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Human Metabolome Database Version 2.5

 

Showing metabocard for Spermine (HMDB01256)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-12 16:04:02
Accession Number HMDB01256
Secondary Accession Numbers Not Available
Common Name Spermine
Description Spermine is a biogenic polyamine formed from spermidine. It is found in a wide variety of organisms and tissues and is an essential growth factor in some bacteria. It is found as a polycation at all pH values. Spermine is associated with nucleic acids, particularly in viruses, and is thought to stabilize the helical structure.
Synonyms
  1. 1,5,10,14-Tetraazatetradecane
  2. 4,9-Diaza-1,12-dodecanediamine
  3. 4,9-Diazadodecamethylenediamine
  4. 4,9-Diazadodecane-1,12-diamine
  5. Diaminopropyltetramethylenediamine
  6. Gerontine
  7. Musculamine
  8. N,N'-Bis(3-aminopropyl)-1,4-tetramethylenediamine
  9. N,N'-Bis(3-aminopropyl)butane-1,4-diamine
  10. N,N'-bis(3-aminopropyl)-1,4-Butanediamine
  11. N1,N4-bis(3-aminopropyl)-1,4-butanediamine
  12. Neuridine
  13. SPM
  14. Spermin
  15. Spermine
  16. Spermine dihydrate
  17. Spermine puriss
  18. diaminopropyl-tetramethylenediamine
Chemical IUPAC Name N,N'-bis(3-aminopropyl)butane-1,4-diamine
Chemical Formula C10H26N4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amines
Class
  • Polyamines
Sub Class
  • Spermines
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • secondary amine
  • secondary aliphatic amine (dialkylamine)
Biofunction
  • Component of Arginine and proline metabolism
  • Component of beta-Alanine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 202.340
Monoisotopic Molecular Weight 202.215744
Isomeric SMILES NCCCNCCCCNCCCN
Canonical SMILES NCCCNCCCCNCCCN
KEGG Compound ID C00750 Link Image
BioCyc ID SPERMINE Link Image
BiGG ID 35875 Link Image
Wikipedia Link Spermine Link Image
NuGOwiki Link HMDB01256 Link Image
Metagene Link HMDB01256 Link Image
METLIN ID 255 Link Image
PubChem Compound 1103 Link Image
PubChem Substance 8027271 Link Image
ChEBI ID 15746 Link Image
CAS Registry Number 71-44-3
InChI Identifier InChI=1/C10H26N4/c11-5-3-9-13-7-1-2-8-14-10-4-6-12/h13-14H,1-12H2
Synthesis Reference Wrede, Fritz; Strack, Erich; Hettche, Otto. Spermine. VII. Z. physiol. Chem. (1928), 173 61-8.
Melting Point (Experimental) 29 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000.0 mg/mL [MEYLAN,WM et al. (1996)]; 2.19 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.66 [Predicted by ALOGPS]; -0.7 [Predicted by PubChem via XLOGP]; -0.68 [MEYLAN,WM & HOWARD,PH (1995)] 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 1RM7 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
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 Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Brain
Erythrocyte
Fibroblasts
Intestine
Liver
Muscle
Neuron
Pancreas
Platelet
Prostate
Skin
Testes
Concentrations (Normal)
Biofluid Blood
Value 9.97 +/- 3.26 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 0.14 +/- 0.01 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Ekegren T, Gomes-Trolin C: Determination of polyamines in human tissues by precolumn derivatization with 9-fluorenylmethyl chloroformate and high-performance liquid chromatography. Anal Biochem. 2005 Mar 15;338(2):179-85. [PubMed Link Image]
Biofluid Saliva
Value 0.04 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Venza M, Visalli M, Cicciu D, Teti D: Determination of polyamines in human saliva by high-performance liquid chromatography with fluorescence detection. J Chromatogr B Biomed Sci Appl. 2001 Jun 5;757(1):111-7. [PubMed Link Image]
Biofluid Urine
Value 0.13 +/- 0.065 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 0.019 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Biofluid Urine
Value 0.08 (0.01-0.28) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • van den Berg GA, Muskiet FA, Kingma AW, van der Slik W, Halie MR: Simultaneous gas-chromatographic determination of free and acetyl-conjugated polyamines in urine. Clin Chem. 1986 Oct;32(10):1930-7. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Spermidine and Spermine Biosynthesis SMP00445 Link Image
General References
  1. Mollica F, Li Volti S, Rapisarda A, Longo G, Pavone L, Vanella A: Increased erythrocytic spermine in Duchenne muscular dystrophy. Pediatr Res. 1980 Nov;14(11):1196-8. [PubMed Link Image]
  2. Swift TA, Dias JA: Effects of the polyamine spermine on binding of follicle-stimulating hormone to membrane-bound immature bovine testis receptors. Biochim Biophys Acta. 1986 Feb 21;885(2):221-30. [PubMed Link Image]
  3. Cipolla BG, Ziade J, Bansard JY, Moulinoux JP, Staerman F, Quemener V, Lobel B, Guille F: Pretherapeutic erythrocyte polyamine spermine levels discriminate high risk relapsing patients with M1 prostate carcinoma. Cancer. 1996 Sep 1;78(5):1055-65. [PubMed Link Image]
  4. Venza M, Visalli M, Cicciu D, Teti D: Determination of polyamines in human saliva by high-performance liquid chromatography with fluorescence detection. J Chromatogr B Biomed Sci Appl. 2001 Jun 5;757(1):111-7. [PubMed Link Image]
  5. Uehara N, Shirakawa S, Uchino H, Saeki Y: Elevated contents of spermidine and spermine in the erythrocytes of cancer patients. Cancer. 1980 Jan 1;45(1):108-11. [PubMed Link Image]
  6. Jensen PK, Therkelsen AJ: Selective inhibition of fibroblasts by spermine in primary cultures of normal human skin epithelial cells. In Vitro. 1982 Oct;18(10):867-71. [PubMed Link Image]
  7. Loser C, Folsch UR, Paprotny C, Creutzfeldt W: Polyamines in colorectal cancer. Evaluation of polyamine concentrations in the colon tissue, serum, and urine of 50 patients with colorectal cancer. Cancer. 1990 Feb 15;65(4):958-66. [PubMed Link Image]
  8. Proctor MS, Fletcher HV Jr, Shukla JB, Rennert OM: Elevated spermidine and spermine levels in the blood of psoriasis patients. J Invest Dermatol. 1975 Oct;65(4):409-11. [PubMed Link Image]
  9. Lorenz B, Francis F, Gempel K, Boddrich A, Josten M, Schmahl W, Schmidt J, Lehrach H, Meitinger T, Strom TM: Spermine deficiency in Gy mice caused by deletion of the spermine synthase gene. Hum Mol Genet. 1998 Mar;7(3):541-7. [PubMed Link Image]
  10. Hosseinkhani H, Azzam T, Tabata Y, Domb AJ: Dextran-spermine polycation: an efficient nonviral vector for in vitro and in vivo gene transfection. Gene Ther. 2004 Jan;11(2):194-203. [PubMed Link Image]
  11. El Baze P, Milano G, Verrando P, Renee N, Ortonne JP: Polyamine levels in normal human skin. A comparative study of pure epidermis, pure dermis, and suction blister fluid. Arch Dermatol Res. 1983;275(4):218-21. [PubMed Link Image]
  12. Wikipedia Link Image
Metabolic Enzymes
  1. Diamine acetyltransferase 2
  2. Diamine acetyltransferase 1
  3. Xanthine dehydrogenase/oxidase
  4. Choline dehydrogenase, mitochondrial
  5. Dimethylglycine dehydrogenase, mitochondrial
  6. Spermine synthase
  7. Spermidine synthase
  8. 4-trimethylaminobutyraldehyde dehydrogenase
  9. Gamma-butyrobetaine dioxygenase
  10. Amiloride-sensitive amine oxidase [copper-containing]
  11. S-methyl-5'-thioadenosine phosphorylase
  12. S-adenosylmethionine decarboxylase proenzyme
  13. Glycine amidinotransferase, mitochondrial
  14. Betaine--homocysteine S-methyltransferase 1
  15. Sarcosine dehydrogenase, mitochondrial
  16. Histidine decarboxylase
  17. Ornithine decarboxylase
  18. Solute carrier family 22 member 1
  19. Spermine oxidase
  20. Agmatinase, mitochondrial
  21. Trimethyllysine dioxygenase, mitochondrial
  22. Betaine--homocysteine S-methyltransferase 2
  23. Spermidine synthase (Spermidine synthase, isoform CRA_a)
  24. cDNA, FLJ94459, Homo sapiens spermine synthase (SMS), mRNA
  25. Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial
  26. Ornithine decarboxylase antizyme 1
  27. Virion infectivity factor
  28. Virion infectivity factor
  29. Virion infectivity factor
  30. Virion infectivity factor
  31. Virion infectivity factor
  32. Virion infectivity factor
  33. Virion infectivity factor
  34. Virion infectivity factor
  35. Virion infectivity factor
  36. Virion infectivity factor
  37. Virion infectivity factor
  38. cDNA, FLJ95932, Homo sapiens polyamine modulated factor 1 binding protein 1(PMFBP1), mRNA
  39. Virion infectivity factor
  40. Polyamine-modulated factor 1
  41. Virion infectivity factor
  42. Virion infectivity factor
  43. Virion infectivity factor
  44. Virion infectivity factor
  45. Virion infectivity factor
  46. Virion infectivity factor
  47. Virion infectivity factor
  48. cDNA FLJ16610 fis, clone TESTI4011532, highly similar to Homo sapiens polyamine modulated factor 1 binding protein 1 (PMFBP1), mRNA
  49. Virion infectivity factor
  50. Virion infectivity factor
  51. Virion infectivity factor
  52. Virion infectivity factor
  53. Virion infectivity factor
  54. Virion infectivity factor
  55. Truncated virion infectivity factor
  56. Virion infectivity factor
  57. Virion infectivity factor
  58. Virion infectivity factor
  59. Virion infectivity factor
  60. Virion infectivity factor
  61. Virion infectivity factor
  62. Virion infectivity factor
  63. Virion infectivity factor
  64. Virion infectivity factor
  65. Virion infectivity factor
  66. Virion infectivity factor
  67. Virion infectivity factor
  68. Virion infectivity factor
  69. Virion infectivity factor
Enzyme 1 [top]
Enzyme 1 ID 5244
Enzyme 1 Name Diamine acetyltransferase 2
Enzyme 1 Synonyms
  1. Polyamine N-acetyltransferase 2
  2. Spermidine/spermine N(1)-acetyltransferase 2
  3. Thialysine N-epsilon-acetyltransferase
Enzyme 1 Gene Name SAT2
Enzyme 1 Protein Sequence >Diamine acetyltransferase 2
MASVRIREAKEGDCGDILRLIRELAEFEKLSDQVKISEEALRADGFGDNPFYHCLVAEIL
PAPGKLLGPCVVGYGIYYFIYSTWKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDK
GCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEGWHFFCFQGEATRKLAGK
Enzyme 1 Number of Residues 170
Enzyme 1 Molecular Weight 19154.9
Enzyme 1 Theoretical pI 5.84
Enzyme 1 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 1 General Function Involved in N-acetyltransferase activity
Enzyme 1 Specific Function Enzyme which catalyzes the acetylation of polyamines. Substrate specificity:norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine [RN:R03910]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID Q96F10 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SAT2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >513 bp
ATGGCTTCCGTGCGGATCCGAGAGGCCAAGGAGGGAGACTGTGGAGATATCCTGAGGCTG
ATTCGGGAGCTAGCCGAATTCGAAAAACTCTCGGATCAGGTGAAGATCAGTGAAGAAGCC
CTGAGAGCAGATGGCTTTGGAGACAATCCTTTCTATCACTGTTTGGTAGCAGAGATTCTT
CCAGCGCCCGGGAAGCTACTGGGGCCCTGCGTGGTGGGCTATGGGATATACTATTTCATC
TACAGTACATGGAAGGGACGCACCATTTATCTGGAGGATATCTATGTGATGCCAGAATAT
CGGGGTCAAGGGATTGGTTCCAAAATAATCAAAAAGGTGGCTGAGGTGGCCTTGGATAAG
GGCTGCTCCCAATTCCGCCTGGCCGTCCTGGACTGGAACCAGAGGGCCATGGACTTGTAC
AAGGCCCTAGGAGCCCAAGATCTGACGGAAGCTGAGGGCTGGCACTTCTTCTGCTTTCAA
GGAGAGGCAACGAGAAAGTTGGCAGGAAAGTGA
Enzyme 1 GenBank Gene ID AF348524 Link Image
Enzyme 1 GeneCard ID SAT2 Link Image
Enzyme 1 GenAtlas ID SAT2 Link Image
Enzyme 1 HGNC ID HGNC:23160 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 17p13.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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 Link Image]
  2. Chen Y, Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW: Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase. Biochem J. 2003 Aug 1;373(Pt 3):661-7. [PubMed Link Image]
  3. 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 Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5258
Enzyme 2 Name Diamine acetyltransferase 1
Enzyme 2 Synonyms
  1. Polyamine N-acetyltransferase 1
  2. Putrescine acetyltransferase
  3. Spermidine/spermine N(1)-acetyltransferase 1
  4. SSAT
  5. SSAT-1
Enzyme 2 Gene Name SAT1
Enzyme 2 Protein Sequence >Diamine acetyltransferase 1
MAKFVIRPATAADCSDILRLIKELAKYEYMEEQVILTEKDLLEDGFGEHPFYHCLVAEVP
KEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMRC
RCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMATEE
Enzyme 2 Number of Residues 171
Enzyme 2 Molecular Weight 20023.8
Enzyme 2 Theoretical pI 4.82
Enzyme 2 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 2 General Function Involved in N-acetyltransferase activity
Enzyme 2 Specific Function Enzyme which catalyzes the acetylation of polyamines. Substrate specificity:norspermidine = spermidine >> spermine > N(1)-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine
Enzyme 2 Pathways
Enzyme 2 Reactions
  • acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine [RN:R03910]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID P21673 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SAT1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >516 bp
ATGGCTAAATTCGTGATCCGCCCAGCCACTGCCGCCGACTGCAGTGACATACTGCGGCTG
ATCAAGGAGCTGGCTAAATATGAATACATGGAAGAACAAGTAATCTTAACTGAAAAAGAT
CTGCTAGAAGATGGTTTTGGAGAGCACCCCTTTTACCACTGCCTGGTTGCAGAAGTGCCG
AAAGAGCACTGGACTCCGGAAGGACACAGCATTGTTGGTTTTGCCATGTACTATTTTACC
TATGACCCGTGGATTGGCAAGTTATTGTATCTTGAGGACTTCTTCGTGATGAGTGATTAT
AGAGGCTTTGGCATAGGATCAGAAATTCTGAAGAATCTAAGCCAGGTTGCAATGAGGTGT
CGCTGCAGCAGCATGCACTTCTTGGTAGCAGAATGGAATGAACCATCCATCAACTTCTAT
AAAAGAAGAGGTGCTTCTGATCTGTCCAGTGAAGAGGGTTGGAGACTGTTCAAGATCGAC
AAGGAGTACTTGCTAAAAATGGCAACAGAGGAGTGA
Enzyme 2 GenBank Gene ID M77693 Link Image
Enzyme 2 GeneCard ID SAT1 Link Image
Enzyme 2 GenAtlas ID SAT1 Link Image
Enzyme 2 HGNC ID HGNC:10540 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Casero RA Jr, Celano P, Ervin SJ, Applegren NB, Wiest L, Pegg AE: Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase. J Biol Chem. 1991 Jan 15;266(2):810-4. [PubMed Link Image]
  2. Xiao L, Celano P, Mank AR, Pegg AE, Casero RA Jr: Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase. Biochem Biophys Res Commun. 1991 Aug 30;179(1):407-15. [PubMed Link Image]
  3. Xiao L, Celano P, Mank AR, Griffin C, Jabs EW, Hawkins AL, Casero RA Jr: Structure of the human spermidine/spermine N1-acetyltransferase gene (exon/intron gene organization and localization to Xp22.1). Biochem Biophys Res Commun. 1992 Sep 30;187(3):1493-502. [PubMed Link Image]
  4. Xiao L, Casero RA Jr: Differential transcription of the human spermidine/spermine N1-acetyltransferase (SSAT) gene in human lung carcinoma cells. Biochem J. 1996 Jan 15;313 ( Pt 2):691-6. [PubMed Link Image]
  5. 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 Link Image]
  6. Casero RA Jr, Celano P, Ervin SJ, Wiest L, Pegg AE: High specific induction of spermidine/spermine N1-acetyltransferase in a human large cell lung carcinoma. Biochem J. 1990 Sep 15;270(3):615-20. [PubMed Link Image]
  7. 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 Link Image]
  8. Bewley MC, Graziano V, Jiang J, Matz E, Studier FW, Pegg AE, Coleman CS, Flanagan JM: Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target. Proc Natl Acad Sci U S A. 2006 Feb 14;103(7):2063-8. Epub 2006 Feb 2. [PubMed Link Image]
  9. Hegde SS, Chandler J, Vetting MW, Yu M, Blanchard JS: Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase. Biochemistry. 2007 Jun 19;46(24):7187-95. Epub 2007 May 22. [PubMed Link Image]
  10. Zhu YQ, Zhu DY, Yin L, Zhang Y, Vonrhein C, Wang DC: Crystal structure of human spermidine/spermine N1-acetyltransferase (hSSAT): the first structure of a new sequence family of transferase homologous superfamily. Proteins. 2006 Jun 1;63(4):1127-31. [PubMed Link Image]
  11. Oosterwijk JC, Richard G, van der Wielen MJ, van de Vosse E, Harth W, Sandkuijl LA, Bakker E, van Ommen GJ: Molecular genetic analysis of two families with keratosis follicularis spinulosa decalvans: refinement of gene localization and evidence for genetic heterogeneity. Hum Genet. 1997 Oct;100(5-6):520-4. [PubMed Link Image]
  12. Gimelli G, Giglio S, Zuffardi O, Alhonen L, Suppola S, Cusano R, Lo Nigro C, Gatti R, Ravazzolo R, Seri M: Gene dosage of the spermidine/spermine N(1)-acetyltransferase ( SSAT) gene with putrescine accumulation in a patient with a Xp21.1p22.12 duplication and keratosis follicularis spinulosa decalvans (KFSD). Hum Genet. 2002 Sep;111(3):235-41. Epub 2002 Aug 1. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5413
Enzyme 3 Name Xanthine dehydrogenase/oxidase
Enzyme 3 Synonyms
  1. Xanthine dehydrogenase
  2. XD
  3. Xanthine oxidase
  4. XO
  5. Xanthine oxidoreductase
Enzyme 3 Gene Name XDH
Enzyme 3 Protein Sequence >Xanthine dehydrogenase/oxidase
MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDR
LQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGI
VMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCC
MNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQAS
TLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFG
AACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISD
LNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSA
FKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKE
ELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLD
PTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRY
ENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDK
VTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDL
KKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKM
LGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGR
HPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGR
LCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKL
EGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGA
LLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAA
SVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLG
YSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAF
VQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAV
GEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVT
GVPENCKPWSVRV
Enzyme 3 Number of Residues 1333
Enzyme 3 Molecular Weight 146423.0
Enzyme 3 Theoretical pI 7.70
Enzyme 3 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • ion binding
  • iron ion binding
  • iron-sulfur cluster binding
  • metal cluster binding
  • metal ion binding
  • molybdenum ion binding
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH or CH2 groups
  • oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
  • oxidoreductase activity, acting on CH or CH2 groups, oxygen as acceptor
  • purine nucleoside binding
  • transition metal ion binding
  • xanthine dehydrogenase activity
  • xanthine oxidase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • xanthine + H2O + O2 = urate + H2O2 [RN:R02107]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID P47989 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name XDH_HUMAN Link Image
Enzyme 3 PDB ID 1V97 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >4002 bp
ATGACAGCAGACAAATTGGTTTTCTTTGTGAATGGCAGAAAGGTGGTGGAGAAAAATGCA
GATCCAGAGACAACCCTTTTGGCCTACCTGAGAAGAAAGTTGGGGCTGAGTGGAACCAAG
CTCGGCTGTGGAGAGGGGGGCTGCGGGGCTTGCACAGTGATGCTCTCCAAGTATGATCGT
CTGCAGAACAAGATCGTCCACTTTTCTGCCAATGCCTGCCTGGCCCCCATCTGCTCCTTG
CACCATGTTGCAGTGACAACTGTGGAAGGAATAGGAAGCACCAAGACGAGGCTGCATCCT
GTGCAGGAGAGAATTGCCAAAAGCCACGGCTCCCAGTGCGGGTTCTGCACCCCTGGCATC
GTCATGAGTATGTACACACTGCTCCGGAATCAGCCCGAGCCCACCATGGAGGAGATTGAG
AATGCCTTCCAAGGAAATCTGTGCCGCTGCACAGGCTACAGACCCATCCTCCAGGGCTTC
CGGACCTTTGCCAGGGATGGTGGATGCTGTGGAGGAGATGGGAATAATCCAAATTGCTGC
ATGAACCAGAAGAAAGACCACTCAGTCAGCCTCTCGCCATCTTTATTCAAACCAGAGGAG
TTCACGCCCCTGGATCCAACCCAGGAGCCCATTTTTCCCCCAGAGTTGCTGAGGCTGAAA
GACACTCCTCGGAAGCAGCTGCGATTTGAAGGGGAGCGTGTGACGTGGATACAGGCCTCA
ACCCTCAAGGAGCTGCTGGACCTCAAGGCTCAGCACCCTGACGCCAAGCTGGTCGTGGGG
AACACGGAGATTGGCATTGAGATGAAGTTCAAGAATATGCTGTTTCCTATGATTGTCTGC
CCAGCCTGGATCCCTGAGCTGAATTCGGTAGAACATGGACCCGACGGTATCTCCTTTGGA
GCTGCTTGCCCCCTGAGCATTGTGGAAAAAACCCTGGTGGATGCTGTTGCTAAGCTTCCT
GCCCAAAAGACAGAGGTGTTCAGAGGGGTCCTGGAGCAGCTGCGCTGGTTTGCTGGGAAG
CAAGTCAAGTCTGTGGCGTCCGTTGGAGGGAACATCATCACTGCCAGCCCCATCTCCGAC
CTCAACCCCGTGTTCATGGCCAGTGGGGCCAAGCTGACACTTGTGTCCAGAGGCACCAGG
AGAACTGTCCAGATGGACCACACCTTCTTCCCTGGCTACAGAAAGACCCTGCTGAGCCCG
GAGGAGATACTGCTCTCCATAGAGATCCCCTACAGCAGGGAGGGGGAGTATTTCTCAGCA
TTCAAGCAGGCCTCCCGGAGAGAAGATGACATTGCCAAGGTAACCAGTGGCATGAGAGTT
TTATTCAAGCCAGGAACCACAGAGGTACAGGAGCTGGCCCTTTGCTATGGTGGAATGGCC
AACAGAACCATCTCAGCCCTCAAGACCACTCAGAGGCAGCTTTCCAAGCTCTGGAAGGAG
GAGCTGCTGCAGGACGTGTGTGCAGGACTGGCAGAGGAGCTGCATCTGCCTCCCGATGCC
CCTGGTGGCATGGTGGACTTCCGGTGCACCCTCACCCTCAGCTTCTTCTTCAAGTTCTAC
CTGACAGTCCTTCAGAAGCTGGGCCAAGAGAACCTGGAAGACAAGTGTGGTAAACTGGAC
CCCACTTTCGCCAGTGCAACTTTACTGTTTCAGAAAGACCCCCCAGCCGATGTCCAGCTC
TTCCAAGAGGTGCCCAAGGGTCAGTCTGAGGAGGACATGGTGGGCCGGCCCCTGCCCCAC
CTGGCAGCGGACATGCAGGCCTCTGGTGAGGCCGTGTACTGTGACGACATTCCTCGCTAC
GAGAATGAGCTGTCTCTCCGGCTGGTCACCAGCACCCGGGCCCACGCCAAGATCAAGTCC
ATAGATACATCAGAAGCTAAGAAGGTTCCAGGGTTTGTTTGTTTCATTTCCGCTGATGAT
GTTCCTGGGAGTAACATAACTGGAATTTGTAATGATGAGACAGTCTTTGCGAAGGATAAG
GTTACTTGTGTTGGGCATATCATTGGTGCTGTGGTTGCTGACACCCCGGAACACACACAG
AGAGCTGCCCAAGGGGTGAAAATCACCTATGAAGAACTACCAGCCATTATCACAATTGAG
GATGCTATAAAGAACAACTCCTTTTATGGACCTGAGCTGAAGATCGAGAAAGGGGACCTA
AAGAAGGGGTTTTCCGAAGCAGATAATGTTGTGTCAGGGGAGATATACATCGGTGGCCAA
GAGCACTTCTACCTGGAGACTCACTGCACCATTGCTGTTCCAAAAGGCGAGGCAGGGGAG
ATGGAGCTCTTTGTGTCTACACAGAACACCATGAAGACCCAGAGCTTTGTTGCAAAAATG
TTGGGGGTTCCAGCAAACCGGATTGTGGTTCGAGTGAAGAGAATGGGAGGAGGCTTTGGA
GGCAAGGAGACCCGGAGCACTGTGGTGTCCACGGCAGTGGCCCTGGCTGCATATAAGACC
GGCCGCCCTGTGCGATGCATGCTGGACCGTGATGAGGACATGCTGATAACTGGTGGCAGA
CATCCCTTCCTGGCCAGATACAAGGTTGGCTTCATGAAGACTGGGACAGTTGTGGCTCTT
GAGGTGGACCACTTCAGCAATGTGGGGAACACCCAGGATCTCTCTCAGAGTATTATGGAA
CGAGCTTTATTCCACATGGACAACTGCTATAAAATCCCCAACATCCGGGGCACTGGGCGG
CTGTGCAAAACCAACCTTCCCTCCAACACGGCCTTCCGGGGCTTTGGGGGGCCCCAGGGG
ATGCTCATTGCCGAGTGCTGGATGAGTGAAGTTGCAGTGACCTGTGGGATGCCTGCAGAG
GAGGTGCGGAGAAAAAACCTGTACAAAGAAGGGGACCTGACACACTTCAACCAGAAGCTT
GAGGGTTTCACCTTGCCCAGATGCTGGGAAGAATGCCTAGCAAGCTCTCAGTATCATGCT
CGGAAGAGTGAGGTTGACAAGTTCAACAAGGAGAATTGTTGGAAAAAGAGAGGATTGTGC
ATAATTCCCACCAAGTTTGGAATAAGCTTCACAGTTCCTTTTCTGAATCAGGCAGGAGCC
CTACTTCATGTGTACACAGATGGCTCTGTGCTGCTGACCCACGGGGGGACTGAGATGGGC
CAAGGCCTTCATACCAAAATGGTCCAGGTGGCCAGTAGAGCTCTGAAAATCCCCACCTCT
AAGATTTATATCAGCGAGACAAGCACTAACACTGTGCCCAACACCTCTCCCACGGCTGCC
TCTGTCAGCGCTGACCTCAATGGACAGGCCGTCTATGCGGCTTGTCAGACCATCTTGAAA
AGGCTGGAACCCTACAAGAAGAAGAATCCCAGTGGCTCCTGGGAAGACTGGGTCACAGCT
GCCTACATGGACACAGTGAGCTTGTCTGCCACTGGGTTTTATAGAACACCCAATCTGGGC
TACAGCTTTGAGACTAACTCAGGGAACCCCTTCCACTACTTCAGCTATGGGGTGGCTTGC
TCTGAAGTAGAAATCGACTGCCTAACAGGAGATCATAAGAACCTCCGCACAGATATTGTC
ATGGATGTTGGCTCCAGTCTAAACCCTGCCATTGATATTGGACAGGTGGAAGGGGCATTT
GTCCAGGGCCTTGGCCTCTTCACCCTAGAGGAGCTACACTATTCCCCCGAGGGGAGCCTG
CACACCCGTGGCCCTAGCACCTACAAGATCCCGGCATTTGGCAGCATCCCCATTGAGTTC
AGGGTGTCCCTGCTCCGCGACTGCCCCAACAAGAAGGCCATCTATGCATCGAAGGCTGTT
GGAGAGCCGCCCCTCTTCCTGGCTGCTTCTATCTTCTTTGCCATCAAAGATGCCATCCGT
GCAGCTCGAGCTCAGCACACAGGTAATAACGTGAAGGAACTCTTCCGGCTAGACAGCCCT
GCCACCCCGGAGAAGATCCGCAATGCCTGCGTGGACAAGTTCACCACCCTGTGTGTCACT
GGTGTCCCAGAAAACTGCAAACCCTGGTCTGTGAGGGTCTAA
Enzyme 3 GenBank Gene ID D11456 Link Image
Enzyme 3 GeneCard ID XDH Link Image
Enzyme 3 GenAtlas ID XDH Link Image
Enzyme 3 HGNC ID HGNC:12805 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2p23.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T: Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene. 1993 Nov 15;133(2):279-84. [PubMed Link Image]
  2. Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1994 Mar 15;199(2):998-1004. [PubMed Link Image]
  3. Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1995 Oct 4;215(1):429. [PubMed Link Image]
  4. Saksela M, Raivio KO: Cloning and expression in vitro of human xanthine dehydrogenase/oxidase. Biochem J. 1996 Apr 1;315 ( Pt 1):235-9. [PubMed Link Image]
  5. 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 Link Image]
  6. Ichida K, Amaya Y, Kamatani N, Nishino T, Hosoya T, Sakai O: Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria. J Clin Invest. 1997 May 15;99(10):2391-7. [PubMed Link Image]
  7. Levartovsky D, Lagziel A, Sperling O, Liberman U, Yaron M, Hosoya T, Ichida K, Peretz H: XDH gene mutation is the underlying cause of classical xanthinuria: a second report. Kidney Int. 2000 Jun;57(6):2215-20. [PubMed Link Image]
  8. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed Link Image]
  9. Yamaguchi Y, Matsumura T, Ichida K, Okamoto K, Nishino T: Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate. J Biochem. 2007 Apr;141(4):513-24. Epub 2007 Feb 14. [PubMed Link Image]
  10. Sakamoto N, Yamamoto T, Moriwaki Y, Teranishi T, Toyoda M, Onishi Y, Kuroda S, Sakaguchi K, Fujisawa T, Maeda M, Hada T: Identification of a new point mutation in the human xanthine dehydrogenase gene responsible for a case of classical type I xanthinuria. Hum Genet. 2001 Apr;108(4):279-83. [PubMed Link Image]
  11. Gok F, Ichida K, Topaloglu R: Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria. Nephrol Dial Transplant. 2003 Nov;18(11):2278-83. [PubMed Link Image]
  12. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5433
Enzyme 4 Name Choline dehydrogenase, mitochondrial
Enzyme 4 Synonyms
  1. CDH
  2. CHD
Enzyme 4 Gene Name CHDH
Enzyme 4 Protein Sequence >Choline dehydrogenase, mitochondrial
MWCLLRGLGRPGALARGALGQQQSLGARALASAGSESRDEYSYVVVGAGSAGCVLAGRLT
EDPAERVLLLEAGPKDVLAGSKRLSWKIHMPAALVANLCDDRYNWCYHTEVQRGLDGRVL
YWPRGRVWGGSSSLNAMVYVRGHAEDYERWQRQGARGWDYAHCLPYFRKAQGHELGASRY
RGADGPLRVSRGKTNHPLHCAFLEATQQAGYPLTEDMNGFQQEGFGWMDMTIHEGKRWSA
ACAYLHPALSRTNLKAEAETLVSRVLFEGTRAVGVEYVKNGQSHRAYASKEVILSGGAIN
SPQLLMLSGIGNADDLKKLGIPVVCHLPGVGQNLQDHLEIYIQQACTRPITLHSAQKPLR
KVCIGLEWLWKFTGEGATAHLETGGFIRSQPGVPHPDIQFHFLPSQVIDHGRVPTQQEAY
QVHVGPMRGTSVGWLKLRSANPQDHPVIQPNYLSTETDIEDFRLCVKLTREIFAQEALAP
FRGKELQPGSHIQSDKEIDAFVRAKADSAYHPSCTCKMGQPSDPTAVVDPQTRVLGVENL
RVVDASIMPSMVSGNLNAPTIMIAEKAADIIKGQPALWDKDVPVYKPRTLATQR
Enzyme 4 Number of Residues 594
Enzyme 4 Molecular Weight 65358.0
Enzyme 4 Theoretical pI 8.36
Enzyme 4 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • purine nucleoside binding
Process
  • alcohol metabolic process
  • metabolic process
  • small molecule metabolic process
Component
Enzyme 4 General Function Involved in oxidoreductase activity, acting on CH-OH group of donors
Enzyme 4 Specific Function Choline + acceptor = betaine aldehyde + reduced acceptor
Enzyme 4 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 4 Reactions
  • choline + acceptor = betaine aldehyde + reduced acceptor [RN:R01025]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 21759795 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8NE62 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name CHDH_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1785 bp
ATGTGGTGTCTCCTACGAGGCCTGGGCCGGCCTGGAGCCCTGGCACGGGGAGCCCTGGGG
CAGCAGCAATCCCTGGGTGCCCGGGCCCTGGCCAGCGCAGGCTCTGAGAGCCGGGACGAG
TACAGCTATGTGGTGGTGGGCGCGGGCTCGGCGGGCTGCGTGCTGGCTGGGAGGCTCACG
GAGGACCCCGCCGAGCGCGTGCTGCTGCTGGAGGCCGGGCCCAAGGACGTGCGCGCGGGG
AGCAAGCGGCTCTCGTGGAAGATCCACATGCCCGCGGCCCTGGTGGCCAACCTGTGCGAC
GACAGGTACAACTGGTGCTACCACACAGAGGTGCAGCGGGGCCTGGACGGCCGCGTGCTG
TACTGGCCACGCGGCCGCGTCTGGGGTGGCTCCTCATCCCTCAATGCCATGGTCTACGTC
CGTGGGCACGCCGAGGACTACGAGCGCTGGCAGCGCCAGGGCGCCCGCGGCTGGGACTAC
GCGCACTGCCTGCCCTACTTCCGCAAGGCGCAGGGCCACGAGCTGGGCGCCAGCCGGTAC
CGGGGCGCCGATGGCCCGCTGCGGGTGTCCCGGGGCAAGACCAACCACCCGCTGCACTGC
GCATTCCTGGAGGCCACGCAGCAGGCCGGCTACCCGCTCACCGAGGACATGAATGGCTTC
CAGCAGGAGGGCTTCGGCTGGATGGACATGACCATCCATGAAGGCAAACGGTGGAGCGCA
GCCTGTGCCTACCTGCACCCAGCACTGAGCCGCACCAACCTCAAGGCCGAGGCCGAGACG
CTTGTGAGCAGGGTGCTATTTGAGGGCACCCGTGCAGTGGGCGTGGAGTATGTCAAGAAT
GGCCAGAGCCACAGGGCTTATGCCAGCAAGGAGGTGATTCTGAGTGGAGGTGCCATCAAC
TCTCCACAGCTGCTCATGCTCTCTGGCATCGGGAATGCTGATGACCTCAAGAAACTGGGC
ATCCCTGTGGTGTGCCACCTACCTGGGGTTGGCCAGAACCTGCAAGACCACCTGGAGATC
TACATTCAGCAGGCATGCACCCGCCCTATCACCCTCCATTCAGCACAGAAGCCCCTGCGG
AAGGTCTGCATTGGTCTGGAGTGGCTCTGGAAATTCACAGGGGAGGGAGCCACTGCCCAT
CTGGAAACAGGTGGGTTCATCCGCAGCCAGCCTGGGGTCCCCCACCCGGACATCCAGTTC
CATTTCCTGCCATCCCAAGTGATTGACCACGGGCGGGTCCCCACCCAGCAGGAGGCTTAC
CAGGTACATGTGGGGCCCATGCGGGGCACGAGTGTGGGCTGGCTCAAACTGAGAAGTGCC
AATCCCCAAGACCACCCTGTGATCCAGCCCAACTACTTGTCAACAGAAACTGATATTGAG
GATTTCCGTCTGTGTGTGAAGCTCACCAGAGAAATTTTTGCACAGGAAGCCCTGGCTCCG
TTCCGAGGGAAAGAGCTCCAGCCAGGAAGCCACATTCAGTCAGATAAAGAGATAGATGCC
TTTGTGCGGGCAAAAGCCGACAGCGCCTACCACCCCTCGTGCACCTGTAAGATGGGCCAG
CCCTCCGATCCCACTGCCGTGGTGGATCCGCAGACAAGGGTCCTCGGGGTGGAAAACCTC
AGGGTCGTCGATGCCTCCATCATGCCTAGCATGGTCAGCGGCAACCTGAACGCCCCCACA
ATCATGATCGCAGAGAAGGCAGCTGACATTATCAAGGGGCAGCCTGCACTCTGGGACAAA
GATGTCCCTGTCTACAAGCCCAGGACGCTGGCCACCCAGCGCTAA
Enzyme 4 GenBank Gene ID BC034502 Link Image
Enzyme 4 GeneCard ID CHDH Link Image
Enzyme 4 GenAtlas ID CHDH Link Image
Enzyme 4 HGNC ID HGNC:24288 Link Image
Enzyme 4 Chromosome Location 3
Enzyme 4 Locus 3p21.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5435
Enzyme 5 Name Dimethylglycine dehydrogenase, mitochondrial
Enzyme 5 Synonyms
  1. ME2GLYDH
Enzyme 5 Gene Name DMGDH
Enzyme 5 Protein Sequence >Dimethylglycine dehydrogenase, mitochondrial
MLRPGAQLLRGLLLRSCPLQGSPGRPRSVCGREGEEKPPLSAETQWKDRAETVIIGGGCV
GVSLAYHLAKAGMKDVVLLEKSELTAGSTWHAAGLTTYFHPGINLKKIHYDSIKLYEKLE
EETGQVVGFHQPGSIRLATTPVRVDEFKYQMTRTGWHATEQYLIEPEKIQEMFPLLNMNK
VLAGLYNPGDGHIDPYSLTMALAAGARKCGALLKYPAPVTSLKARSDGTWDVETPQGSMR
ANRIVNAAGFWAREVGKMIGLEHPLIPVQHQYVVTSTISEVKALKRELPVLRDLEGSYYL
RQERDGLLFGPYESQEKMKVQDSWVTNGVPPGFGKELFESDLDRIMEHIKAAMEMVPVLK
KADIINVVNGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGVGKYLSDWILHGEP
PFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYQRLES
KCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFEPVGSEYKQVMQRVAVTDLSPFGKF
NIKGQDSIRLLDHLFANVIPKVGFTNISHMLTPKGRVYAELTVSHQSPGEFLLITGSGSE
LHDLRWIEEEAVKGGYDVEIKNITDELGVLGVAGPQARKVLQKLTSEDLSDDVFKFLQTK
SLKVSNIPVTAIRISYTGELGWELYHRREDSVALYDAIMNAGQEEGIDNFGTYAMNALRL
EKAFRAWGLEMNCDTNPLEAGLEYFVKLNKPADFIGKQALKQIKAKGLKRRLVCLTLATD
DVDPEGNESIWYNGKVVGNTTSGSYSYSIQKSLAFAYVPVQLSEVGQQVEVELLGKNYPA
VIIQEPLVLTEPTRNRLQKKGGKDKT
Enzyme 5 Number of Residues 866
Enzyme 5 Molecular Weight 96810.1
Enzyme 5 Theoretical pI 7.69
Enzyme 5 GO Classification
Function
  • aminomethyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • oxidoreductase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glycine catabolic process
  • glycine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 5 General Function Involved in oxidoreductase activity
Enzyme 5 Specific Function N,N-dimethylglycine + acceptor + H(2)O = sarcosine + formaldehyde + reduced acceptor
Enzyme 5 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 5 Reactions
  • N,N-dimethylglycine + acceptor + H2O = sarcosine + formaldehyde + reduced acceptor [RN:R01565]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 24797151 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9UI17 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name M2GD_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2601 bp
ATGCTCCGTCCCGGCGCGCAGCTGCTGCGGGGCCTCCTGCTGCGGAGCTGCCCGCTGCAG
GGCTCCCCCGGGCGCCCGCGCTCTGTCTGCGGCCGGGAAGGAGAGGAAAAACCACCCTTA
TCTGCAGAAACACAATGGAAAGACAGAGCAGAAACAGTGATAATTGGAGGTGGCTGTGTT
GGTGTGAGTCTGGCTTATCACCTGGCCAAAGCAGGGATGAAAGATGTGGTCCTGCTGGAG
AAATCAGAGCTCACGGCTGGATCTACCTGGCACGCAGCAGGTTTAACAACTTACTTTCAT
CCTGGAATAAACTTGAAGAAAATACATTATGATAGCATCAAACTTTATGAGAAACTGGAA
GAAGAAACTGGTCAGGTGGTGGGATTCCATCAGCCAGGTAGTATCAGACTTGCTACCACC
CCTGTAAGGGTAGATGAATTTAAATATCAAATGACTCGGACTGGCTGGCATGCAACAGAA
CAGTATCTCATTGAACCTGAAAAAATTCAAGAGATGTTCCCTTTACTCAACATGAATAAG
GTTTTAGCTGGATTGTATAATCCTGGAGATGGTCACATTGATCCTTATTCTCTAACTATG
GCACTGGCTGCTGGGGCTAGGAAATGTGGTGCCCTTTTAAAATATCCTGCACCAGTAACT
TCTCTGAAAGCCAGGTCAGATGGAACATGGGACGTTGAAACACCACAGGGGTCTATGAGA
GCAAATAGAATTGTGAATGCTGCAGGATTTTGGGCTCGTGAAGTAGGTAAAATGATTGGA
CTAGAACATCCTCTCATTCCGGTTCAACATCAATATGTTGTTACATCGACTATATCTGAA
GTGAAAGCTTTGAAACGAGAACTGCCTGTGCTCCGTGACCTGGAAGGATCATATTATCTC
CGACAGGAAAGGGATGGGCTTTTGTTTGGTCCATATGAAAGTCAAGAGAAAATGAAAGTT
CAGGACTCCTGGGTCACCAATGGAGTTCCTCCAGGTTTTGGAAAGGAACTCTTTGAGTCT
GATCTAGATCGAATCATGGAACACATCAAAGCTGCCATGGAAATGGTTCCTGTCTTGAAA
AAGGCTGACATCATCAATGTTGTCAATGGTCCTATCACGTATTCTCCTGACATTCTGCCT
ATGGTGGGGCCCCATCAGGGGGTCAGAAACTACTGGGTGGCTATAGGCTTTGGATATGGC
ATAATCCACGCTGGTGGGGTAGGGAAATATCTCAGTGACTGGATCCTGCATGGAGAACCT
CCTTTTGATCTGATAGAATTGGATCCTAATCGCTATGGCAAATGGACAACAACCCAGTAC
ACTGAGGCCAAAGCAAGAGAATCATATGGATTCAACAATATTGTTGGTTATCCTAAAGAA
GAACGGTTTGCTGGGAGGCCGACTCAACGAGTCAGTGGGCTCTATCAAAGGCTGGAGTCT
AAGTGTTCCATGGGGTTCCATGCTGGCTGGGAGCAGCCGCACTGGTTCTACAAACCAGGC
CAGGACACTCAGTACAGGCCAAGTTTTCGCCGCACAAACTGGTTTGAGCCTGTGGGCTCG
GAGTATAAACAGGTTATGCAAAGAGTAGCGGTAACTGACCTATCACCATTTGGCAAGTTT
AACATCAAAGGCCAAGATTCCATTAGACTACTGGACCATCTCTTTGCAAATGTCATTCCA
AAGGTGGGTTTTACAAATATAAGTCACATGTTAACACCCAAGGGTCGAGTGTATGCTGAG
CTGACTGTTTCTCACCAATCTCCTGGGGAGTTTCTTTTAATTACTGGCTCTGGATCAGAA
CTTCATGATCTTAGATGGATTGAAGAAGAAGCAGTCAAAGGTGGATATGATGTTGAAATT
AAAAACATAACTGATGAGCTTGGAGTTCTTGGAGTTGCTGGGCCACAGGCAAGAAAGGTC
CTTCAGAAACTGACCTCTGAAGATCTTAGTGATGATGTTTTCAAGTTTCTTCAAACCAAG
TCCTTAAAGGTTTCCAACATTCCTGTCACTGCTATTAGGATATCTTATACTGGTGAGCTG
GGTTGGGAGCTGTATCACAGAAGAGAAGATTCTGTGGCGCTGTATGACGCTATCATGAAT
GCAGGCCAGGAGGAGGGAATCGACAATTTTGGAACCTATGCCATGAATGCCTTACGCCTG
GAGAAAGCCTTCAGAGCCTGGGGGTTAGAGATGAACTGTGATACAAATCCTTTGGAAGCT
GGACTGGAATATTTTGTGAAGTTAAATAAGCCAGCAGACTTCATAGGAAAGCAAGCACTG
AAACAGATTAAAGCCAAGGGGCTGAAACGAAGACTGGTCTGCCTCACCTTGGCAACGGAT
GATGTTGATCCAGAGGGAAATGAAAGCATCTGGTACAATGGCAAGGTGGTTGGCAACACG
ACATCTGGAAGCTATAGCTACAGCATCCAGAAGAGTCTGGCTTTCGCATATGTCCCTGTA
CAACTAAGTGAAGTGGGACAGCAAGTGGAAGTTGAACTATTAGGCAAAAATTACCCAGCA
GTCATCATACAAGAACCTTTGGTATTGACCGAACCAACCAGAAACCGGCTTCAGAAAAAA
GGTGGAAAGGACAAAACTTGA
Enzyme 5 GenBank Gene ID NM_013391.2 Link Image
Enzyme 5 GeneCard ID DMGDH Link Image
Enzyme 5 GenAtlas ID DMGDH Link Image
Enzyme 5 HGNC ID HGNC:24475 Link Image
Enzyme 5 Chromosome Location 5
Enzyme 5 Locus 5q14.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Binzak BA, Vockley JG, Jenkins RB, Vockley J: Structure and analysis of the human dimethylglycine dehydrogenase gene. Mol Genet Metab. 2000 Mar;69(3):181-7. [PubMed Link Image]
  2. Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J: Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency. Am J Hum Genet. 2001 Apr;68(4):839-47. Epub 2001 Feb 28. [PubMed Link Image]
  3. 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 Link Image]
  4. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  5. Moolenaar SH, Poggi-Bach J, Engelke UF, Corstiaensen JM, Heerschap A, de Jong JG, Binzak BA, Vockley J, Wevers RA: Defect in dimethylglycine dehydrogenase, a new inborn error of metabolism: NMR spectroscopy study. Clin Chem. 1999 Apr;45(4):459-64. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5449
Enzyme 6 Name Spermine synthase
Enzyme 6 Synonyms
  1. SPMSY
  2. Spermidine aminopropyltransferase
Enzyme 6 Gene Name SMS
Enzyme 6 Protein Sequence >Spermine synthase
MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFAN
LRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAI
DRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRA
IMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDV
LDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILD
LSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTV
WKKAKP
Enzyme 6 Number of Residues 366
Enzyme 6 Molecular Weight 41267.9
Enzyme 6 Theoretical pI 4.62
Enzyme 6 GO Classification
Function
  • catalytic activity
  • spermine synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
  • spermine biosynthetic process
Component
Enzyme 6 General Function Involved in spermine synthase activity
Enzyme 6 Specific Function Required for normal viability, growth and fertility
Enzyme 6 Pathways
Enzyme 6 Reactions
  • S-adenosylmethioninamine + spermidine = S-methyl-5'-thioadenosine + spermine [RN:R02869]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 2198557 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P52788 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name SPSY_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1101 bp
ATGGCAGCAGCACGGCACAGCACGCTCGACTTCATGCTCGGCGCCAAAGCTGATGGTGAG
ACCATTCTAAAAGGCCTCCAGTCCATTTTCCAGGAGCAGGGGATGGCGGAGTCGGTGCAC
ACCTGGCAGGACCATGGCTATTTAGCAACCTACACAAACAAGAACGGCAGCTTTGCCAAT
TTGAGAATTTACCCACATGGATTGGTGTTGCTGGACCTTCAGAGTTATGATGGTGATGCG
CAAGGCAAAGAAGAGATCGACAGTATTTTGAACAAAGTAGAGGAAAGAATGAAAGAATTG
AGTCAGGACAGTACTGGGCGGGTGAAACGATTACCACCCATAGTGCGAGGAGGAGCCATC
GACAGATACTGGCCCACCGCCGACGGGCGCCTGGTTGAATATGACATAGATGAAGTGGTA
TATGACGAAGATTCACCTTATCAAAATATAAAAATTCTACACTCGAAGCAGTTTGGAAAT
ATTCTCATCCTTAGTGGGGATGTTAATTTGGCAGAGAGTGATTTGGCATATACCCGGGCC
ATCATGGGCAGTGGCAAAGAAGATTACACTGGCAAAGATGTACTCATTCTGGGAGGTGGA
GACGGAGGCATATTGTGTGAAATAGTCAAACTAAAACCAAAGATGGTCACTATGGTAGAG
ATTGACCAAATGGTGATTGATGGGTGTAAGAAATACATGCGAAAAACGTGTGGCGATGTC
TTAGACAATCTTAAAGGAGACTGCTATCAGGTTCTAATAGAAGACTGTATCCCGGTACTG
AAGAGGTACGCCAAAGAAGGGAGAGAATTTGATTATGTGATTAATGATTTGACAGCTGTT
CCAATCTCCACGTCTCCAGAAGAAGATTCCACATGGGAGTTTCTCAGACTGATTCTTGAC
CTCTCAATGAAAGTGTTGAAACAGGATGGGAAATATTTTACACAGGGGAACTGTGTCAAT
CTGACAGAAGCACTGTCGCTCTATGAAGAACAGCTGGGGCGCCTGTATTGTCCTGTGGAA
TTTTCAAAGGAGATCGTCTGTGTCCCTTCATACTTGGAATTGTGGGTATTTTACACTGTT
TGGAAGAAAGCTAAACCCTGA
Enzyme 6 GenBank Gene ID AD001528 Link Image
Enzyme 6 GeneCard ID SMS Link Image
Enzyme 6 GenAtlas ID SMS Link Image
Enzyme 6 HGNC ID HGNC:11123 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Korhonen VP, Halmekyto M, Kauppinen L, Myohanen S, Wahlfors J, Keinanen T, Hyvonen T, Alhonen L, Eloranta T, Janne J: Molecular cloning of a cDNA encoding human spermine synthase. DNA Cell Biol. 1995 Oct;14(10):841-7. [PubMed Link Image]
  2. Grieff M, Whyte MP, Thakker RV, Mazzarella R: Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX. Genomics. 1997 Sep 1;44(2):227-31. [PubMed Link Image]
  3. 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 Link Image]
  4. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. Cason AL, Ikeguchi Y, Skinner C, Wood TC, Holden KR, Lubs HA, Martinez F, Simensen RJ, Stevenson RE, Pegg AE, Schwartz CE: X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome. Eur J Hum Genet. 2003 Dec;11(12):937-44. [PubMed Link Image]
  8. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  9. 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 Link Image]
  10. Wu H, Min J, Zeng H, McCloskey DE, Ikeguchi Y, Loppnau P, Michael AJ, Pegg AE, Plotnikov AN: Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J Biol Chem. 2008 Jun 6;283(23):16135-46. Epub 2008 Mar 26. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5450
Enzyme 7 Name Spermidine synthase
Enzyme 7 Synonyms
  1. SPDSY
  2. Putrescine aminopropyltransferase
Enzyme 7 Gene Name SRM
Enzyme 7 Protein Sequence >Spermidine synthase
MEPGPDGPAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYG
NVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV
VQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGP
AESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPT
YPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALND
VS
Enzyme 7 Number of Residues 302
Enzyme 7 Molecular Weight 33824.5
Enzyme 7 Theoretical pI 5.17
Enzyme 7 GO Classification
Function
  • catalytic activity
Process
Component
Enzyme 7 General Function Involved in catalytic activity
Enzyme 7 Specific Function S-adenosylmethioninamine + putrescine = 5'-S- methyl-5'-thioadenosine + spermidine
Enzyme 7 Pathways
Enzyme 7 Reactions
  • S-adenosylmethioninamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine [RN:R01920]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 56204109 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P19623 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name SPEE_HUMAN Link Image
Enzyme 7 PDB ID 1ZDZ Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >909 bp
ATGGAGCCCGGCCCCGACGGCCCCGCCGCCTCCGGCCCCGCCGCCATCCGCGAGGGCTGG
TTCCGCGAGACCTGCAGCCTGTGGCCCGGCCAGGCCCTGTCACTGCAGGTGGAGCAGCTG
CTCCACCACCGGCGCTCGCGCTACCAGGACATCCTCGTCTTCCGCAGTAAGACCTATGGC
AACGTGCTGGTGTTGGACGGTGTCATCCAGTGCACGGAGAGAGACGAGTTCTCCTACCAG
GAGATGATCGCCAACCTGCCTCTCTGCAGCCACCCCAACCCGCGAAAGGTGCTGATCATC
GGGGGCGGAGATGGAGGTGTCCTGCGGGAGGTGGTGAAGCACCCCTCCGTGGAGTCCGTG
GTCCAGTGTGAGATCGACGAGGATGTCATCCAAGTCTCCAAGAAGTTCCTGCCAGGCATG
GCCATTGGCTACTCTAGCTCGAAGCTGACCCTACATGTGGGTGACGGTTTTGAGTTCATG
AAACAGAATCAGGATGCCTTCGACGTGATCATCACTGACTCCTCAGACCCCATGGGCCCC
GCCGAAAGTCTCTTCAAGGAGTCCTATTACCAGCTCATGAAGACAGCCCTCAAGGAAGAT
GGTGTCCTCTGCTGCCAGGGCGAGTGCCAGTGGCTGCACCTGGACCTCATCAAGGAGATG
CGGCAGTTCTGCCAGTCCCTGTTCCCCGTGGTGGCCTATGCCTACTGCACCATCCCCACC
TACCCCAGCGGCCAGATCGGCTTCATGCTGTGCAGCAAGAACCCGAGCACGAACTTCCAG
GAGCCGGTGCAGCCGCTGACACAGCAGCAGGTGGCGCAGATGCAGCTGAAGTACTACAAC
TCCGACGTGCACCGCGCCGCCTTTGTGCTGCCCGAGTTTGCCCGCAAGGCCCTGAATGAT
GTGAGCTGA
Enzyme 7 GenBank Gene ID AL109811 Link Image
Enzyme 7 GeneCard ID SRM Link Image
Enzyme 7 GenAtlas ID SRM Link Image
Enzyme 7 HGNC ID HGNC:11296 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1p36-p22
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Wahlfors J, Alhonen L, Kauppinen L, Hyvonen T, Janne J, Eloranta TO: Human spermidine synthase: cloning and primary structure. DNA Cell Biol. 1990 Mar;9(2):103-10. [PubMed Link Image]
  2. Myohanen S, Kauppinen L, Wahlfors J, Alhonen L, Janne J: Human spermidine synthase gene: structure and chromosomal localization. DNA Cell Biol. 1991 Jul-Aug;10(6):467-74. [PubMed Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5526
Enzyme 8 Name 4-trimethylaminobutyraldehyde dehydrogenase
Enzyme 8 Synonyms
  1. TMABADH
  2. Aldehyde dehydrogenase E3 isozyme
  3. Aldehyde dehydrogenase family 9 member A1
  4. Gamma-aminobutyraldehyde dehydrogenase
  5. R-aminobutyraldehyde dehydrogenase
Enzyme 8 Gene Name ALDH9A1
Enzyme 8 Protein Sequence >4-trimethylaminobutyraldehyde dehydrogenase
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKA
AFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYY
AGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFK
PSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKI
MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI
LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIY
VPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLA
AGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQL
KTVCVEMGDVESAF
Enzyme 8 Number of Residues 494
Enzyme 8 Molecular Weight 53801.5
Enzyme 8 Theoretical pI 5.61
Enzyme 8 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 8 General Function Involved in oxidoreductase activity
Enzyme 8 Specific Function Converts gamma-trimethylaminobutyraldehyde into gamma- butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction
Enzyme 8 Pathways
Enzyme 8 Reactions
  • 4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH + 2 H+ [RN:R03283]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 7248636 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P49189 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name AL9A1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1485 bp
ATGAGCACTGGCACCTTCGTCGTGTCGCAGCCGCTCAATTACCGCGGCGGGGCCCGCGTG
GAGCCGGCGGACGCCTCCGGTACCGAGAAAGCTTTCGAGCCAGCAACCGGCCGAGTGATA
GCTACTTTCACATGTTCAGGAGAAAAGGAAGTAAATTTGGCTGTTCAAAATGCAAAGGCT
GCTTTTAAAATATGGAGTCAAAAATCTGGCATGGAGCGTTGCCGAATCCTTTTGGAGGCT
GCCAGGATAATAAGGGAACGGGAGGATGAAATTGCTACTATGGAGTGCATCAACAATGGC
AAGTCCATCTTTGAGGCCCGCTTGGACATTGACATTTCCTGGCAGTGCCTGGAGTATTAT
GCGGGCTTGGCTGCATCCATGGCTGGTGAACACATCCAGCTCCCAGGTGGATCGTTTGGT
TATACCAGAAGAGAACCACTTGGGGTATGTGTGGGAATAGGAGCATGGAACTACCCCTTT
CAGATTGCCTCTTGGAAGTCGGCTCCAGCATTAGCCTGTGGTAATGCCATGGTCTTTAAA
CCTTCTCCCTTTACACCTGTTTCTGCATTGCTACTGGCTGAAATCTACAGTGAGGCTGGT
GTACCTCCTGGGCTCTTCAATGTGGTGCAGGGAGGGGCTGCCACAGGCCAGTTTCTGTGT
CAGCATCCCGATGTGGCCAAAGTCTCCTTCACTGGAAGTGTGCCCACTGGCATGAAGATC
ATGGAGATGTCAGCTAAAGGAATCAAACCTGTTACCTTGGAACTTGGAGGCAAATCTCCA
CTCATCATCTTCTCAGACTGTGATATGAACAATGCTGTAAAGGGGGCGCTGATGGCCAAC
TTCCTCACACAAGGCCAGGTTTGCTGTAATGGCACAAGAGTATTTGTGCAGAAAGAAATT
CTTGATAAATTTACAGAGGAAGTGGTGAAACAGACCCAAAGGATTAAAATTGGAGATCCC
CTTCTGGAAGATACAAGGATGGGTCCACTCATCAACCGACCACACCTGGAGCGAGTCCTT
GGGTTTGTCAAAGTGGCAAAGGAGCAGGGTGCTAAAGTGTTATGTGGTGGAGATATATAT
GTACCTGAAGATCCCAAATTAAAGGATGGATATTACATGAGACCTTGTGTATTAACTAAT
TGCAGAGACGACATGACCTGTGTGAAGGAAGAGATCTTTGGGCCTGTTATGTCCATTTTA
TCATTTGACACTGAAGCTGAGGTTCTAGAAAGAGCCAATGATACCACTTTTGGACTAGCA
GCTGGCGTCTTTACCAGGGACATCCAACGGGCTCATAGAGTGGTAGCTGAGCTTCAGGCT
GGGACGTGCTTCATTAACAACTATAACGTCAGCCCAGTGGAGTTGCCCTTTGGTGGATAT
AAGAAGTCAGGATTTGGCAGAGAGAACGGCCGTGTGACAATCGAATATTATTCACAGCTG
AAGACTGTGTGTGTGGAGATGGGTGATGTGGAATCTGCTTTTTGA
Enzyme 8 GenBank Gene ID AF172093 Link Image
Enzyme 8 GeneCard ID ALDH9A1 Link Image
Enzyme 8 GenAtlas ID ALDH9A1 Link Image
Enzyme 8 HGNC ID HGNC:412 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1q23.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Lin SW, Chen JC, Hsu LC, Hsieh CL, Yoshida A: Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics. 1996 Jun 15;34(3):376-80. [PubMed Link Image]
  2. Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ: Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4. [PubMed Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. Kikonyogo A, Pietruszko R: Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem J. 1996 May 15;316 ( Pt 1):317-24. [PubMed Link Image]
  6. Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur J Biochem. 1993 Dec 1;218(2):311-20. [PubMed Link Image]
  7. Kurys G, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J Biol Chem. 1989 Mar 15;264(8):4715-21. [PubMed Link Image]
  8. 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 Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5619
Enzyme 9 Name Gamma-butyrobetaine dioxygenase
Enzyme 9 Synonyms
  1. Gamma-butyrobetaine hydroxylase
  2. Gamma-BBH
  3. Gamma-butyrobetaine,2-oxoglutarate dioxygenase
Enzyme 9 Gene Name BBOX1
Enzyme 9 Protein Sequence >Gamma-butyrobetaine dioxygenase
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDV
NIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSEL
QLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHT
WQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQK
LKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISR
HLEGAYADWDVVMSRLRILRQRVENGN
Enzyme 9 Number of Residues 387
Enzyme 9 Molecular Weight 44714.6
Enzyme 9 Theoretical pI 6.73
Enzyme 9 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
  • transition metal ion binding
Process
  • betaine metabolic process
  • carnitine biosynthetic process
  • carnitine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
Enzyme 9 General Function Involved in iron ion binding
Enzyme 9 Specific Function Catalyzes the formation of L-carnitine from gamma- butyrobetaine
Enzyme 9 Pathways
Enzyme 9 Reactions
  • 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2 [RN:R02397]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID O75936 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name BODG_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1164 bp
ATGGCTTGTACCATCCAAAAGGCAGAAGCACTTGACGGGGCTCATTTGATGCAGATCCTC
TGGTATGATGAGGAAGAGTCTCTCTACCCAGCTGTATGGTTGAGAGACAACTGTCCGTGC
TCTGATTGCTACCTGGATTCTGCAAAAGCACGGAAACTTCTAGTGGAAGCTCTTGATGTG
AACATTGGAATTAAAGGCTTGATATTTGACAGAAAAAAGGTGTACATCACATGGCCCGAT
GAGCATTACAGTGAATTCCAGGCTGATTGGCTGAAGAAAAGATGCTTTTCCAAGCAGGCC
AGAGCAAAGCTCCAAAGAGAATTGTTTTTTCCAGAATGCCAATACTGGGGCTCAGAGCTC
CAGCTACCCACTTTGGATTTTGAAGATGTTTTAAGATATGATGAACATGCATACAAGTGG
CTCTCCACCCTCAAGAAAGTAGGCATAGTAAGACTCACCGGAGCATCTGACAAACCAGGA
GAAGTTTCAAAACTTGGGAAAAGGATGGGTTTCCTCTATCTCACATTTTATGGACATACT
TGGCAAGTGCAAGACAAAATCGATGCAAACAATGTGGCTTACACAACTGGGAAGCTAAGC
TTTCACACTGATTATCCAGCCCTCCATCATCCACCTGGGGTTCAGCTTCTTCACTGCATA
AAGCAAACAGTCACAGGGGGTGATTCAGAAATTGTAGATGGGTTTAATGTGTGCCAAAAA
CTAAAGAAAAATAATCCTCAGGCATTCCAGATTTTGTCCTCTACCTTTGTGGACTTTACA
GACATTGGAGTGGATTACTGTGATTTTTCTGTACAATCAAAACATAAAATTATAGAGTTA
GATGATAAAGGCCAAGTGGTTCGCATCAACTTCAATAACGCAACTAGGGACACAATATTT
GATGTACCTGTTGAAAGAGTTCAGCCTTTTTATGCTGCTCTGAAGGAGTTTGTTGACCTC
ATGAACAGCAAAGAATCCAAGTTTACCTTCAAGATGAATCCAGGTGATGTGATTACTTTT
GATAACTGGCGCTTACTTCATGGCCGACGTAGCTATGAAGCAGGAACTGAGATATCCCGC
CATCTAGAAGGAGCTTATGCTGACTGGGATGTGGTCATGTCAAGGCTTCGTATCTTAAGG
CAGAGGGTGGAGAATGGAAACTGA
Enzyme 9 GenBank Gene ID AF082868 Link Image
Enzyme 9 GeneCard ID BBOX1 Link Image
Enzyme 9 GenAtlas ID BBOX1 Link Image
Enzyme 9 HGNC ID HGNC:964 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 11p14.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Vaz FM, van Gool S, Ofman R, Ijlst L, Wanders RJ: Carnitine biosynthesis: identification of the cDNA encoding human gamma-butyrobetaine hydroxylase. Biochem Biophys Res Commun. 1998 Sep 18;250(2):506-10. [PubMed Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5627
Enzyme 10 Name Amiloride-sensitive amine oxidase [copper-containing]
Enzyme 10 Synonyms
  1. DAO
  2. Diamine oxidase
  3. Amiloride-binding protein
  4. ABP
  5. Histaminase
  6. Kidney amine oxidase
  7. KAO
Enzyme 10 Gene Name ABP1
Enzyme 10 Protein Sequence >Amiloride-sensitive amine oxidase [copper-containing]
MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSS
TTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLP
GPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNG
KFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGP
RLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYG
GHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMH
ATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENIT
NPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRTYRLQIHSM
ADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWHPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRD
NGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV
Enzyme 10 Number of Residues 751
Enzyme 10 Molecular Weight 85377.1
Enzyme 10 Theoretical pI 7.10
Enzyme 10 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
Enzyme 10 General Function Involved in copper ion binding
Enzyme 10 Specific Function Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function
Enzyme 10 Pathways
Enzyme 10 Reactions
  • histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2 [RN:R02150]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-19
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 73486661 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P19801 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name ABP1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2256 bp
ATGCCGGCCCTGGGCTGGGCCGTGGCTGCCATCCTGATGCTGCAGACGGCCATGGCGGAG
CCCTCCCCGGGGACTCTGCCCAGGAAGGCAGGGGTGTTTTCAGACCTAAGCAACCAAGAG
CTGAAGGCAGTGCACAGCTTCCTCTGGTCCAAGAAGGAGCTGAGGCTGCAGCCCTCCAGT
ACCACCACCATGGCCAAGAACACCGTGTTTCTCATCGAGATGCTGCTGCCCAAGAAGTAC
CATGTGCTGAGGTTTCTGGATAAAGGTGAAAGGCATCCTGTGCGGGAAGCCCGTGCCGTC
ATCTTCTTTGGTGACCAGGAGCATCCCAATGTCACCGAGTTTGCTGTGGGGCCCCTGCCA
GGGCCCTGCTACATGCGAGCACTGTCCCCCAGGCCTGGGTACCAGTCCTCCTGGGCATCG
AGGCCCATCTCCACAGCAGAGTATGCCCTCCTCTACCACACCCTGCAGGAAGCCACCAAG
CCCCTGCATCAGTTCTTCCTCAATACCACAGGCTTCTCATTCCAAGACTGCCATGACAGA
TGCCTGGCCTTCACCGATGTGGCCCCCCGGGGTGTGGCTTCTGGCCAGCGCCGCAGTTGG
CTTATCATACAGCGCTATGTAGAAGGCTACTTTCTGCACCCCACTGGGCTGGAGCTCCTC
GTGGATCATGGGAGCACAGATGCTGGGCACTGGGCCGTGGAGCAGGTGTGGTACAACGGG
AAGTTCTATGGGAGCCCAGAGGAACTGGCTCGGAAGTATGCAGATGGAGAGGTGGACGTG
GTGGTCCTGGAGGACCCGCTGCCTGGGGGCAAGGGGCATGACAGCACAGAGGAGCCGCCC
CTCTTCTCCTCCCACAAGCCCCGCGGGGACTTCCCCAGCCCCATCCATGTGAGCGGCCCC
CGCTTGGTCCAGCCCCACGGCCCTCGCTTCAGGCTGGAGGGCAACGCTGTGCTCTACGGC
GGCTGGAGCTTTGCCTTCCGGCTGCGCTCCTCCTCCGGGCTGCAGGTCCTGAACGTGCAC
TTCGGCGGAGAGCGCATTGCCTATGAGGTCAGCGTGCAAGAGGCAGTGGCGCTGTATGGA
GGACACACACCTGCAGGCATGCAGACCAAGTACCTCGATGTCGGCTGGGGCCTGGGCAGC
GTCACTCATGAGTTAGCCCCCGGCATCGACTGCCCGGAGACCGCCACCTTCCTGGACACT
TTCCACTACTATGATGCCGATGACCCGGTCCATTATCCCCGAGCCCTCTGCCTCTTTGAA
ATGCCCACAGGGGTGCCCCTTCGGCGGCACTTTAATTCCAACTTTAAAGGTGGCTTCAAC
TTCTATGCGGGGCTGAAGGGCCAGGTGCTGGTGCTGCGGACAACTTCAACTGTCTACAAT
TATGATTACATTTGGGACTTTATCTTCTACCCCAACGGGGTGATGGAGGCCAAGATGCAT
GCCACTGGCTACGTCCACGCCACCTTCTACACCCCCGAGGGGCTGCGCCACGGCACTCGC
CTGCACACCCACCTGATTGGCAACATACACACTCACTTGGTGCACTACCGCGTAGACCTG
GATGTGGCAGGCACCAAGAACAGCTTCCAGACACTGCAGATGAAGCTAGAAAACATCACC
AACCCCTGGAGCCCAAGACACCGCGTGGTCCAGCCAACTCTGGAGCAGACGCAGTACTCC
TGGGAGCGCCAGGCGGCCTTCCGCTTCAAAAGGAAGCTGCCTAAGTACCTGCTCTTTACC
AGCCCCCAGGAGAACCCCTGGGGCCACAAGCGCACGTACCGCCTGCAGATCCACTCCATG
GCCGACCAGGTGCTGCCCCCAGGCTGGCAGGAGGAGCAGGCCATCACCTGGGCAAGGTAC
CCCCTGGCAGTGACCAAGTACCGGGAGTCGGAGCTGTGCAGCAGCAGCATCTACCACCAG
AACGACCCCTGGCACCCGCCCGTGGTCTTTGAGCAGTTTCTTCACAACAACGAGAACATT
GAAAATGAGGACCTGGTGGCCTGGGTGACGGTGGGCTTCCTGCACATCCCCCACTCAGAG
GACATTCCCAACACAGCCACACCTGGGAACTCCGTGGGCTTCCTGCTCCGGCCATTCAAC
TTCTTCCCAGAGGACCCCTCCCTGGCATCCAGAGACACTGTGATCGTGTGGCCTCGGGAC
AACGGCCCCAACTACGTCCAGCGCTGGATCCCTGAGGACAGGGACTGCTCGATGCCTCCC
CCTTTTAGCTACAATGGGACCTATAGACCTGTGTGA
Enzyme 10 GenBank Gene ID NM_001091.2 Link Image
Enzyme 10 GeneCard ID ABP1 Link Image
Enzyme 10 GenAtlas ID ABP1 Link Image
Enzyme 10 HGNC ID HGNC:80 Link Image
Enzyme 10 Chromosome Location 7
Enzyme 10 Locus 7q34-q36
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Barbry P, Champe M, Chassande O, Munemitsu S, Champigny G, Lingueglia E, Maes P, Frelin C, Tartar A, Ullrich A, et al.: Human kidney amiloride-binding protein: cDNA structure and functional expression. Proc Natl Acad Sci U S A. 1990 Oct;87(19):7347-51. [PubMed Link Image]
  2. Chassande O, Renard S, Barbry P, Lazdunski M: The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter. J Biol Chem. 1994 May 20;269(20):14484-9. [PubMed Link Image]
  3. Zhang X, Kim J, McIntire WS: cDNA sequences of variant forms of human placenta diamine oxidase. Biochem Genet. 1995 Aug;33(7-8):261-8. [PubMed Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. Novotny WF, Chassande O, Baker M, Lazdunski M, Barbry P: Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues. J Biol Chem. 1994 Apr 1;269(13):9921-5. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5634
Enzyme 11 Name S-methyl-5'-thioadenosine phosphorylase
Enzyme 11 Synonyms
  1. 5'-methylthioadenosine phosphorylase
  2. MTA phosphorylase
  3. MTAPase
Enzyme 11 Gene Name MTAP
Enzyme 11 Protein Sequence >S-methyl-5'-thioadenosine phosphorylase
MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLAR
HGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMR
PQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR
AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTL
KENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH
Enzyme 11 Number of Residues 283
Enzyme 11 Molecular Weight 31235.8
Enzyme 11 Theoretical pI 7.21
Enzyme 11 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside metabolic process
Component
Enzyme 11 General Function Involved in transferase activity, transferring pentosyl groups
Enzyme 11 Specific Function Plays a major role in polyamine metabolism and is important for the salvage of both adenine and methionine
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate [RN:R01402]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 847724 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q13126 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name MTAP_HUMAN Link Image
Enzyme 11 PDB ID 1SD2 Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >852 bp
ATGGCCTCTGGCACCACCACCACCGCCGTGAAGATTGGAATAATTGGTGGAACAGGCCTG
GATGATCCAGAAATTTTAGAAGGAAGAACTGAAAAATATGTGGATACTCCATTTGGCAAG
CCATCTGATGCCTTAATTTTGGGGAAGATAAAAAATGTTGATTGCATCCTCCTTGCAAGG
CATGGAAGGCAGCACACCATCATGCCTTCAAAGGTCAACTACCAGGCGAACATCTGGGCT
TTGAAGGAAGAGGGCTGTACACATGTCATAGTGACCACAGCTTGTGGCTCCTTGAGGGAG
GAGATTCAGCCCGGCGATATTGTCATTATTGATCAGTTCATTGACAGGACCACTATGAGA
CCTCAGTCCTTCTATGATGGAAGTCATTCTTGTGCCAGAGGAGTGTGCCATATTCCAATG
GCTGAGCCGTTTTGCCCCAAAACGAGAGAGGTTCTTATAGAGACTGCTAAGAAGCTAGGA
CTCCGGTGCCACTCAAAGGGGACAATGGTCACAATCGAGGGACCTCGTTTTAGCTCCCGG
GCAGAAAGCTTCATGTTCCGCACCTGGGGGGCGGATGTTATCAACATGACCACAGTTCCA
GAGGTGGTTCTTGCTAAGGAGGCTGGAATTTGTTACGCAAGTATCGCCATGGCGACAGAT
TATGACTGCTGGAAGGAGCACGAGGAAGCAGTTTCGGTGGACCGGGTCTTAAAGACCCTG
AAAGAAAACGCTAATAAAGCCAAAAGCTTACTGCTCACTACCATACCTCAGATAGGGTCC
ACAGAATGGTCAGAAACCCTCCATAACCTGAAGAATATGGCCCAGTTTTCTGTTTTATTA
CCAAGACATTAA
Enzyme 11 GenBank Gene ID U22233 Link Image
Enzyme 11 GeneCard ID MTAP Link Image
Enzyme 11 GenAtlas ID MTAP Link Image
Enzyme 11 HGNC ID HGNC:7413 Link Image
Enzyme 11 Chromosome Location 9
Enzyme 11 Locus 9p21
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Olopade OI, Pomykala HM, Hagos F, Sveen LW, Espinosa R 3rd, Dreyling MH, Gursky S, Stadler WM, Le Beau MM, Bohlander SK: Construction of a 2.8-megabase yeast artificial chromosome contig and cloning of the human methylthioadenosine phosphorylase gene from the tumor suppressor region on 9p21. Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6489-93. [PubMed Link Image]
  2. Nobori T, Takabayashi K, Tran P, Orvis L, Batova A, Yu AL, Carson DA: Genomic cloning of methylthioadenosine phosphorylase: a purine metabolic enzyme deficient in multiple different cancers. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):6203-8. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. 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 Link Image]
  5. Della Ragione F, Takabayashi K, Mastropietro S, Mercurio C, Oliva A, Russo GL, Della Pietra V, Borriello A, Nobori T, Carson DA, Zappia V: Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA. Biochem Biophys Res Commun. 1996 Jun 25;223(3):514-9. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. 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 Link Image]
  8. Appleby TC, Erion MD, Ealick SE: The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis. Structure. 1999 Jun 15;7(6):629-41. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5657
Enzyme 12 Name S-adenosylmethionine decarboxylase proenzyme
Enzyme 12 Synonyms
  1. AdoMetDC
  2. SAMDC
  3. S-adenosylmethionine decarboxylase alpha chain
  4. S-adenosylmethionine decarboxylase beta chain
Enzyme 12 Gene Name AMD1
Enzyme 12 Protein Sequence >S-adenosylmethionine decarboxylase proenzyme
MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQ
EAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKP
SHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEIL
MSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYW
TIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQ
KIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS
Enzyme 12 Number of Residues 334
Enzyme 12 Molecular Weight 38339.3
Enzyme 12 Theoretical pI 5.78
Enzyme 12 GO Classification
Function
  • adenosylmethionine decarboxylase activity
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
  • spermidine biosynthetic process
  • spermine biosynthetic process
Component
Enzyme 12 General Function Involved in adenosylmethionine decarboxylase activity
Enzyme 12 Specific Function S-adenosyl-L-methionine = (5-deoxy-5- adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2)
Enzyme 12 Pathways
Enzyme 12 Reactions
  • S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2 [RN:R00178]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 55664717 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P17707 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name DCAM_HUMAN Link Image
Enzyme 12 PDB ID 1MSV Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1005 bp
ATGGAAGCTGCACATTTTTTCGAAGGGACCGAGAAGCTGCTGGAGGTTTGGTTCTCCCGG
CAGCAGCCCGACGCAAACCAAGGATCTGGGGATCTTCGCACTATCCCAAGATCTGAGTGG
GACATACTTTTGAAGGATGTGCAATGTTCAATCATAAGTGTGACAAAAACTGACAAGCAG
GAAGCTTATGTACTCAGTGAGAGTAGCATGTTTGTCTCCAAGAGACGTTTCATTTTGAAG
ACATGTGGTACCACCCTCTTGCTGAAAGCACTGGTTCCCCTGTTGAAGCTTGCTAGGGAT
TACAGTGGGTTTGACTCAATTCAAAGCTTCTTTTATTCTCGTAAGAATTTCATGAAGCCT
TCTCACCAAGGGTACCCACACCGGAATTTCCAGGAAGAAATAGAGTTTCTTAATGCAATT
TTCCCAAATGGAGCAGCATATTGTATGGGACGTATGAATTCTGACTGTTGGTACTTATAT
ACTCTGGATTTCCCAGAGAGTCGGGTAATCAGTCAGCCAGATCAAACCTTGGAAATTCTG
ATGAGTGAGCTTGACCCAGCAGTTATGGACCAGTTCTACATGAAAGATGGTGTTACTGCA
AAGGATGTCACTCGTGAGAGTGGAATTCGTGACCTGATACCAGGTTCTGTCATTGATGCC
ACAATGTTCAATCCTTGTGGGTATTCGATGAATGGAATGAAATCGGATGGAACTTATTGG
ACTATTCACATCACTCCAGAACCAGAATTTTCTTATGTTAGCTTTGAAACAAACTTAAGT
CAGACCTCCTATGATGACCTGATCAGGAAAGTTGTAGAAGTCTTCAAGCCAGGAAAATTT
GTGACCACCTTGTTTGTTAATCAGAGTTCTAAATGTCGCACAGTGCTTGCTTCGCCCCAG
AAGATTGAAGGTTTTAAGCGTCTTGATTGCCAGAGTGCTATGTTCAATGATTACAATTTT
GTTTTTACCAGTTTTGCTAAGAAGCAGCAACAACAGCAGAGTTGA
Enzyme 12 GenBank Gene ID AL357515 Link Image
Enzyme 12 GeneCard ID AMD1 Link Image
Enzyme 12 GenAtlas ID AMD1 Link Image
Enzyme 12 HGNC ID HGNC:457 Link Image
Enzyme 12 Chromosome Location 6
Enzyme 12 Locus 6q21
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Pajunen A, Crozat A, Janne OA, Ihalainen R, Laitinen PH, Stanley B, Madhubala R, Pegg AE: Structure and regulation of mammalian S-adenosylmethionine decarboxylase. J Biol Chem. 1988 Nov 15;263(32):17040-9. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. 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 Link Image]
  4. Stanley BA, Pegg AE: Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity. J Biol Chem. 1991 Oct 5;266(28):18502-6. [PubMed Link Image]
  5. Xiong H, Pegg AE: Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate. J Biol Chem. 1999 Dec 3;274(49):35059-66. [PubMed Link Image]
  6. Xiong H, Stanley BA, Pegg AE: Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase. Biochemistry. 1999 Feb 23;38(8):2462-70. [PubMed Link Image]
  7. 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 Link Image]
  8. Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE: The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold. Structure. 1999 May;7(5):583-95. [PubMed Link Image]
  9. Tolbert WD, Ekstrom JL, Mathews II, Secrist JA 3rd, Kapoor P, Pegg AE, Ealick SE: The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase. Biochemistry. 2001 Aug 14;40(32):9484-94. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5702
Enzyme 13 Name Glycine amidinotransferase, mitochondrial
Enzyme 13 Synonyms
  1. L-arginine:glycine amidinotransferase
  2. Transamidinase
Enzyme 13 Gene Name GATM
Enzyme 13 Protein Sequence >Glycine amidinotransferase, mitochondrial
MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQSTQAATASSRNSCAADDKATEPL
PKDCPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGHYFPKDHL
KKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEII
EAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTAPKPTMADELYNQDYPIHSVEDRHKLAA
QGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPN
PMHIDATFNIIGPGIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSM
NVLMLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQS
YLD
Enzyme 13 Number of Residues 423
Enzyme 13 Molecular Weight 48455.0
Enzyme 13 Theoretical pI 8.15
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Amino acid transport and metabolism
Enzyme 13 Specific Function Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. May be involved in the response to heart failure by elevating local creatine synthesis
Enzyme 13 Pathways
  • Arginine and Proline Metabolism (map00330 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 13 Reactions
  • L-arginine + glycine = L-ornithine + guanidinoacetate [RN:R00565]
Enzyme 13 Pfam Domain Function Not Available
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID P50440 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name GATM_HUMAN Link Image
Enzyme 13 PDB ID 3JDW Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1272 bp
ATGCTGCGGGTGCGGTGTCTGCGCGGCGGGAGCCGCGGCGCCGAGGCGGTGCACTACATC
GGATCTCGGCTTGGACGAACCTTGACAGGATGGGTGCAGCGAACTTTCCAGAGCACCCAG
GCAGCTACGGCTTCCTCCCGGAACTCCTGTGCAGCTGACGACAAAGCCACTGAGCCTCTG
CCCAAGGACTGCCCTGTCTCTTCTTACAACGAATGGGACCCCTTAGAGGAAGTGATAGTG
GGCAGAGCAGAAAACGCCTGTGTTCCACCGTTCACCATCGAGGTGAAGGCCAACACATAT
GAAAAGTACTGGCCATTTTACCAGAAGCAAGGAGGGCATTATTTTCCCAAAGATCATTTG
AAAAAGGCTGTTGCTGAAATTGAAGAAATGTGCAATATTTTAAAAACGGAAGGAGTGACA
GTAAGGAGGCCTGACCCCATTGACTGGTCATTGAAGTATAAAACTCCTGATTTTGAGTCT
ACGGGTTTATACAGTGCAATGCCTCGAGACATCCTGATAGTTGTGGGCAATGAGATTATC
GAGGCTCCCATGGCATGGCGTTCACGCTTCTTTGAGTACCGAGCGTACAGGTCAATTATC
AAAGACTACTTCCACCGTGGCGCCAAGTGGACAACAGCTCCTAAGCCCACAATGGCTGAT
GAGCTTTATAACCAGGATTATCCCATCCACTCTGTAGAAGACAGACACAAATTGGCTGCT
CAGGGAAAATTTGTGACAACTGAGTTTGAGCCATGCTTTGATGCTGCTGACTTCATTCGA
GCTGGAAGAGATATTTTTGCACAGAGAAGCCAGGTTACAAACTACCTAGGCATTGAATGG
ATGCGTAGGCATCTTGCTCCAGACTACAGAGTGCATATCATCTCCTTTAAAGATCCCAAT
CCCATGCATATTGATGCTACCTTCAACATCATTGGACCTGGTATTGTGCTTTCCAACCCT
GACCGACCATGTCACCAGATTGATCTTTTCAAGAAAGCAGGATGGACTATCATTACTCCT
CCAACACCAATCATCCCAGACGATCATCCACTCTGGATGTCATCCAAATGGCTTTCCATG
AATGTCTTAATGCTAGATGAAAAACGTGTTATGGTGGATGCCAATGAAGTTCCAATTCAA
AAGATGTTTGAAAAGCTGGGTATCACTACCATTAAAGTTAACATTCGTAATGCCAATTCC
CTGGGAGGAGGCTTCCATTGCTGGACCTGCGATGTCCGGCGCCGAGGCACCCTACAGTCC
TACTTGGACTGA
Enzyme 13 GenBank Gene ID S68805 Link Image
Enzyme 13 GeneCard ID GATM Link Image
Enzyme 13 GenAtlas ID GATM Link Image
Enzyme 13 HGNC ID HGNC:4175 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 15q21.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Humm A, Huber R, Mann K: The amino acid sequences of human and pig L-arginine:glycine amidinotransferase. FEBS Lett. 1994 Feb 14;339(1-2):101-7. [PubMed Link Image]
  2. 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 Link Image]
  3. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  4. 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 Link Image]
  5. Gross MD, Eggen MA, Simon AM, Van Pilsum JF: The purification and characterization of human kidney L-arginine:glycine amidinotransferase. Arch Biochem Biophys. 1986 Dec;251(2):747-55. [PubMed Link Image]
  6. Humm A, Fritsche E, Mann K, Gohl M, Huber R: Recombinant expression and isolation of human L-arginine:glycine amidinotransferase and identification of its active-site cysteine residue. Biochem J. 1997 Mar 15;322 ( Pt 3):771-6. [PubMed Link Image]
  7. Humm A, Fritsche E, Steinbacher S: Structure and reaction mechanism of L-arginine:glycine amidinotransferase. Biol Chem. 1997 Mar-Apr;378(3-4):193-7. [PubMed Link Image]
  8. Cullen ME, Yuen AH, Felkin LE, Smolenski RT, Hall JL, Grindle S, Miller LW, Birks EJ, Yacoub MH, Barton PJ: Myocardial expression of the arginine:glycine amidinotransferase gene is elevated in heart failure and normalized after recovery: potential implications for local creatine synthesis. Circulation. 2006 Jul 4;114(1 Suppl):I16-20. [PubMed Link Image]
  9. McMinn J, Wei M, Schupf N, Cusmai J, Johnson EB, Smith AC, Weksberg R, Thaker HM, Tycko B: Unbalanced placental expression of imprinted genes in human intrauterine growth restriction. Placenta. 2006 Jun-Jul;27(6-7):540-9. Epub 2005 Aug 24. [PubMed Link Image]
  10. Monk D, Arnaud P, Apostolidou S, Hills FA, Kelsey G, Stanier P, Feil R, Moore GE: Limited evolutionary conservation of imprinting in the human placenta. Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6623-8. Epub 2006 Apr 13. [PubMed Link Image]
  11. 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 Link Image]
  12. Humm A, Fritsche E, Steinbacher S, Huber R: Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. EMBO J. 1997 Jun 16;16(12):3373-85. [PubMed Link Image]
  13. Fritsche E, Humm A, Huber R: Substrate binding and catalysis by L-arginine:glycine amidinotransferase--a mutagenesis and crystallographic study. Eur J Biochem. 1997 Jul 15;247(2):483-90. [PubMed Link Image]
  14. Fritsche E, Humm A, Huber R: The ligand-induced structural changes of human L-Arginine:Glycine amidinotransferase. A mutational and crystallographic study. J Biol Chem. 1999 Jan 29;274(5):3026-32. [PubMed Link Image]
  15. Item CB, Stockler-Ipsiroglu S, Stromberger C, Muhl A, Alessandri MG, Bianchi MC, Tosetti M, Fornai F, Cioni G: Arginine:glycine amidinotransferase deficiency: the third inborn error of creatine metabolism in humans. Am J Hum Genet. 2001 Nov;69(5):1127-33. Epub 2001 Sep 10. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5831
Enzyme 14 Name Betaine--homocysteine S-methyltransferase 1
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name BHMT
Enzyme 14 Protein Sequence >Betaine--homocysteine S-methyltransferase 1
MPPVGGKKAKKGILERLNAGEIVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLH
REFLRAGSNVMQTFTFYASEDKLENRGNYVLEKISGQEVNEAACDIARQVADEGDALVAG
GVSQTPSYLSCKSETEVKKVFLQQLEVFMKKNVDFLIAEYFEHVEEAVWAVETLIASGKP
VAATMCIGPEGDLHGVPPGECAVRLVKAGASIIGVNCHFDPTISLKTVKLMKEGLEAARL
KAHLMSQPLAYHTPDCNKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCC
GFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWVRARARKEYWENLRIASG
RPYNPSMSKPDGWGVTKGTAELMQQKEATTEQQLKELFEKQKFKSQ
Enzyme 14 Number of Residues 406
Enzyme 14 Molecular Weight 44998.2
Enzyme 14 Theoretical pI 7.04
Enzyme 14 GO Classification
Function
  • S-methyltransferase activity
  • betaine-homocysteine S-methyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • homocysteine S-methyltransferase activity
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine biosynthetic process
  • sulfur amino acid biosynthetic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 14 General Function Involved in zinc ion binding
Enzyme 14 Specific Function Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline
Enzyme 14 Pathways
Enzyme 14 Reactions
  • trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine [RN:R02821]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 4530461 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q93088 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name BHMT1_HUMAN Link Image
Enzyme 14 PDB ID 1LT8 Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1221 bp
ATGCCACCCGTTGGGGGCAAAAAGGCCAAGAAGGGCATCCTAGAACGTTTAAATGCTGGA
GAGATTGTGATTGGAGATGGAGGGTTTGTCTTTGCACTGGAGAAGAGGGGCTACGTAAAG
GCAGGACCCTGGACTCCTGAAGCTGCTGTGGAGCACCCAGAAGCAGTTCGCCAGCTTCAT
CGAGAGTTCCTCAGAGCTGGCTCAAACGTCATGCAGACCTTCACCTTCTATGCGAGTGAA
GACAAGCTGGAGAACAGGGGCAACTATGTCTTAGAGAAGATATCTGGGCAGGAAGTCAAT
GAAGCTGCTTGCGACATCGCCCGACAAGTGGCTGATGAAGGAGATGCTTTGGTAGCAGGA
GGAGTGAGTCAGACACCTTCATACCTTAGCTGCAAGAGTGAAACTGAAGTCAAAAAAGTA
TTTCTGCAACAGTTAGAGGTCTTTATGAAGAAGAACGTGGACTTCTTGATTGCAGAGTAT
TTTGAACACGTTGAAGAAGCTGTGTGGGCAGTTGAAACCTTGATAGCATCCGGTAAACCT
GTGGCAGCAACCATGTGCATTGGCCCAGAAGGAGATTTGCATGGCGTGCCCCCCGGCGAG
TGTGCAGTGCGCCTGGTGAAAGCAGGAGCATCCATCATTGGTGTGAACTGCCACTTTGAC
CCCACCATTAGTTTAAAAACAGTGAAGCTCATGAAGGAGGGCTTGGAGGCTGCCCGACTG
AAAGCTCACCTGATGAGCCAGCCCTTGGCTTACCACACTCCTGACTGCAACAAGCAGGGA
TTCATCGATCTCCCAGAATTCCCATTTGGACTGGAACCCAGAGTTGCCACCAGATGGGAT
ATTCAAAAATACGCCAGAGAGGCCTACAACCTGGGGGTCAGGTACATTGGCGGGTGCTGT
GGATTTGAGCCCTACCACATCAGGGCAATTGCAGAGGAGCTGGCCCCAGAAAGGGGCTTT
TTGCCACCAGCTTCAGAAAAACATGGCAGCTGGGGAAGTGGTTTGGACATGCACACCAAA
CCCTGGGTTAGAGCAAGGGCCAGGAAGGAATACTGGGAGAATCTTCGGATAGCCTCAGGC
CGGCCATACAACCCTTCAATGTCAAAGCCAGATGGCTGGGGAGTGACCAAAGGAACAGCC
GAGCTGATGCAGCAGAAAGAAGCCACAACTGAGCAGCAGCTGAAAGAGCTCTTTGAAAAA
CAAAAATTCAAATCACAGTAG
Enzyme 14 GenBank Gene ID AF118378 Link Image
Enzyme 14 GeneCard ID BHMT Link Image
Enzyme 14 GenAtlas ID BHMT Link Image
Enzyme 14 HGNC ID HGNC:1047 Link Image
Enzyme 14 Chromosome Location 5
Enzyme 14 Locus 5q13.1-q15
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Garrow TA: Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase. J Biol Chem. 1996 Sep 13;271(37):22831-8. [PubMed Link Image]
  2. Park EI, Garrow TA: Interaction between dietary methionine and methyl donor intake on rat liver betaine-homocysteine methyltransferase gene expression and organization of the human gene. J Biol Chem. 1999 Mar 19;274(12):7816-24. [PubMed Link Image]
  3. 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 Link Image]
  4. Sunden SL, Renduchintala MS, Park EI, Miklasz SD, Garrow TA: Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene. Arch Biochem Biophys. 1997 Sep 1;345(1):171-4. [PubMed Link Image]
  5. Millian NS, Garrow TA: Human betaine-homocysteine methyltransferase is a zinc metalloenzyme. Arch Biochem Biophys. 1998 Aug 1;356(1):93-8. [PubMed Link Image]
  6. Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML: Betaine-homocysteine methyltransferase: zinc in a distorted barrel. Structure. 2002 Sep;10(9):1159-71. [PubMed Link Image]
  7. Weisberg IS, Park E, Ballman KV, Berger P, Nunn M, Suh DS, Breksa AP 3rd, Garrow TA, Rozen R: Investigations of a common genetic variant in betaine-homocysteine methyltransferase (BHMT) in coronary artery disease. Atherosclerosis. 2003 Apr;167(2):205-14. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6073
Enzyme 15 Name Sarcosine dehydrogenase, mitochondrial
Enzyme 15 Synonyms
  1. SarDH
  2. BPR-2
Enzyme 15 Gene Name SARDH
Enzyme 15 Protein Sequence >Sarcosine dehydrogenase, mitochondrial
MASLSRALRVAAAHPRQSPTRGMGPCNLSSAAGPTAEKSVPYQRTLKEGQGTSVVAQGPS
RPLPSTANVVVIGGGSLGCQTLYHLAKLGMSGAVLLERERLTSGTTWHTAGLLWQLRPSD
VEVELLAHTRRVVSRELEEETGLHTGWIQNGGLFIASNRQRLDEYKRLMSLGKAYGVESH
VLSPAETKTLYPLMNVDDLYGTLYVPHDGTMDPAGTCTTLARAASARGAQVIENCPVTGI
RVWTDDFGVRRVAGVETQHGSIQTPCVVNCAGVWASAVGRMAGVKVPLVAMHHAYVVTER
IEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWEVFTQH
IEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGC
GQELAHWIIHGRPEKDMHGYDIRRFHHSLTDHPRWIRERSHESYAKNYSVVFPHDEPLAG
RNMRRDPLHEELLGQGCVFQERHGWERPGWFHPRGPAPVLEYDYYGAYGSRAHEDYAYRR
LLADEYTFAFPPHHDTIKKECLACRGAAAVFDMSYFGKFYLVGLDARKAADWLFSADVSR
PPGSTVYTCMLNHRGGTESDLTVSRLAPSHQASPLAPAFEGDGYYLAMGGAVAQHNWSHI
TTVLQDQKSQCQLIDSSEDLGMISIQGPASRAILQEVLDADLSNEAFPFSTHKLLRAAGH
LVRAMRLSFVGELGWELHIPKASCVPVYRAVMAAGAKHGLINAGYRAIDSLSIEKGYRHW
HADLRPDDSPLEAGLAFTCKLKSPVPFLGREALEQQRAAGLRRRLVCFTMEDKVPMFGLE
AIWRNGQVVGHVRRADFGFAIDKTIAYGYIHDPSGGPVSLDFVKSGDYALERMGVTYGAQ
AHLKSPFDPNNKRVKGIY
Enzyme 15 Number of Residues 918
Enzyme 15 Molecular Weight 101036.0
Enzyme 15 Theoretical pI 7.26
Enzyme 15 GO Classification
Function
  • aminomethyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • oxidoreductase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glycine catabolic process
  • glycine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 15 General Function Involved in oxidoreductase activity
Enzyme 15 Specific Function Sarcosine + acceptor + H(2)O = glycine + formaldehyde + reduced acceptor
Enzyme 15 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 15 Reactions
  • sarcosine + acceptor + H2O = glycine + formaldehyde + reduced acceptor [RN:R00611]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 5902974 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9UL12 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name SARDH_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >2757 bp
ATGGCCTCACTGAGCCGAGCCCTACGTGTGGCTGCTGCCCACCCTCGCCAGAGCCCTACC
CGGGGCATGGGGCCATGCAACCTGTCCAGCGCAGCTGGCCCCACAGCCGAGAAGAGTGTG
CCATATCAGCGGACCCTGAAGGAGGGACAGGGCACCTCGGTGGTGGCCCAAGGCCCAAGC
CGGCCCCTGCCCAGCACGGCCAACGTGGTGGTCATTGGTGGAGGCAGCTTGGGCTGCCAG
ACCCTGTACCACCTGGCCAAGCTGGGCATGAGTGGGGCGGTGCTGCTGGAGCGGGAGCGG
CTGACCTCCGGGACCACCTGGCACACGGCAGGCCTGCTGTGGCAGCTGCGGCCCAGTGAC
GTGGAGGTGGAGCTTCTGGCCCACACTCGGCGGGTGGTGAGCCGGGAGCTGGAGGAGGAG
ACGGGACTACACACGGGCTGGATCCAGAATGGGGGCCTCTTCATCGCGTCCAACCGGCAG
CGCCTGGACGAGTACAAGAGGCTCATGTCGCTGGGCAAGGCGTATGGTGTGGAATCCCAT
GTGCTGAGCCCGGCAGAGACCAAGACTCTGTACCCGCTGATGAATGTGGACGACCTCTAC
GGGACCCTGTATGTGCCGCACGACGGTACCATGGACCCCGCTGGCACCTGTACCACCCTC
GCCAGGGCAGCTTCTGCCCGAGGAGCACAGGTCATTGAGAACTGCCCAGTGACCGGCATT
CGTGTGTGGACGGATGATTTTGGGGTGCGGCGGGTCGCGGGTGTGGAGACTCAGCATGGT
TCCATCCAGACACCCTGCGTGGTCAACTGTGCAGGAGTGTGGGCAAGTGCTGTGGGCCGG
ATGGCTGGAGTCAAGGTCCCGCTGGTGGCCATGCACCATGCCTATGTCGTCACCGAGCGC
ATCGAGGGGATTCAGAACATGCCCAATGTCCGTGATCATGATGCCTCTGTCTACCTCCGC
CTCCAAGGGGATGCCTTGTCTGTGGGTGGCTATGAGGCCAACCCCATCTTTTGGGAGGAG
GTGTCAGACAAGTTTGCCTTCGGCCTCTTTGACCTGGACTGGGAGGTGTTCACCCAGCAC
ATTGAAGGCGCCATCAACAGGGTCCCCGTGCTGGAGAAGACAGGAATCAAGTCCACGGTC
TGCGGCCCTGAATCCTTCACGCCCGACCACAAGCCCCTGATGGGGGAGGCACCTGAGCTC
CGAGGGTTCTTCCTGGGCTGTGGCTTCAACAGCGCAGGAATGATGCTGGGTGGTGGCTGT
GGGCAGGAGCTGGCCCACTGGATCATCCATGGGCGCCCGGAGAAGGACATGCATGGCTAT
GACATCAGGCGCTTCCATCACTCGCTCACGGACCACCCCCGCTGGATCCGAGAGCGAAGC
CATGAGTCCTACGCCAAGAACTACTCCGTCGTCTTCCCCCACGATGAGCCGCTGGCCGGG
CGCAACATGAGGAGAGACCCGCTGCATGAGGAACTCCTTGGACAAGGCTGCGTGTTCCAG
GAGCGGCATGGCTGGGAGCGACCGGGATGGTTTCATCCCCGAGGCCCAGCTCCGGTCCTC
GAGTACGACTACTACGGGGCTTACGGGAGCCGCGCGCACGAGGACTACGCCTACCGCAGG
CTGCTGGCAGACGAGTACACCTTCGCCTTCCCGCCCCACCACGACACGATCAAGAAGGAG
TGCCTGGCCTGCAGAGGGGCCGCCGCTGTGTTTGACATGTCCTACTTCGGGAAGTTCTAC
CTGGTGGGGCTGGATGCAAGGAAGGCTGCCGACTGGCTCTTCTCCGCAGATGTCAGCCGA
CCCCCAGGCTCCACCGTGTACACGTGCATGCTCAACCACCGTGGGGGCACCGAGAGTGAC
CTGACTGTCAGCCGCCTGGCACCCAGCCACCAGGCCTCCCCGCTGGCCCCCGCCTTTGAA
GGGGACGGTTACTACCTGGCCATGGGCGGGGCCGTGGCCCAGCACAACTGGTCCCACATC
ACCACCGTGCTGCAGGACCAGAAGTCCCAGTGCCAGCTCATCGACAGCTCCGAGGACCTG
GGTATGATCAGTATCCAGGGCCCAGCCAGCCGAGCCATTTTGCAGGAGGTGCTGGACGCA
GACCTGAGCAACGAGGCCTTCCCGTTCTCCACCCACAAGCTACTGAGAGCCGCAGGGCAC
CTGGTCCGAGCCATGCGGCTGTCCTTTGTGGGGGAGCTGGGCTGGGAGCTGCACATTCCA
AAGGCGTCCTGCGTGCCTGTGTACCGGGCTGTGATGGCCGCGGGTGCCAAGCACGGCCTC
ATCAACGCAGGGTACCGCGCCATCGACTCCCTGAGCATTGAGAAAGGCTACCGGCACTGG
CACGCGGACCTGCGGCCAGACGACAGCCCCCTGGAGGCAGGCCTGGCCTTCACCTGCAAG
CTCAAGTCGCCGGTGCCCTTCCTGGGGAGGGAGGCCCTGGAGCAGCAGCGGGCCGCAGGC
CTCCGCCGGCGCCTGGTGTGCTTCACCATGGAGGACAAAGTACCCATGTTTGGCCTGGAG
GCCATCTGGAGGAACGGCCAAGTGGTGGGCCATGTCCGGAGGGCTGACTTTGGGTTCGCC
ATCGACAAGACCATCGCCTACGGTTACATCCATGACCCCAGCGGTGGGCCGGTCTCGCTG
GACTTTGTGAAGAGCGGGGACTATGCCCTGGAGAGAATGGGGGTGACCTATGGTGCCCAG
GCTCACCTGAAGTCGCCCTTCGACCCCAACAACAAGAGGGTGAAGGGAATCTACTGA
Enzyme 15 GenBank Gene ID AF095735 Link Image
Enzyme 15 GeneCard ID SARDH Link Image
Enzyme 15 GenAtlas ID SARDH Link Image
Enzyme 15 HGNC ID HGNC:10536 Link Image
Enzyme 15 Chromosome Location 9
Enzyme 15 Locus 9q33-q34
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Eschenbrenner M, Jorns MS: Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia. Genomics. 1999 Aug 1;59(3):300-8. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. 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 Link Image]
  4. Gilbert JR, Kumar A, Newey S, Rao N, Ioannou P, Qiu H, Lin D, Xu P, Pettenati MJ, Pericak-Vance MA: Physical and cDNA mapping in the DBH region of human chromosome 9q34. Hum Hered. 2000 May-Jun;50(3):151-7. [PubMed Link Image]
  5. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6167
Enzyme 16 Name Histidine decarboxylase
Enzyme 16 Synonyms
  1. HDC
Enzyme 16 Gene Name HDC
Enzyme 16 Protein Sequence >Histidine decarboxylase
MMEPEEYRERGREMVDYICQYLSTVRERRVTPDVQPGYLRAQLPESAPEDPDSWDSIFGD
IERIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNVM
DWLAKMLGLPEHFLHHHPSSQGGGVLQSTVSESTLIALLAARKNKILEMKTSEPDADESC
LNARLVAYASDQAHSSVEKAGLISLVKMKFLPVDDNFSLRGEALQKAIEEDKQRGLVPVF
VCATLGTTGVCAFDCLSELGPICAREGLWLHIDAAYAGTAFLCPEFRGFLKGIEYADSFT
FNPSKWMMVHFDCTGFWVKDKYKLQQTFSVNPIYLRHANSGVATDFMHWQIPLSRRFRSV
KLWFVIRSFGVKNLQAHVRHGTEMAKYFESLVRNDPSFEIPAKRHLGLVVFRLKGPNCLT
ENVLKEIAKAGRLFLIPATIQDKLIIRFTVTSQFTTRDDILRDWNLIRDAATLILSQHCT
SQPSPRVGNLISQIRGARAWACGTSLQSVSGAGDDPVQARKIIKQPQRVGAGPMKRENGL
HLETLLDPVDDCFSEEAPDATKHKLSSFLFSYLSVQTKKKTVRSLSCNSVPVSAQKPLPT
EASVKNGGSSRVRIFSRFPEDMMMLKKSAFKKLIKFYSVPSFPECSSQCGLQLPCCPLQA
MV
Enzyme 16 Number of Residues 662
Enzyme 16 Molecular Weight 74139.8
Enzyme 16 Theoretical pI 8.06
Enzyme 16 GO Classification
Function
  • binding
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • cofactor binding
  • lyase activity
  • pyridoxal phosphate binding
Process
  • carboxylic acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular metabolic process
  • metabolic process
  • organic acid metabolic process
  • oxoacid metabolic process
Component
Enzyme 16 General Function Involved in carboxy-lyase activity
Enzyme 16 Specific Function L-histidine = histamine + CO(2)
Enzyme 16 Pathways
Enzyme 16 Reactions
  • L-histidine = histamine + CO2 [RN:R01167]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 32109 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P19113 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name DCHS_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1989 bp
ATGATGGAGCCTGAGGAGTACAGAGAGAGAGGGAGAGAGATGGTGGATTACATCTGCCAG
TACCTGAGCACTGTGCGGGAGAGACGTGTGACGCCAGACGTGCAGCCTGGCTACCTGCGA
GCCCAGCTGCCTGAGAGTGCTCCTGAGGACCCCGACAGCTGGGACAGCATCTTTGGGGAC
ATTGAACGAATCATCATGCCTGGGGTGGTACATTGGCAGAGCCCCCATATGCACGCCTAC
TACCCAGCCCTCACCTCTTGGCCCTCCCTGCTAGGAGACATGCTGGCTGATGCCATCAAC
TGCTTGGGATTCACCTGGGCATCCAGCCCTGCGTGTACAGAGCTGGAGATGAACGTCATG
GACTGGTTGGCAAAAATGCTGGGACTTCCAGAGCACTTCTTGCACCACCACCCCAGCAGC
CAGGGCGGAGGCGTCCTGCAGCAGACGGTCAGTGAATCCACTTTGATTGCCCTGCTGGCA
GCAAGGAAGAACAAAATCCTGGAAATGAAAACGTCTGAGCCCGATGCTGATGAGTCCTGC
CTAAATGCCCGACTCGTGGCCTATGCCTCTGACCAGGCTCACTCCTCTGTGGAAAAGGCT
GGTTTGATTTCCCTTGTGAAGATGAAATTTCTGCCTGTGGATGACAACTTCTCACTCCGA
GGGGAAGCTCTTCAGAAGGCCATCGAGGAAGACAAGCAGCGGGGCTTGGTGCCCGTCTTT
GTCTGTGCAACACTAGGGACCACTGGGGTCTGTGCATTTGACTGCCTGTCAGAGCTGGGC
CCCATCTGTGCCCGTGAGGGGCTGTGGCTCCACATCGATGCTGCTTATGCAGGCACTGCC
TTCCTGTGCCCCGAGTTCCGGGGGTTTCTGAAGGGGATTGAGTATGCCGACTCCTTCACC
TTTAATCCTTCCAAGTGGATGATGGTGCATTTTGACTGTACTGGGTTCTGGGTCAAGGAC
AAGTACAAGCTGCAGCAGACCTTCAGTGTGAATCCCATCTACCTCAGGCATGCCAACTCA
GGCGTGGCCACCGACTTCATGCACTGGCAGATCCCCCTGAGCCGACGGTTTCGCTCTGTT
AAACTCTGGTTCGTGATTCGGTCCTTCGGGGTGAAGAATCTTCAAGCACATGTCAGACAT
GGTACTGAAATGGCTAAATATTTTGAATCTCTGGTCAGAAACGACCCTTCCTTTGAAATT
CCTGCCAAGAGGCACCTTGGCCTGGTGGTTTTTCGTCTAAAGGGTCCTAATTGTCTCACA
GAAAATGTGTTAAAGGAAATAGCTAAAGCTGGCCGTCTCTTCCTCATCCCGGCCACTATC
CAGGACAAGTTAATCATCCGTTTCACTGTGACATCCCAGTTTACCACTAGGGATGACATC
CTGAGAGACTGGAATCTCATTCGAGATGCTGCCACTCTCATCCTGAGTCAGCACTGTACT
TCCCAACCCAGCCCTCGGGTTGGGAACCTCATCTCCCAAATCAGGGGTGCCAGAGCCTGG
GCCTGTGGAACGTCCCTTCAGTCTGTCAGTGGGGCAGGAGATGATCCAGTCCAGGCCAGG
AAGATCATCAAGCAGCCTCAGCGTGTGGGAGCCGGTCCCATGAAAAGGGAAAATGGCCTC
CATCTTGAAACCCTGCTGGACCCAGTTGATGACTGCTTTTCAGAAGAGGCCCCAGATGCC
ACCAAGCACAAGCTGTCCTCCTTCCTGTTCAGTTACTTGTCTGTGCAGACTAAGAAGAAG
ACGGTGCGCTCCCTCAGTTGCAACAGTGTGCCAGTGAGTGCTCAGAAGCCACTGCCCACA
GAGGCCTCTGTGAAGAATGGGGGCTCCTCCAGGGTCAGAATCTTTTCCAGGTTTCCAGAA
GACATGATGATGCTGAAGAAAAGTGCCTTCAAAAAACTCATCAAATTCTACAGCGTCCCC
AGCTTTCCTGAATGCAGCTCTCAATGTGGACTCCAGCTGCCCTGTTGCCCTCTGCAGGCC
ATGGTTTAG
Enzyme 16 GenBank Gene ID X54297 Link Image
Enzyme 16 GeneCard ID HDC Link Image
Enzyme 16 GenAtlas ID HDC Link Image
Enzyme 16 HGNC ID HGNC:4855 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 15q21-q22
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Yamauchi K, Sato R, Tanno Y, Ohkawara Y, Maeyama K, Watanabe T, Satoh K, Yoshizawa M, Shibahara S, Takishima T: Nucleotide sequence of the cDNA encoding L-histidine decarboxylase derived from human basophilic leukemia cell line, KU-812-F. Nucleic Acids Res. 1990 Oct 11;18(19):5891. [PubMed Link Image]
  2. Zahnow CA, Yi HF, McBride OW, Joseph DR: Cloning of the cDNA encoding human histidine decarboxylase from an erythroleukemia cell line and mapping of the gene locus to chromosome 15. DNA Seq. 1991;1(6):395-400. [PubMed Link Image]
  3. Mamune-Sato R, Yamauchi K, Tanno Y, Ohkawara Y, Ohtsu H, Katayose D, Maeyama K, Watanabe T, Shibahara S, Takishima T: Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells. Eur J Biochem. 1992 Oct 15;209(2):533-9. [PubMed Link Image]
  4. Yatsunami K, Ohtsu H, Tsuchikawa M, Higuchi T, Ishibashi K, Shida A, Shima Y, Nakagawa S, Yamauchi K, Yamamoto M, et al.: Structure of the L-histidine decarboxylase gene. J Biol Chem. 1994 Jan 14;269(2):1554-9. [PubMed Link Image]
  5. 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 Link Image]
  6. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6322
Enzyme 17 Name Ornithine decarboxylase
Enzyme 17 Synonyms
  1. ODC
Enzyme 17 Gene Name ODC1
Enzyme 17 Protein Sequence >Ornithine decarboxylase
MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALP
RVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQI
KYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLL
LERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPG
SEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQ
TGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTC
DGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQF
QNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV
Enzyme 17 Number of Residues 461
Enzyme 17 Molecular Weight 51147.7
Enzyme 17 Theoretical pI 4.88
Enzyme 17 GO Classification
Function
  • catalytic activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
Component
Enzyme 17 General Function Involved in catalytic activity
Enzyme 17 Specific Function L-ornithine = putrescine + CO(2)
Enzyme 17 Pathways
Enzyme 17 Reactions
  • L-ornithine = putrescine + CO2 [RN:R00670]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 29893806 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P11926 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name DCOR_HUMAN Link Image
Enzyme 17 PDB ID 1D7K Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1386 bp
ATGAACAACTTTGGTAATGAAGAGTTTGACTGCCACTTCCTCGATGAAGGTTTTACTGCC
AAGGACATTCTGGACCAGAAAATTAATGAAGTTTCTTCTTCTGATGATAAGGATGCCTTC
TATGTGGCAGACCTGGGAGACATTCTAAAGAAACATCTGAGGTGGTTAAAAGCTCTCCCT
CGTGTCACCCCCTTTTATGCAGTCAAATGTAATGATAGCAAAGCCATCGTGAAGACCCTT
GCTGCTACCGGGACAGGATTTGACTGTGCTAGCAAGACTGAAATACAGTTGGTGCAGAGT
CTGGGGGTGCCTCCAGAGAGGATTATCTATGCAAATCCTTGTAAACAAGTATCTCAAATT
AAGTATGCTGCTAATAATGGAGTCCAGATGATGACTTTTGATAGTGAAGTTGAGTTGATG
AAAGTTGCCAGAGCACATCCCAAAGCAAAGTTGGTTTTGCGGATTGCCACTGATGATTCC
AAAGCAGTCTGTCGTCTCAGTGTGAAATTCGGTGCCACGCTCAGAACCAGCAGGCTCCTT
TTGGAACGGGCGAAAGAGCTAAATATCGATGTTGTTGGTGTCAGCTTCCATGTAGGAAGC
GGCTGTACCGATCCTGAGACCTTCGTGCAGGCAATCTCTGATGCCCGCTGTGTTTTTGAC
ATGGGGGCTGAGGTTGGTTTCAGCATGTATCTGCTTGATATTGGCGGTGGCTTTCCTGGA
TCTGAGGATGTGAAACTTAAATTTGAAGAGATCACCGGCGTAATCAACCCAGCGTTGGAC
AAATACTTTCCGTCAGACTCTGGAGTGAGAATCATAGCTGAGCCCGGCAGATACTATGTT
GCATCAGCTTTCACGCTTGCAGTTAATATCATTGCCAAGAAAATTGTATTAAAGGAACAG
ACGGGCTCTGATGACGAAGATGAGTCGAGTGAGCAGACCTTTATGTATTATGTGAATGAT
GGCGTCTATGGATCATTTAATTGCATACTCTATGACCACGCACATGTAAAGCCCCTTCTG
CAAAAGAGACCTAAACCAGATGAGAAGTATTATTCATCCAGCATATGGGGACCAACATGT
GATGGCCTCGATCGGATTGTTGAGCGCTGTGACCTGCCTGAAATGCATGTGGGTGATTGG
ATGCTCTTTGAAAACATGGGCGCTTACACTGTTGCTGCTGCCTCTACGTTCAATGGCTTC
CAGAGGCCGACGATCTACTATGTGATGTCAGGGCCTGCGTGGCAACTCATGCAGCAATTC
CAGAACCCCGACTTCCCACCCGAAGTAGAGGAACAGGATGCCAGCACCCTGCCTGTGTCT
TGTGCCTGGGAGAGTGGGATGAAACGCCACAGAGCAGCCTGTGCTTCGGCTAGTATTAAT
GTGTAG
Enzyme 17 GenBank Gene ID M16650 Link Image
Enzyme 17 GeneCard ID ODC1 Link Image
Enzyme 17 GenAtlas ID ODC1 Link Image
Enzyme 17 HGNC ID HGNC:8109 Link Image
Enzyme 17 Chromosome Location 2
Enzyme 17 Locus 2p25
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Hickok NJ, Seppanen PJ, Gunsalus GL, Janne OA: Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA. DNA. 1987 Jun;6(3):179-87. [PubMed Link Image]
  2. Fitzgerald MC, Flanagan MA: Characterization and sequence analysis of the human ornithine decarboxylase gene. DNA. 1989 Nov;8(9):623-34. [PubMed Link Image]
  3. van Steeg H, van Oostrom CT, Martens JW, van Kreyl C, Schepens J, Wieringa B: Nucleotide sequence of the human ornithine decarboxylase gene. Nucleic Acids Res. 1989 Nov 11;17(21):8855-6. [PubMed Link Image]
  4. Hickok NJ, Wahlfors J, Crozat A, Halmekyto M, Alhonen L, Janne J, Janne OA: Human ornithine decarboxylase-encoding loci: nucleotide sequence of the expressed gene and characterization of a pseudogene. Gene. 1990 Sep 14;93(2):257-63. [PubMed Link Image]
  5. Moshier JA, Gilbert JD, Skunca M, Dosescu J, Almodovar KM, Luk GD: Isolation and expression of a human ornithine decarboxylase gene. J Biol Chem. 1990 Mar 25;265(9):4884-92. [PubMed Link Image]
  6. Moshier JA, Osborne DL, Skunca M, Dosescu J, Gilbert JD, Fitzgerald MC, Polidori G, Wagner RL, Friezner Degen SJ, Luk GD, et al.: Multiple promoter elements govern expression of the human ornithine decarboxylase gene in colon carcinoma cells. Nucleic Acids Res. 1992 May 25;20(10):2581-90. [PubMed Link Image]
  7. Wright PS, Cooper JR, Cross-Doersen DE, Miller JA, Chmielewski PA, Wagner RL, Streng KA, Flanagan MA: Regulation of ornithine decarboxylase mRNA levels in human breast cancer cells: pattern of expression and involvement of core enhancer promoter element. Cell Growth Differ. 1995 Sep;6(9):1097-102. [PubMed Link Image]
  8. 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 Link Image]
  9. Hsieh JT, Denning MF, Heidel SM, Verma AK: Expression of human chromosome 2 ornithine decarboxylase gene in ornithine decarboxylase-deficient Chinese hamster ovary cells. Cancer Res. 1990 Apr 15;50(8):2239-44. [PubMed Link Image]
  10. Kaczmarek L, Calabretta B, Ferrari S, de Riel JK: Cell-cycle-dependent expression of human ornithine decarboxylase. J Cell Physiol. 1987 Sep;132(3):545-51. [PubMed Link Image]
  11. Bauer PM, Fukuto JM, Buga GM, Pegg AE, Ignarro LJ: Nitric oxide inhibits ornithine decarboxylase by S-nitrosylation. Biochem Biophys Res Commun. 1999 Aug 27;262(2):355-8. [PubMed Link Image]
  12. Bauer PM, Buga GM, Fukuto JM, Pegg AE, Ignarro LJ: Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme. J Biol Chem. 2001 Sep 14;276(37):34458-64. Epub 2001 Jul 18. [PubMed Link Image]
  13. Leong WF, Chow VT: Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell Microbiol. 2006 Apr;8(4):565-80. [PubMed Link Image]
  14. Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, Hackert ML: Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding. J Mol Biol. 2000 Jan 7;295(1):7-16. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 8073
Enzyme 18 Name Solute carrier family 22 member 1
Enzyme 18 Synonyms
  1. Organic cation transporter 1
  2. hOCT1
Enzyme 18 Gene Name SLC22A1
Enzyme 18 Protein Sequence >Solute carrier family 22 member 1
MPTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQ
RCGWSPAEELNYTVPGLGPAGEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGP
CQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFFFGSLGVGYFADRFGRKLCLL
GTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMY
QMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIK
IMDHIAQKNGKLPPADLKMLSLEEDVTEKLSPSFADLFRTPRLRKRTFILMYLWFTDSVL
YQGLILHMGATSGNLYLDFLYSALVEIPGAFIALITIDRVGRIYPMAMSNLLAGAACLVM
IFISPDLHWLNIIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGIIT
PFIVFRLREVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETMKDAENLGRKAKPKEN
TIYLKVQTSEPSGT
Enzyme 18 Number of Residues 554
Enzyme 18 Molecular Weight 61187.4
Enzyme 18 Theoretical pI 6.81
Enzyme 18 GO Classification
Function
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 18 General Function Involved in ion transmembrane transporter activity
Enzyme 18 Specific Function Translocates a broad array of organic cations with various structures and molecular weights including the model compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-methylnicotinamide (NMN), 4-(4-(dimethylamino)styryl)- N-methylpyridinium (ASP), the endogenous compounds choline, guanidine, histamine, epinephrine, adrenaline, noradrenaline and dopamine, and the drugs quinine, and metformin. The transport of organic cations is inhibited by a broad array of compounds like tetramethylammonium (TMA), cocaine, lidocaine, NMDA receptor antagonists, atropine, prazosin, cimetidine, TEA and NMN, guanidine, cimetidine, choline, procainamide, quinine, tetrabutylammonium, and tetrapentylammonium. Translocates organic cations in an electrogenic and pH-independent manner. Translocates organic cations across the plasma membrane in both directions. Transports the polyamines spermine and spermidine. Transports pramipexole across the basolateral membrane of the proximal tubular epithelial cells. The choline transport is activated by MMTS. Regulated by various intracellular signaling pathways including inhibition by protein kinase A activation, and endogenously activation by the calmodulin complex, the calmodulin- dependent kinase II and LCK tyrosine kinase
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 22-42 150-170 177-197 207-229 236-256 263-283 348-368 377-397 403-423 432-452 465-485 493-513
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 2511670 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID O15245 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name S22A1_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1665 bp
ATGCCCACCGTGGATGACATTCTGGAGCAGGTTGGGGAGTCTGGCTGGTTCCAGAAGCAA
GCCTTCCTCATCTTATGCCTGCTGTCGGCTGCCTTTGCGCCCATCTGTGTGGGCATCGTC
TTCCTGGGTTTCACACCTGACCACCACTGCCAGAGCCCTGGGGTGGCTGAGCTGAGCCAG
CGCTGTGGCTGGAGCCCTGCGGAGGAGCTGAACTATACAGTGCCAGGCCTGGGGCCCGCG
GGCGAGGCCTTCCTTGGCCAGTGCAGGCGCTATGAAGTGGACTGGAACCAGAGCGCCCTC
AGCTGTGTAGACCCCCTGGCTAGCCTGGCCACCAACAGGAGCCACCTGCCGCTGGGTCCC
TGCCAGGATGGCTGGGTGTATGACACGCCCGGCTCTTCCATCGTCACTGAGTTCAACCTG
GTGTGTGCTGACTCCTGGAAGCTGGACCTCTTTCAGTCCTGTTTGAATGCGGGCTTCTTC
TTTGGCTCTCTCGGTGTTGGCTACTTTGCAGACAGGTTTGGCCGTAAGCTGTGTCTCCTG
GGAACTGTGCTGGTCAACGCGGTGTCGGGCGTGCTCATGGCCTTCTCGCCCAACTACATG
TCCATGCTGCTCTTCCGCCTGCTGCAGGGCCTGGTCAGCAAGGGCAACTGGATGGCTGGC
TACACCCTAATCACAGAATTTGTTGGCTCGGGCTCCAGAAGAACGGTGGCGATCATGTAC
CAGATGGCCTTCACGGTGGGGCTGGTGGCGCTTACCGGGCTGGCCTACGCCCTGCCTCAC
TGGCGCTGGCTGCAGCTGGCAGTCTCCCTGCCCACCTTCCTCTTCCTGCTCTACTACTGG
TGTGTGCCGGAGTCCCCTCGGTGGCTGTTATCACAAAAAAGAAACACTGAAGCAATAAAG
ATAATGGACCACATCGCTCAAAAGAATGGGAAGTTGCCTCCTGCTGATTTAAAGATGCTT
TCCCTCGAAGAGGATGTCACCGAAAAGCTGAGCCCTTCATTTGCAGACCTGTTCCGCACG
CCGCGCCTGAGGAAGCGCACCTTCATCCTGATGTACCTGTGGTTCACGGACTCTGTGCTC
TATCAGGGGCTCATCCTGCACATGGGCGCCACCAGCGGGAACCTCTACCTGGATTTCCTT
TACTCCGCTCTGGTCGAAATCCCGGGGGCCTTCATAGCCCTCATCACCATTGACCGCGTG
GGCCGCATCTACCCCATGGCCATGTCAAATTTGTTGGCGGGGGCAGCCTGCCTCGTCATG
ATTTTTATCTCACCTGACCTGCACTGGTTAAACATCATAATCATGTGTGTTGGCCGAATG
GGAATCACCATTGCAATACAAATGATCTGCCTGGTGAATGCTGAGCTGTACCCCACATTC
GTCAGGAACCTCGGAGTGATGGTGTGTTCCTCCCTGTGTGACATAGGTGGGATAATCACC
CCCTTCATAGTCTTCAGGCTGAGGGAGGTCTGGCAAGCCTTGCCCCTCATTTTGTTTGCG
GTGTTGGGCCTGCTTGCCGCGGGAGTGACGCTACTTCTTCCAGAGACCAAGGGGGTCGCT
TTGCCAGAGACCATGAAGGACGCCGAGAACCTTGGGAGAAAAGCAAAGCCCAAAGAAAAC
ACGATTTACCTTAAGGTCCAAACCTCAGAACCCTCGGGCACCTGA
Enzyme 18 GenBank Gene ID X98332 Link Image
Enzyme 18 GeneCard ID SLC22A1 Link Image
Enzyme 18 GenAtlas ID SLC22A1 Link Image
Enzyme 18 HGNC ID HGNC:10963 Link Image
Enzyme 18 Chromosome Location 6
Enzyme 18 Locus 6q26
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Gorboulev V, Ulzheimer JC, Akhoundova A, Ulzheimer-Teuber I, Karbach U, Quester S, Baumann C, Lang F, Busch AE, Koepsell H: Cloning and characterization of two human polyspecific organic cation transporters. DNA Cell Biol. 1997 Jul;16(7):871-81. [PubMed Link Image]
  2. Zhang L, Dresser MJ, Gray AT, Yost SC, Terashita S, Giacomini KM: Cloning and functional expression of a human liver organic cation transporter. Mol Pharmacol. 1997 Jun;51(6):913-21. [PubMed Link Image]
  3. Hayer M, Bonisch H, Bruss M: Molecular cloning, functional characterization and genomic organization of four alternatively spliced isoforms of the human organic cation transporter 1 (hOCT1/SLC22A1). Ann Hum Genet. 1999 Nov;63(Pt 6):473-82. [PubMed Link Image]
  4. 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 Link Image]
  5. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  6. 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 Link Image]
  7. Zhang L, Schaner ME, Giacomini KM: Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa). J Pharmacol Exp Ther. 1998 Jul;286(1):354-61. [PubMed Link Image]
  8. van Montfoort JE, Muller M, Groothuis GM, Meijer DK, Koepsell H, Meier PJ: Comparison of "type I" and "type II" organic cation transport by organic cation transporters and organic anion-transporting polypeptides. J Pharmacol Exp Ther. 2001 Jul;298(1):110-5. [PubMed Link Image]
  9. Ciarimboli G, Struwe K, Arndt P, Gorboulev V, Koepsell H, Schlatter E, Hirsch JR: Regulation of the human organic cation transporter hOCT1. J Cell Physiol. 2004 Dec;201(3):420-8. [PubMed Link Image]
  10. Muller J, Lips KS, Metzner L, Neubert RH, Koepsell H, Brandsch M: Drug specificity and intestinal membrane localization of human organic cation transporters (OCT). Biochem Pharmacol. 2005 Dec 5;70(12):1851-60. Epub 2005 Nov 2. [PubMed Link Image]
  11. Kimura N, Masuda S, Tanihara Y, Ueo H, Okuda M, Katsura T, Inui K: Metformin is a superior substrate for renal organic cation transporter OCT2 rather than hepatic OCT1. Drug Metab Pharmacokinet. 2005 Oct;20(5):379-86. [PubMed Link Image]
  12. Saborowski M, Kullak-Ublick GA, Eloranta JJ: The human organic cation transporter-1 gene is transactivated by hepatocyte nuclear factor-4alpha. J Pharmacol Exp Ther. 2006 May;317(2):778-85. Epub 2006 Jan 25. [PubMed Link Image]
  13. Amphoux A, Vialou V, Drescher E, Bruss M, Mannoury La Cour C, Rochat C, Millan MJ, Giros B, Bonisch H, Gautron S: Differential pharmacological in vitro properties of organic cation transporters and regional distribution in rat brain. Neuropharmacology. 2006 Jun;50(8):941-52. Epub 2006 Mar 31. [PubMed Link Image]
  14. Dias V, Ribeiro V: The expression of the solute carriers NTCP and OCT-1 is regulated by cholesterol in HepG2 cells. Fundam Clin Pharmacol. 2007 Aug;21(4):445-50. [PubMed Link Image]
  15. Kerb R, Brinkmann U, Chatskaia N, Gorbunov D, Gorboulev V, Mornhinweg E, Keil A, Eichelbaum M, Koepsell H: Identification of genetic variations of the human organic cation transporter hOCT1 and their functional consequences. Pharmacogenetics. 2002 Nov;12(8):591-5. [PubMed Link Image]
  16. Shu Y, Leabman MK, Feng B, Mangravite LM, Huang CC, Stryke D, Kawamoto M, Johns SJ, DeYoung J, Carlson E, Ferrin TE, Herskowitz I, Giacomini KM: Evolutionary conservation predicts function of variants of the human organic cation transporter, OCT1. Proc Natl Acad Sci U S A. 2003 May 13;100(10):5902-7. Epub 2003 Apr 28. [PubMed Link Image]
  17. Sakata T, Anzai N, Shin HJ, Noshiro R, Hirata T, Yokoyama H, Kanai Y, Endou H: Novel single nucleotide polymorphisms of organic cation transporter 1 (SLC22A1) affecting transport functions. Biochem Biophys Res Commun. 2004 Jan 16;313(3):789-93. [PubMed Link Image]
  18. Itoda M, Saito Y, Maekawa K, Hichiya H, Komamura K, Kamakura S, Kitakaze M, Tomoike H, Ueno K, Ozawa S, Sawada J: Seven novel single nucleotide polymorphisms in the human SLC22A1 gene encoding organic cation transporter 1 (OCT1). Drug Metab Pharmacokinet. 2004 Aug;19(4):308-12. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 8133
Enzyme 19 Name Spermine oxidase
Enzyme 19 Synonyms
  1. Polyamine oxidase 1
  2. PAO-1
  3. PAOh1
Enzyme 19 Gene Name SMOX
Enzyme 19 Protein Sequence >Spermine oxidase
MQSCESSGDSADDPLSRGLRRRGQPRVVVIGAGLAGLAAAKALLEQGFTDVTVLEASSHI
GGRVQSVKLGHATFELGATWIHGSHGNPIYHLAEANGLLEETTDGERSVGRISLYSKNGV
ACYLTNHGRRIPKDVVEEFSDLYNEVYNLTQEFFRHDKPVNAESQNSVGVFTREEVRNRI
RNDPDDPEATKRLKLAMIQQYLKVESCESSSHSMDEVSLSAFGEWTEIPGAHHIIPSGFM
RVVELLAEGIPAHVIQLGKPVRCIHWDQASARPRGPEIEPRGEGDHNHDTGEGGQGGEEP
RGGRWDEDEQWSVVVECEDCELIPADHVIVTVSLGVLKRQYTSFFRPGLPTEKVAAIHRL
GIGTTDKIFLEFEEPFWGPECNSLQFVWEDEAESHTLTYPPELWYRKICGFDVLYPPERY
GHVLSGWICGEEALVMEKCDDEAVAEICTEMLRQFTGNPNIPKPRRILRSAWGSNPYFRG
SYSYTQVGSSGADVEKLAKPLPYTESSKTAPMQVLFSGEATHRKYYSTTHGALLSGQREA
ARLIEMYRDLFQQGT
Enzyme 19 Number of Residues 555
Enzyme 19 Molecular Weight 61818.8
Enzyme 19 Theoretical pI 5.15
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 19 Specific Function Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions
  • spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2 [RN:R09076]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 28559074 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9NWM0 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name SMOX_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1668 bp
ATGCAAAGTTGTGAATCCAGTGGTGACAGTGCGGATGACCCTCTCAGTCGCGGCCTACGG
AGAAGGGGACAGCCTCGTGTGGTGGTGATCGGCGCCGGCTTGGCTGGCCTGGCTGCAGCC
AAAGCACTTCTTGAGCAGGGTTTCACGGATGTCACTGTGCTTGAGGCTTCCAGCCACATC
GGAGGCCGTGTGCAGAGTGTGAAACTTGGACACGCCACCTTTGAGCTGGGAGCCACCTGG
ATCCATGGCTCCCATGGGAACCCTATCTATCATCTAGCAGAAGCCAACGGCCTCCTGGAA
GAGACAACCGATGGGGAACGCAGCGTGGGCCGCATCAGCCTCTATTCCAAGAATGGCGTG
GCCTGCTACCTTACCAACCACGGCCGCAGGATCCCCAAGGACGTGGTTGAGGAATTCAGC
GATTTATACAACGAGGTCTATAACTTGACCCAGGAGTTCTTCCGGCACGATAAACCAGTC
AATGCTGAAAGTCAAAATAGCGTGGGGGTGTTCACCCGAGAGGAGGTGCGTAACCGCATC
AGGAATGACCCTGACGACCCAGAGGCTACCAAGCGCCTGAAGCTCGCCATGATCCAGCAG
TACCTGAAGGTGGAGAGCTGTGAGAGCAGCTCACACAGCATGGACGAGGTGTCCCTGAGC
GCCTTCGGGGAGTGGACCGAGATCCCCGGCGCTCACCACATCATCCCCTCGGGCTTCATG
CGGGTTGTGGAGCTGCTGGCGGAGGGCATCCCTGCCCACGTCATCCAGCTAGGGAAACCT
GTCCGCTGCATTCACTGGGACCAGGCCTCAGCCCGCCCCAGAGGCCCTGAGATTGAGCCC
CGGGGTGAGGGCGACCACAATCACGACACTGGGGAGGGTGGCCAGGGTGGAGAGGAGCCC
CGGGGGGGCAGGTGGGATGAGGATGAGCAGTGGTCGGTGGTGGTGGAGTGCGAGGACTGT
GAGCTGATCCCGGCGGACCATGTGATTGTGACCGTGTCGCTAGGTGTGCTAAAGAGGCAG
TACACCAGTTTCTTCCGGCCAGGCCTGCCCACAGAGAAGGTGGCTGCCATCCACCGCCTG
GGCATTGGCACCACCGACAAGATCTTTCTGGAATTCGAGGAGCCCTTCTGGGGCCCTGAG
TGCAACAGCCTACAGTTTGTGTGGGAGGACGAAGCAGAGAGCCACACCCTCACCTACCCA
CCTGAGCTCTGGTACCGCAAGATCTGCGGCTTTGATGTCCTCTACCCGCCTGAGCGCTAC
GGCCATGTGCTGAGCGGCTGGATCTGCGGGGAGGAGGCCCTCGTCATGGAGAAGTGTGAT
GACGAGGCAGTGGCCGAGATCTGCACGGAGATGCTGCGTCAGTTCACAGGGAACCCCAAC
ATTCCAAAACCTCGGCGAATCTTGCGCTCGGCCTGGGGCAGCAACCCTTACTTCCGCGGC
TCCTATTCATACACGCAGGTGGGCTCCAGCGGGGCGGATGTGGAGAAGCTGGCCAAGCCC
CTGCCGTACACAGAGAGCTCAAAGACAGCGCCCATGCAGGTGCTGTTTTCCGGTGAGGCC
ACCCACCGCAAGTACTATTCCACCACCCACGGTGCTCTGCTGTCCGGCCAGCGTGAGGCT
GCCCGCCTCATTGAGATGTACCGAGACCTCTTCCAGCAGGGGACCTGA
Enzyme 19 GenBank Gene ID NM_175839.1 Link Image
Enzyme 19 GeneCard ID SMOX Link Image
Enzyme 19 GenAtlas ID SMOX Link Image
Enzyme 19 HGNC ID HGNC:15862 Link Image
Enzyme 19 Chromosome Location 2
Enzyme 19 Locus 20p13
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Wang Y, Devereux W, Woster PM, Stewart TM, Hacker A, Casero RA Jr: Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure. Cancer Res. 2001 Jul 15;61(14):5370-3. [PubMed Link Image]
  2. Murray-Stewart T, Wang Y, Devereux W, Casero RA Jr: Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics. Biochem J. 2002 Dec 15;368(Pt 3):673-7. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA Jr: Properties of purified recombinant human polyamine oxidase, PAOh1/SMO. Biochem Biophys Res Commun. 2003 May 16;304(4):605-11. [PubMed Link Image]
  9. Vujcic S, Diegelman P, Bacchi CJ, Kramer DL, Porter CW: Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin. Biochem J. 2002 Nov 1;367(Pt 3):665-75. [PubMed Link Image]
  10. Seiler N: Catabolism of polyamines. Amino Acids. 2004 Jun;26(3):217-33. Epub 2004 Apr 20. [PubMed Link Image]
  11. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 8199
Enzyme 20 Name Agmatinase, mitochondrial
Enzyme 20 Synonyms
  1. Agmatine ureohydrolase
  2. AUH
Enzyme 20 Gene Name AGMAT
Enzyme 20 Protein Sequence >Agmatinase, mitochondrial
MLRLLASGCARGPGPGVGARPAAGLFHPGRRQSRQASDAPRNQPPSPEFVARPVGVCSMM
RLPVQTSPEGLDAAFIGVPLDTGTSNRPGARFGPRRIREESVMLGTVNPSTGALPFQSLM
VADLGDVNVNLYNLQDSCRRIQEAYEKIVAAGCIPLTLGGDHTITYPILQAMAKKHGPVG
LLHVDAHTDTTDKALGEKLYHGAPFRRCVDEGLLDCKRVVQIGIRGSSTTLDPYRYNRSQ
GFRVVLAEDCWMKSLVPLMGEVRQQMGGKPIYISFDIDALDPAYAPGTGTPEIAGLTPSQ
ALEIIRGCQGLNVMGCDLVEVSPPYDLSGNTALLAANLLFEMLCALPKVTTV
Enzyme 20 Number of Residues 352
Enzyme 20 Molecular Weight 37660.1
Enzyme 20 Theoretical pI 7.66
Enzyme 20 GO Classification
Function
  • agmatinase activity
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • ion binding
  • metal ion binding
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
Component
Enzyme 20 General Function Involved in agmatinase activity
Enzyme 20 Specific Function Agmatine + H(2)O = putrescine + urea
Enzyme 20 Pathways
Enzyme 20 Reactions
  • agmatine + H2O = putrescine + urea [RN:R01157]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 10440052 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9BSE5 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name SPEB_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1059 bp
ATGCTGAGGCTGCTGGCGTCCGGGTGCGCCCGGGGCCCGGGGCCCGGCGTGGGCGCGCGT
CCTGCCGCAGGGCTCTTTCATCCGGGGCGCCGCCAGAGCCGCCAGGCTTCCGATGCGCCC
CGGAACCAGCCCCCCAGCCCCGAGTTCGTGGCCCGGCCGGTGGGCGTCTGCTCCATGATG
CGCCTGCCGGTGCAGACCTCCCCCGAGGGGCTGGACGCTGCCTTCATCGGGGTGCCCCTG
GATACTGGGACCTCCAACCGGCCTGGGGCGAGATTCGGACCTCGCCGCATCCGGGAAGAA
TCAGTGATGCTTCGGACAGTCAATCCTAGCACGGGGGCCCTCCCCTTCCAGTCCCTCATG
GTTGCAGACCTAGGCGATGTGAATGTCAATCTTTACAACCTTCAGGACAGCTGCCGGCGA
ATTCAAGAGGCCTGTGAGAAAATTGTAGCAGCTGGCTGTATTCCTCTGACCTTGGGTGGA
GATCACACAATCACATATCCCATATTGCAAGCGATGGCAAAAAAGCATGGCCCAGTGGGG
CTGCTGCACGTGGATGCGCACACGGACACGACCGACAAGGCCCTAGGAGAGAAGCTCTAC
CACGGGGCGCCCTTCCGCCGGTGTGTGGATGAGGGTCTCCTGGACTGTAAGCGTGTGGTG
CAGATTGGCATCCGGGGCTCTTCCACGACCTTGGATCCCTACAGATACAACCGGAGCCAG
GGCTTCCGGGTAGTCCTGGCTGAAGACTGCTGGATGAAGTCGCTGGTTCCTCTGATGGGG
GAAGTCAGGCAGCAGATGGGAGGCAAACCCATTTATATCAGCTTTGATATTGACGCTCTG
GATCCTGCCTATGCGCCAGGGACAGGGACACCTGAAATTGCTGGTCTCACTCCTAGTCAG
GCTCTGGAGATCATCAGGGGTTGTCAAGGCCTGAACGTGATGGGCTGTGATCTTGTCGAA
GTTTCACCACCGTATGATCTTTCTGGGAACACAGCCCTGCTGGCGGCTAACCTGCTGTTT
GAGATGCTATGTGCTCTCCCCAAAGTGACAACCGTCTGA
Enzyme 20 GenBank Gene ID AK027037 Link Image
Enzyme 20 GeneCard ID AGMAT Link Image
Enzyme 20 GenAtlas ID AGMAT Link Image
Enzyme 20 HGNC ID HGNC:18407 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 1p36.21
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Mistry SK, Burwell TJ, Chambers RM, Rudolph-Owen L, Spaltmann F, Cook WJ, Morris SM Jr: Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus. Am J Physiol Gastrointest Liver Physiol. 2002 Feb;282(2):G375-81. [PubMed Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 9242
Enzyme 21 Name Trimethyllysine dioxygenase, mitochondrial
Enzyme 21 Synonyms
  1. Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
  2. Epsilon-trimethyllysine hydroxylase
  3. TML hydroxylase
  4. TML-alpha-ketoglutarate dioxygenase
  5. TML dioxygenase
  6. TMLD
Enzyme 21 Gene Name TMLHE
Enzyme 21 Protein Sequence >Trimethyllysine dioxygenase, mitochondrial
MWYHRLSHLHSRLQDLLKGGVIYPALPQPNFKSLLPLAVHWHHTASKSLTCAWQQHEDHF
ELKYANTVMRFDYVWLRDHCRSASCYNSKTHQRSLDTASVDLCIKPKTIRLDETTLFFTW
PDGHVTKYDLNWLVKNSYEGQKQKVIQPRILWNAEIYQQAQVPSVDCQSFLETNEGLKKF
LQNFLLYGIAFVENVPPTQEHTEKLAERISLIRETIYGRMWYFTSDFSRGDTAYTKLALD
RHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAEQVLQKAPEEFELLSKVPLKHE
YIEDVGECHNHMIGIGPVLNIYPWNKELYLIRYNNYDRAVINTVPYDVVHRWYTAHRTLT
IELRRPENEFWVKLKPGRVLFIDNWRVLHGRECFTGYRQLCGCYLTRDDVLNTARLLGLQ
A
Enzyme 21 Number of Residues 421
Enzyme 21 Molecular Weight 49517.2
Enzyme 21 Theoretical pI 7.79
Enzyme 21 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
  • transition metal ion binding
  • trimethyllysine dioxygenase activity
  • vitamin binding
Process
  • betaine metabolic process
  • carnitine biosynthetic process
  • carnitine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
Enzyme 21 General Function Involved in oxidation reduction
Enzyme 21 Specific Function Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML)
Enzyme 21 Pathways
Enzyme 21 Reactions
  • N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2 [RN:R03451]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID Q9NVH6 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name TMLH_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1266 bp
ATGTGGTACCACAGATTGTCCCACCTACACAGCAGGCTTCAGGACTTGCTGAAGGGAGGA
GTCATATATCCGGCCCTTCCACAGCCCAACTTCAAAAGCTTACTTCCTTTAGCTGTCCAT
TGGCACCATACAGCCTCCAAGTCTCTGACTTGTGCTTGGCAGCAACATGAAGATCATTTT
GAGCTGAAATATGCTAATACCGTGATGCGCTTTGATTACGTCTGGCTTCGAGACCACTGC
CGCTCAGCATCGTGCTACAACTCTAAGACTCACCAGCGCAGCCTGGATACTGCCAGTGTG
GATTTATGTATCAAGCCAAAGACCATTCGTCTGGATGAGACCACACTCTTTTTCACTTGG
CCAGATGGTCATGTGACTAAATATGATTTGAATTGGCTGGTGAAAAACAGCTATGAAGGG
CAGAAACAAAAAGTCATCCAGCCTAGAATACTATGGAATGCTGAAATCTACCAGCAAGCC
CAAGTTCCATCGGTAGATTGCCAGAGCTTCTTAGAAACCAACGAGGGACTGAAGAAGTTT
CTGCAAAACTTTCTGCTCTATGGAATTGCATTCGTAGAAAATGTCCCTCCCACTCAAGAG
CACACAGAGAAGTTGGCAGAAAGGATCAGCTTAATCAGAGAAACCATTTATGGGAGGATG
TGGTATTTCACTTCAGACTTCTCCAGAGGTGACACTGCGTACACCAAGCTAGCTCTGGAT
CGGCACACTGACACTACCTATTTTCAAGAGCCCTGTGGCATTCAAGTGTTTCATTGTCTT
AAACATGAAGGAACTGGTGGCAGGACACTGCTAGTAGATGGATTCTATGCAGCAGAACAG
GTACTTCAAAAGGCACCTGAGGAATTTGAACTCCTCAGTAAAGTGCCATTGAAGCATGAA
TATATTGAAGATGTTGGAGAATGTCACAACCACATGATTGGGATTGGGCCAGTCTTAAAT
ATCTACCCATGGAATAAAGAGCTGTATTTGATCAGGTACAACAACTATGACCGGGCTGTC
ATCAATACCGTTCCTTATGATGTCGTCCATCGCTGGTATACAGCACACCGGACTCTAACG
ATAGAGTTGAGGAGACCTGAGAATGAGTTTTGGGTCAAACTAAAGCCTGGCAGGGTCCTA
TTTATAGACAACTGGCGTGTCCTACATGGCAGGGAATGCTTCACTGGCTACCGCCAACTG
TGTGGCTGCTATTTAACAAGAGATGATGTATTAAACACTGCTCGCCTCTTGGGGCTTCAG
GCTTAA
Enzyme 21 GenBank Gene ID AF373407 Link Image
Enzyme 21 GeneCard ID TMLHE Link Image
Enzyme 21 GenAtlas ID TMLHE Link Image
Enzyme 21 HGNC ID HGNC:18308 Link Image
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Vaz FM, Ofman R, Westinga K, Back JW, Wanders RJ: Molecular and Biochemical Characterization of Rat epsilon -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis. J Biol Chem. 2001 Sep 7;276(36):33512-7. Epub 2001 Jun 28. [PubMed Link Image]
  2. 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 Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. 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 Link Image]
  5. Monfregola J, Cevenini A, Terracciano A, van Vlies N, Arbucci S, Wanders RJ, D'Urso M, Vaz FM, Ursini MV: Functional analysis of TMLH variants and definition of domains required for catalytic activity and mitochondrial targeting. J Cell Physiol. 2005 Sep;204(3):839-47. [PubMed Link Image]
  6. 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 Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 9885
Enzyme 22 Name Betaine--homocysteine S-methyltransferase 2
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name BHMT2
Enzyme 22 Protein Sequence >Betaine--homocysteine S-methyltransferase 2
MAPAGRPGAKKGILERLESGEVVIGDGSFLITLEKRGYVKAGLWTPEAVIEHPDAVRQLH
MEFLRAGSNVMQTFTFSASEDNMESKWEDVNAAACDLAREVAGKGDALVAGGICQTSIYK
YQKDEARIKKLFRQQLEVFAWKNVDFLIAEYFEHVEEAVWAVEVLKESDRPVAVTMCIGP
EGDMHDITPGECAVRLVKAGASIVGVNCRFGPDTSLKTMELMKEGLEWAGLKAHLMVQPL
GFHAPDCGKEGFVDLPEYPFGLESRVATRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRA
IAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRARARREYWENLLPASGRPFCPSLSK
PDF
Enzyme 22 Number of Residues 363
Enzyme 22 Molecular Weight 40353.8
Enzyme 22 Theoretical pI 5.68
Enzyme 22 GO Classification
Function
  • S-methyltransferase activity
  • betaine-homocysteine S-methyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • homocysteine S-methyltransferase activity
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine biosynthetic process
  • sulfur amino acid biosynthetic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 22 General Function Involved in zinc ion binding
Enzyme 22 Specific Function Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline
Enzyme 22 Pathways
Enzyme 22 Reactions
  • trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine [RN:R02821]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 11907831 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q9H2M3 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name BHMT2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1092 bp
ATGGCACCTGCTGGACGCCCGGGGGCCAAGAAGGGGATTTTGGAGCGCCTGGAGAGTGGG
GAGGTTGTGATTGGAGATGGCAGCTTTCTCATTACTCTGGAGAAGAGAGGCTATGTGAAG
GCTGGGCTCTGGACTCCAGAGGCAGTGATAGAACACCCAGACGCAGTTCGTCAACTTCAC
ATGGAATTCTTGAGAGCAGGATCAAATGTCATGCAGACTTTTACCTTTTCTGCCAGTGAG
GACAATATGGAAAGCAAGTGGGAAGATGTAAATGCTGCTGCCTGTGACCTCGCCAGGGAA
GTGGCTGGCAAAGGTGATGCTTTGGTAGCAGGGGGGATCTGCCAGACATCAATATACAAA
TACCAGAAGGATGAAGCTAGAATTAAAAAACTTTTTCGACAACAGCTAGAAGTTTTTGCC
TGGAAAAATGTGGACTTCTTGATTGCAGAGTATTTTGAGCACGTTGAAGAAGCTGTGTGG
GCTGTGGAAGTCTTAAAAGAATCAGATAGACCCGTGGCAGTTACCATGTGCATAGGCCCA
GAGGGAGACATGCATGATATAACCCCCGGAGAATGTGCTGTGAGGCTGGTGAAGGCAGGG
GCTTCCATCGTTGGCGTGAACTGCCGCTTTGGGCCCGACACCAGCTTGAAGACGATGGAG
CTCATGAAGGAGGGTCTTGAGTGGGCAGGGCTGAAAGCGCACCTCATGGTGCAGCCTCTG
GGGTTCCACGCGCCTGACTGTGGCAAAGAGGGGTTTGTGGATCTCCCAGAATATCCCTTT
GGACTGGAGTCCAGAGTTGCCACCAGATGGGATATTCAAAAATACGCCAGAGAGGCCTAC
AACCTGGGGGTCAGGTACATTGGCGGGTGCTGTGGATTTGAGCCCTACCACATCAGGGCA
ATTGCAGAGGAGCTGGCCCCAGAAAGGGGCTTTTTGCCACCAGCTTCAGAAAAACACGGC
AGCTGGGGAAGTGGTTTGGACATGCACACCAAACCCTGGATTAGAGCAAGGGCTCGAAGG
GAGTATTGGGAGAATCTGCTGCCAGCTTCAGGCAGACCTTTCTGTCCTTCGCTGTCAAAG
CCAGACTTCTAA
Enzyme 22 GenBank Gene ID AF257473 Link Image
Enzyme 22 GeneCard ID BHMT2 Link Image
Enzyme 22 GenAtlas ID BHMT2 Link Image
Enzyme 22 HGNC ID HGNC:1048 Link Image
Enzyme 22 Chromosome Location 5
Enzyme 22 Locus 5q13
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Chadwick LH, McCandless SE, Silverman GL, Schwartz S, Westaway D, Nadeau JH: Betaine-homocysteine methyltransferase-2: cDNA cloning, gene sequence, physical mapping, and expression of the human and mouse genes. Genomics. 2000 Nov 15;70(1):66-73. [PubMed Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 13000
Enzyme 23 Name Spermidine synthase (Spermidine synthase, isoform CRA_a)
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name SRM
Enzyme 23 Protein Sequence >Spermidine synthase (Spermidine synthase, isoform CRA_a)
MEPGPDGPAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYG
NVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV
VQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGP
AESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPT
YPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALND
VS
Enzyme 23 Number of Residues 302
Enzyme 23 Molecular Weight 33825
Enzyme 23 Theoretical pI Not Available
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function Not Available
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID B1AKP9 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name B1AKP9_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence Not Available
Enzyme 23 GenBank Gene ID Not Available
Enzyme 23 GeneCard ID B1AKP9 Link Image
Enzyme 23 GenAtlas ID Not Available
Enzyme 23 HGNC ID Not Available
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References Not Available
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 13125
Enzyme 24 Name cDNA, FLJ94459, Homo sapiens spermine synthase (SMS), mRNA
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name Not Available
Enzyme 24 Protein Sequence >cDNA, FLJ94459, Homo sapiens spermine synthase (SMS), mRNA
AAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFANL
RIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAID
RYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAI
MGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDVL
DNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILDL
SMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVW
KKAKP
Enzyme 24 Number of Residues 366
Enzyme 24 Molecular Weight 41268
Enzyme 24 Theoretical pI Not Available
Enzyme 24 GO Classification Not Available
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function Not Available
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID B2R9M0 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name B2R9M0_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID Not Available
Enzyme 24 GeneCard ID B2R9M0 Link Image
Enzyme 24 GenAtlas ID Not Available
Enzyme 24 HGNC ID Not Available
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs Not Available
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 14510
Enzyme 25 Name Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial
Enzyme 25 Synonyms
  1. PDPr
Enzyme 25 Gene Name PDPR
Enzyme 25 Protein Sequence >Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial
MMFYRLLSIVGRQRASPGWQNWSSARNSTSAAEARSMALPTQAQVVICGGGITGTSVAYH
LSKMGWKDIVLLEQGRLAAGSTRFCAGILSTARHLTIEQKMADYSNKLYYQLEQETGIQT
GYTRTGSIFLAQTQDRLISLKRINAGLNVIGIPSEIISPKKVAELHHLLNVHDLVGAMHV
PEDAVVSSADVALALASAASQNGVQIYDRTSVLHVMVKKGQVTGVETDKGQIECQYFVNC
AGQWAYELGLSNEEPVSIPLHACEHFYLLTRPLETPLQSSTPTIVDADGRIYIRNWQGGI
LSGGFEKNPKPIFTEGKNQLEIQNLQEDWDHFEPLLSSLLRRMPELETLEIMKLVNCPET
FTPDMRCIMGESPAVQGYFVLAGMNSAGLSFGGGAGKYLAEWMVHGYPSENVWELDLKRF
GALQSSRTFLRHRVMEVMPLMYDLKVPRWDFQTGRQLRTSPLYDRLDAQGARWMEKHGFE
RPKYFVPPDKDLLALEQSKTFYKPDWFDIVESEVKCCKEAVCVIDMSSFTKFEITSTGDQ
ALEVLQYLFSNDLDVPVGHIVHTGMLNEGGGYENDCSIARLNKRSFFMISPTDQQVHCWA
WLKKHMPKDSNLLLEDVTWKYTALNLIGPRAVDVLSELSYAPMTPDHFPSLFCKEMSVGY
ANGIRVMSMTHTGEPGFMLYIPIEYALHVYNEVMSVGQKYGIRNAGYYALRSLRIEKFFA
FWGQDINNLTTPLECGRESRVKLEKGMDFIGRDALLQQKQNGVYKRLTMFILDDHDSDLD
LWPWWGEPIYRNGQYVGKTTSSAYSYSLERHVCLGFVHNFSEDTGEEQVVTADFINRGEY
EIDIAGYRFQAKAKLYPVASLFTQKRRKDDMELSDLHGK
Enzyme 25 Number of Residues 879
Enzyme 25 Molecular Weight 99363.7
Enzyme 25 Theoretical pI 6.31
Enzyme 25 GO Classification
Function
  • aminomethyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • oxidoreductase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glycine catabolic process
  • glycine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 25 General Function Involved in oxidoreductase activity
Enzyme 25 Specific Function Decreases the sensitivity of PDP1 to magnesium ions, and this inhibition is reversed by the polyamine spermine
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 194306651 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q8NCN5 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PDPR_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >2640 bp
ATGATGTTCTACCGGTTGCTGTCGATTGTTGGAAGACAAAGAGCCAGCCCAGGATGGCAG
AACTGGTCCTCTGCAAGAAACAGCACGTCAGCTGCCGAGGCGCGTTCCATGGCCCTGCCC
ACCCAGGCACAGGTGGTCATCTGTGGAGGTGGAATCACGGGCACTTCTGTGGCCTATCAC
CTCTCCAAAATGGGGTGGAAGGATATTGTCCTTTTGGAGCAGGGCAGGCTGGCTGCTGGC
TCTACCAGGTTCTGTGCTGGCATCCTGAGCACTGCCAGGCACTTGACCATTGAGCAGAAG
ATGGCAGACTACTCAAACAAACTCTACTATCAGTTAGAGCAAGAAACAGGGATCCAAACA
GGTTACACAAGGACAGGCTCAATCTTTCTGGCCCAAACTCAGGACCGACTGATCTCCCTG
AAGCGCATCAACGCAGGGCTGAATGTTATAGGTATCCCTTCTGAGATCATCTCCCCCAAG
AAAGTGGCCGAGCTTCACCATCTCCTCAACGTGCACGACCTGGTGGGGGCCATGCATGTT
CCCGAGGATGCAGTGGTGTCTTCCGCTGACGTGGCTCTTGCCCTGGCAAGTGCTGCCTCC
CAAAATGGTGTTCAGATCTATGACCGGACATCTGTTCTTCATGTAATGGTCAAAAAAGGT
CAAGTTACTGGAGTGGAGACCGATAAAGGACAGATTGAATGCCAGTATTTTGTCAACTGT
GCTGGCCAGTGGGCATACGAGCTGGGTCTGTCCAACGAGGAGCCGGTTAGTATCCCGCTA
CATGCCTGCGAACACTTCTACCTCCTGACTCGCCCCTTGGAGACCCCTCTGCAGAGCAGC
ACACCAACTATTGTGGATGCTGATGGAAGAATTTATATTCGGAACTGGCAGGGTGGCATC
CTGTCTGGGGGCTTTGAGAAGAACCCGAAACCAATTTTCACTGAGGGCAAGAACCAGCTG
GAGATTCAGAATCTACAGGAAGACTGGGATCACTTTGAGCCTCTGTTGAGTTCCCTTCTG
AGGAGGATGCCAGAATTAGAGACTCTGGAGATCATGAAGTTGGTGAACTGCCCAGAGACC
TTCACACCAGACATGAGGTGCATCATGGGCGAGTCTCCTGCAGTGCAGGGCTACTTTGTC
CTGGCAGGAATGAACTCTGCTGGCCTTTCATTTGGTGGAGGAGCCGGAAAGTACCTTGCC
GAATGGATGGTACATGGTTATCCCTCAGAAAACGTTTGGGAATTGGACCTGAAACGTTTT
GGAGCCCTCCAGAGCAGCCGCACCTTTCTGCGCCACCGGGTCATGGAAGTCATGCCTTTG
ATGTATGATCTGAAGGTTCCCCGCTGGGACTTCCAGACCGGTAGGCAGTTACGCACCTCT
CCTCTCTACGACCGGCTGGATGCACAGGGAGCCAGGTGGATGGAGAAACATGGATTTGAG
AGGCCAAAGTACTTTGTTCCCCCCGACAAGGACCTCCTGGCATTGGAGCAGAGCAAGACT
TTCTATAAGCCAGATTGGTTTGACATCGTGGAGTCTGAAGTCAAGTGCTGTAAGGAAGCT
GTGTGTGTCATTGACATGTCCTCTTTCACAAAGTTTGAGATAACATCCACTGGGGATCAG
GCATTAGAAGTTCTACAGTACCTCTTCTCCAATGACCTGGATGTGCCTGTGGGCCACATT
GTGCATACTGGCATGCTCAACGAGGGTGGAGGGTATGAAAATGACTGCAGCATAGCACGA
CTGAACAAGCGCAGTTTCTTCATGATCTCTCCAACCGACCAGCAGGTCCACTGTTGGGCC
TGGCTTAAGAAACACATGCCGAAAGACAGCAACCTGCTCCTGGAGGACGTCACCTGGAAG
TACACAGCCCTCAATCTGATTGGCCCTCGAGCTGTGGATGTGCTGTCTGAGTTGTCCTAT
GCCCCTATGACTCCAGACCACTTCCCAAGCCTCTTTTGCAAGGAGATGAGTGTGGGCTAT
GCAAATGGGATCCGGGTGATGAGCATGACGCACACAGGAGAGCCAGGATTCATGCTCTAC
ATCCCCATAGAGTACGCCCTGCATGTATACAATGAAGTGATGAGTGTTGGCCAGAAATAC
GGAATCCGGAATGCTGGGTATTACGCTCTTCGCAGTCTCCGAATTGAGAAGTTTTTTGCC
TTCTGGGGTCAGGATATAAATAACCTCACCACGCCCCTGGAATGTGGACGAGAGTCTCGG
GTGAAATTAGAGAAGGGCATGGATTTCATTGGTCGCGACGCCCTCCTGCAGCAGAAGCAG
AATGGAGTGTATAAACGCCTCACCATGTTCATCCTGGACGACCATGATTCAGACCTAGAC
CTTTGGCCTTGGTGGGGAGAGCCCATTTACCGGAATGGGCAGTATGTTGGCAAGACCACC
AGCAGTGCCTACAGCTACAGCCTGGAGCGCCACGTTTGCCTGGGCTTTGTGCACAATTTT
TCTGAGGACACGGGGGAAGAGCAAGTGGTGACAGCAGATTTCATCAACCGGGGAGAGTAT
GAGATTGACATCGCGGGATACCGCTTCCAGGCCAAGGCCAAGCTCTACCCTGTCGCCTCC
CTCTTCACCCAGAAGCGCCGAAAGGATGACATGGAGCTGAGTGACTTACATGGGAAGTGA
Enzyme 25 GenBank Gene ID NM_017990.3 Link Image
Enzyme 25 GeneCard ID PDPR Link Image
Enzyme 25 GenAtlas ID PDPR Link Image
Enzyme 25 HGNC ID HGNC:55066 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 16q22.1
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Ohara O, Nagase T, Mitsui G, Kohga H, Kikuno R, Hiraoka S, Takahashi Y, Kitajima S, Saga Y, Koseki H: Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method. DNA Res. 2002 Apr 30;9(2):47-57. [PubMed Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 16970
Enzyme 26 Name Ornithine decarboxylase antizyme 1
Enzyme 26 Synonyms
  1. ODC-Az
Enzyme 26 Gene Name OAZ1
Enzyme 26 Protein Sequence >Ornithine decarboxylase antizyme 1
MVKSSLQRILNSHCFAREKEGDKPSATIHASRTMPLLSLHSRGGSSSESSRVSLHCCSNP
GPGPRWCSDAPHPPLKIPGGRGNSQRDHNLSANLFYSDDRLNVTEELTSNDKTRILNVQS
RLTDAKRINWRTVLSGGSLYIEIPGGALPEGSKDSFAVLLEFAEEQLRADHVFICFHKNR
EDRAALLRTFSFLGFEIVRPGHPLVPKRPDACFMAYTFERESSGEEEE
Enzyme 26 Number of Residues 228
Enzyme 26 Molecular Weight 25405.3
Enzyme 26 Theoretical pI 7.57
Enzyme 26 GO Classification
Function
  • enzyme inhibitor activity
  • enzyme regulator activity
  • ornithine decarboxylase inhibitor activity
Process
Component
Enzyme 26 General Function Involved in enzyme inhibitor activity
Enzyme 26 Specific Function Binds to, and destabilizes, ornithine decarboxylase which is then degraded. Also inhibits cellular uptake of polyamines by inactivating the polyamine uptake transporter. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 57790284 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P54368 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name OAZ1_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >696 bp


>1 BP
AATGGTGAAATCCTCCCTGCAGCGGATCCTCAATAGCCACTGCTTCGCCAGAGAGAAGGA
AGGGGATAAACCCAGCGCCACCATCCACGCCAGCCGCACCATGCCGCTCCTAAGCCTGCA
CAGCCGCGGCGGCAGCAGCAGTGAGAGTTCCAGGGTCTCCCTCCACTGCTGTAGTAACCC
GGGTCCGGGGCCTCGGTGGTGCTCTGATGCCCCTCACCCACCCCTGAAGATCCCAGGTGG
GCGAGGGAATAGTCAGAGGGATCACAATCTTTCAGCTAACTTATTCTACTCCGATGATCG
GCTGAATGTAACAGAGGAACTAACGTCCAACGACAAGACGAGGATTCTCAACGTCCAGTC
CAGGCTCACAGACGCCAAACGCATTAACTGGCGAACAGTGCTGAGTGGCGGCAGCCTCTA
CATCGAGATCCCGGGCGGCGCGCTGCCCGAGGGGAGCAAGGACAGCTTTGCAGTTCTCCT
GGAGTTCGCTGAGGAGCAGCTGCGAGCCGACCATGTCTTCATTTGCTTCCACAAGAACCG
CGAGGACAGAGCCGCCTTGCTCCGAACCTTCAGCTTTTTGGGCTTTGAGATTGTGAGACC
GGGGCATCCCCTTGTCCCCAAGAGACCCGACGCTTGCTTCATGGCCTACACGTTCGAGAG
AGAGTCTTCGGGAGAGGAGGAGGAGTAG
Enzyme 26 GenBank Gene ID AY865622 Link Image
Enzyme 26 GeneCard ID OAZ1 Link Image
Enzyme 26 GenAtlas ID OAZ1 Link Image
Enzyme 26 HGNC ID HGNC:8095 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 19p13.3
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Tewari DS, Qian Y, Thornton RD, Pieringer J, Taub R, Mochan E, Tewari M: Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme. Biochim Biophys Acta. 1994 Dec 14;1209(2):293-5. [PubMed Link Image]
  2. Yang D, Takii T, Hayashi H, Itoh S, Hayashi M, Onozaki K: Molcecular cloning of human antizyme cDNA. Biochem Mol Biol Int. 1996 Apr;38(5):957-64. [PubMed Link Image]
  3. Hayashi T, Matsufuji S, Hayashi S: Characterization of the human antizyme gene. Gene. 1997 Dec 12;203(2):131-9. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Lin Y, Martin J, Gruendler C, Farley J, Meng X, Li BY, Lechleider R, Huff C, Kim RH, Grasser WA, Paralkar V, Wang T: A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs). BMC Cell Biol. 2002 Jun 21;3:15. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 17736
Enzyme 27 Name Virion infectivity factor
Enzyme 27 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 27 Gene Name vif
Enzyme 27 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLG
DARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAI
RKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 27 Number of Residues 192
Enzyme 27 Molecular Weight 22512.8
Enzyme 27 Theoretical pI 10.40
Enzyme 27 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 27 General Function Involved in viral infectious cycle
Enzyme 27 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 326421 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P69721 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name VIF_HV1BR Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAGGGAAAGCTAGGGGATGGTTTTAT
AGACATCACTATGAAAGCCCTCATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAGATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
CTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GAACTAGCAGACCAACTAATTCATCTGTATTACTTTGACTGTTTTTCAGACTCTGCTATA
AGAAAGGCCTTATTAGGACATATAGTTAGCCCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATACTTGGCACTAGCAGCATTAATAACACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTACGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCACACAATGAATGGACACTAG
Enzyme 27 GenBank Gene ID K02013 Link Image
Enzyme 27 GeneCard ID vif Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Wain-Hobson S, Sonigo P, Danos O, Cole S, Alizon M: Nucleotide sequence of the AIDS virus, LAV. Cell. 1985 Jan;40(1):9-17. [PubMed Link Image]
  2. Zimmerman C, Klein KC, Kiser PK, Singh AR, Firestein BL, Riba SC, Lingappa JR: Identification of a host protein essential for assembly of immature HIV-1 capsids. Nature. 2002 Jan 3;415(6867):88-92. [PubMed Link Image]
  3. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 17737
Enzyme 28 Name Virion infectivity factor
Enzyme 28 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 28 Gene Name vif
Enzyme 28 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWHSLVKHHMYVSKKAKNWFYRHHYESRHPKVSSEVHIPLG
DARLVVRTYWGLQTGEKDWHLGHGVSIEWRQKRYSTQLDPDLADQLIHLYYFDCFSESAI
RQAILGHIVSPRCDYQAGHNKVGSLQYLALTALIAPKKTRPPLPSVRKLTEDRWNKPQQT
KGHRGSHTMNGH
Enzyme 28 Number of Residues 192
Enzyme 28 Molecular Weight 22722.9
Enzyme 28 Theoretical pI 10.42
Enzyme 28 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 28 General Function Involved in viral infectious cycle
Enzyme 28 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 60231 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P04599 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name VIF_HV1MA Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAGGTGGACAGGATGAGGATTAGAACA
TGGCACAGTTTAGTAAAACATCATATGTATGTCTCAAAGAAAGCTAAAAATTGGTTTTAT
AGACATCACTATGAAAGCAGGCATCCAAAAGTAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAGATTAGTAGTAAGAACATATTGGGGTCTGCAAACAGGAGAAAAAGACTGGCAC
TTGGGTCATGGGGTCTCCATAGAATGGAGGCAGAAAAGATATAGCACACAACTAGATCCT
GACCTAGCAGACCAACTGATTCATCTGTACTATTTTGATTGTTTTTCAGAATCTGCCATA
AGACAAGCCATATTAGGACATATAGTTAGTCCTAGGTGTGATTATCAAGCAGGACATAAC
AAGGTAGGATCTTTACAGTATTTGGCACTAACAGCATTAATAGCACCAAAAAAGACAAGG
CCACCTTTGCCTAGTGTTAGGAAGCTAACAGAAGATAGATGGAACAAGCCCCAGCAGACC
AAGGGCCACAGAGGGAGCCACACAATGAATGGACATTAG
Enzyme 28 GenBank Gene ID X04415 Link Image
Enzyme 28 GeneCard ID vif Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Alizon M, Wain-Hobson S, Montagnier L, Sonigo P: Genetic variability of the AIDS virus: nucleotide sequence analysis of two isolates from African patients. Cell. 1986 Jul 4;46(1):63-74. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 17738
Enzyme 29 Name Virion infectivity factor
Enzyme 29 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 29 Gene Name vif
Enzyme 29 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISGKAKGWSYRHHYESTNPRISSEVHIPLG
DAKLVVTTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPGLADRLIHLYYFDCFSDSAI
RKSILGHIVSPSCEYQAGHNKVGSLQYLALAALTTPRRIKPPFPSVTKLTEDRWNKPQKT
KGHRGSHTMTGH
Enzyme 29 Number of Residues 192
Enzyme 29 Molecular Weight 22345.5
Enzyme 29 Theoretical pI 10.48
Enzyme 29 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 29 General Function Involved in viral infectious cycle
Enzyme 29 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 1055032 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q89428 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name VIF_HV1B9 Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATATTTCAGGGAAAGCTAAGGGATGGTCTTAT
AGACATCACTATGAAAGCACTAATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAAATTGGTAGTAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
TTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GGCCTAGCAGACCGACTAATTCATCTGTATTACTTTGATTGTTTTTCAGACTCTGCTATA
AGAAAGTCCATATTAGGACATATAGTTAGCCCTAGTTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAGTACTTGGCACTAGCAGCATTAACAACACCAAGAAGGATAAAG
CCACCCTTTCCTAGTGTTACGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCATACAATGACTGGACACTAG
Enzyme 29 GenBank Gene ID U39362 Link Image
Enzyme 29 GeneCard ID vif Link Image
Enzyme 29 GenAtlas ID Not Available
Enzyme 29 HGNC ID Not Available
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Collman R, Balliet JW, Gregory SA, Friedman H, Kolson DL, Nathanson N, Srinivasan A: An infectious molecular clone of an unusual macrophage-tropic and highly cytopathic strain of human immunodeficiency virus type 1. J Virol. 1992 Dec;66(12):7517-21. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 17739
Enzyme 30 Name Virion infectivity factor
Enzyme 30 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 30 Gene Name vif
Enzyme 30 Protein Sequence >Virion infectivity factor
MENRWQLMIVWQVDRMRINTWKSLVKYHMYVSKKAKGWSYRHHFQSRHPRVSSEVHIPLE
EVKLVITTYWGLHPGEREWHLGQGVSIEWRQGKYRTQIDPGLADQLIHIYYFDCFSESAI
RKAILGHRISPRCNYQAGHNKVGSLQYLALTALIAPEKTKPPLPSVQKLVEDRWNKPQET
RGHRGSHTMNGH
Enzyme 30 Number of Residues 192
Enzyme 30 Molecular Weight 22628.9
Enzyme 30 Theoretical pI 10.33
Enzyme 30 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 30 General Function Involved in viral infectious cycle
Enzyme 30 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 5668941 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q9QSR2 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name VIF_HV1VI Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGTTGATGATTGTGTGGCAGGTAGACAGGATGAGGATTAACACA
TGGAAAAGTTTAGTAAAATATCATATGTATGTTTCAAAGAAAGCCAAAGGATGGTCTTAT
AGACATCACTTTCAAAGCAGGCATCCAAGAGTAAGTTCAGAAGTACACATCCCACTAGAG
GAAGTTAAATTAGTAATAACAACATATTGGGGGCTGCACCCAGGAGAAAGAGAATGGCAT
CTGGGTCAGGGAGTCTCCATAGAATGGAGGCAGGGGAAGTATAGGACACAAATAGACCCT
GGCCTGGCGGACCAACTGATCCATATATATTATTTTGATTGTTTTTCAGAATCTGCCATA
AGGAAAGCCATATTAGGACATAGAATTAGCCCTAGGTGTAACTATCAAGCAGGACATAAT
AAGGTAGGATCCCTACAATATTTGGCACTAACAGCATTAATAGCTCCAGAGAAGACAAAG
CCACCGCTGCCTAGTGTCCAGAAACTAGTAGAGGACAGATGGAACAAGCCCCAGGAGACC
AGGGGCCACAGAGGGAGCCATACAATGAATGGGCACTAG
Enzyme 30 GenBank Gene ID AF077336 Link Image
Enzyme 30 GeneCard ID vif Link Image
Enzyme 30 GenAtlas ID Not Available
Enzyme 30 HGNC ID Not Available
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Laukkanen T, Carr JK, Janssens W, Liitsola K, Gotte D, McCutchan FE, Op de Coul E, Cornelissen M, Heyndrickx L, van der Groen G, Salminen MO: Virtually full-length subtype F and F/D recombinant HIV-1 from Africa and South America. Virology. 2000 Mar 30;269(1):95-104. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 17740
Enzyme 31 Name Virion infectivity factor
Enzyme 31 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 31 Gene Name vif
Enzyme 31 Protein Sequence >Virion infectivity factor
MENRWQVMVVWQVDRMKIRKWNSLVKHHMYVSKKAKGWYYRHHYETHHPKISSEVHIPVG
QARLVTVTYWGLTTGEQSWHLGHGVSIEWRLRKYKTQVDPEMADKLIHLHYFDCFTASAI
RQAVLGRPVLPRCEYPAGHKQVGTLQYLALTAWVGAKKRKPPLPSVTKLTEDRWNEHQKM
QGHRGNPIMNGH
Enzyme 31 Number of Residues 192
Enzyme 31 Molecular Weight 22603.1
Enzyme 31 Theoretical pI 10.51
Enzyme 31 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 31 General Function Involved in viral infectious cycle
Enzyme 31 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 3288391 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID O91081 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name VIF_HV1YF Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGGTTGTGTGGCAAGTGGACAGGATGAAAATCAGGAAA
TGGAATAGCTTAGTAAAACATCATATGTATGTGTCAAAAAAGGCAAAAGGATGGTATTAT
AGACATCATTATGAAACACATCACCCAAAAATAAGTTCAGAAGTACATATCCCAGTAGGT
CAGGCAAGATTAGTGACAGTCACTTATTGGGGGCTAACAACAGGAGAACAGTCTTGGCAT
CTAGGACATGGAGTATCCATAGAATGGAGACTAAGAAAATACAAGACACAAGTTGATCCT
GAAATGGCAGACAAGCTAATACATCTTCATTATTTTGATTGTTTTACAGCCTCTGCCATA
AGGCAAGCGGTCTTAGGGAGACCAGTATTACCTAGGTGTGAATATCCAGCAGGGCACAAA
CAGGTAGGCACCCTACAATATCTAGCACTAACAGCCTGGGTGGGAGCAAAGAAGAGAAAG
CCACCCTTACCTAGTGTGACTAAGCTAACAGAAGATAGATGGAACGAGCACCAGAAGATG
CAGGGCCACAGAGGGAACCCTATAATGAATGGGCACTAG
Enzyme 31 GenBank Gene ID AJ006022 Link Image
Enzyme 31 GeneCard ID vif Link Image
Enzyme 31 GenAtlas ID Not Available
Enzyme 31 HGNC ID Not Available
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Simon F, Mauclere P, Roques P, Loussert-Ajaka I, Muller-Trutwin MC, Saragosti S, Georges-Courbot MC, Barre-Sinoussi F, Brun-Vezinet F: Identification of a new human immunodeficiency virus type 1 distinct from group M and group O. Nat Med. 1998 Sep;4(9):1032-7. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 17741
Enzyme 32 Name Virion infectivity factor
Enzyme 32 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 32 Gene Name vif
Enzyme 32 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMKIRTWNSLVKHHMYISKRAAGWFYRHHYESRHPRVSSEVHIPLE
EDSKLVIITYWGLHTGERDWHLGQGVSIEWRQKRYRTQVDPGLADQLIHLHYFDCFSDSA
IRKAILGQRVSPRCNYQAGHNKVGSLQYLALTALITPKKIKPPLPSVRKLVEDRWNNPQK
TRGHRGSHTMNGH
Enzyme 32 Number of Residues 193
Enzyme 32 Molecular Weight 22832.1
Enzyme 32 Theoretical pI 10.61
Enzyme 32 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 32 General Function Involved in viral infectious cycle
Enzyme 32 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID P0C1L9 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name VIF_HV1M2 Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence Not Available
Enzyme 32 GenBank Gene ID Not Available
Enzyme 32 GeneCard ID vif Link Image
Enzyme 32 GenAtlas ID Not Available
Enzyme 32 HGNC ID Not Available
Enzyme 32 Chromosome Location Not Available
Enzyme 32 Locus Not Available
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Triques K, Bourgeois A, Vidal N, Mpoudi-Ngole E, Mulanga-Kabeya C, Nzilambi N, Torimiro N, Saman E, Delaporte E, Peeters M: Near-full-length genome sequencing of divergent African HIV type 1 subtype F viruses leads to the identification of a new HIV type 1 subtype designated K. AIDS Res Hum Retroviruses. 2000 Jan 20;16(2):139-51. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 17742
Enzyme 33 Name Virion infectivity factor
Enzyme 33 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 33 Gene Name vif
Enzyme 33 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRINTWKSLVKYHMYVSKKANRWRYRHHYDSNHPKISSEVHIPLG
DAELVVTTYWGLHTGEREWHLGQGVSIEWRLKKYRTQVDPGLADQLIHIYYFDCFSESAI
RKALLGHRVSPRCEYQAGHTQVGSLQYLALTALIAPKKTKPPVPSVQKLVEDRWNKPQKT
RGHRGSHTMSGQ
Enzyme 33 Number of Residues 192
Enzyme 33 Molecular Weight 22570.8
Enzyme 33 Theoretical pI 10.34
Enzyme 33 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 33 General Function Involved in viral infectious cycle
Enzyme 33 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 157885895 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P0C1K6 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name VIF_HV197 Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAGGTAGACAGGATGAGGATTAATACA
TGGAAAAGTCTAGTAAAATACCATATGTACATTTCAAGGAAAGCTAGAAGATGGTTTTAT
AGACATCATTATGACAGCAATCATCCAAAAATAAGCTCAGAGGTACACATCCCACTAGGG
GATGCTGAATTAGTAGTGACAACATATTGGGGTCTGCATACAGGAGAAAGAGAATGGCAT
TTGGGTCAGGGGGTCTCCATAGAATGGAGGCTGAAAAGGTACAGAACACAAGTAGACCCT
GGCCTGGCAGACCAACTAATTCATATGCATTACTTTGATTGTTTTTCAGAATCTGCCATA
AGGAAGGCCATATTAGGACATAGAGTTAGCCCTAGGTGTGAATATCAAGCAGGACATAAT
AAGGTAGGATCTTTGCAATATCTGGCATTAGCAGCATTAATAAACCCAAAAAGGACAAAG
CCACCTTTGCCTAGTGTTAAAAAACTAGTAGAGGATCGATGGAACAAGCCCCAGAAGACC
AGGGGCCACAGAGAGAACCAAACAATGAATGGACACTAG
Enzyme 33 GenBank Gene ID AM884182 Link Image
Enzyme 33 GeneCard ID vif Link Image
Enzyme 33 GenAtlas ID Not Available
Enzyme 33 HGNC ID Not Available
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Triques K, Bourgeois A, Vidal N, Mpoudi-Ngole E, Mulanga-Kabeya C, Nzilambi N, Torimiro N, Saman E, Delaporte E, Peeters M: Near-full-length genome sequencing of divergent African HIV type 1 subtype F viruses leads to the identification of a new HIV type 1 subtype designated K. AIDS Res Hum Retroviruses. 2000 Jan 20;16(2):139-51. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 17743
Enzyme 34 Name Virion infectivity factor
Enzyme 34 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 34 Gene Name vif
Enzyme 34 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHRMYVSGKARGWFYRHHYESPHPRISSEVHIPLG
DARLVITTYWGLHTGERDWHLGQGVSIEWRKRRYSTQVDPELADQLIHLHYFDCFSDSAI
RKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKVKPPLPSVTKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 34 Number of Residues 192
Enzyme 34 Molecular Weight 22519.8
Enzyme 34 Theoretical pI 10.57
Enzyme 34 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 34 General Function Involved in viral infectious cycle
Enzyme 34 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 327462 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID P04598 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name VIF_HV1B5 Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCGTATGTATGTTTCAGGGAAAGCTAGGGGATGGTTTTAT
AGACATCACTATGAAAGCCCTCATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAGATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
TTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAGGAGATATAGCACACAAGTAGACCCT
GAACTAGCAGACCAACTAATTCATCTGCATTACTTTGATTGTTTTTCAGACTCTGCTATA
AGAAAGGCCTTATTAGGACACATAGTTAGCCCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATACTTGGCACTAGCAGCATTAATAACACCAAAAAAGGTAAAG
CCACCTTTGCCTAGTGTTACGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGAAGCCACACAATGAATGGACACTAG
Enzyme 34 GenBank Gene ID K02012 Link Image
Enzyme 34 GeneCard ID vif Link Image
Enzyme 34 GenAtlas ID Not Available
Enzyme 34 HGNC ID Not Available
Enzyme 34 Chromosome Location Not Available
Enzyme 34 Locus Not Available
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Ratner L, Haseltine W, Patarca R, Livak KJ, Starcich B, Josephs SF, Doran ER, Rafalski JA, Whitehorn EA, Baumeister K, et al.: Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature. 1985 Jan 24-30;313(6000):277-84. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 17744
Enzyme 35 Name Virion infectivity factor
Enzyme 35 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 35 Gene Name vif
Enzyme 35 Protein Sequence >Virion infectivity factor
MENRRQVMIVWQADRMRIRTWKSLVKHHMYISKKAKGRFYRHHYESTHPRISSEVHIPLG
DARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADHLIHLHYFDCFSDSAI
RKAILGHRVSPICEFQAGHNKVGPLQYLALTALITPKKIKPPLPSVKKLTEDRWNKPQKT
KGHRGSHTINGH
Enzyme 35 Number of Residues 192
Enzyme 35 Molecular Weight 22487.9
Enzyme 35 Theoretical pI 10.75
Enzyme 35 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 35 General Function Involved in viral infectious cycle
Enzyme 35 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 328034 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P05898 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name VIF_HV1MN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >579 bp
ATGGAAAACAGACGGCAGGTGATGATTGTGTGGCAAGCAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATATTTCAAAGAAAGCTAAAGGACGGTTTTAT
AGACATCACTATGAAAGCACTCATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAGATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
TTAGGTCAGGGAGTCTCCATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GACCTAGCAGACCACCTAATTCATCTGCATTACTTTGATTGTTTTTCAGACTCTGCCATA
AGAAAGGCCATATTAGGACATAGAGTTAGTCCTATTTGTGAATTTCAAGCAGGACATAAC
AAGGTAGGACCTCTACAGTACTTGGCACTAACAGCATTAATAACACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTAAGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCATACAATCAATGGGCACTAG
Enzyme 35 GenBank Gene ID M17449 Link Image
Enzyme 35 GeneCard ID vif Link Image
Enzyme 35 GenAtlas ID Not Available
Enzyme 35 HGNC ID Not Available
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Gurgo C, Guo HG, Franchini G, Aldovini A, Collalti E, Farrell K, Wong-Staal F, Gallo RC, Reitz MS Jr: Envelope sequences of two new United States HIV-1 isolates. Virology. 1988 Jun;164(2):531-6. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 17745
Enzyme 36 Name Virion infectivity factor
Enzyme 36 Synonyms
  1. Vif
  2. SOR protein
Enzyme 36 Gene Name vif
Enzyme 36 Protein Sequence >Virion infectivity factor
MENRWQVMVVWQVDXMKIRTWNSLVKHHMYVSKKAKGWYYRHHYETKHPKTSSEVHIPVG
XAXLVIVTYWGLTTGEQPWHLGHXVSIEWRQGKYKTQVDPEMADKLIHCYYFNCFTASAI
RQAVLGRPVLPRCXYPAGHXQVGTLQYLAXTAXVGVKKRRPPLPSVTKLTEDRWNERQKT
QGHRGNPIMNGP
Enzyme 36 Number of Residues 192
Enzyme 36 Molecular Weight 21915.2
Enzyme 36 Theoretical pI 10.34
Enzyme 36 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 36 General Function Involved in viral infectious cycle
Enzyme 36 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 8920154 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q9IDV7 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name VIF_HV1YB Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGGTTGTGTGGCAAGTGGACARGATGAAAATCAGGACA
TGGAATAGCTTAGTAAAACACCATATGTATGTGTCAAAAAAGGCAAAAGGGTGGTATTAT
AGACATCATTATGAAACAAAGCATCCAAAGACAAGTTCAGAAGTRCATATCCCAGTAGGT
CMGGCAARATTAGTGATAGTCACTTATTGGGGACTAACAACAGGAGAACAGCCTTGGCAT
CTAGGACATRGAGTATCCATAGAATGGAGACAAGGAAAATACAAGACACAAGTTGATCCT
GAAATGGCAGACAAGCTAATACATTGTTATTATTTTAATTGTTTTACAGCTTCTGCCATA
AGGCAAGCGGTCTTAGGGAGACCAGTGTTACCTAGGTGTGAMTATCCGGCAGGGCACAAM
CAGGTAGGCACTCTACAATATCTAGCAMTAACAGCCTRGGTGGGAGTAAAGAAGAGAAGG
CCACCCTTACCTAGTGTGACTAAGTTAACAGAAGATAGATGGAACGAGCGCCAGAAGACG
CAGGGCCACAGAGGGAACCCTATAATGAATGGGCCCTAG
Enzyme 36 GenBank Gene ID AJ271370 Link Image
Enzyme 36 GeneCard ID vif Link Image
Enzyme 36 GenAtlas ID Not Available
Enzyme 36 HGNC ID Not Available
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Roques P, Robertson DL, Souquiere S, Apetrei C, Nerrienet E, Barre-Sinoussi F, Muller-Trutwin M, Simon F: Phylogenetic characteristics of three new HIV-1 N strains and implications for the origin of group N. AIDS. 2004 Jul 2;18(10):1371-81. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 17746
Enzyme 37 Name Virion infectivity factor
Enzyme 37 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 37 Gene Name vif
Enzyme 37 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRINTWKSLVKYHMYVSKKANRWFYRHHYDSHHPKISSEVHIPLG
EARLVVTTYWGLHTGEKEWHLGQGVSIEWRKRRYSTQVDPGLADQLIHMYYFDCFAESAI
RKAILGHIVSPSCEYQAGHNKVGSLQYLALAALIAPKKIKPPLPSVRKLTEDRWNKPQKT
KGRRGSHTMNGH
Enzyme 37 Number of Residues 192
Enzyme 37 Molecular Weight 22555.9
Enzyme 37 Theoretical pI 10.45
Enzyme 37 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 37 General Function Involved in viral infectious cycle
Enzyme 37 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 328159 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID P18805 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name VIF_HV1ND Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAACACA
TGGAAAAGTTTAGTAAAATACCATATGTATGTTTCAAAGAAAGCTAACAGATGGTTTTAT
AGACATCACTATGACAGCCACCACCCAAAAATAAGTTCAGAAGTACACATCCCACTAGGA
GAAGCTAGACTGGTAGTAACAACATATTGGGGTCTGCATACAGGAGAAAAAGAATGGCAT
CTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAGGAGATATAGCACACAAGTAGACCCT
GGCCTGGCAGACCAACTAATTCATATGTATTATTTTGATTGTTTTGCAGAATCTGCTATA
AGAAAAGCCATATTAGGACATATAGTTAGTCCTAGTTGTGAGTATCAAGCAGGACATAAC
AAGGTAGGATCCTTACAGTATTTGGCACTAGCAGCATTAATAGCACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTAGGAAGCTAACAGAAGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCGCAGAGGGAGCCATACAATGAATGGACATTAG
Enzyme 37 GenBank Gene ID M27323 Link Image
Enzyme 37 GeneCard ID vif Link Image
Enzyme 37 GenAtlas ID Not Available
Enzyme 37 HGNC ID Not Available
Enzyme 37 Chromosome Location Not Available
Enzyme 37 Locus Not Available
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Spire B, Sire J, Zachar V, Rey F, Barre-Sinoussi F, Galibert F, Hampe A, Chermann JC: Nucleotide sequence of HIV1-NDK: a highly cytopathic strain of the human immunodeficiency virus. Gene. 1989 Sep 30;81(2):275-84. [PubMed Link Image]
  2. Bouyac M, Rey F, Nascimbeni M, Courcoul M, Sire J, Blanc D, Clavel F, Vigne R, Spire B: Phenotypically Vif- human immunodeficiency virus type 1 is produced by chronically infected restrictive cells. J Virol. 1997 Mar;71(3):2473-7. [PubMed Link Image]
  3. Bouyac M, Courcoul M, Bertoia G, Baudat Y, Gabuzda D, Blanc D, Chazal N, Boulanger P, Sire J, Vigne R, Spire B: Human immunodeficiency virus type 1 Vif protein binds to the Pr55Gag precursor. J Virol. 1997 Dec;71(12):9358-65. [PubMed Link Image]
  4. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 17747
Enzyme 38 Name cDNA, FLJ95932, Homo sapiens polyamine modulated factor 1 binding protein 1(PMFBP1), mRNA
Enzyme 38 Synonyms Not Available
Enzyme 38 Gene Name Not Available
Enzyme 38 Protein Sequence >cDNA, FLJ95932, Homo sapiens polyamine modulated factor 1 binding protein 1(PMFBP1), mRNA
MKDEAGERDREVSSLNSKLLSLQLDIKNLHDVCKRQRKTLQDNQLCMEEAMNSSHDKKQA
QALAFEESEVEFGSSKQCHLRQLQQLKKKLLVLQQELEFHTEELQTSYYSLRQYQSILEK
QTSDLVLLHHHCKLKEDEVILYEEEMGNHNENTGEKLHLAQEQLALAGDKIASLERSLNL
YRDKYQSSLSNIELLECQVKMLQGELGGIMGQEPENKGDHSKVRIYTSPCMIQEHQETQK
RLSEVWQKVSQQDDLIQELRNKLACSNALVLEREKALIKLQADFASCTATHRYPPSSSEE
CEDIKKILKHLQEQKDSQCLHVEEYQNLVKDLRVELEAVSEQKRNIMKDMMKLELDLHGL
REETSAHIERKDKDITILQCRLQELQLEFTETQKLTLKKDKFLQEKDEMLQELEKKLTQV
QNSLLKKEKELEKQQCMATELEMTVKEAKQDKSKEAECKALQAEVQKLKNSLEEAKQQER
LAAQQAAQCKEEAALAGCHLEDTQRKLQKGLLLDKQKADTIQELQRELQMLQKESSMAEK
EQTSNRKRVEELSLELSEALRKLENSDKEKRQLQKTVAEQDMKMNDMLDRIKHQHREQGS
IKCKLEEDLQEATKLLEDKREQLKKSKEHEKLMEGELEALRQEFKKKDKTLKENSRKLEE
ENENLRAELQCCSTQLESSLNKYNTSQQVIQDLNKEIALQKESLMSLQAQLDKALQKEKH
YLQTTITKEAYDALSRKSAACQDDLTQALEKLNHVTSETKSLQQSLTQTQEKKAQLEEEI
IAYEERMKKLNTELRKLRGFHQESELEVHAFDKKLEEMSCQVLQWQKQHQNDLKMLAAKE
EQLREFQEEMAALKENLLEDDKEPCCLPQWSVPKDTCRLYRGNDQIMTNLEQWAKQQKVA
NEKLGNQLREQVNYIAKLSGEKDHLHSVMVHLQQENKKLKKEIEEKKMKAENTRLCTKAL
GPSRTESTQREKVCGTLGWKGLPQDMGQRMDLTKYIGMPHCPGSSYC
Enzyme 38 Number of Residues 1007
Enzyme 38 Molecular Weight 117479.0
Enzyme 38 Theoretical pI 6.17
Enzyme 38 GO Classification Not Available
Enzyme 38 General Function Replication, recombination and repair
Enzyme 38 Specific Function Not Available
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function Not Available
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 189054649 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID B2RCA2 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name B2RCA2_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >3024 bp
ATGAAAGATGAGGCGGGGGAGAGAGACAGAGAAGTGAGCAGCCTGAACAGCAAGCTGTTA
AGCCTGCAACTTGACATCAAGAATCTGCACGATGTCTGCAAGAGACAGAGGAAGACCTTG
CAGGACAATCAGCTCTGCATGGAGGAGGCAATGAACAGCAGCCACGACAAGAAGCAAGCA
CAGGCATTAGCATTCGAGGAGTCAGAGGTGGAATTTGGGTCCAGTAAACAGTGTCATCTG
AGACAACTCCAGCAACTGAAGAAAAAATTGCTGGTCCTTCAACAAGAACTGGAGTTTCAC
ACAGAGGAGTTGCAGACTTCTTACTATTCTCTCCGCCAGTATCAGTCCATCCTAGAGAAG
CAGACTTCCGACCTGGTTCTTCTGCACCATCACTGCAAACTGAAAGAAGATGAGGTGATT
CTCTATGAGGAGGAAATGGGAAATCACAACGAGAACACAGGGGAGAAGCTCCATTTGGCG
CAGGAGCAACTCGCCTTGGCCGGGGACAAGATCGCCTCTCTAGAGAGGAGCTTAAACCTC
TACAGGGATAAATACCAGTCTTCCCTGAGCAACATCGAGTTACTAGAATGCCAAGTGAAG
ATGTTGCAGGGGGAACTCGGCGGGATCATGGGTCAGGAGCCTGAGAACAAGGGTGATCAT
TCAAAGGTACGGATATACACTTCTCCTTGCATGATTCAAGAGCATCAGGAGACTCAGAAA
CGACTGTCTGAAGTCTGGCAAAAGGTCTCTCAACAGGATGATCTCATTCAAGAACTTCGA
AATAAGCTGGCCTGCAGTAACGCTTTGGTTCTGGAGCGTGAAAAGGCTTTGATAAAACTA
CAAGCCGATTTTGCTTCCTGTACAGCCACCCACAGATACCCTCCTAGCTCCTCAGAAGAG
TGTGAAGACATCAAAAAGATACTGAAGCACTTGCAGGAGCAGAAAGACAGCCAGTGCCTG
CATGTGGAGGAGTACCAGAACCTGGTGAAGGATCTGCGCGTGGAACTAGAGGCCGTGTCG
GAACAGAAGAGAAACATCATGAAGGACATGATGAAGCTGGAGCTGGACCTGCACGGACTG
CGGGAGGAGACATCTGCCCACATTGAGAGGAAGGATAAGGACATCACCATCCTGCAGTGC
CGGCTGCAGGAGCTGCAGCTGGAGTTCACCGAGACCCAAAAGCTCACTTTGAAGAAAGAC
AAGTTCCTCCAAGAGAAAGATGAGATGCTGCAAGAGCTGGAGAAGAAACTGACACAGGTT
CAGAACAGCCTCCTGAAAAAGGAGAAGGAGCTGGAGAAGCAGCAGTGCATGGCCACAGAA
CTTGAAATGACAGTCAAGGAGGCTAAGCAGGACAAGTCCAAGGAGGCGGAGTGCAAGGCC
CTGCAGGCTGAGGTCCAGAAGCTGAAGAACAGTCTCGAAGAGGCCAAGCAGCAGGAGAGG
CTGGCTGCTCAGCAAGCAGCCCAGTGCAAAGAAGAGGCTGCACTGGCAGGCTGTCACCTG
GAGGACACCCAGAGGAAACTGCAGAAGGGTCTCCTCCTGGACAAGCAGAAGGCAGACACC
ATCCAGGAACTACAGAGAGAACTTCAGATGCTGCAGAAGGAGTCCTCGATGGCTGAGAAG
GAACAAACCTCCAACAGAAAACGGGTGGAGGAGCTGTCATTAGAACTCTCTGAAGCCCTG
AGGAAGCTTGAAAATTCAGACAAGGAAAAGAGGCAGCTTCAGAAGACAGTGGCTGAGCAG
GATATGAAAATGAATGACATGCTTGATCGTATCAAGCACCAGCACAGGGAGCAAGGCTCC
ATCAAATGCAAGTTAGAAGAAGATCTTCAGGAGGCCACAAAGCTTCTGGAGGACAAACGG
GAGCAGTTGAAGAAGAGCAAAGAGCATGAGAAGCTGATGGAGGGAGAACTTGAAGCTTTG
CGGCAGGAATTTAAAAAGAAAGACAAGACGTTGAAAGAGAATTCCAGAAAGTTGGAGGAA
GAAAATGAGAATCTCCGAGCAGAGCTACAGTGTTGTTCTACACAACTGGAATCCTCTCTC
AACAAATACAACACCAGCCAGCAAGTCATCCAAGACTTGAATAAAGAGATAGCCCTTCAG
AAGGAGTCCTTAATGAGCCTGCAGGCCCAGCTGGACAAAGCTCTGCAGAAGGAGAAGCAC
TATCTCCAGACTACCATCACCAAAGAAGCCTATGATGCATTATCCCGGAAGTCAGCCGCC
TGCCAGGATGACCTGACACAAGCCCTCGAGAAGCTCAATCACGTGACCTCAGAGACAAAG
AGCCTGCAGCAAAGCTTGACACAGACCCAAGAGAAGAAAGCTCAGCTGGAAGAGGAAATC
ATTGCTTATGAGGAAAGGATGAAAAAGCTCAATACGGAATTAAGAAAACTGCGGGGCTTC
CACCAGGAGAGTGAGCTGGAGGTGCACGCCTTTGACAAGAAGCTAGAGGAGATGAGCTGC
CAGGTGCTGCAGTGGCAGAAGCAACACCAGAATGACCTCAAGATGCTGGCAGCCAAAGAG
GAGCAGCTCAGGGAGTTCCAGGAGGAGATGGCCGCCTTAAAAGAGAACCTCCTTGAGGAC
GATAAGGAGCCCTGCTGCCTGCCCCAGTGGTCTGTGCCCAAAGACACCTGTAGGCTCTAC
CGAGGGAATGATCAGATTATGACCAACTTGGAGCAATGGGCAAAACAGCAGAAGGTCGCC
AATGAGAAACTAGGAAACCAGCTCCGAGAGCAGGTGAACTACATTGCCAAGCTGAGTGGC
GAAAAGGACCACCTCCACAGTGTAATGGTCCACTTGCAGCAGGAAAACAAGAAGCTGAAG
AAGGAGATAGAAGAGAAGAAGATGAAAGCCGAGAACACAAGGCTATGCACCAAAGCCCTA
GGCCCGAGCAGAACGGAGTCCACACAGAGGGAGAAAGTGTGCGGCACCTTGGGCTGGAAG
GGGTTGCCCCAGGATATGGGTCAAAGAATGGACCTCACCAAGTACATCGGGATGCCCCAC
TGCCCGGGTTCCTCATACTGCTAG
Enzyme 38 GenBank Gene ID AK315004 Link Image
Enzyme 38 GeneCard ID Not Available
Enzyme 38 GenAtlas ID Not Available
Enzyme 38 HGNC ID HGNC:17728 Link Image
Enzyme 38 Chromosome Location Not Available
Enzyme 38 Locus Not Available
Enzyme 38 SNPs Not Available
Enzyme 38 General References Not Available
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 17748
Enzyme 39 Name Virion infectivity factor
Enzyme 39 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 39 Gene Name vif
Enzyme 39 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLG
DARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAI
RKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 39 Number of Residues 192
Enzyme 39 Molecular Weight 22512.8
Enzyme 39 Theoretical pI 10.40
Enzyme 39 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 39 General Function Involved in viral infectious cycle
Enzyme 39 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 328556 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P69720 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name VIF_HV1B1 Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAGGGAAAGCTAGGGGATGGTTTTAT
AGACATCACTATGAAAGCCCTCATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAGATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
CTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GAACTAGCAGACCAACTAATTCATCTGTATTACTTTGACTGTTTTTCAGACTCTGCTATA
AGAAAGGCCTTATTAGGACACATAGTTAGCCCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATACTTGGCACTAGCAGCATTAATAACACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTACGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCACACAATGAATGGACACTAG
Enzyme 39 GenBank Gene ID K02083 Link Image
Enzyme 39 GeneCard ID vif Link Image
Enzyme 39 GenAtlas ID Not Available
Enzyme 39 HGNC ID Not Available
Enzyme 39 Chromosome Location Not Available
Enzyme 39 Locus Not Available
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Ratner L, Haseltine W, Patarca R, Livak KJ, Starcich B, Josephs SF, Doran ER, Rafalski JA, Whitehorn EA, Baumeister K, et al.: Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature. 1985 Jan 24-30;313(6000):277-84. [PubMed Link Image]
  2. Muesing MA, Smith DH, Cabradilla CD, Benton CV, Lasky LA, Capon DJ: Nucleic acid structure and expression of the human AIDS/lymphadenopathy retrovirus. Nature. 1985 Feb 7-13;313(6002):450-8. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 17749
Enzyme 40 Name Polyamine-modulated factor 1
Enzyme 40 Synonyms
  1. PMF-1
Enzyme 40 Gene Name PMF1
Enzyme 40 Protein Sequence >Polyamine-modulated factor 1
MAEASSANLGSGCEEKRHEGSSSESVPPGTTISRVKLLDTMVDTFLQKLVAAGSYQRFTD
CYKCFYQLQPAMTQQIYDKFIAQLQTSIREEISDIKEEGNLEAVLNALDKIVEEGKVRKE
PAWRPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLADAVLAGRRQVEELQLQV
QAQQQAWQALHREQRELVAVLREPE
Enzyme 40 Number of Residues 205
Enzyme 40 Molecular Weight 23339.2
Enzyme 40 Theoretical pI 5.18
Enzyme 40 GO Classification Not Available
Enzyme 40 General Function Involved in leucine zipper domain binding
Enzyme 40 Specific Function Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 88900509 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q6P1K2 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name PMF1_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >618 bp
ATGGCCGAAGCAAGTAGCGCCAATCTAGGCAGCGGCTGTGAGGAAAAAAGGCATGAGGGG
TCGTCTTCGGAATCTGTGCCACCCGGCACTACCATTTCGAGGGTGAAGCTCCTCGACACC
ATGGTGGACACTTTTCTTCAGAAGCTGGTCGCCGCCGGCAGCTACCAGAGATTCACTGAC
TGCTATAAGTGCTTCTACCAGTTGCAGCCTGCGATGACACAGCAAATCTATGACAAGTTT
ATAGCTCAGTTGCAGACATCTATCCGGGAGGAAATCTCTGACATCAAAGAGGAGGGGAAC
CTAGAAGCTGTCTTGAATGCCTTGGATAAAATTGTGGAAGAAGGCAAAGTCCGCAAAGAG
CCAGCCTGGCGCCCCAGCGGGATCCCAGAGAAGGATCTGCACAGTGTTATGGCACCCTAC
TTCCTGCAGCAACGGGACACCCTGCGGCGCCATGTGCAGAAACAGGAGGCCGAGAACCAG
CAGCTGGCAGATGCCGTCCTGGCAGGGCGGAGGCAGGTGGAGGAGCTGCAGCTACAGGTC
CAGGCCCAGCAGCAGGCCTGGCAGGCTCTACACAGAGAACAGAGGGAGCTGGTTGCTGTG
CTGAGGGAGCCTGAGTGA
Enzyme 40 GenBank Gene ID NM_007221.2 Link Image
Enzyme 40 GeneCard ID PMF1 Link Image
Enzyme 40 GenAtlas ID PMF1 Link Image
Enzyme 40 HGNC ID HGNC:9112 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 1q12
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Wang Y, Devereux W, Stewart TM, Casero RA Jr: Cloning and characterization of human polyamine-modulated factor-1, a transcriptional cofactor that regulates the transcription of the spermidine/spermine N(1)-acetyltransferase gene. J Biol Chem. 1999 Jul 30;274(31):22095-101. [PubMed Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. Wang Y, Devereux W, Stewart TM, Casero RA Jr: Characterization of the interaction between the transcription factors human polyamine modulated factor (PMF-1) and NF-E2-related factor 2 (Nrf-2) in the transcriptional regulation of the spermidine/spermine N1-acetyltransferase (SSAT) gene. Biochem J. 2001 Apr 1;355(Pt 1):45-9. [PubMed Link Image]
  7. Wang Y, Devereux W, Stewart TM, Casero RA Jr: Polyamine-modulated factor 1 binds to the human homologue of the 7a subunit of the Arabidopsis COP9 signalosome: implications in gene expression. Biochem J. 2002 Aug 15;366(Pt 1):79-86. [PubMed Link Image]
  8. Obuse C, Iwasaki O, Kiyomitsu T, Goshima G, Toyoda Y, Yanagida M: A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1. Nat Cell Biol. 2004 Nov;6(11):1135-41. Epub 2004 Oct 24. [PubMed Link Image]
  9. Kline SL, Cheeseman IM, Hori T, Fukagawa T, Desai A: The human Mis12 complex is required for kinetochore assembly and proper chromosome segregation. J Cell Biol. 2006 Apr 10;173(1):9-17. Epub 2006 Apr 3. [PubMed Link Image]
  10. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  11. 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 Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 17750
Enzyme 41 Name Virion infectivity factor
Enzyme 41 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 41 Gene Name vif
Enzyme 41 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSKKASRWFYRHHYDSPHPKISSEVHIPLG
EARLVVKTYWGLHTGERDWHLGQGVSIEWRKRRYSTQVDPGLADQLIHMYYFDCFSEAAI
RKAILGHIVSHRCEYQAGHSKVGSLQYLALTALIAPKKIKPPLPSVRKLTEDRWNKPQKT
KGHKGAIQ
Enzyme 41 Number of Residues 188
Enzyme 41 Molecular Weight 22158.6
Enzyme 41 Theoretical pI 10.63
Enzyme 41 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 41 General Function Involved in viral infectious cycle
Enzyme 41 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 329402 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID P04596 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name VIF_HV1Z6 Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >567 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAAAGAAAGCTAGCAGATGGTTTTAT
AGACATCACTATGACAGCCCCCACCCAAAAATAAGTTCAGAAGTACACATTCCACTAGGA
GAAGCTAGACTGGTAGTAAAAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
CTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAGGAGATATAGCACACAAGTAGACCCT
GGCCTGGCAGACCAACTAATTCATATGTATTATTTTGATTGTTTTTCAGAAGCTGCCATA
AGAAAAGCCATATTAGGACATATAGTCAGTCATAGGTGTGAGTATCAAGCAGGACATAGC
AAGGTAGGATCCTTACAGTATTTGGCACTAACAGCATTAATAGCACCAAAAAAGATAAAG
CCGCCTTTGCCTAGTGTTAGGAAGTTAACAGAAGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAAAGGAGCCATACAATGA
Enzyme 41 GenBank Gene ID K03458 Link Image
Enzyme 41 GeneCard ID vif Link Image
Enzyme 41 GenAtlas ID Not Available
Enzyme 41 HGNC ID Not Available
Enzyme 41 Chromosome Location Not Available
Enzyme 41 Locus Not Available
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Srinivasan A, Anand R, York D, Ranganathan P, Feorino P, Schochetman G, Curran J, Kalyanaraman VS, Luciw PA, Sanchez-Pescador R: Molecular characterization of human immunodeficiency virus from Zaire: nucleotide sequence analysis identifies conserved and variable domains in the envelope gene. Gene. 1987;52(1):71-82. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 17751
Enzyme 42 Name Virion infectivity factor
Enzyme 42 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 42 Gene Name vif
Enzyme 42 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRINTWKSLVKYHMHISRKARGWFYRHHFESTHPRISSEVHIPLG
EARLVITTYWGLNTGEREWHLGQGVSIEWRLKRYSTQVEPGLADQLIHMHYFDCFSESAI
RKAILGRVVRPRCNYPAGHKQVGTLQYLALTALVAPKKIKPPLPSVRKLVEDRWNKPQKT
RGHRGSHTMNGH
Enzyme 42 Number of Residues 192
Enzyme 42 Molecular Weight 22633.1
Enzyme 42 Theoretical pI 10.98
Enzyme 42 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 42 General Function Involved in viral infectious cycle
Enzyme 42 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 3114567 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID O70897 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name VIF_HV190 Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAACACA
TGGAAAAGCTTAGTAAAGTACCATATGCATATTTCAAGGAAAGCTAGAGGATGGTTTTAT
AGACATCATTTTGAAAGCACTCATCCAAGGATAAGTTCAGAAGTACACATCCCATTAGGA
GAAGCTAGGTTAGTCATAACCACATACTGGGGTCTGAATACAGGAGAAAGAGAATGGCAT
TTAGGCCAGGGAGTCTCCATAGAATGGAGACTGAAAAGGTATAGCACACAAGTAGAGCCT
GGCCTGGCAGACCAACTAATTCATATGCATTATTTTGATTGTTTTTCAGAATCTGCCATA
AGGAAAGCCATATTAGGACGTGTAGTTAGACCTAGGTGTAACTATCCAGCAGGACATAAA
CAGGTAGGAACTCTACAATACTTGGCATTAACAGCATTAGTGGCACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTAGAAAGCTAGTAGAGGATAGATGGAACAAGCCCCAGAAGACC
AGGGGCCACAGAGGGAGCCACACAATGAATGGACACTAG
Enzyme 42 GenBank Gene ID AF005496 Link Image
Enzyme 42 GeneCard ID vif Link Image
Enzyme 42 GenAtlas ID Not Available
Enzyme 42 HGNC ID Not Available
Enzyme 42 Chromosome Location Not Available
Enzyme 42 Locus Not Available
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Gao F, Robertson DL, Carruthers CD, Morrison SG, Jian B, Chen Y, Barre-Sinoussi F, Girard M, Srinivasan A, Abimiku AG, Shaw GM, Sharp PM, Hahn BH: A comprehensive panel of near-full-length clones and reference sequences for non-subtype B isolates of human immunodeficiency virus type 1. J Virol. 1998 Jul;72(7):5680-98. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 17752
Enzyme 43 Name Virion infectivity factor
Enzyme 43 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 43 Gene Name vif
Enzyme 43 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLG
DARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAI
RKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 43 Number of Residues 192
Enzyme 43 Molecular Weight 22512.8
Enzyme 43 Theoretical pI 10.40
Enzyme 43 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 43 General Function Involved in viral infectious cycle
Enzyme 43 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 327747 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID P69723 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name VIF_HV1H2 Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAGGGAAAGCTAGGGGATGGTTTTAT
AGACATCACTATGAAAGCCCTCATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAGATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
TTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GAACTAGCAGACCAACTAATTCATCTGTATTACTTTGACTGTTTTTCAGACTCTGCTATA
AGAAAGGCCTTATTAGGACACATAGTTAGCCCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATACTTGGCACTAGCAGCATTAATAACACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTACGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCACACAATGAATGGACACTAG
Enzyme 43 GenBank Gene ID K03455 Link Image
Enzyme 43 GeneCard ID vif Link Image
Enzyme 43 GenAtlas ID Not Available
Enzyme 43 HGNC ID Not Available
Enzyme 43 Chromosome Location Not Available
Enzyme 43 Locus Not Available
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Ratner L, Fisher A, Jagodzinski LL, Mitsuya H, Liou RS, Gallo RC, Wong-Staal F: Complete nucleotide sequences of functional clones of the AIDS virus. AIDS Res Hum Retroviruses. 1987 Spring;3(1):57-69. [PubMed Link Image]
  2. Goncalves J, Jallepalli P, Gabuzda DH: Subcellular localization of the Vif protein of human immunodeficiency virus type 1. J Virol. 1994 Feb;68(2):704-12. [PubMed Link Image]
  3. Goncalves J, Shi B, Yang X, Gabuzda D: Biological activity of human immunodeficiency virus type 1 Vif requires membrane targeting by C-terminal basic domains. J Virol. 1995 Nov;69(11):7196-204. [PubMed Link Image]
  4. Karczewski MK, Strebel K: Cytoskeleton association and virion incorporation of the human immunodeficiency virus type 1 Vif protein. J Virol. 1996 Jan;70(1):494-507. [PubMed Link Image]
  5. Yang X, Goncalves J, Gabuzda D: Phosphorylation of Vif and its role in HIV-1 replication. J Biol Chem. 1996 Apr 26;271(17):10121-9. [PubMed Link Image]
  6. Goncalves J, Korin Y, Zack J, Gabuzda D: Role of Vif in human immunodeficiency virus type 1 reverse transcription. J Virol. 1996 Dec;70(12):8701-9. [PubMed Link Image]
  7. Camaur D, Trono D: Characterization of human immunodeficiency virus type 1 Vif particle incorporation. J Virol. 1996 Sep;70(9):6106-11. [PubMed Link Image]
  8. Bouyac M, Courcoul M, Bertoia G, Baudat Y, Gabuzda D, Blanc D, Chazal N, Boulanger P, Sire J, Vigne R, Spire B: Human immunodeficiency virus type 1 Vif protein binds to the Pr55Gag precursor. J Virol. 1997 Dec;71(12):9358-65. [PubMed Link Image]
  9. Yang X, Gabuzda D: Mitogen-activated protein kinase phosphorylates and regulates the HIV-1 Vif protein. J Biol Chem. 1998 Nov 6;273(45):29879-87. [PubMed Link Image]
  10. Yu X, Yu Y, Liu B, Luo K, Kong W, Mao P, Yu XF: Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science. 2003 Nov 7;302(5647):1056-60. Epub 2003 Oct 16. [PubMed Link Image]
  11. Mehle A, Strack B, Ancuta P, Zhang C, McPike M, Gabuzda D: Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J Biol Chem. 2004 Feb 27;279(9):7792-8. Epub 2003 Dec 13. [PubMed Link Image]
  12. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
  13. Douaisi M, Dussart S, Courcoul M, Bessou G, Lerner EC, Decroly E, Vigne R: The tyrosine kinases Fyn and Hck favor the recruitment of tyrosine-phosphorylated APOBEC3G into vif-defective HIV-1 particles. Biochem Biophys Res Commun. 2005 Apr 15;329(3):917-24. [PubMed Link Image]
  14. Russell RA, Pathak VK: Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J Virol. 2007 Aug;81(15):8201-10. Epub 2007 May 23. [PubMed Link Image]
  15. Wang J, Shackelford JM, Casella CR, Shivers DK, Rapaport EL, Liu B, Yu XF, Finkel TH: The Vif accessory protein alters the cell cycle of human immunodeficiency virus type 1 infected cells. Virology. 2007 Mar 15;359(2):243-52. Epub 2006 Oct 23. [PubMed Link Image]
  16. He Z, Zhang W, Chen G, Xu R, Yu XF: Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction. J Mol Biol. 2008 Sep 12;381(4):1000-11. Epub 2008 Jun 28. [PubMed Link Image]
  17. Izumi T, Takaori-Kondo A, Shirakawa K, Higashitsuji H, Itoh K, Io K, Matsui M, Iwai K, Kondoh H, Sato T, Tomonaga M, Ikeda S, Akari H, Koyanagi Y, Fujita J, Uchiyama T: MDM2 is a novel E3 ligase for HIV-1 Vif. Retrovirology. 2009 Jan 7;6:1. [PubMed Link Image]
  18. Kataropoulou A, Bovolenta C, Belfiore A, Trabatti S, Garbelli A, Porcellini S, Lupo R, Maga G: Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase. Nucleic Acids Res. 2009 Jun;37(11):3660-9. Epub 2009 Apr 15. [PubMed Link Image]
  19. Mercenne G, Bernacchi S, Richer D, Bec G, Henriet S, Paillart JC, Marquet R: HIV-1 Vif binds to APOBEC3G mRNA and inhibits its translation. Nucleic Acids Res. 2010 Jan;38(2):633-46. Epub 2009 Nov 12. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 17753
Enzyme 44 Name Virion infectivity factor
Enzyme 44 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 44 Gene Name vif
Enzyme 44 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISRKAKGWFYRHHYESTHPRISSEVHIPPG
DERLVITTYWGLHTGERDWHLGQGVSIEWRKRRYSTQVDPDLADQLIHLYYFDCFSESAI
RKPSLGHIVSPRCEYQAGHNKVGSLQYLALAALTTPKKIKPPLPSVKKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 44 Number of Residues 192
Enzyme 44 Molecular Weight 22686.9
Enzyme 44 Theoretical pI 10.45
Enzyme 44 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 44 General Function Involved in viral infectious cycle
Enzyme 44 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 328570 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID P05900 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name VIF_HV1RH Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATATTTCAAGGAAAGCTAAGGGATGGTTTTAT
AGACATCACTATGAAAGCACTCATCCAAGAATAAGTTCAGAGGTACACATCCCACCAGGG
GATGAAAGGTTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
TTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAGGAGATATAGCACACAAGTAGACCCT
GACCTAGCAGACCAACTAATTCACCTGTACTATTTTGATTGTTTTTCAGAATCTGCTATA
AGAAAGCCATCATTAGGACATATAGTTAGTCCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAGTACCTGGCACTAGCAGCATTAACAACACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTAAGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCATACAATGAATGGACACTAG
Enzyme 44 GenBank Gene ID M17451 Link Image
Enzyme 44 GeneCard ID vif Link Image
Enzyme 44 GenAtlas ID Not Available
Enzyme 44 HGNC ID Not Available
Enzyme 44 Chromosome Location Not Available
Enzyme 44 Locus Not Available
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Starcich BR, Hahn BH, Shaw GM, McNeely PD, Modrow S, Wolf H, Parks ES, Parks WP, Josephs SF, Gallo RC, et al.: Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS. Cell. 1986 Jun 6;45(5):637-48. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 17754
Enzyme 45 Name Virion infectivity factor
Enzyme 45 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 45 Gene Name vif
Enzyme 45 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWHSLVKHHMYVSKKARGWFYRPHYASRHPRVSSEVHIPLG
DATLVVTTYWGLHTGEKDWQLGHGVSIEWRQRRYRTQVEPDLADHLIHLHYFDCFSDSAI
RKAILGQIVSPRCEYQAGHNQVGSLQYLALKVLVTSKRSRPPLPSVTELAEDRWNKPQKT
RGHRENPTMNGH
Enzyme 45 Number of Residues 192
Enzyme 45 Molecular Weight 22662.8
Enzyme 45 Theoretical pI 10.40
Enzyme 45 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 45 General Function Involved in viral infectious cycle
Enzyme 45 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 3403228 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID O89941 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name VIF_HV1SE Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAGGTAGACAGGATGAGGATTAGAACA
TGGCACAGTTTGGTAAAACATCATATGTATGTCTCAAAGAAAGCTAGAGGCTGGTTTTAT
AGACCTCACTATGCAAGCAGGCATCCAAGAGTAAGTTCAGAAGTACACATCCCACTAGGA
GATGCTACACTAGTAGTAACAACATATTGGGGGCTGCATACAGGAGAAAAAGACTGGCAA
TTGGGTCATGGGGTCTCCATAGAGTGGAGGCAGAGAAGATATAGAACACAAGTAGAGCCT
GACCTAGCAGACCATCTGATTCATCTGCATTATTTTGATTGTTTTTCAGACTCTGCCATA
AGGAAAGCCATATTAGGACAAATAGTTAGCCCTAGGTGTGAATATCAAGCAGGACATAAT
CAGGTAGGATCTCTACAATATTTGGCATTGAAAGTATTAGTAACATCAAAAAGGAGTAGG
CCACCTTTGCCCAGTGTTACGGAATTAGCAGAAGATAGATGGAACAAGCCCCAGAAGACC
AGGGGCCACAGAGAGAACCCTACAATGAATGGGCATTAG
Enzyme 45 GenBank Gene ID AF061642 Link Image
Enzyme 45 GeneCard ID vif Link Image
Enzyme 45 GenAtlas ID Not Available
Enzyme 45 HGNC ID Not Available
Enzyme 45 Chromosome Location Not Available
Enzyme 45 Locus Not Available
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Carr JK, Salminen MO, Albert J, Sanders-Buell E, Gotte D, Birx DL, McCutchan FE: Full genome sequences of human immunodeficiency virus type 1 subtypes G and A/G intersubtype recombinants. Virology. 1998 Jul 20;247(1):22-31. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 17755
Enzyme 46 Name Virion infectivity factor
Enzyme 46 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 46 Gene Name vif
Enzyme 46 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSKKAKGWFYRHHYESTHPRISSEVHIPLG
DATLVVTTYWGLHTGEREWHLGQGASIEWRKKRYSTQVDPGLADQLIHTYYFDCFSESAI
RNAILGNIVSPRCEYPAGHNKVGSLQYLALAALIKPKKIKPPLPSVTKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 46 Number of Residues 192
Enzyme 46 Molecular Weight 22365.6
Enzyme 46 Theoretical pI 10.43
Enzyme 46 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 46 General Function Involved in viral infectious cycle
Enzyme 46 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 328445 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID P20890 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name VIF_HV1OY Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAAAGAAAGCTAAGGGATGGTTTTAT
AGACATCACTATGAAAGCACTCATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTACCTTGGTAGTAACAACATATTGGGGTCTGCATACAGGAGAAAGAGAATGGCAT
TTGGGCCAGGGAGCCTCTATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GGCCTAGCAGACCAACTAATTCATACATATTATTTTGATTGTTTTTCAGAATCTGCTATA
AGAAATGCCATACTAGGAAATATAGTTAGTCCTAGGTGTGAATATCCAGCAGGACATAAC
AAGGTAGGATCTCTACAATACTTGGCACTAGCAGCATTGATAAAACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTACGAAACTAACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCATACAATGAATGGACACTAG
Enzyme 46 GenBank Gene ID M26727 Link Image
Enzyme 46 GeneCard ID vif Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID Not Available
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Huet T, Dazza MC, Brun-Vezinet F, Roelants GE, Wain-Hobson S: A highly defective HIV-1 strain isolated from a healthy Gabonese individual presenting an atypical western blot. AIDS. 1989 Nov;3(11):707-15. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 17756
Enzyme 47 Name Virion infectivity factor
Enzyme 47 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 47 Gene Name vif
Enzyme 47 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLG
DARLVITTYWGLHTGERDWHLGQGVSIKWRKKRYSTQVDPELADQLIHLYYFDCFSDSAI
RKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKT
KGHRRSHTMNGH
Enzyme 47 Number of Residues 192
Enzyme 47 Molecular Weight 22611.0
Enzyme 47 Theoretical pI 10.61
Enzyme 47 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 47 General Function Involved in viral infectious cycle
Enzyme 47 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 459459 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID P31820 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name VIF_HV1NA Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAGGGAAAGCTAGGGGATGGTTTTAT
AGACATCACTATGAAAGCCCTCATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAGATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
CTGGGTAAGGGAGTCTCCATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GAACTAGCAGACCAACTAATTCATCTGTATTACTTTGACTGTTTTTCAGACTCTGCTATA
AGAAAGGCCTTATTAGGACACATAGTTAGCCCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATACTTGGCACTAGCAGCATTAATAACACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTACGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCACACAATGAATGGACACTAG
Enzyme 47 GenBank Gene ID Z30607 Link Image
Enzyme 47 GeneCard ID vif Link Image
Enzyme 47 GenAtlas ID Not Available
Enzyme 47 HGNC ID Not Available
Enzyme 47 Chromosome Location Not Available
Enzyme 47 Locus Not Available
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Sakai K, Ma XY, Gordienko I, Volsky DJ: Recombinational analysis of a natural noncytopathic human immunodeficiency virus type 1 (HIV-1) isolate: role of the vif gene in HIV-1 infection kinetics and cytopathicity. J Virol. 1991 Nov;65(11):5765-73. [PubMed Link Image]
  2. Ma XY, Sova P, Chao W, Volsky DJ: Cysteine residues in the Vif protein of human immunodeficiency virus type 1 are essential for viral infectivity. J Virol. 1994 Mar;68(3):1714-20. [PubMed Link Image]
  3. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 17757
Enzyme 48 Name cDNA FLJ16610 fis, clone TESTI4011532, highly similar to Homo sapiens polyamine modulated factor 1 binding protein 1 (PMFBP1), mRNA
Enzyme 48 Synonyms Not Available
Enzyme 48 Gene Name Not Available
Enzyme 48 Protein Sequence >cDNA FLJ16610 fis, clone TESTI4011532, highly similar to Homo sapiens polyamine modulated factor 1 binding protein 1 (PMFBP1), mRNA
MGNHNENTGEKLHLAQEQLALAGDKIASLERSLNLYRDKYQSSLSNIELLECQVKMLQGE
LGGIMGQEPENKGDHSKVRIYTSPCMIQEHQETQKRLSEVWQKVSQQDDLIQELRNKLAC
SNALVLEREKALIKLQADFASCTATHRYPPSSSEECEDIKKILKHLQEQKDSQCLHVEEY
QNLVKDLRVELEAVSEQKRNIMKDMMKLELDLHGLREETSAHIERKDKDITILQCRLQEL
QLEFTETQKLTLKKDKFLQEKDEMLQELEKKLTQVQNSLLKKEKELEKQQCMATELEMTV
KEAKQDKSKEAECKALQAEVQKLKNSLEEAKQQERLAAQQAAQCKEEAALAGCHLEDTQR
KLQKGLLLDKQKADTIQELQRELQMLQKESSMAEKEQTSNRKRVEELSLELSEALRKLEN
SDKEKRQLQKTVAEQDMKMNDMLDRIKHQHREQGSIKCKLEEDLQEATKLLEDKREQLKK
SKEHEKLMEGELEALRQEFKKKDKTLKENSRKLEEENENLRAELQCCSTQLESSLNKYNT
SQQVIQDLNKEIALQKESLMSLQAQLDKALQKEKHYLQTTITKEAYDALSRKSAACQDDL
TQALEKLNHVTSETKSLQQSLTQTQEKKAQLEEEIIAYEERMKKLNTELRKLRGFHQESE
LEVHAFDKKLEEMSCQVLQWQKQHQNDLKMLAAKEEQLREFQEEMAALKENLLEDDKEPC
CLPQWSVPKDTCRLYRGNDQIMTNLEQWAKQQKVANEKLGNQLREQVNYIAKLSGEKDRE
PTRASSPNTTRPSSPSHSHLHSVMVHLQQENKKLKKEIEEKKMKAENTRLCTKALGPSRT
ESTQREKVCGTLGWKGLPQDMGQRMDLTKYIGMPHCPGSSYC
Enzyme 48 Number of Residues 882
Enzyme 48 Molecular Weight 102485.0
Enzyme 48 Theoretical pI 6.49
Enzyme 48 GO Classification Not Available
Enzyme 48 General Function Replication, recombination and repair
Enzyme 48 Specific Function Not Available
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function Not Available
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 193783819 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID B3KVI9 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name B3KVI9_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >2649 bp
ATGGGAAATCACAACGAGAACACAGGGGAGAAGCTCCATTTGGCGCAGGAGCAACTCGCC
TTGGCCGGGGACAAGATCGCCTCTCTAGAGAGGAGCTTAAACCTCTACAGGGATAAATAC
CAGTCTTCCCTGAGCAACATCGAGTTACTAGAATGCCAAGTGAAGATGTTGCAGGGGGAA
CTCGGCGGGATCATGGGTCAGGAGCCTGAGAACAAGGGTGATCATTCAAAGGTACGGATA
TACACTTCTCCTTGCATGATTCAAGAGCATCAGGAGACTCAGAAACGACTGTCTGAAGTC
TGGCAAAAGGTCTCTCAACAGGATGATCTCATTCAAGAACTTCGAAATAAGCTGGCCTGC
AGTAACGCTTTGGTTCTGGAGCGTGAAAAGGCTTTGATAAAACTACAAGCCGATTTTGCT
TCCTGTACAGCCACCCACAGATACCCTCCTAGCTCCTCAGAAGAGTGTGAAGACATCAAA
AAGATACTGAAGCACTTGCAGGAGCAGAAAGACAGCCAGTGCCTGCATGTGGAGGAGTAC
CAGAACCTGGTGAAGGATCTGCGCGTGGAACTAGAGGCCGTGTCGGAACAGAAGAGAAAC
ATCATGAAGGACATGATGAAGCTGGAGCTGGACCTGCACGGACTGCGGGAGGAGACATCT
GCCCACATTGAGAGGAAGGATAAGGACATCACCATCCTGCAGTGCCGGCTGCAGGAGCTG
CAGCTGGAGTTCACCGAGACCCAAAAGCTCACTTTGAAGAAAGACAAGTTCCTCCAAGAG
AAAGATGAGATGCTGCAAGAGCTGGAGAAGAAACTGACACAGGTTCAGAACAGCCTCCTG
AAAAAGGAGAAGGAGCTGGAGAAGCAGCAGTGCATGGCCACAGAACTTGAAATGACAGTC
AAGGAGGCTAAGCAGGACAAGTCCAAGGAGGCGGAGTGCAAGGCCCTGCAGGCTGAGGTC
CAGAAGCTGAAGAACAGTCTCGAAGAGGCCAAGCAGCAGGAGAGGCTGGCTGCTCAGCAA
GCAGCCCAGTGCAAAGAAGAGGCTGCACTGGCAGGCTGTCACCTGGAGGACACCCAGAGG
AAACTGCAGAAGGGTCTCCTCCTGGACAAGCAGAAGGCAGACACCATCCAGGAACTACAG
AGAGAACTTCAGATGCTGCAGAAGGAGTCCTCGATGGCTGAGAAGGAACAAACCTCCAAC
AGAAAACGGGTGGAGGAGCTGTCATTAGAACTCTCTGAAGCCCTGAGGAAGCTTGAAAAT
TCAGACAAGGAAAAGAGGCAGCTTCAGAAGACAGTGGCTGAGCAGGATATGAAAATGAAT
GACATGCTTGATCGTATCAAGCACCAGCACAGGGAGCAAGGCTCCATCAAATGCAAGTTA
GAAGAAGATCTTCAGGAGGCCACAAAGCTTCTGGAGGACAAACGGGAGCAGTTGAAGAAG
AGCAAAGAGCATGAGAAGCTGATGGAGGGAGAACTTGAAGCTTTGCGGCAGGAATTTAAA
AAGAAAGACAAGACGTTGAAAGAGAATTCCAGAAAGTTGGAGGAAGAAAATGAGAATCTC
CGAGCAGAGCTACAGTGTTGTTCTACACAACTGGAATCCTCTCTCAACAAATACAACACC
AGCCAGCAAGTCATCCAAGACTTGAATAAAGAGATAGCCCTTCAGAAGGAGTCCTTAATG
AGCCTGCAGGCCCAGCTGGACAAAGCTCTGCAGAAGGAGAAGCACTATCTCCAGACTACC
ATCACCAAAGAAGCCTATGATGCATTATCCCGGAAGTCAGCCGCCTGCCAGGATGACCTG
ACACAAGCCCTCGAGAAGCTCAATCACGTGACCTCAGAGACAAAGAGCCTGCAGCAAAGC
TTGACACAGACCCAAGAGAAGAAAGCTCAGCTGGAAGAGGAAATCATTGCTTATGAGGAA
AGGATGAAAAAGCTCAATACGGAATTAAGAAAACTGCGGGGCTTCCACCAGGAGAGTGAG
CTGGAGGTGCACGCCTTTGACAAGAAGCTAGAGGAGATGAGCTGCCAGGTGCTGCAGTGG
CAGAAGCAACACCAGAATGACCTCAAGATGCTGGCAGCCAAAGAGGAGCAGCTCAGGGAG
TTCCAGGAGGAGATGGCCGCCTTAAAAGAGAACCTCCTTGAGGACGATAAGGAGCCCTGC
TGCCTGCCCCAGTGGTCTGTGCCCAAAGACACCTGTAGGCTCTACCGAGGGAATGATCAG
ATTATGACCAACTTGGAGCAATGGGCAAAACAGCAGAAGGTCGCCAATGAGAAACTAGGA
AACCAGCTCCGAGAGCAGGTGAACTACATTGCCAAGCTGAGTGGCGAAAAGGACAGGGAA
CCAACCAGAGCCAGCAGCCCCAACACAACCCGTCCTTCCTCTCCTTCCCACAGCCACCTC
CACAGTGTAATGGTCCACTTGCAGCAGGAAAACAAGAAGCTGAAGAAGGAGATAGAAGAG
AAGAAGATGAAAGCCGAGAACACAAGGCTATGCACCAAAGCCCTAGGCCCGAGCAGAACG
GAGTCCACACAGAGGGAGAAAGTGTGCGGCACCTTGGGCTGGAAGGGGTTGCCCCAGGAT
ATGGGTCAAAGAATGGACCTCACCAAGTACATCGGGATGCCCCACTGCCCGGGTTCCTCA
TACTGCTAG
Enzyme 48 GenBank Gene ID AK122925 Link Image
Enzyme 48 GeneCard ID Not Available
Enzyme 48 GenAtlas ID Not Available
Enzyme 48 HGNC ID HGNC:17728 Link Image
Enzyme 48 Chromosome Location Not Available
Enzyme 48 Locus Not Available
Enzyme 48 SNPs Not Available
Enzyme 48 General References
  1. 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 Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 17758
Enzyme 49 Name Virion infectivity factor
Enzyme 49 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 49 Gene Name vif
Enzyme 49 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRINTWKSLVKYHMNVSKKARKWLYRHHYDSNHPKISSEVHIPLG
EAILVITTYWGLQTGERDWHLGQGVSIEWRQRRYRTQVDPGLADQLIHMCYFDCFSDSAI
RKAILGQIVSPRCDYQAGHNKVGSLQYLALTALIRPKRRKPPLPSVQKLVEDRWNKPQKT
TGHRESHTMNGH
Enzyme 49 Number of Residues 192
Enzyme 49 Molecular Weight 22679.0
Enzyme 49 Theoretical pI 10.48
Enzyme 49 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 49 General Function Involved in viral infectious cycle
Enzyme 49 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 4336332 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q9WC55 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name VIF_HV1S2 Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAGGTAGACAGGATGAGGATTAACACA
TGGAAAAGTTTAGTAAAGTACCATATGAATGTTTCAAAGAAAGCTAGAAAATGGCTGTAT
AGGCATCACTATGACAGCAATCATCCAAAAATAAGTTCAGAAGTACACATCCCACTAGGA
GAGGCTATATTAGTAATAACAACATATTGGGGTCTGCAGACAGGAGAAAGAGATTGGCAC
TTGGGTCAGGGAGTCTCCATAGAATGGAGGCAGAGAAGGTACAGAACACAAGTAGACCCT
GGCCTGGCAGACCAACTAATTCATATGTGTTACTTTGATTGTTTTTCAGACTCTGCCATA
AGGAAGGCCATATTAGGACAAATAGTTAGCCCTAGGTGTGACTACCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATATCTGGCACTAACAGCATTAATAAGACCAAAAAGGAGAAAG
CCACCTTTGCCTAGTGTTCAGAAACTAGTAGAGGATAGATGGAACAAGCCCCAGAAGACC
ACGGGCCACAGAGAGAGCCATACCATGAATGGACACTAG
Enzyme 49 GenBank Gene ID AF082394 Link Image
Enzyme 49 GeneCard ID vif Link Image
Enzyme 49 GenAtlas ID Not Available
Enzyme 49 HGNC ID Not Available
Enzyme 49 Chromosome Location Not Available
Enzyme 49 Locus Not Available
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Laukkanen T, Albert J, Liitsola K, Green SD, Carr JK, Leitner T, McCutchan FE, Salminen MO: Virtually full-length sequences of HIV type 1 subtype J reference strains. AIDS Res Hum Retroviruses. 1999 Feb 10;15(3):293-7. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 17759
Enzyme 50 Name Virion infectivity factor
Enzyme 50 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 50 Gene Name vif
Enzyme 50 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIKTWNSLVKHHMYVSKKAKKWVYRHHYESTNPKTSSEVHIPVG
DARLVITTYWGLHTGERDWHLGHGVSIEWRQERYSTQIDPDLADQLIHLHYFDCFSDSAI
RKAILGHRVSPICDYQAGHRKVGSLQYLALTALISPKRTKPPLPSVRKLVEDRWNKPQKT
RGHRGSHTMNGH
Enzyme 50 Number of Residues 192
Enzyme 50 Molecular Weight 22588.8
Enzyme 50 Theoretical pI 10.45
Enzyme 50 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 50 General Function Involved in viral infectious cycle
Enzyme 50 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 6580987 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q9Q719 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name VIF_HV1V9 Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAGGTAGACAGGATGAGGATTAAAACA
TGGAACAGCTTAGTAAAGCATCATATGTATGTTTCAAAGAAAGCTAAAAAATGGGTTTAT
AGACATCATTATGAAAGTACTAACCCAAAGACAAGTTCAGAAGTACACATCCCAGTAGGG
GATGCTAGGTTAGTCATAACAACATATTGGGGTCTGCATACCGGAGAAAGAGACTGGCAT
TTGGGTCATGGAGTCTCCATAGAATGGAGACAGGAAAGGTATAGCACACAAATAGACCCT
GACCTGGCAGATCAACTAATTCATTTGCATTATTTTGATTGTTTTTCAGACTCTGCCATA
AGGAAAGCTATATTAGGACATAGAGTTAGTCCCATTTGTGACTATCAAGCAGGACATAGA
AAGGTAGGATCTTTACAATATTTGGCACTGACAGCATTAATATCACCAAAAAGGACAAAG
CCACCTTTGCCTAGTGTTAGAAAACTAGTAGAGGATAGATGGAACAAGCCCCAGAAGACC
AGGGGCCACAGAGGGAGCCACACAATGAATGGACACTAG
Enzyme 50 GenBank Gene ID AF190127 Link Image
Enzyme 50 GeneCard ID vif Link Image
Enzyme 50 GenAtlas ID Not Available
Enzyme 50 HGNC ID Not Available
Enzyme 50 Chromosome Location Not Available
Enzyme 50 Locus Not Available
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Janssens W, Laukkanen T, Salminen MO, Carr JK, Van der Auwera G, Heyndrickx L, van der Groen G, McCutchan FE: HIV-1 subtype H near-full length genome reference strains and analysis of subtype-H-containing inter-subtype recombinants. AIDS. 2000 Jul 28;14(11):1533-43. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 17760
Enzyme 51 Name Virion infectivity factor
Enzyme 51 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 51 Gene Name vif
Enzyme 51 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWNSLVKHHMYISGKAKGWIYKHHYESTNPRVSSEVQIPLG
DARLVITTYWGLHTGERDWHLGQGVSMEWRTRRYSTQVDPDLADQLIHLYYFDCFSESAI
RNAILGHIVSPRCEYQAGHSKVGSLQYLALTALIKPKKIKPPLPSVKKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 51 Number of Residues 192
Enzyme 51 Molecular Weight 22442.7
Enzyme 51 Theoretical pI 10.31
Enzyme 51 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 51 General Function Involved in viral infectious cycle
Enzyme 51 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 327816 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID P20877 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name VIF_HV1JR Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAACAGTTTAGTAAAACACCATATGTATATTTCAGGGAAAGCTAAGGGATGGATTTAT
AAACATCACTATGAAAGCACTAATCCAAGAGTAAGTTCAGAAGTACAAATCCCACTAGGG
GATGCTAGATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
TTGGGTCAGGGAGTCTCCATGGAATGGAGGACAAGGAGATATAGCACACAAGTAGACCCT
GACCTAGCAGACCAACTAATTCATCTGTATTACTTTGATTGTTTTTCAGAATCTGCTATA
AGGAATGCCATATTAGGACATATAGTTAGTCCTAGATGTGAATATCAAGCAGGACATAGC
AAGGTAGGATCTCTACAGTACTTGGCACTAACAGCATTAATAAAACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTAAGAAACTAACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCATACAATGAATGGACACTAG
Enzyme 51 GenBank Gene ID M38429 Link Image
Enzyme 51 GeneCard ID vif Link Image
Enzyme 51 GenAtlas ID Not Available
Enzyme 51 HGNC ID Not Available
Enzyme 51 Chromosome Location Not Available
Enzyme 51 Locus Not Available
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 17761
Enzyme 52 Name Virion infectivity factor
Enzyme 52 Synonyms
  1. Vif
  2. SOR protein
  3. Virion infectivity factor p17
  4. Virion infectivity factor p7
Enzyme 52 Gene Name vif
Enzyme 52 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRINTWKRLVKHHMYISRKAKDWFYRHHYESTNPKISSEVHIPLG
DAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLHYFDCFSESAI
RNTILGRIVSPRCEYQAGHNKVGSLQYLALAALIKPKQIKPPLPSVRKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 52 Number of Residues 192
Enzyme 52 Molecular Weight 22699.0
Enzyme 52 Theoretical pI 10.49
Enzyme 52 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 52 General Function Involved in viral infectious cycle
Enzyme 52 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 328420 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID P12504 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name VIF_HV1N5 Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAACACA
TGGAAAAGATTAGTAAAACACCATATGTATATTTCAAGGAAAGCTAAGGACTGGTTTTAT
AGACATCACTATGAAAGTACTAATCCAAAAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAAATTAGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
TTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GACCTAGCAGACCAACTAATTCATCTGCACTATTTTGATTGTTTTTCAGAATCTGCTATA
AGAAATACCATATTAGGACGTATAGTTAGTCCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAGTACTTGGCACTAGCAGCATTAATAAAACCAAAACAGATAAAG
CCACCTTTGCCTAGTGTTAGGAAACTGACAGAGGACAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCATACAATGAATGGACACTAG
Enzyme 52 GenBank Gene ID M19921 Link Image
Enzyme 52 GeneCard ID vif Link Image
Enzyme 52 GenAtlas ID Not Available
Enzyme 52 HGNC ID Not Available
Enzyme 52 Chromosome Location Not Available
Enzyme 52 Locus Not Available
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Schwartz S, Felber BK, Pavlakis GN: Expression of human immunodeficiency virus type 1 vif and vpr mRNAs is Rev-dependent and regulated by splicing. Virology. 1991 Aug;183(2):677-86. [PubMed Link Image]
  2. Hoglund S, Ohagen A, Lawrence K, Gabuzda D: Role of vif during packing of the core of HIV-1. Virology. 1994 Jun;201(2):349-55. [PubMed Link Image]
  3. Simon JH, Sheehy AM, Carpenter EA, Fouchier RA, Malim MH: Mutational analysis of the human immunodeficiency virus type 1 Vif protein. J Virol. 1999 Apr;73(4):2675-81. [PubMed Link Image]
  4. Yang S, Sun Y, Zhang H: The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle. J Biol Chem. 2001 Feb 16;276(7):4889-93. Epub 2000 Nov 8. [PubMed Link Image]
  5. Khan MA, Aberham C, Kao S, Akari H, Gorelick R, Bour S, Strebel K: Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA. J Virol. 2001 Aug;75(16):7252-65. [PubMed Link Image]
  6. Hassaine G, Courcoul M, Bessou G, Barthalay Y, Picard C, Olive D, Collette Y, Vigne R, Decroly E: The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein. J Biol Chem. 2001 May 18;276(20):16885-93. Epub 2001 Feb 27. [PubMed Link Image]
  7. Khan MA, Akari H, Kao S, Aberham C, Davis D, Buckler-White A, Strebel K: Intravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif function. J Virol. 2002 Sep;76(18):9112-23. [PubMed Link Image]
  8. Kao S, Khan MA, Miyagi E, Plishka R, Buckler-White A, Strebel K: The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity. J Virol. 2003 Nov;77(21):11398-407. [PubMed Link Image]
  9. Lake JA, Carr J, Feng F, Mundy L, Burrell C, Li P: The role of Vif during HIV-1 infection: interaction with novel host cellular factors. J Clin Virol. 2003 Feb;26(2):143-52. [PubMed Link Image]
  10. Marin M, Rose KM, Kozak SL, Kabat D: HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat Med. 2003 Nov;9(11):1398-403. Epub 2003 Oct 5. [PubMed Link Image]
  11. Mehle A, Goncalves J, Santa-Marta M, McPike M, Gabuzda D: Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev. 2004 Dec 1;18(23):2861-6. [PubMed Link Image]
  12. Mehle A, Strack B, Ancuta P, Zhang C, McPike M, Gabuzda D: Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J Biol Chem. 2004 Feb 27;279(9):7792-8. Epub 2003 Dec 13. [PubMed Link Image]
  13. Feng F, Davis A, Lake JA, Carr J, Xia W, Burrell C, Li P: Ring finger protein ZIN interacts with human immunodeficiency virus type 1 Vif. J Virol. 2004 Oct;78(19):10574-81. [PubMed Link Image]
  14. Luo K, Xiao Z, Ehrlich E, Yu Y, Liu B, Zheng S, Yu XF: Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc Natl Acad Sci U S A. 2005 Aug 9;102(32):11444-9. Epub 2005 Aug 2. [PubMed Link Image]
  15. Farrow MA, Somasundaran M, Zhang C, Gabuzda D, Sullivan JL, Greenough TC: Nuclear localization of HIV type 1 Vif isolated from a long-term asymptomatic individual and potential role in virus attenuation. AIDS Res Hum Retroviruses. 2005 Jun;21(6):565-74. [PubMed Link Image]
  16. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 17762
Enzyme 53 Name Virion infectivity factor
Enzyme 53 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 53 Gene Name vif
Enzyme 53 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRAWKSLVKHHMYISGKARGWFYRHHYESPHPRISSEVHIPLG
DAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLYYFDCFSESAI
RKAILGYRVSPRCEYQAGHNKVGSLQYLALTALITPKKTKPPLPSVKKLTEDRWNKPQKT
KGHRGSRTMNGH
Enzyme 53 Number of Residues 192
Enzyme 53 Molecular Weight 22601.9
Enzyme 53 Theoretical pI 10.53
Enzyme 53 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 53 General Function Involved in viral infectious cycle
Enzyme 53 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein Not Available
Enzyme 53 UniProtKB/Swiss-Prot ID P35964 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name VIF_HV1Y2 Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence Not Available
Enzyme 53 GenBank Gene ID Not Available
Enzyme 53 GeneCard ID vif Link Image
Enzyme 53 GenAtlas ID Not Available
Enzyme 53 HGNC ID Not Available
Enzyme 53 Chromosome Location Not Available
Enzyme 53 Locus Not Available
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Li Y, Hui H, Burgess CJ, Price RW, Sharp PM, Hahn BH, Shaw GM: Complete nucleotide sequence, genome organization, and biological properties of human immunodeficiency virus type 1 in vivo: evidence for limited defectiveness and complementation. J Virol. 1992 Nov;66(11):6587-600. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 17763
Enzyme 54 Name Virion infectivity factor
Enzyme 54 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 54 Gene Name vif
Enzyme 54 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLG
DARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAI
RKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 54 Number of Residues 192
Enzyme 54 Molecular Weight 22512.8
Enzyme 54 Theoretical pI 10.40
Enzyme 54 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 54 General Function Involved in viral infectious cycle
Enzyme 54 Specific Function Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin- proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology. Interacts with host ABCE1, which seems to be involved in lentiviruses capsid formation and displays RNase L inhibitor activity. This interaction may play a role in protecting viral RNA from damage during viral assembly. May interact with host SAT, which is a regulator of polyamine cell level. This interaction may be relevant since polyamines affect viral RNA properties
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 328454 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID P69722 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name VIF_HV112 Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAGGGAAAGCTAGGGGATGGTTTTAT
AGACATCACTATGAAAGCCCTCATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAGATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
TTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GAACTAGCAGACCAACTAATTCATCTGTATTACTTTGACTGTTTTTCAGACTCTGCTATA
AGAAAGGCCTTATTAGGACACATAGTTAGCCCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATACTTGGCACTAGCAGCATTAATAACACCAAAAAAGATAAAG
CCACCTTTGCCTAGTGTTACGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCACACAATGAATGGACACTAG
Enzyme 54 GenBank Gene ID M11840 Link Image
Enzyme 54 GeneCard ID vif Link Image
Enzyme 54 GenAtlas ID Not Available
Enzyme 54 HGNC ID Not Available
Enzyme 54 Chromosome Location Not Available
Enzyme 54 Locus Not Available
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Arya SK, Gallo RC: Three novel genes of human T-lymphotropic virus type III: immune reactivity of their products with sera from acquired immune deficiency syndrome patients. Proc Natl Acad Sci U S A. 1986 Apr;83(7):2209-13. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 17764
Enzyme 55 Name Truncated virion infectivity factor
Enzyme 55 Synonyms
  1. Vif
  2. SOR protein
  3. Truncated p17
Enzyme 55 Gene Name vif
Enzyme 55 Protein Sequence >Truncated virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLG
DARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAI
RKALLGHIVSPR
Enzyme 55 Number of Residues 132
Enzyme 55 Molecular Weight 15854.1
Enzyme 55 Theoretical pI 10.02
Enzyme 55 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 55 General Function Involved in viral infectious cycle
Enzyme 55 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 665535 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID Q70623 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name VIF_HV1LW Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >399 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAGGGAAAGCTAGGGGATGGTTTTAT
AGACATCACTATGAAAGCCCTCATCCAAGAATAAGTTCAGAAGTACACATCCCACTAGGG
GATGCTAGATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
TTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAAGAGATATAGCACACAAGTAGACCCT
GAACTAGCAGACCAACTAATTCATCTGTATTACTTTGACTGTTTTTCAGACTCTGCTATA
AGAAAGGCCTTATTAGGACACATAGTTAGCCCTAGGTGA
Enzyme 55 GenBank Gene ID U12055 Link Image
Enzyme 55 GeneCard ID vif Link Image
Enzyme 55 GenAtlas ID Not Available
Enzyme 55 HGNC ID Not Available
Enzyme 55 Chromosome Location Not Available
Enzyme 55 Locus Not Available
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Reitz MS Jr, Hall L, Robert-Guroff M, Lautenberger J, Hahn BM, Shaw GM, Kong LI, Weiss SH, Waters D, Gallo RC, et al.: Viral variability and serum antibody response in a laboratory worker infected with HIV type 1 (HTLV type IIIB). AIDS Res Hum Retroviruses. 1994 Sep;10(9):1143-55. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 17765
Enzyme 56 Name Virion infectivity factor
Enzyme 56 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 56 Gene Name vif
Enzyme 56 Protein Sequence >Virion infectivity factor
MENRWQVLIVWQIDRQKVKAWNSLVKYHKYMSKKAANWRYRHHYESRNPKVSSAVYIPVA
EADIVVTTYWGLMPGEREEHLGHGVSIEWQYKEYKTQIDPETADRMIHLHYFTCFTESAI
RKAILGQRVLTKCEYLAGHSQVGTLQFLALKAVVKVKRNKPPLPSVQRLTEDRWNKPWKI
RDQLGSHSMNGH
Enzyme 56 Number of Residues 192
Enzyme 56 Molecular Weight 22657.0
Enzyme 56 Theoretical pI 10.20
Enzyme 56 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 56 General Function Involved in viral infectious cycle
Enzyme 56 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 469242 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID Q79667 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name VIF_HV1MV Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTACTGATAGTATGGCAAATAGACAGACAGAAAGTGAAAGCA
TGGAACAGCCTGGTGAAATACCATAAATACATGTCTAAGAAGGCCGCGAACTGGCGTTAT
AGGCATCATTATGAATCCAGGAATCCAAAAGTCAGTTCGGCGGTGTATATTCCAGTAGCA
GAAGCTGATATAGTGGTCACCACATATTGGGGATTAATGCCAGGGGAAAGAGAGGAACAC
TTGGGACATGGGGTTAGTATAGAATGGCAATACAAGGAGTATAAAACACAGATTGATCCT
GAAACAGCAGACAGGATGATACATCTGCATTATTTCACATGTTTTACAGAATCAGCAATC
AGGAAGGCCATTCTAGGGCAGAGAGTGCTGACCAAGTGTGAATACCTGGCAGGACATAGT
CAGGTAGGGACACTACAATTCTTAGCCTTGAAAGCAGTAGTGAAAGTAAAAAGAAATAAG
CCTCCCCTACCCAGTGTCCAGAGATTAACAGAAGATAGATGGAACAAGCCCTGGAAAATC
AGGGACCAGCTAGGGAGCCATTCAATGAATGGACACTAG
Enzyme 56 GenBank Gene ID L20571 Link Image
Enzyme 56 GeneCard ID vif Link Image
Enzyme 56 GenAtlas ID Not Available
Enzyme 56 HGNC ID Not Available
Enzyme 56 Chromosome Location Not Available
Enzyme 56 Locus Not Available
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Gurtler LG, Hauser PH, Eberle J, von Brunn A, Knapp S, Zekeng L, Tsague JM, Kaptue L: A new subtype of human immunodeficiency virus type 1 (MVP-5180) from Cameroon. J Virol. 1994 Mar;68(3):1581-5. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 17766
Enzyme 57 Name Virion infectivity factor
Enzyme 57 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 57 Gene Name vif
Enzyme 57 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMKIRTWNSLVKHHMYVSKKAQGWFYRHHYESRHSRVSSEVHIPLG
EARLVVRTYWGLHTGEKDWHLGHGVSIEWRLKRYSTQVDPDLADHLIHLHYFDCFSESAI
RRAILGQIVRPRCEYQAGHNKVGSLQYLALKALVTPTRAKPPLPSVKKLTEDRWNKPQKT
RGHRGSRTLNRH
Enzyme 57 Number of Residues 192
Enzyme 57 Molecular Weight 22798.1
Enzyme 57 Theoretical pI 10.84
Enzyme 57 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 57 General Function Involved in viral infectious cycle
Enzyme 57 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 328907 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID P24737 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name VIF_HV1U4 Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTATGGCAGGTAGACAGGATGAAGATTAGAACA
TGGAACAGTTTAGTAAAACATCACATGTATGTCTCCAAGAAAGCTCAAGGTTGGTTTTAT
AGACATCACTATGAAAGTAGACATTCAAGAGTAAGTTCAGAAGTACACATCCCACTAGGG
GAAGCTAGATTAGTAGTAAGAACATATTGGGGTCTGCATACAGGAGAAAAAGACTGGCAC
TTGGGTCATGGGGTCTCCATAGAATGGAGGCTGAAAAGATATAGCACACAAGTAGATCCT
GACCTAGCAGACCATCTAATTCACCTGCATTATTTTGACTGTTTTTCAGAATCTGCCATA
AGGAGAGCCATATTAGGACAAATAGTTAGACCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATATTTGGCTCTGAAAGCATTAGTAACCCCAACAAGGGCAAAG
CCACCTTTGCCTAGTGTTAAGAAATTAACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AGGGGCCACAGAGGGAGCCGTACGCTGAATAGGCATTAG
Enzyme 57 GenBank Gene ID M62320 Link Image
Enzyme 57 GeneCard ID vif Link Image
Enzyme 57 GenAtlas ID Not Available
Enzyme 57 HGNC ID Not Available
Enzyme 57 Chromosome Location Not Available
Enzyme 57 Locus Not Available
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Oram JD, Downing RG, Roff M, Clegg JC, Serwadda D, Carswell JW: Nucleotide sequence of a Ugandan HIV-1 provirus reveals genetic diversity from other HIV-1 isolates. AIDS Res Hum Retroviruses. 1990 Sep;6(9):1073-8. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 17767
Enzyme 58 Name Virion infectivity factor
Enzyme 58 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 58 Gene Name vif
Enzyme 58 Protein Sequence >Virion infectivity factor
MENRWQVLIVWQVDRMKIRTWNSLVKHHMYVSRRASGWYYRHHYESRHPKISSEVHIPLG
EARLVIITYWGLQTGERDWHLGHGVSIEWRLRRYSTRVDPGLADQLIHMHYFDCFADSAI
RKAILGHRVSSRCDYQAGHNKVGSLQYLALTALIKPKKIKPPLPSVKKLVEDRWNKPQKT
RDRRGNHTMNGH
Enzyme 58 Number of Residues 192
Enzyme 58 Molecular Weight 22762.1
Enzyme 58 Theoretical pI 10.77
Enzyme 58 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 58 General Function Involved in viral infectious cycle
Enzyme 58 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 58 Pathways Not Available
Enzyme 58 Reactions Not Available
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 2194189 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID O12159 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name VIF_HV192 Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGCTGATTGTATGGCAAGTAGACAGGATGAAGATTAGAACA
TGGAATAGTTTAGTAAAGCACCACATGTATGTTTCAAGGAGAGCTAGTGGATGGTATTAT
AGACATCATTATGAAAGCAGACATCCAAAAATAAGTTCAGAAGTACACATTCCATTAGGG
GAGGCTAGATTAGTAATAATAACATATTGGGGTTTGCAAACAGGAGAAAGAGATTGGCAT
TTGGGTCATGGAGTCTCCATAGAGTGGAGACTGAGAAGATATAGCACACGAGTAGACCCT
GGCCTGGCAGACCAACTAATTCATATGCATTATTTTGATTGTTTTGCAGACTCTGCCATA
AGGAAAGCCATATTAGGACATAGAGTTAGCTCTAGGTGTGACTATCAAGCAGGACATAAT
AAGGTAGGATCTCTACAATACCTGGCACTGACAGCATTGATAAAACCAAAAAAGATAAAG
CCACCTCTGCCTAGTGTTAAGAAATTAGTAGAGGATAGATGGAACAAGCCCCAGAAGACC
AGGGACCGCAGAGGGAACCATACAATGAATGGACACTAG
Enzyme 58 GenBank Gene ID U52953 Link Image
Enzyme 58 GeneCard ID vif Link Image
Enzyme 58 GenAtlas ID Not Available
Enzyme 58 HGNC ID Not Available
Enzyme 58 Chromosome Location Not Available
Enzyme 58 Locus Not Available
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Gao F, Morrison SG, Robertson DL, Thornton CL, Craig S, Karlsson G, Sodroski J, Morgado M, Galvao-Castro B, von Briesen H, Beddows S, Weber J, Sharp PM, Shaw GM, Hahn BH: Molecular cloning and analysis of functional envelope genes from human immunodeficiency virus type 1 sequence subtypes A through G. The WHO and NIAID Networks for HIV Isolation and Characterization. J Virol. 1996 Mar;70(3):1651-67. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 17768
Enzyme 59 Name Virion infectivity factor
Enzyme 59 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 59 Gene Name vif
Enzyme 59 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIKTWKSLVKHHMYVSKKANRWFYRHHYESPHPKISSEVHIPLG
EARLVIKTYWGLHTGEREWHLGQGVSIEWRKRRYSTQVDPGLADQLIHMYYFDCFSESAI
RKAILGDIVSPRCEYQAGHNKVGSLQYLALTALIAPKQIKPPLPSVRKLTEDRWNKPQQT
RGHRGSHTMNGH
Enzyme 59 Number of Residues 192
Enzyme 59 Molecular Weight 22689.1
Enzyme 59 Theoretical pI 10.48
Enzyme 59 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 59 General Function Involved in viral infectious cycle
Enzyme 59 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions Not Available
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 326680 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID P04597 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name VIF_HV1EL Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAAAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAAAGAAAGCTAACAGATGGTTTTAT
AGACATCACTATGAAAGCCCCCACCCAAAAATAAGTTCAGAAGTACACATCCCACTAGGA
GAAGCTAGACTGGTAATAAAAACATATTGGGGTCTGCATACAGGAGAAAGAGAATGGCAT
CTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAGGAGATATAGCACACAAGTAGACCCT
GGCCTGGCAGACCAACTAATTCATATGTATTATTTTGATTGTTTTTCAGAATCTGCTATA
AGAAAAGCCATATTAGGAGATATAGTTAGTCCTAGGTGTGAGTATCAAGCAGGACATAAC
AAGGTAGGATCCCTACAGTATTTGGCACTAACAGCATTAATAGCACCAAAACAGATAAAG
CCACCTTTGCCTAGTGTTAGGAAGCTAACAGAAGATAGATGGAACAAGCCCCAGCAGACC
AGGGGCCACAGAGGGAGCCATACAATGAATGGGCATTAG
Enzyme 59 GenBank Gene ID K03454 Link Image
Enzyme 59 GeneCard ID vif Link Image
Enzyme 59 GenAtlas ID Not Available
Enzyme 59 HGNC ID Not Available
Enzyme 59 Chromosome Location Not Available
Enzyme 59 Locus Not Available
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Alizon M, Wain-Hobson S, Montagnier L, Sonigo P: Genetic variability of the AIDS virus: nucleotide sequence analysis of two isolates from African patients. Cell. 1986 Jul 4;46(1):63-74. [PubMed Link Image]
  2. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 17769
Enzyme 60 Name Virion infectivity factor
Enzyme 60 Synonyms
  1. Vif
  2. SOR protein
Enzyme 60 Gene Name vif
Enzyme 60 Protein Sequence >Virion infectivity factor
MENRWQVVIVWQVDRMRIRTWNSLVKHHMYVSKKAKGWFYRHHYESRHPRVSSEVHIPLR
DATLVVRTYWGLHAGEKDWQLGHGVSIEWRQKRYSTQIDPNTADHLIHLYYFDCFSESAI
RKAILGEIVSPRCEYPAGHNKVGSLQYLASKALVTPTRKRPPLPSVGKLAEDRWNKPQKT
RDHRENPTMNGH
Enzyme 60 Number of Residues 192
Enzyme 60 Molecular Weight 22684.8
Enzyme 60 Theoretical pI 10.42
Enzyme 60 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 60 General Function Involved in viral infectious cycle
Enzyme 60 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • None
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 2570331 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID O41799 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name VIF_HV19N Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGGTGATTGTGTGGCAGGTAGACAGGATGAGGATTAGAACA
TGGAACAGTTTAGTAAAACATCATATGTATGTCTCAAAGAAAGCTAAAGGCTGGTTTTAT
AGACATCACTATGAAAGCAGGCATCCAAGAGTAAGTTCAGAAGTACACATCCCACTAAGA
GATGCTACACTAGTAGTAAGAACATATTGGGGTCTGCATGCAGGAGAAAAAGACTGGCAA
TTGGGCCATGGGGTTTCCATAGAATGGAGGCAGAAAAGATATAGTACACAAATAGACCCT
AACACAGCAGACCATCTGATTCATCTGTATTATTTTGACTGTTTTTCAGAATCTGCCATA
AGAAAAGCCATATTAGGAGAGATAGTTAGCCCTAGGTGTGAATACCCAGCAGGACATAAT
AAGGTAGGATCTCTACAATATCTGGCATCGAAAGCATTAGTAACACCAACAAGGAAAAGG
CCACCTTTGCCAAGTGTTGGGAAATTAGCAGAAGATAGATGGAACAAGCCCCAGAAGACC
AGGGACCACAGAGAGAACCCTACAATGAATGGACATTAG
Enzyme 60 GenBank Gene ID U88826 Link Image
Enzyme 60 GeneCard ID vif Link Image
Enzyme 60 GenAtlas ID Not Available
Enzyme 60 HGNC ID Not Available
Enzyme 60 Chromosome Location Not Available
Enzyme 60 Locus Not Available
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Gao F, Robertson DL, Carruthers CD, Morrison SG, Jian B, Chen Y, Barre-Sinoussi F, Girard M, Srinivasan A, Abimiku AG, Shaw GM, Sharp PM, Hahn BH: A comprehensive panel of near-full-length clones and reference sequences for non-subtype B isolates of human immunodeficiency virus type 1. J Virol. 1998 Jul;72(7):5680-98. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 17770
Enzyme 61 Name Virion infectivity factor
Enzyme 61 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 61 Gene Name vif
Enzyme 61 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRINTWKSLVKYHMHISKKAKGWFYRHHFESRHPKISSEVHIPLE
TAELVITTYWGLLPGEREWHLGQGVSIEWRQGRYRTQIDPGLADQLIHIYYFDCFSESAI
RKAILGHKISPRCNYQAGHNKVGSLQYLALTALIAPKKTKPPLPSVQKLVEDRWNKPQKT
RGHRESHTMNGH
Enzyme 61 Number of Residues 192
Enzyme 61 Molecular Weight 22641.0
Enzyme 61 Theoretical pI 10.43
Enzyme 61 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 61 General Function Involved in viral infectious cycle
Enzyme 61 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 3114550 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID O70887 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name VIF_HV193 Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAGGTAGACAGGATGAGGATTAACACA
TGGAAAAGTTTAGTAAAATACCATATGCATATTTCAAAGAAAGCCAAAGGATGGTTTTAT
AGACATCACTTTGAAAGCAGGCATCCAAAAATAAGTTCAGAAGTACACATCCCACTAGAG
ACAGCTGAATTAGTAATAACAACATACTGGGGGCTGCTTCCAGGAGAAAGAGAATGGCAT
CTGGGTCAGGGAGTCTCCATAGAATGGAGGCAGGGGAGGTATAGAACACAAATAGACCCT
GGCCTGGCAGACCAACTGATCCATATATATTATTTTGATTGTTTTTCAGAATCTGCCATA
AGGAAAGCCATATTAGGACATAAAATTAGCCCTAGGTGTAACTATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATACTTGGCACTAACAGCATTAATAGCTCCAAAAAAGACAAAG
CCGCCTTTGCCTAGTGTCCAGAAACTAGTAGAAGACAGATGGAACAAGCCCCAGAAGACC
AGGGGCCACAGAGAGAGCCATACAATGAATGGACACTAG
Enzyme 61 GenBank Gene ID AF005494 Link Image
Enzyme 61 GeneCard ID vif Link Image
Enzyme 61 GenAtlas ID Not Available
Enzyme 61 HGNC ID Not Available
Enzyme 61 Chromosome Location Not Available
Enzyme 61 Locus Not Available
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Gao F, Robertson DL, Carruthers CD, Morrison SG, Jian B, Chen Y, Barre-Sinoussi F, Girard M, Srinivasan A, Abimiku AG, Shaw GM, Sharp PM, Hahn BH: A comprehensive panel of near-full-length clones and reference sequences for non-subtype B isolates of human immunodeficiency virus type 1. J Virol. 1998 Jul;72(7):5680-98. [PubMed Link Image]
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 17771
Enzyme 62 Name Virion infectivity factor
Enzyme 62 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 62 Gene Name vif
Enzyme 62 Protein Sequence >Virion infectivity factor
GVSIEWTKKRYSTQVDPDLADRLIHLYYFDCFSESAIRNAILGALVSGRCEYQAGHNKVG
SLQYLALTALITPKKTKPPLPSVRKLTEDRWNKPQKTKGHRGSHTMNGH
Enzyme 62 Number of Residues 109
Enzyme 62 Molecular Weight 12308.0
Enzyme 62 Theoretical pI 10.23
Enzyme 62 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 62 General Function Involved in viral infectious cycle
Enzyme 62 Specific Function Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin- proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology. Interacts with host ABCE1, which seems to be involved in lentiviruses capsid formation and displays RNase L inhibitor activity. This interaction may play a role in protecting viral RNA from damage during viral assembly. May interact with host SAT, which is a regulator of polyamine cell level. This interaction may be relevant since polyamines affect viral RNA properties
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions Not Available
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • None
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 328634 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID P05899 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name VIF_HV1SC Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >330 bp
GGAGTCTCCATAGAATGGACGAAAAAGAGATATAGCACACAAGTAGACCCTGACCTAGCA
GACCGACTAATTCATCTGTATTATTTTGATTGTTTTTCAGAGTCTGCTATAAGAAATGCC
ATATTAGGAGCTTTAGTTAGTGGTAGGTGTGAATATCAAGCAGGACATAACAAGGTAGGA
TCTCTACAGTACTTGGCACTAACAGCATTAATAACACCAAAAAAGACAAAGCCACCTTTG
CCTAGTGTTAGGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACCAAGGGCCAC
AGAGGGAGCCATACAATGAATGGACACTAG
Enzyme 62 GenBank Gene ID M17450 Link Image
Enzyme 62 GeneCard ID vif Link Image
Enzyme 62 GenAtlas ID Not Available
Enzyme 62 HGNC ID Not Available
Enzyme 62 Chromosome Location Not Available
Enzyme 62 Locus Not Available
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Gurgo C, Guo HG, Franchini G, Aldovini A, Collalti E, Farrell K, Wong-Staal F, Gallo RC, Reitz MS Jr: Envelope sequences of two new United States HIV-1 isolates. Virology. 1988 Jun;164(2):531-6. [PubMed Link Image]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 17772
Enzyme 63 Name Virion infectivity factor
Enzyme 63 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 63 Gene Name vif
Enzyme 63 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWNSLVKHHMYVSRRAKGWFYRHHYESRHPKVSSEVHIPLE
DDSKLVIITYWGLHTGERDWHLGHGVSIEWRQKRYRTQVDPDLADQLIHLRYFDCFSESA
IRNAILGHRVSPRCNYQAGHNKVGSLQYLALTALITPKKIKPPLPSVRKLVEDRWNNPQK
TKGHRGSHTMNGH
Enzyme 63 Number of Residues 193
Enzyme 63 Molecular Weight 22956.2
Enzyme 63 Theoretical pI 10.61
Enzyme 63 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 63 General Function Involved in viral infectious cycle
Enzyme 63 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions Not Available
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein Not Available
Enzyme 63 UniProtKB/Swiss-Prot ID P0C1L8 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name VIF_HV1MP Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence Not Available
Enzyme 63 GenBank Gene ID Not Available
Enzyme 63 GeneCard ID vif Link Image
Enzyme 63 GenAtlas ID Not Available
Enzyme 63 HGNC ID Not Available
Enzyme 63 Chromosome Location Not Available
Enzyme 63 Locus Not Available
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Triques K, Bourgeois A, Vidal N, Mpoudi-Ngole E, Mulanga-Kabeya C, Nzilambi N, Torimiro N, Saman E, Delaporte E, Peeters M: Near-full-length genome sequencing of divergent African HIV type 1 subtype F viruses leads to the identification of a new HIV type 1 subtype designated K. AIDS Res Hum Retroviruses. 2000 Jan 20;16(2):139-51. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 17773
Enzyme 64 Name Virion infectivity factor
Enzyme 64 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 64 Gene Name vif
Enzyme 64 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRINTWKSLVKYHMNVSKKARQWLYRHHYDSRHPKISSEVHIPLG
EARLVVTTYWGLQTGERDWHLGQGVSIEWRRKRYRTQVDPGLADQLIHMHYFDCFSDSAI
RKAILGQIVSPRCDYQAGHNKVGSLQYLALTALIKPKRRKPPLPSVQKLVEDRWNKPQKT
RDHRESHTMNGH
Enzyme 64 Number of Residues 192
Enzyme 64 Molecular Weight 22869.2
Enzyme 64 Theoretical pI 10.71
Enzyme 64 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 64 General Function Involved in viral infectious cycle
Enzyme 64 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 64 Pathways Not Available
Enzyme 64 Reactions Not Available
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • None
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 4336341 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID Q9WC64 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name VIF_HV1S9 Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAGGTAGACAGGATGAGGATTAACACA
TGGAAAAGTTTAGTAAAGTACCATATGAATGTTTCAAAGAAAGCTAGACAATGGCTGTAT
AGACATCACTATGATAGCCGTCATCCAAAAATAAGTTCAGAAGTACACATCCCACTAGGA
GAGGCTAGATTAGTAGTAACAACATATTGGGGTCTGCAAACAGGAGAAAGAGATTGGCAC
TTGGGTCAGGGAGTCTCCATAGAATGGAGGCGGAAAAGGTACAGAACACAAGTAGACCCT
GGCCTGGCAGACCAACTAATTCATATGCATTACTTTGATTGTTTTTCAGACTCTGCCATA
AGGAAGGCCATATTAGGACAAATAGTTAGCCCTAGGTGTGACTACCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATATCTGGCATTAACAGCATTAATAAAACCAAAAAGGAGAAAG
CCACCTTTGCCTAGTGTTCAGAAACTAGTAGAGGATAGATGGAACAAGCCCCAGAAGACC
AGGGACCACAGAGAGAGCCATACCATGAATGGACACTAG
Enzyme 64 GenBank Gene ID AF082395 Link Image
Enzyme 64 GeneCard ID vif Link Image
Enzyme 64 GenAtlas ID Not Available
Enzyme 64 HGNC ID Not Available
Enzyme 64 Chromosome Location Not Available
Enzyme 64 Locus Not Available
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Laukkanen T, Albert J, Liitsola K, Green SD, Carr JK, Leitner T, McCutchan FE, Salminen MO: Virtually full-length sequences of HIV type 1 subtype J reference strains. AIDS Res Hum Retroviruses. 1999 Feb 10;15(3):293-7. [PubMed Link Image]
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 17774
Enzyme 65 Name Virion infectivity factor
Enzyme 65 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 65 Gene Name vif
Enzyme 65 Protein Sequence >Virion infectivity factor
MENRWQVLIVWQVDRMKIRTWNSLVKHHMHISRRANGWVYRHHYDSRHPKVSSEVHIPLG
EARLIIKTYWGLQTGERDWHLGHGVSIEWRLRSYNTQVDPGLADHLIHMHYFDCFAESAI
RKAILGYRVSPRCDYQAGHNKVGSLQYLALTALIKPKKAKPPLPSVSKLVEDKWNKPQKT
RGRRGNHTMNGH
Enzyme 65 Number of Residues 192
Enzyme 65 Molecular Weight 22533.8
Enzyme 65 Theoretical pI 10.71
Enzyme 65 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 65 General Function Involved in viral infectious cycle
Enzyme 65 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 65 Pathways Not Available
Enzyme 65 Reactions Not Available
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • None
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 1353863 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID Q75003 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name VIF_HV1ET Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGCTGATTGTGTGGCAGGTAGACAGGATGAAGATTAGAACA
TGGAATAGTTTAGTAAAGCACCATATGCATATTTCAAGGAGAGCTAATGGATGGGTTTAT
AGACATCATTATGACAGCAGACATCCAAAGGTAAGTTCAGAAGTACACATCCCATTAGGG
GAGGCTAGATTAATAATAAAAACATATTGGGGTTTGCAAACAGGAGAAAGAGATTGGCAT
TTGGGTCATGGAGTCTCCATAGAATGGAGATTGAGAAGCTATAACACACAAGTAGACCCT
GGCCTGGCAGACCACCTAATTCATATGCATTATTTTGATTGTTTTGCAGAATCTGCCATA
AGGAAAGCCATATTAGGATATAGAGTTAGCCCTAGGTGTGACTATCAAGCAGGACATAAT
AAGGTAGGATCTCTACAATACTTGGCACTGACAGCATTGATAAAGCCAAAAAAGGCAAAG
CCACCTCTGCCTAGTGTTAGTAAATTAGTAGAGGATAAATGGAACAAGCCCCAGAAGACC
AGGGGCCGCAGAGGGAACCATACAATGAATGGGCACTAG
Enzyme 65 GenBank Gene ID U46016 Link Image
Enzyme 65 GeneCard ID vif Link Image
Enzyme 65 GenAtlas ID Not Available
Enzyme 65 HGNC ID Not Available
Enzyme 65 Chromosome Location Not Available
Enzyme 65 Locus Not Available
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References
  1. Salminen MO, Johansson B, Sonnerborg A, Ayehunie S, Gotte D, Leinikki P, Burke DS, McCutchan FE: Full-length sequence of an ethiopian human immunodeficiency virus type 1 (HIV-1) isolate of genetic subtype C. AIDS Res Hum Retroviruses. 1996 Sep 20;12(14):1329-39. [PubMed Link Image]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 17775
Enzyme 66 Name Virion infectivity factor
Enzyme 66 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 66 Gene Name vif
Enzyme 66 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISKKAKGWFYRHHYESTHPRVSSEVHIPLG
DAKLVITTYWGLHTGEREWHLGQGVAIEWRKKKYSTQVDPGLADQLIHLHYFDCFSESAI
KNAILGYRVSPRCEYQAGHNKVGSLQYLALAALITPKKTKPPLPSVKKLTEDRWNKPQKT
KGHRGSHTMNGH
Enzyme 66 Number of Residues 192
Enzyme 66 Molecular Weight 22459.9
Enzyme 66 Theoretical pI 10.51
Enzyme 66 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 66 General Function Involved in viral infectious cycle
Enzyme 66 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions Not Available
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 328663 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID P03402 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name VIF_HV1A2 Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATATTTCAAAGAAAGCTAAAGGATGGTTTTAT
AGACATCACTATGAAAGTACTCATCCAAGAGTAAGTTCAGAAGTACACATCCCCCTAGGG
GATGCTAAATTGGTAATAACAACATATTGGGGTCTGCATACAGGAGAAAGAGAATGGCAT
TTGGGCCAGGGAGTCGCCATAGAATGGAGGAAAAAGAAATATAGCACACAAGTAGACCCT
GGCCTAGCAGACCAACTAATTCATCTGCATTATTTTGATTGTTTTTCAGAATCTGCTATA
AAAAATGCCATATTAGGATATAGAGTTAGTCCTAGGTGTGAATATCAAGCAGGACATAAC
AAGGTAGGATCTCTACAATACTTGGCACTAGCAGCATTAATAACACCAAAAAAGACAAAG
CCACCTTTGCCTAGTGTTAAGAAACTGACAGAGGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAGAGGGAGCCATACAATGAATGGACACTAG
Enzyme 66 GenBank Gene ID K02007 Link Image
Enzyme 66 GeneCard ID vif Link Image
Enzyme 66 GenAtlas ID Not Available
Enzyme 66 HGNC ID Not Available
Enzyme 66 Chromosome Location Not Available
Enzyme 66 Locus Not Available
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Sanchez-Pescador R, Power MD, Barr PJ, Steimer KS, Stempien MM, Brown-Shimer SL, Gee WW, Renard A, Randolph A, Levy JA, et al.: Nucleotide sequence and expression of an AIDS-associated retrovirus (ARV-2). Science. 1985 Feb 1;227(4686):484-92. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 17776
Enzyme 67 Name Virion infectivity factor
Enzyme 67 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 67 Gene Name vif
Enzyme 67 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRINTWKSLVKYHMHISKKANRWYYRHHYESRHPKISSEVHIPLG
DAELVVTTYWGLLTGERDWHLGQGVSIEWRLKRYRTQVEPDLADQLIHIYYFDCFSESAV
RKAILGHRVSPRCECQAGHNKVGSLQYLALTALVAPRRPKPPVPSVKKLVEDRWNKPQKT
RGHRGSQTMNGH
Enzyme 67 Number of Residues 192
Enzyme 67 Molecular Weight 22688.0
Enzyme 67 Theoretical pI 10.42
Enzyme 67 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 67 General Function Involved in viral infectious cycle
Enzyme 67 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 67 Pathways Not Available
Enzyme 67 Reactions Not Available
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • None
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein Not Available
Enzyme 67 UniProtKB/Swiss-Prot ID P0C1K5 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name VIF_HV196 Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence Not Available
Enzyme 67 GenBank Gene ID Not Available
Enzyme 67 GeneCard ID vif Link Image
Enzyme 67 GenAtlas ID Not Available
Enzyme 67 HGNC ID Not Available
Enzyme 67 Chromosome Location Not Available
Enzyme 67 Locus Not Available
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Triques K, Bourgeois A, Vidal N, Mpoudi-Ngole E, Mulanga-Kabeya C, Nzilambi N, Torimiro N, Saman E, Delaporte E, Peeters M: Near-full-length genome sequencing of divergent African HIV type 1 subtype F viruses leads to the identification of a new HIV type 1 subtype designated K. AIDS Res Hum Retroviruses. 2000 Jan 20;16(2):139-51. [PubMed Link Image]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 17777
Enzyme 68 Name Virion infectivity factor
Enzyme 68 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 68 Gene Name vif
Enzyme 68 Protein Sequence >Virion infectivity factor
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSKKASRWFYRHHYDSPHPKISSEVHIPLG
EAMLVVKTYWGLHTGERDWHLGQGVSIEWRKRRYSTQVDPGLADQLIHMYYFDCFSEAAI
RKAILGHIVSHRCEYQAGHSKVGSLQYLALTALVAPKKIKPPLPSVRKLTEDRWNKPQKT
KGHKGSHTMNGH
Enzyme 68 Number of Residues 192
Enzyme 68 Molecular Weight 22572.1
Enzyme 68 Theoretical pI 10.56
Enzyme 68 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 68 General Function Involved in viral infectious cycle
Enzyme 68 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 68 Pathways Not Available
Enzyme 68 Reactions Not Available
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • None
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 329382 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID P12503 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name VIF_HV1Z2 Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAGAACA
TGGAAAAGTTTAGTAAAACACCATATGTATGTTTCAAAGAAAGCTAGCAGATGGTTTTAT
AGACATCACTATGACAGCCCCCACCCAAAAATAAGTTCAGAAGTACACATTCCACTAGGA
GAAGCTATGCTGGTAGTAAAAACATATTGGGGTCTGCATACAGGAGAAAGAGACTGGCAT
CTGGGTCAGGGAGTCTCCATAGAATGGAGGAAAAGGAGATATAGCACACAAGTAGACCCT
GGCCTGGCAGACCAACTAATTCATATGTATTATTTTGATTGTTTTTCAGAAGCTGCCATA
AGAAAAGCCATATTAGGACATATAGTCAGTCATAGGTGTGAGTATCAAGCAGGACATAGC
AAGGTAGGATCCTTACAGTATTTGGCACTAACAGCATTAGTAGCACCAAAAAAGATAAAG
CCGCCTTTGCCTAGTGTTAGGAAGTTAACAGAAGATAGATGGAACAAGCCCCAGAAGACC
AAGGGCCACAAAGGGAGCCATACAATGAATGGACATTAG
Enzyme 68 GenBank Gene ID M22639 Link Image
Enzyme 68 GeneCard ID vif Link Image
Enzyme 68 GenAtlas ID Not Available
Enzyme 68 HGNC ID Not Available
Enzyme 68 Chromosome Location Not Available
Enzyme 68 Locus Not Available
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Rose KM, Marin M, Kozak SL, Kabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med. 2004 Jun;10(6):291-7. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 17778
Enzyme 69 Name Virion infectivity factor
Enzyme 69 Synonyms
  1. Vif
  2. SOR protein
  3. p17
  4. p7
Enzyme 69 Gene Name vif
Enzyme 69 Protein Sequence >Virion infectivity factor
MENRWQVLIVWQVDRQKVKAWNSLVKYHKYRSRKTENWWYRHHYESRNPRVSSSVYIPVG
VAHVVVTTYWGLMPGERDEHLGHGVSIEWRYKKYKTQIDPETADRMIHLHYFTCFTASAV
RKAILGQRVLTKCEYPTGHSQVGTLQLLALRAVVKARSRKPPLPSVQKLTEDRWNKHLRI
RDQLKSPSMNGH
Enzyme 69 Number of Residues 192
Enzyme 69 Molecular Weight 22742.1
Enzyme 69 Theoretical pI 10.71
Enzyme 69 GO Classification
Function
Process
  • reproductive process
  • viral infectious cycle
  • viral reproductive process
Component
Enzyme 69 General Function Involved in viral infectious cycle
Enzyme 69 Specific Function Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells
Enzyme 69 Pathways Not Available
Enzyme 69 Reactions Not Available
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • None
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 463060 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID Q77374 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name VIF_HV1AN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >579 bp
ATGGAAAACAGATGGCAGGTACTGATAGTATGGCAAGTGGACAGACAGAAAGTGAAAGCG
TGGAACAGCCTAGTGAAATACCATAAGTACAGGTCTAGAAAGACCGAGAACTGGTGGTAC
AGACATCATTATGAATCCAGAAATCCAAGAGTTAGTTCAAGTGTATATATTCCAGTAGGG
GTGGCCCATGTAGTAGTAACCACATATTGGGGATTGATGCCAGGGGAAAGAGATGAACAT
TTGGGACATGGGGTTAGTATAGAATGGCGTTATAAGAAGTATAAAACACAGATTGACCCT
GAAACAGCAGACAGGATGATACATCTGCATTATTTTACCTGTTTTACAGCATCAGCAGTC
AGGAAAGCCATCCTAGGACAGAGAGTACTGACCAAGTGTGAATACCCTACAGGACATAGT
CAGGTAGGGACACTACAACTGCTAGCTCTAAGAGCAGTAGTAAAAGCAAGAAGCAGGAAG
CCTCCCCTACCCAGTGTCCAGAAATTAACAGAAGATAGATGGAACAAGCACCTGAGAATC
AGGGACCAGCTAAAGAGCCCTTCAATGAATGGGCACTAG
Enzyme 69 GenBank Gene ID L20587 Link Image
Enzyme 69 GeneCard ID vif Link Image
Enzyme 69 GenAtlas ID Not Available
Enzyme 69 HGNC ID Not Available
Enzyme 69 Chromosome Location Not Available
Enzyme 69 Locus Not Available
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Vanden Haesevelde M, Decourt JL, De Leys RJ, Vanderborght B, van der Groen G, van Heuverswijn H, Saman E: Genomic cloning and complete sequence analysis of a highly divergent African human immunodeficiency virus isolate. J Virol. 1994 Mar;68(3):1586-96. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available