTTGGCTACAGCTCGGTGGTGTGTGTCTGCAATGGTACA
TACTGTGATTCTCTGGACCCCTTGACCCTGCCTGACCCTGGCACCTTCAGCCGCTTTGAG
AGCACTCGCAGCGGGCGCCGAATGGAGCTGAGTCTGGGGACCATCCAGGCCAATCGCACA
GGCACAGGGTTGCTGTTGACCTTGCAGCCAGATCAGAAATTCCAGAAAGTGAAGGGATTT
GGAGGGGCCATGACGGATGCTGCTGCCCTCAACATCCTTGCCCTGTCACCTGCTGCACGG
AATTTGCTACTCAAATCATACTTCTCCGAAGAAGGAATTGAATACAACATCATCCGGGTC
CCCATGGCCAGCTGTGACTTCTCCATCCGCACCTATACCTATGACGACAGCCCTGATGAC
TTCCAGCTGCTCAACTTCAGCCTTCCAGAGGAAGATGTCAAGCTCAAGATACCACTGATT
CACCAAGCTCTGGAGTTGGCCAACCGCTCTGTCTCACTCTTCGCCAGTCCCTGGACATCA
CCCACTTGGCTCAAGACTAATGGGGCTGTGAATGGGAAGGGAACACTCAAGGGTCAAGCA
GGGGATCTCTACCACAAGACCTGGGCCAGATACTTTGTCAAGTTCCTGGATGCCTACGCG
GAGCACAAGTTACGGTTCTGGGCAGTGACAGCCGAGAACGAGCCTACTGCAGGGCTCCTT
ACCGGGTACCCCTTCCAATGCTTGGGTTTCACTCCTGAGCACCAGCGAGACTTCATCGCC
CGTGACCTGGGTCCCATCCTCGCCAACAGCACACACCGCGACGTCCGACTGTTGATGCTG
GATGACCAGCGCTTACTGTTGCCTCGCTGGGCCCAGGTGGTGCTGGCAGACCCAGAAGCA
GCTAAGTATGTTCATGGCATTGCTGTACATTGGTACCTGGACTTCCTGGCTCCAGCAAAA
GCCACCCTGGGGGAGACGCACCGCCTGTTCCCCAACACCATGCTCTTTGCCTCAGAGGCC
TGTGTGGGCTCCAAGTTCTGGGAGCAGAGTGTGCGGCTGGGCTCCTGGGATCGAGGGATG
CGGTACAGCCACAGTATCATCACAAACCTCCTCTACCATGTGGTCGGCTGGACCGACTGG
AACCTCGCCCTAAATCCTGAAGGGGGACCCAACTGGGTGCGCAATTTTGTTGATAGCCCC
ATCATTGTGGATATCGCCAAGGACACATTTTACAAGCAGCCTATGTTTTACCACCTTGGC
CACTTCAGCAAGTTCATTCCTGAGGGCTCGCAGAGAGTGGGGCTGGTTGCCAGTAAGAAG
AGCGACTTGGACACGGTGGCACTGTTACGTCCTGACGGCTCTGCGGTTGCGGTCGTGCTG
AACCGCTCCTCTAAGGACGTGCCTCTCACCATCAAGGATCCCGCCGTGGGCTTCATGGAA
ACTGTCTCACCTGGCTACTCCATTCACACCTACCTGTGGCGTCGCCAGTGA
Enzyme 1 GenBank Gene ID BC112823 Link Image
Enzyme 1 GeneCard ID GBA Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Chromosome:1
Enzyme 1 Locus 1q21
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 604
Enzyme 2 Name Beta-1,4-galactosyltransferase 1
Enzyme 2 Synonyms
  1. Beta-1,4-GalTase 1
  2. Beta4Gal-T1
  3. b4Gal-T1
  4. UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1
  5. UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1
  6. Lactose synthase A protein
  7. N-acetyllactosamine synthase
  8. Nal synthetase
  9. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
  10. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
  11. Processed beta-1,4-galactosyltransferase 1
Enzyme 2 Gene Name B4GALT1
Enzyme 2 Protein Sequence >Beta-1,4-galactosyltransferase 1
MKFREPLLGGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLRRLPQLVGVHPPL
QGSSHGAAAIGQPSGELRLRGVAPPPPLQNSSKPRSRAPSNLDAYSHPGPGPGPGSNLTS
APVPSTTTRSLTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPH
KVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAKLLNVGFKEAL
KDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQ
FLSINGFPNNYWGWGGEDDDIYNRLAFRGMSVSRPNAVIGKCRMIRHSRDKKNEPNPQRF
DRIAHTKETMLSDGLNSLTYMVLEVQRYPLYTKITVDIGTPS
Enzyme 2 Number of Residues 402
Enzyme 2 Molecular Weight 44842.2
Enzyme 2 Theoretical pI 9.60
Enzyme 2 GO Classification
Function
Process
Component
Enzyme 2 General Function Involved in alpha-tubulin binding
Enzyme 2 Specific Function The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix
Enzyme 2 Pathways
  • Protein modification
  • protein glycosylation
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 25-44
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 382 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P08037 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name B4GT1_BOVIN Link Image
Enzyme 2 PDB ID 1FR8 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1209 bp
ATGAAGTTTCGGGAGCCGCTCCTGGGCGGCAGTGCCGCGATGCCGGGCGCGTCCCTGCAG
CGGGCCTGCCGCCTCCTCGTGGCTGTCTGCGCCCTGCATCTTGGCGTCACCCTCGTCTAT
TACCTGGCCGGCCGAGACCTAAGACGCCTGCCTCAGCTGGTCGGAGTCCACCCACCGCTT
CAGGGAAGCTCTCACGGCGCCGCCGCTATCGGGCAGCCCTCCGGGGAGCTCCGGCTGCGA
GGGGTCGCACCGCCGCCGCCTTTGCAGAACTCTTCCAAGCCGCGCTCGCGGGCCCCCTCC
AACCTAGACGCGTACTCTCACCCCGGCCCTGGCCCGGGCCCGGGGAGCAACTTGACTTCG
GCCCCAGTGCCCTCCACCACAACACGCTCGCTGACCGCATGCCCTGAGGAGTCCCCGCTG
CTCGTCGGCCCCATGCTGATTGAGTTTAACATACCTGTGGACCTGAAGCTTATCGAGCAG
CAGAACCCGAAGGTGAAGTTGGGTGGTCGCTACACCCCCATGGACTGCATCTCTCCTCAC
AAGGTGGCCATCATCATTCTATTCCGCAACCGGCAGGAACACCTCAAGTACTGGCTGTAT
TACTTGCACCCAATGGTACAGCGTCAGCAGTTAGACTATGGCATCTATGTTATCAACCAG
GCTGGAGAGTCCATGTTCAACCGCGCAAAGCTCCTCAATGTTGGCTTTAAAGAGGCCTTG
AAGGACTATGACTACAACTGCTTTGTGTTTAGCGATGTGGACCTCATCCCAATGAACGAC
CATAACACCTACAGGTGCTTTTCACAGCCACGGCACATTTCTGTAGCAATGGATAAGTTT
GGATTTAGCCTACCTTACGTGCAGTATTTTGGAGGTGTCTCTGCTCTAAGTAAACAACAG
TTTCTCAGCATCAATGGATTTCCTAATAACTACTGGGGCTGGGGAGGTGAAGATGATGAC
ATTTATAACAGATTAGCTTTTAGAGGCATGTCTGTGTCTCGCCCAAATGCTGTGATCGGG
AAGTGTCGGATGATCCGCCACTCGAGAGACAAGAAAAATGAACCTAATCCTCAGAGGTTT
GACCGAATTGCACATACAAAGGAGACAATGCTCTCTGATGGTTTGAACTCACTCACCTAC
ATGGTGTTAGAGGTCCAGAGGTACCCGTTGTATACCAAAATCACAGTGGACATCGGGACG
CCGAGCTAG
Enzyme 2 GenBank Gene ID X14558 Link Image
Enzyme 2 GeneCard ID B4GALT1 Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Chromosome:9
Enzyme 2 Locus 9p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 912
Enzyme 3 Name Hexokinase-1
Enzyme 3 Synonyms
  1. Hexokinase type I
  2. HK I
  3. Brain form hexokinase
Enzyme 3 Gene Name HK1
Enzyme 3 Protein Sequence >Hexokinase-1
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLLDIMNRFKKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEQNRPVHMESEVYDTPENIMH
GSGSQLFDHVLECLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDQAILITWTKRFKARGA
EGNYVVKLLDKAIKKRGDYDANIVAVVNDTVGTMIDCGYDDQHCEVGLIIGTGTNACYME
ELRQIDFGWGDDGRMCINTEWGDLGDDGSLEDIRKEFDREFRRGSLNPGKQRFEKMVSGR
YMEDVVRLVLVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGLHNAKEILTRLG
VERSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKSTPRLRTTVRVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGTGKGAAMVTAVAYRLAEQHRQIEETLAHFRLS
KQTLMEVKKRLRTEMEMGLRKETNSNATVNMLPSFLRSIPDGTEDGDFLALDLGGTNFRV
LLVKIRSGKKSTVEMHNKIYRIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAVKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGNQRQMCINMEWGAFGDNGCSDD
IRTDFDKVVDEYSLNSGNQRFENMISGIYLGEIVRNILIDFTKKGFLFRGQISEPLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAA
VVEKIRENRGLDRLNVTVGVDGTLYKLHPQFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRGESAIS
Enzyme 3 Number of Residues 918
Enzyme 3 Molecular Weight 103063.6
Enzyme 3 Theoretical pI 7.04
Enzyme 3 GO Classification
Function
Process
Component
Enzyme 3 General Function Involved in ATP binding
Enzyme 3 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 3 Pathways
  • Carbohydrate metabolism
  • hexose metabolism
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 163152 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P27595 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name HXK1_BOVIN Link Image
Enzyme 3 PDB ID 1HKB Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID M65140 Link Image
Enzyme 3 GeneCard ID HK1 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Chromosome:1
Enzyme 3 Locus 10q22
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 913
Enzyme 4 Name Kininogen-2
Enzyme 4 Synonyms
  1. Kininogen II
  2. Thiol proteinase inhibitor
  3. Kininogen-2 heavy chain
  4. Bradykinin
  5. Kallidin I
  6. Lysyl-bradykinin
  7. Kallidin II
  8. Kininogen-2 light chain
Enzyme 4 Gene Name KNG2
Enzyme 4 Protein Sequence >Kininogen-2
MKLITILFLCSRLLPSLTQESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITE
VARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGQCTATVAKRGNMKFSV
AIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKE
VKRAQKQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRI
SSFSQKCDLYPGEDFLPPMVCVGCPKPIPVDSPDLEEALNHSIAKLNAEHDGTFYFKIDT
VKKATVQVVGGLKYSIVFIARETTCSKGSNEELTKSCEINIHGQILHCDANVYVVPWEEK
VYPTVNCQPLGQTSLMKRPPGFSPFRSVQVMKTEGSTTVSLPHSAMSPVQDEERDSGKEQ
GPTHGHGWDHGKQIKLHGLGLGHKHKHDQGHGHHRSHGLGHGHQKQHGLGHGHKHGHGHG
KHKNKGKNNGKHYDWRTPYLASSYEDSTTSSAQTQEKTEETTLSSLAQPGVAITFPDFQD
SDLIATVMPNTLPPHTESDDDWIPDIQTEPNSLAFKLISDFPETTSPKCPSRPWKPVNGV
NPTVEMKESHDFDLVDALL
Enzyme 4 Number of Residues 619
Enzyme 4 Molecular Weight 68709.6
Enzyme 4 Theoretical pI 6.55
Enzyme 4 GO Classification
Function
Process
Component
Enzyme 4 General Function Inorganic ion transport and metabolism
Enzyme 4 Specific Function (1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin- induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects:(4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW- kininogen is in contrast to HMW-kininogen not involved in blood clotting
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-18
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 494 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P01045 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name KNG2_BOVIN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1860 bp
ATGAAATTAATCACCATCCTTTTCCTTTGTTCCAGGCTGCTACCAAGTTTAACCCAAGAG
TCCTCTCAAGAAATCGACTGCAATGACCAGGATGTATTTAAAGCTGTGGACGCTGCTCTG
ACAAAATACAACAGTGAAAACAAGAGTGGCAACCAGTTTGTATTGTACCGCATAACCGAG
GTCGCCAGAATGGATAATCCTGACACATTTTATTCCTTGAAGTACCAAATCAAGGAGGGC
GACTGTCCTTTTCAAAGTAACAAAACTTGGCAGGACTGTGACTACAAGGACTCTGCACAA
GCTGCCACAGGACAGTGCACAGCGACCGTGGCCAAGAGAGGGAATATGAAGTTCTCCGTG
GCTATCCAGACCTGCCTGATCACTCCAGCCGAGGGCCCCGTGGTGACAGCCCAGTATGAG
TGCCTTGGCTGTGTGCATCCCATATCTACCAAGAGCCCCGACTTGGAGCCTGTTCTGAGA
TATGCCATCCAATATTTTAACAACAACACCAGTCATTCCCACCTCTTTGATCTGAAAGAA
GTAAAAAGAGCCCAAAAACAGGTGGTGTCTGGATGGAACTATGAAGTTAATTACTCAATT
GCACAAACTAATTGTTCCAAGGAGGAATTTTCATTCTTAACTCCAGACTGCAAGTCCCTT
TCAAGTGGTGATACTGGTGAATGTACAGATAAAGCACATGTAGATGTCAAGCTAAGAATT
TCTTCCTTCTCGCAGAAATGTGACCTTTATCCAGGGGAGGATTTTTTACCCCCCATGGTT
TGTGTCGGCTGCCCCAAACCTATACCTGTTGACAGCCCAGACCTGGAGGAAGCTCTGAAC
CATTCCATCGCAAAGCTTAATGCAGAGCATGATGGAACCTTCTATTTCAAGATTGACACT
GTGAAAAAAGCAACAGTACAGGTGGTAGGTGGATTGAAGTATTCTATTGTGTTCATAGCA
AGGGAAACCACATGTTCTAAGGGAAGTAATGAAGAGCTGACCAAGAGTTGTGAGATCAAT
ATACATGGTCAAATTCTACACTGTGATGCTAATGTCTATGTGGTGCCTTGGGAGGAAAAA
GTTTACCCTACTGTCAACTGTCAACCACTTGGACAGACCTCACTCATGAAAAGGCCTCCG
GGTTTTTCACCTTTCCGATCAGTTCAAGTGATGAAAACTGAAGGAAGCACAACTGTAAGT
CTACCCCACTCTGCCATGTCACCTGTACAAGATGAAGAGCGGGATTCAGGAAAAGAACAA
GGACCCACTCATGGGCATGGCTGGGACCATGGAAAGCAAATAAAATTACATGGCCTTGGC
CTTGGCCATAAACATAAGCATGACCAAGGTCATGGGCACCATAGAAGTCATGGTCTTGGC
CATGGACATCAAAAGCAACATGGTCTTGGCCATGGACATAAGCATGGTCATGGCCACGGA
AAACATAAAAACAAAGGAAAAAACAATGGAAAGCATTATGATTGGAGGACACCCTATTTG
GCAAGTTCTTATGAAGATAGCACTACATCCTCTGCACAGACGCAAGAGAAGACAGAAGAG
ACAACACTCTCTTCCCTAGCCCAGCCAGGTGTAGCCATTACCTTTCCTGACTTTCAGGAC
TCAGATCTCATTGCAACTGTGATGCCTAATACACTACCACCTCACACAGAGAGTGATGAT
GACTGGATCCCTGACATCCAGACAGAGCCAAATAGCCTTGCATTTAAATTGATTTCAGAT
TTTCCAGAAACAACCTCCCCCAAATGTCCTAGTCGCCCCTGGAAGCCAGTTAATGGAGTG
AATCCAACTGTGGAAATGAAAGAGTCTCATGATTTTGATCTTGTTGATGCTCTTCTTTAA
Enzyme 4 GenBank Gene ID V01492 Link Image
Enzyme 4 GeneCard ID KNG2 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
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 914
Enzyme 5 Name Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
Enzyme 5 Synonyms
  1. UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa
  2. N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa
  3. N-acetylglucosaminyltransferase IVa
  4. GlcNAc-T IVa
  5. GnT-IVa
  6. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form
Enzyme 5 Gene Name MGAT4A
Enzyme 5 Protein Sequence >Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
MRLRNGTVATVLAFITSFLTLSWYTTWQNGKEKVIAYQREFLALKERLRIAEHRISQRSS
ELSAIVQQFKRVEAETNRSKDPVNKFSDDTLKILKELTSKKSLQVPSIYYHLPHLLQNEG
SLQPAVQIGNGRTGVSIVMGIPTVKREVKSYLIETLHSLIDNLYPEEKLDCVIVVFIGET
DTDYVNGVVANLEKEFSKEISSGLVEIISPPESYYPDLTNLKETFGDSKERVRWRTKQNL
DYCFLMMYAQEKGTYYIQLEDDIIVKQNYFNTIKNFALQLSSEEWMILEFSQLGFIGKMF
QAPDLTLIVEFIFMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIRFRPSLFQ
HVGLHSSLTGKIQKLTDKDYMKPLLLKIHVNPPAEVSTSLKVYQGHTLEKTYMGEDFFWA
ITPVAGDYILFKFDKPVNVESYLFHSGNQDHPGDILLNTTVEVLPLKSEGLDISKETKDK
RLEDGYFRIGKFENGVAEGMVDPSLNPISAFRLSVIQNSAVWAILNEIHIKKVTN
Enzyme 5 Number of Residues 535
Enzyme 5 Molecular Weight 61617.4
Enzyme 5 Theoretical pI 7.00
Enzyme 5 GO Classification
Function
Process
Component
Enzyme 5 General Function Involved in alpha-1,3-mannosylglycoprotein 4-beta-N-ace
Enzyme 5 Specific Function Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N- linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells
Enzyme 5 Pathways
  • Protein modification
  • protein glycosylation
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 7-27
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 3273235 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O77836 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name MGT4A_BOVIN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1608 bp
ATGAGGCTCCGAAATGGAACTGTAGCCACTGTTTTAGCATTTATCACCTCGTTCCTCACT
TTATCTTGGTATACAACATGGCAAAATGGGAAAGAAAAAGTGATTGCTTATCAACGAGAA
TTTCTTGCTCTGAAAGAACGTCTCCGAATAGCTGAACATCGAATCTCTCAGCGCTCTTCT
GAGCTCAGTGCCATTGTACAGCAATTCAAGCGTGTAGAAGCAGAAACAAACAGGAGTAAG
GATCCAGTGAATAAATTTTCAGATGATACCCTAAAGATACTAAAGGAGTTAACAAGCAAA
AAGTCTCTTCAAGTGCCAAGTATTTATTATCATTTGCCTCATTTATTGCAAAATGAAGGA
AGCCTTCAACCTGCCGTGCAGATCGGAAATGGACGAACAGGAGTTTCAATAGTAATGGGA
ATTCCTACAGTGAAGAGAGAAGTTAAATCTTACCTCATAGAAACTCTTCATTCCCTTATT
GATAATCTGTATCCTGAAGAGAAGTTGGACTGTGTTATAGTAGTCTTCATAGGAGAGACA
GATACTGATTATGTAAATGGTGTTGTAGCCAACCTGGAGAAAGAATTTTCTAAAGAAATC
AGTTCTGGCTTGGTGGAAATAATATCACCTCCTGAAAGCTATTATCCTGACCTGACGAAC
TTAAAGGAGACATTTGGAGATTCTAAAGAAAGAGTAAGATGGAGAACAAAGCAAAACCTA
GATTATTGTTTTCTAATGATGTATGCTCAGGAAAAAGGCACATACTACATCCAGCTTGAA
GATGATATTATTGTCAAACAGAATTACTTTAACACCATAAAGAATTTTGCACTTCAACTT
TCTTCTGAGGAATGGATGATACTTGAGTTCTCCCAGCTGGGATTCATTGGTAAAATGTTT
CAAGCACCTGACCTCACTCTGATTGTGGAATTCATATTTATGTTCTATAAGGAGAAGCCC
ATCGACTGGCTCTTGGACCATATTCTGTGGGTCAAAGTCTGCAACCCGGAAAAAGATGCA
AAACACTGTGATCGACAGAAGGCAAATCTGCGAATTCGTTTCAGACCGTCCCTTTTCCAA
CACGTTGGTCTGCATTCTTCACTCACAGGAAAAATTCAGAAACTCACGGATAAAGATTAC
ATGAAACCATTACTGCTCAAAATCCATGTAAACCCCCCTGCAGAGGTATCTACTTCTTTG
AAGGTCTACCAAGGTCATACACTGGAGAAAACTTACATGGGTGAGGACTTCTTCTGGGCT
ATAACCCCAGTAGCTGGAGACTACATCCTATTTAAATTCGACAAGCCAGTCAATGTGGAA
AGTTATTTGTTCCATAGTGGCAACCAGGATCATCCAGGGGATATTCTGCTCAACACAACG
GTGGAAGTTCTGCCTTTGAAGAGTGAAGGTTTGGACATCAGCAAAGAAACCAAAGACAAA
CGATTAGAAGATGGCTATTTCAGAATAGGGAAATTTGAAAACGGTGTTGCGGAAGGGATG
GTGGATCCCAGCCTAAACCCCATTTCGGCCTTCCGACTTTCAGTTATTCAGAATTCTGCT
GTTTGGGCCATTCTTAATGAGATCCATATTAAAAAAGTCACAAACTGA
Enzyme 5 GenBank Gene ID AB000628 Link Image
Enzyme 5 GeneCard ID MGAT4A Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Chromosome:2
Enzyme 5 Locus 2q12
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 915
Enzyme 6 Name Phosphatidylinositol 3-kinase regulatory subunit alpha
Enzyme 6 Synonyms
  1. PI3-kinase p85 subunit alpha
  2. PtdIns-3-kinase p85-alpha
  3. PI3K
Enzyme 6 Gene Name PIK3R1
Enzyme 6 Protein Sequence >Phosphatidylinositol 3-kinase regulatory subunit alpha
MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEAKPEEIGWLNGYN
ETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGPSKTEADSEQQASTLPDLAE
QFAPPDVAPPLLIKLVEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDTASLDLEMFDVH
VLADAFKRYLLDLPNPVIPVAVSSELISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTL
QYLLKHFFKLSQTSSKNLLNARVLSELFSPLLFRFPAASSENTEHLIKIIEILISTEWNE
RQPAPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDA
STKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKL
DVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEDYTRTSQEIQMK
RTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNETEIQRIMHNYEKLKSRISEIVD
SRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGN
ENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACS
VVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYA
QQRR
Enzyme 6 Number of Residues 724
Enzyme 6 Molecular Weight 83496.5
Enzyme 6 Theoretical pI 6.03
Enzyme 6 GO Classification
Function
Process
Component
Enzyme 6 General Function Replication, recombination and repair
Enzyme 6 Specific Function Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 163477 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P23727 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name P85A_BOVIN Link Image
Enzyme 6 PDB ID 1PBW Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID M61745 Link Image
Enzyme 6 GeneCard ID PIK3R1 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Chromosome:5
Enzyme 6 Locus 5q13.1
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 916
Enzyme 7 Name AMP-activated protein kinase gamma subunit
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name PRKAG3
Enzyme 7 Protein Sequence >AMP-activated protein kinase gamma subunit
MSFLEQGDSTSWPSPAMTTSAEISLGEQRTKVSRWKSQEDVEERELPGLEGGPQSRAAAE
STGLEATFPKATPLAQATPLSAVGTPTTERDSLPSDCTASASSSSTDDLDQGIEFSAPAA
WGDELGLVEERPAQCPSPQVPVLRLGWDDELRKPGAQVYMHFMQEHTCYDAMATSSKLVI
FDTMLQIKKAFFALVANGVRAAPLWDSKKQSFVGMLTITDFILVLHRYYRFPLVQIYEIE
EHKIETWREIYLQGCFKPLVSISPSDSLFEAVYTLIKNRIHRLPVLDPVSGAVLHILTHK
RLLKFLHIFQRTLLPRPSFLYRTIQDLGIGTFRDLAVVLETAPILTALDIFVDRRVSALP
VINEAGQVVGLYSRFDVIHLAAQQTYNHLDISVGEALRRRTLCLEGVLSCQPHETLGEVI
DRIAREQVHRLVLVDETQHLLGVVSLSDILQALVLSPAGIDALGA
Enzyme 7 Number of Residues 465
Enzyme 7 Molecular Weight 51522.5
Enzyme 7 Theoretical pI 5.31
Enzyme 7 GO Classification
Function
Process
Component
Enzyme 7 General Function Involved in kinase activity
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 56406642 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q4G3U3 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name Q4G3U3_BOVIN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AY692035 Link Image
Enzyme 7 GeneCard ID PRKAG3 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Chromosome:2
Enzyme 7 Locus 2q35
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 917
Enzyme 8 Name RAC-alpha serine/threonine-protein kinase
Enzyme 8 Synonyms
  1. RAC-PK-alpha
  2. Protein kinase B
  3. PKB
Enzyme 8 Gene Name AKT1
Enzyme 8 Protein Sequence >RAC-alpha serine/threonine-protein kinase
MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDLEQRESPLNNFSVAQC
QLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEETMDF
RSGSPGENSGAEEMEVSLAKPKHRVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKI
LKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLS
RERVFSEDRARFYGAEIVSALDYLHSEKEVVYRDLKLENLMLDKDGHIKITDFGLCKEGI
KDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFEL
ILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFASIVWQDVYEKK
LSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMEGVDSERRPHFPQFSYSASATA
Enzyme 8 Number of Residues 480
Enzyme 8 Molecular Weight 55748.0
Enzyme 8 Theoretical pI 5.70
Enzyme 8 GO Classification
Function
Process
Component
Enzyme 8 General Function Involved in ATP binding
Enzyme 8 Specific Function General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2, thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin- induced activation of glycogen synthase
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 631 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q01314 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name AKT1_BOVIN Link Image
Enzyme 8 PDB ID 1MRY Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1443 bp
ATGAACGACGTGGCCATCGTGAAGGAGGGCTGGCTGCACAAGCGAGGTGAGTACATCAAG
ACGTGGCGGCCGCGTTACTTCCTCCTGAAGAACGATGGCACGTTCATTGGCTACAAGGAG
CGGCCGCAGGACCTGGAGCAGCGTGAGTCGCCCCTCAACAACTTCTCCGTGGCCCAATGC
CAGCTGATGAAGACGGAGCGGCCGCGGCCCAACACCTTCATCATCCGCTGCCTGCAGTGG
ACCACGGTCATCGAGCGCACGTTCCACGTGGAGACGCCCGAGGAGCGGGAGGAGTGGACC
ACCGCCATCCAGACGGTGGCCGACGGGCTCAAGAGGCAGGAGGAGGAGACGATGGACTTC
CGGTCGGGCTCACCCGGCGAGAACTCGGGGGCCGAGGAGATGGAGGTGTCGCTGGCCAAG
CCCAAGCACCGCGTGACCATGAATGAGTTTGAGTACGTGAAGCTGCTGGGCAAAGGCACT
TTCGGGAAGGTGATCCTGGTGAAGGAGAAGGCCACAGCGGCCTACTACGCCATGAAGATC
CTAAAGAAGGAGGTCATCGTGGCCAAGGACGAGGTGGCCCACACGCTCACAGAGAACCGC
GTTCTCCAGAACTCCCGGCACCCGTCCCTGACGGCCCTGAAGTACTCCTTCCAGACACAC
GACCGCCTGTGCTTCGTCATGGAGTACGCTAACGGGGGCGAGCTTTTCTTCCACCTGTCC
CGGGAGCGGGTGTTTTCCGAGGACCGGGCCCGTTTCTACGGCGCCGAGATCGTGTCGGCC
CTGGATTACCTGCACTCGGAAAAGGAAGTGGTGTACAGGGACCTCAAGCTGGAGAACCTC
ATGCTGGACAAGGACGGGCACATCAAGATCACCGACTTCGGACTGTGCAAGGAGGGCATC
AAGGATGGCGCCACCATGAAGACTTTCTGCGGGACCCCCGAATACCTGGCTCCCGAGGTG
CTGGAGGACAACGACTACGGCCGGGCAGTGGACTGGTGGGGGCTGGGTGTGGTCATGTAC
GAGATGATGTGCGGCCGCCTGCCCTTCTACAACCAGGACCACGAGAAGCTCTTTGAGCTC
ATTCTCATGGAGGAGATCCGCTTCCCCCGCACACTCAGCCCGGAGGCCAAGTCCCTGCTC
TCTGGGCTACTCAAGAAGGACCCCAAGCAGCGGCTTGGTGGGGGCTCTGAGGACGCCAAG
GAGATCATGCAGCACCGATTCTTCGCCAGCATCGTGTGGCAGGACGTGTACGAGAAGAAG
CTCAGCCCGCCCTTCAAGCCTCAGGTCACATCTGAGACGGACACCAGGTATTTTGATGAG
GAGTTCACGGCCCAGATGATCACCATTACGCCACCTGACCAAGACGACAGCATGGAGGGG
GTGGACAGCGAACGGAGGCCCCACTTCCCCCAGTTCTCCTACTCGGCCAGCGCGACGGCC
TGA
Enzyme 8 GenBank Gene ID X61036 Link Image
Enzyme 8 GeneCard ID AKT1 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Chromosome:1
Enzyme 8 Locus 14q32.32|14q32.32
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 918
Enzyme 9 Name Kininogen-1
Enzyme 9 Synonyms
  1. Kininogen I
  2. Thiol proteinase inhibitor
  3. Kininogen-1 heavy chain
  4. Bradykinin
  5. Kallidin I
  6. Lysyl-bradykinin
  7. Kallidin II
  8. Kininogen-1 light chain
Enzyme 9 Gene Name KNG1
Enzyme 9 Protein Sequence >Kininogen-1
MKLITILFLCSRLLPSLTQESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITE
VARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGECTATVAKRGNMKFSV
AIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKE
VKRAQRQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRI
SSFSQKCDLYPVKDFVQPPTRLCAGCPKPIPVDSPDLEEPLSHSIAKLNAEHDGAFYFKI
DTVKKATVQVVAGLKYSIVFIARETTCSKGSNEELTKSCEINIHGQILHCDANVYVVPWE
EKVYPTVNCQPLGQTSLMKRPPGFSPFRSVQVMKTEGSTTVSLPHSAMSPVQDEERDSGK
EQGPTHGHGWDHGKQIKLHGLGLGHKHKHDQGHGHHGSHGLGHGHQKQHGLGHGHKHGHG
HGKHKNKGKNNGKHYDWRTPYLASSYEDSTTSSAQTQEKTEETTLSSLAQPGVAITFPDF
QDSDLIATVMPNTLPPHTESDDDWIPDIQTEPNSLAFKLISDFPETTSPKCPSRPWKPVN
GVNPTVEMKESHDFDLVDALL
Enzyme 9 Number of Residues 621
Enzyme 9 Molecular Weight 68889.8
Enzyme 9 Theoretical pI 6.61
Enzyme 9 GO Classification
Function
Process
Component
Enzyme 9 General Function Inorganic ion transport and metabolism
Enzyme 9 Specific Function (1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin- induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects:(4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW- kininogen is in contrast to HMW-kininogen not involved in blood clotting
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-18
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 492 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P01044 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name KNG1_BOVIN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1866 bp
ATGAAATTAATCACCATCCTTTTCCTTTGTTCCAGGCTGCTACCAAGTTTAACCCAAGAG
TCCTCTCAAGAAATCGACTGCAACGACCAGGATGTATTTAAAGCTGTGGACGCTGCTCTG
ACAAAATACAACAGTGAAAACAAGAGTGGCAACCAGTTTGTATTGTACCGCATAACCGAG
GTCGCCAGAATGGATAATCCTGACACATTTTATTCCTTGAAGTACCAAATCAAGGAGGGC
GACTGTCCTTTTCAAAGTAACAAAACTTGGCAGGACTGTGACTACAAGGACTCTGCACAA
GCTGCCACAGGAGAGTGCACAGCGACCGTGGCCAAGAGAGGGAATATGAAGTTCTCCGTG
GCTATCCAGACCTGCCTGATCACTCCAGCCGAGGGCCCCGTGGTGACAGCCCAGTATGAG
TGCCTTGGCTGTGTGCATCCCATATCTACCAAGAGCCCCGACTTGGAGCCTGTTCTGAGA
TATGCCATCCAATATTTTAACAACAACACCAGTCATTCCCACCTCTTTGATCTGAAAGAA
GTAAAAAGAGCCCAAAGACAGGTGGTGTCTGGATGGAACTATGAAGTTAATTACTCAATT
GCACAAACTAATTGTTCCAAGGAGGAATTTTCATTCTTAACTCCAGACTGCAAGTCCCTT
TCAAGTGGTGATACTGGTGAATGTACAGATAAAGCACATGTAGATGTCAAGCTAAGAATT
TCTTCCTTCTCGCAGAAATGTGACCTTTATCCAGTGAAGGATTTTGTACAACCACCCACC
AGGCTTTGTGCCGGCTGCCCCAAACCTATACCTGTTGACAGCCCAGACCTGGAGGAGCCT
CTGAGCCATTCCATCGCAAAGCTTAATGCAGAGCATGATGGAGCCTTCTATTTCAAGATT
GACACTGTGAAAAAAGCAACAGTACAGGTGGTAGCTGGATTGAAGTATTCTATTGTGTTC
ATAGCAAGGGAAACCACATGTTCTAAGGGAAGTAATGAAGAGCTGACCAAGAGTTGTGAG
ATCAATATACATGGTCAAATTCTACACTGTGATGCTAATGTCTATGTGGTGCCTTGGGAG
GAAAAAGTTTACCCTACTGTCAACTGTCAACCACTTGGACAGACCTCACTCATGAAAAGG
CCTCCGGGTTTTTCACCTTTCCGATCAGTTCAAGTGATGAAAACTGAAGGAAGCACAACT
GTAAGTCTACCCCACTCTGCCATGTCACCTGTACAAGATGAAGAGCGGGATTCAGGAAAA
GAACAAGGACCCACTCATGGGCATGGCTGGGACCATGGAAAGCAAATAAAATTACATGGC
CTTGGCCTTGGCCATAAACATAAGCATGACCAAGGTCATGGGCACCATGGAAGTCATGGT
CTTGGCCATGGACATCAAAAGCAACATGGTCTTGGCCATGGACATAAGCATGGTCATGGC
CACGGAAAACATAAAAACAAAGGAAAAAACAATGGAAAGCATTATGATTGGAGGACACCC
TATTTGGCAAGTTCTTATGAAGATAGCACTACATCCTCTGCACAGACGCAAGAGAAGACA
GAAGAGACAACACTCTCTTCCCTAGCCCAGCCAGGTGTAGCCATTACCTTTCCTGACTTT
CAGGACTCAGATCTCATTGCAACTGTGATGCCTAATACACTACCACCTCACACAGAGAGT
GATGATGACTGGATCCCTGACATCCAGACAGAGCCAAATAGCCTTGCATTTAAATTGATT
TCAGACTTTCCAGAAACAACCTCCCCCAAATGTCCTAGTCGCCCCTGGAAGCCAGTTAAT
GGAGTGAATCCAACTGTGGAAATGAAAGAGTCTCATGATTTTGATCTTGTTGATGCTCTT
CTTTAA
Enzyme 9 GenBank Gene ID V01491 Link Image
Enzyme 9 GeneCard ID KNG1 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Chromosome:3
Enzyme 9 Locus 3q27
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available