|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5244 |
| Enzyme 1 Name |
Diamine acetyltransferase 2 |
| Enzyme 1 Synonyms |
- Polyamine N-acetyltransferase 2
- Spermidine/spermine N(1)-acetyltransferase 2
- 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 |
|
| 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 |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 1 Reactions |
- acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine [RN:R03910]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q96F10  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
SAT2_HUMAN  |
| 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  |
| Enzyme 1 GeneCard ID |
SAT2  |
| Enzyme 1 GenAtlas ID |
SAT2  |
| Enzyme 1 HGNC ID |
HGNC:23160  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
17p13.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5258 |
| Enzyme 2 Name |
Diamine acetyltransferase 1 |
| Enzyme 2 Synonyms |
- Polyamine N-acetyltransferase 1
- Putrescine acetyltransferase
- Spermidine/spermine N(1)-acetyltransferase 1
- SSAT
- 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 |
|
| 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 |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 2 Reactions |
- acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine [RN:R03910]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P21673  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
SAT1_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
SAT1  |
| Enzyme 2 GenAtlas ID |
SAT1  |
| Enzyme 2 HGNC ID |
HGNC:10540  |
| Enzyme 2 Chromosome Location |
Not Available |
| Enzyme 2 Locus |
Not Available |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5413 |
| Enzyme 3 Name |
Xanthine dehydrogenase/oxidase |
| Enzyme 3 Synonyms |
- Xanthine dehydrogenase
- XD
- Xanthine oxidase
- XO
- 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 |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P47989  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
XDH_HUMAN  |
| Enzyme 3 PDB ID |
1V97  |
| 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  |
| Enzyme 3 GeneCard ID |
XDH  |
| Enzyme 3 GenAtlas ID |
XDH  |
| Enzyme 3 HGNC ID |
HGNC:12805  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
2p23.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5433 |
| Enzyme 4 Name |
Choline dehydrogenase, mitochondrial |
| Enzyme 4 Synonyms |
- CDH
- 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
)
|
| Enzyme 4 Reactions |
- choline + acceptor = betaine aldehyde + reduced acceptor [RN:R01025]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
21759795  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q8NE62  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
CHDH_HUMAN  |
| 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  |
| Enzyme 4 GeneCard ID |
CHDH  |
| Enzyme 4 GenAtlas ID |
CHDH  |
| Enzyme 4 HGNC ID |
HGNC:24288  |
| Enzyme 4 Chromosome Location |
3 |
| Enzyme 4 Locus |
3p21.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5435 |
| Enzyme 5 Name |
Dimethylglycine dehydrogenase, mitochondrial |
| Enzyme 5 Synonyms |
- 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
)
|
| Enzyme 5 Reactions |
- N,N-dimethylglycine + acceptor + H2O = sarcosine + formaldehyde + reduced acceptor [RN:R01565]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
24797151  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9UI17  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
M2GD_HUMAN  |
| 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  |
| Enzyme 5 GeneCard ID |
DMGDH  |
| Enzyme 5 GenAtlas ID |
DMGDH  |
| Enzyme 5 HGNC ID |
HGNC:24475  |
| Enzyme 5 Chromosome Location |
5 |
| Enzyme 5 Locus |
5q14.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5449 |
| Enzyme 6 Name |
Spermine synthase |
| Enzyme 6 Synonyms |
- SPMSY
- 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 |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
2198557  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P52788  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
SPSY_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
SMS  |
| Enzyme 6 GenAtlas ID |
SMS  |
| Enzyme 6 HGNC ID |
HGNC:11123  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5450 |
| Enzyme 7 Name |
Spermidine synthase |
| Enzyme 7 Synonyms |
- SPDSY
- 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 |
|
| 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 |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
56204109  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P19623  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
SPEE_HUMAN  |
| Enzyme 7 PDB ID |
1ZDZ  |
| 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  |
| Enzyme 7 GeneCard ID |
SRM  |
| Enzyme 7 GenAtlas ID |
SRM  |
| Enzyme 7 HGNC ID |
HGNC:11296  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
1p36-p22 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- 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
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5526 |
| Enzyme 8 Name |
4-trimethylaminobutyraldehyde dehydrogenase |
| Enzyme 8 Synonyms |
- TMABADH
- Aldehyde dehydrogenase E3 isozyme
- Aldehyde dehydrogenase family 9 member A1
- Gamma-aminobutyraldehyde dehydrogenase
- 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 |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
7248636  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P49189  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
AL9A1_HUMAN  |
| 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  |
| Enzyme 8 GeneCard ID |
ALDH9A1  |
| Enzyme 8 GenAtlas ID |
ALDH9A1  |
| Enzyme 8 HGNC ID |
HGNC:412  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
1q23.1 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- 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
]
- 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- 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
]
- 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
]
- 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
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5619 |
| Enzyme 9 Name |
Gamma-butyrobetaine dioxygenase |
| Enzyme 9 Synonyms |
- Gamma-butyrobetaine hydroxylase
- Gamma-BBH
- 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 |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
Not Available |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
O75936  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
BODG_HUMAN  |
| 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  |
| Enzyme 9 GeneCard ID |
BBOX1  |
| Enzyme 9 GenAtlas ID |
BBOX1  |
| Enzyme 9 HGNC ID |
HGNC:964  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
11p14.2 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| 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 |
- DAO
- Diamine oxidase
- Amiloride-binding protein
- ABP
- Histaminase
- Kidney amine oxidase
- 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 |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
73486661  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P19801  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
ABP1_HUMAN  |
| 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  |
| Enzyme 10 GeneCard ID |
ABP1  |
| Enzyme 10 GenAtlas ID |
ABP1  |
| Enzyme 10 HGNC ID |
HGNC:80  |
| Enzyme 10 Chromosome Location |
7 |
| Enzyme 10 Locus |
7q34-q36 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- 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
]
- 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
]
- 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
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5634 |
| Enzyme 11 Name |
S-methyl-5'-thioadenosine phosphorylase |
| Enzyme 11 Synonyms |
- 5'-methylthioadenosine phosphorylase
- MTA phosphorylase
- 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 |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
847724  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q13126  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
MTAP_HUMAN  |
| Enzyme 11 PDB ID |
1SD2  |
| 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  |
| Enzyme 11 GeneCard ID |
MTAP  |
| Enzyme 11 GenAtlas ID |
MTAP  |
| Enzyme 11 HGNC ID |
HGNC:7413  |
| Enzyme 11 Chromosome Location |
9 |
| Enzyme 11 Locus |
9p21 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5657 |
| Enzyme 12 Name |
S-adenosylmethionine decarboxylase proenzyme |
| Enzyme 12 Synonyms |
- AdoMetDC
- SAMDC
- S-adenosylmethionine decarboxylase alpha chain
- 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 |
- Arginine and Proline Metabolism (map00330
)
|
| 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 |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
55664717  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P17707  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
DCAM_HUMAN  |
| Enzyme 12 PDB ID |
1MSV  |
| 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  |
| Enzyme 12 GeneCard ID |
AMD1  |
| Enzyme 12 GenAtlas ID |
AMD1  |
| Enzyme 12 HGNC ID |
HGNC:457  |
| Enzyme 12 Chromosome Location |
6 |
| Enzyme 12 Locus |
6q21 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5702 |
| Enzyme 13 Name |
Glycine amidinotransferase, mitochondrial |
| Enzyme 13 Synonyms |
- L-arginine:glycine amidinotransferase
- 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
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 13 Reactions |
- L-arginine + glycine = L-ornithine + guanidinoacetate [RN:R00565]
|
| Enzyme 13 Pfam Domain Function |
Not Available |
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
Not Available |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P50440  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
GATM_HUMAN  |
| Enzyme 13 PDB ID |
3JDW  |
| 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  |
| Enzyme 13 GeneCard ID |
GATM  |
| Enzyme 13 GenAtlas ID |
GATM  |
| Enzyme 13 HGNC ID |
HGNC:4175  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
15q21.1 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Methionine Metabolism (map00271
)
|
| Enzyme 14 Reactions |
- trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine [RN:R02821]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
4530461  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q93088  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
BHMT1_HUMAN  |
| Enzyme 14 PDB ID |
1LT8  |
| 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  |
| Enzyme 14 GeneCard ID |
BHMT  |
| Enzyme 14 GenAtlas ID |
BHMT  |
| Enzyme 14 HGNC ID |
HGNC:1047  |
| Enzyme 14 Chromosome Location |
5 |
| Enzyme 14 Locus |
5q13.1-q15 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Garrow TA: Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase. J Biol Chem. 1996 Sep 13;271(37):22831-8. [PubMed
]
- 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
]
- 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
]
- 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
]
- Millian NS, Garrow TA: Human betaine-homocysteine methyltransferase is a zinc metalloenzyme. Arch Biochem Biophys. 1998 Aug 1;356(1):93-8. [PubMed
]
- 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
]
- 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
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6073 |
| Enzyme 15 Name |
Sarcosine dehydrogenase, mitochondrial |
| Enzyme 15 Synonyms |
- SarDH
- 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
)
|
| Enzyme 15 Reactions |
- sarcosine + acceptor + H2O = glycine + formaldehyde + reduced acceptor [RN:R00611]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
5902974  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9UL12  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
SARDH_HUMAN  |
| 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  |
| Enzyme 15 GeneCard ID |
SARDH  |
| Enzyme 15 GenAtlas ID |
SARDH  |
| Enzyme 15 HGNC ID |
HGNC:10536  |
| Enzyme 15 Chromosome Location |
9 |
| Enzyme 15 Locus |
9q33-q34 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6167 |
| Enzyme 16 Name |
Histidine decarboxylase |
| Enzyme 16 Synonyms |
- 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 |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
32109  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P19113  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
DCHS_HUMAN  |
| 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  |
| Enzyme 16 GeneCard ID |
HDC  |
| Enzyme 16 GenAtlas ID |
HDC  |
| Enzyme 16 HGNC ID |
HGNC:4855  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
15q21-q22 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6322 |
| Enzyme 17 Name |
Ornithine decarboxylase |
| Enzyme 17 Synonyms |
- 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 |
|
| 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 |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 17 Reactions |
- L-ornithine = putrescine + CO2 [RN:R00670]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
29893806  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P11926  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
DCOR_HUMAN  |
| Enzyme 17 PDB ID |
1D7K  |
| 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  |
| Enzyme 17 GeneCard ID |
ODC1  |
| Enzyme 17 GenAtlas ID |
ODC1  |
| Enzyme 17 HGNC ID |
HGNC:8109  |
| Enzyme 17 Chromosome Location |
2 |
| Enzyme 17 Locus |
2p25 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- 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
]
- Fitzgerald MC, Flanagan MA: Characterization and sequence analysis of the human ornithine decarboxylase gene. DNA. 1989 Nov;8(9):623-34. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Organic cation transporter 1
- 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 |
|
| 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  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
O15245  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
S22A1_HUMAN  |
| 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  |
| Enzyme 18 GeneCard ID |
SLC22A1  |
| Enzyme 18 GenAtlas ID |
SLC22A1  |
| Enzyme 18 HGNC ID |
HGNC:10963  |
| Enzyme 18 Chromosome Location |
6 |
| Enzyme 18 Locus |
6q26 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
8133 |
| Enzyme 19 Name |
Spermine oxidase |
| Enzyme 19 Synonyms |
- Polyamine oxidase 1
- PAO-1
- 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 |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
28559074  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9NWM0  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
SMOX_HUMAN  |
| 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  |
| Enzyme 19 GeneCard ID |
SMOX  |
| Enzyme 19 GenAtlas ID |
SMOX  |
| Enzyme 19 HGNC ID |
HGNC:15862  |
| Enzyme 19 Chromosome Location |
2 |
| Enzyme 19 Locus |
20p13 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- 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
]
- 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
]
- 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- 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
]
- 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
]
- Seiler N: Catabolism of polyamines. Amino Acids. 2004 Jun;26(3):217-33. Epub 2004 Apr 20. [PubMed
]
- 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
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
8199 |
| Enzyme 20 Name |
Agmatinase, mitochondrial |
| Enzyme 20 Synonyms |
- Agmatine ureohydrolase
- 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 |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 20 Reactions |
- agmatine + H2O = putrescine + urea [RN:R01157]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
10440052  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q9BSE5  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
SPEB_HUMAN  |
| 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  |
| Enzyme 20 GeneCard ID |
AGMAT  |
| Enzyme 20 GenAtlas ID |
AGMAT  |
| Enzyme 20 HGNC ID |
HGNC:18407  |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
1p36.21 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
9242 |
| Enzyme 21 Name |
Trimethyllysine dioxygenase, mitochondrial |
| Enzyme 21 Synonyms |
- Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
- Epsilon-trimethyllysine hydroxylase
- TML hydroxylase
- TML-alpha-ketoglutarate dioxygenase
- TML dioxygenase
- 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 |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
Not Available |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9NVH6  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
TMLH_HUMAN  |
| 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  |
| Enzyme 21 GeneCard ID |
TMLHE  |
| Enzyme 21 GenAtlas ID |
TMLHE  |
| Enzyme 21 HGNC ID |
HGNC:18308  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 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 |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Methionine Metabolism (map00271
)
|
| Enzyme 22 Reactions |
- trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine [RN:R02821]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
11907831  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q9H2M3  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
BHMT2_HUMAN  |
| 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  |
| Enzyme 22 GeneCard ID |
BHMT2  |
| Enzyme 22 GenAtlas ID |
BHMT2  |
| Enzyme 22 HGNC ID |
HGNC:1048  |
| Enzyme 22 Chromosome Location |
5 |
| Enzyme 22 Locus |
5q13 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
Not Available |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
B1AKP9  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
B1AKP9_HUMAN  |
| 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  |
| 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  |
| 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 |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
Not Available |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
B2R9M0  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
B2R9M0_HUMAN  |
| 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  |
| 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 |
- 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 |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
194306651  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q8NCN5  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
PDPR_HUMAN  |
| 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  |
| Enzyme 25 GeneCard ID |
PDPR  |
| Enzyme 25 GenAtlas ID |
PDPR  |
| Enzyme 25 HGNC ID |
HGNC:55066  |
| Enzyme 25 Chromosome Location |
1 |
| Enzyme 25 Locus |
16q22.1 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
16970 |
| Enzyme 26 Name |
Ornithine decarboxylase antizyme 1 |
| Enzyme 26 Synonyms |
- 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 |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
57790284  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
P54368  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
OAZ1_HUMAN  |
| 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  |
| Enzyme 26 GeneCard ID |
OAZ1  |
| Enzyme 26 GenAtlas ID |
OAZ1  |
| Enzyme 26 HGNC ID |
HGNC:8095  |
| Enzyme 26 Chromosome Location |
1 |
| Enzyme 26 Locus |
19p13.3 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- 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
]
- 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
]
- Hayashi T, Matsufuji S, Hayashi S: Characterization of the human antizyme gene. Gene. 1997 Dec 12;203(2):131-9. [PubMed
]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- 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
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
17736 |
| Enzyme 27 Name |
Virion infectivity factor |
| Enzyme 27 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
326421  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
P69721  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1BR  |
| 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  |
| Enzyme 27 GeneCard ID |
vif  |
| 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  |
| Enzyme 27 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
17737 |
| Enzyme 28 Name |
Virion infectivity factor |
| Enzyme 28 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
60231  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
P04599  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1MA  |
| 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  |
| Enzyme 28 GeneCard ID |
vif  |
| 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  |
| Enzyme 28 General References |
- 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
]
- 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
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
17738 |
| Enzyme 29 Name |
Virion infectivity factor |
| Enzyme 29 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
1055032  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q89428  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1B9  |
| 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  |
| Enzyme 29 GeneCard ID |
vif  |
| 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  |
| Enzyme 29 General References |
- 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
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
17739 |
| Enzyme 30 Name |
Virion infectivity factor |
| Enzyme 30 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
5668941  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q9QSR2  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1VI  |
| 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  |
| Enzyme 30 GeneCard ID |
vif  |
| 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  |
| Enzyme 30 General References |
- 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
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
17740 |
| Enzyme 31 Name |
Virion infectivity factor |
| Enzyme 31 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
3288391  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
O91081  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1YF  |
| 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  |
| Enzyme 31 GeneCard ID |
vif  |
| 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  |
| Enzyme 31 General References |
- 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
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
17741 |
| Enzyme 32 Name |
Virion infectivity factor |
| Enzyme 32 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
Not Available |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
P0C1L9  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1M2  |
| 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  |
| 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  |
| Enzyme 32 General References |
- 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
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
17742 |
| Enzyme 33 Name |
Virion infectivity factor |
| Enzyme 33 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
157885895  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
P0C1K6  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
VIF_HV197  |
| 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  |
| Enzyme 33 GeneCard ID |
vif  |
| 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  |
| Enzyme 33 General References |
- 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
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
17743 |
| Enzyme 34 Name |
Virion infectivity factor |
| Enzyme 34 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
327462  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
P04598  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1B5  |
| 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  |
| Enzyme 34 GeneCard ID |
vif  |
| 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  |
| Enzyme 34 General References |
- 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
]
- 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
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
17744 |
| Enzyme 35 Name |
Virion infectivity factor |
| Enzyme 35 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
328034  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
P05898  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1MN  |
| 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  |
| Enzyme 35 GeneCard ID |
vif  |
| 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  |
| Enzyme 35 General References |
- 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
]
- 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
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
17745 |
| Enzyme 36 Name |
Virion infectivity factor |
| Enzyme 36 Synonyms |
- Vif
- 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 |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
8920154  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q9IDV7  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1YB  |
| 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  |
| Enzyme 36 GeneCard ID |
vif  |
| 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  |
| Enzyme 36 General References |
- 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
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
17746 |
| Enzyme 37 Name |
Virion infectivity factor |
| Enzyme 37 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
328159  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
P18805  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1ND  |
| 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  |
| Enzyme 37 GeneCard ID |
vif  |
| 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  |
| Enzyme 37 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
189054649  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
B2RCA2  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
B2RCA2_HUMAN  |
| 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  |
| Enzyme 38 GeneCard ID |
Not Available |
| Enzyme 38 GenAtlas ID |
Not Available |
| Enzyme 38 HGNC ID |
HGNC:17728  |
| 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 |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
328556  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
P69720  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1B1  |
| 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  |
| Enzyme 39 GeneCard ID |
vif  |
| 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  |
| Enzyme 39 General References |
- 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
]
- 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
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
17749 |
| Enzyme 40 Name |
Polyamine-modulated factor 1 |
| Enzyme 40 Synonyms |
- 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 |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
88900509  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
Q6P1K2  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
PMF1_HUMAN  |
| 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  |
| Enzyme 40 GeneCard ID |
PMF1  |
| Enzyme 40 GenAtlas ID |
PMF1  |
| Enzyme 40 HGNC ID |
HGNC:9112  |
| Enzyme 40 Chromosome Location |
1 |
| Enzyme 40 Locus |
1q12 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
17750 |
| Enzyme 41 Name |
Virion infectivity factor |
| Enzyme 41 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
329402  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
P04596  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1Z6  |
| 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  |
| Enzyme 41 GeneCard ID |
vif  |
| 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  |
| Enzyme 41 General References |
- 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
]
- 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
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
17751 |
| Enzyme 42 Name |
Virion infectivity factor |
| Enzyme 42 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
3114567  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
O70897  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
VIF_HV190  |
| 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  |
| Enzyme 42 GeneCard ID |
vif  |
| 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  |
| Enzyme 42 General References |
- 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
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
17752 |
| Enzyme 43 Name |
Virion infectivity factor |
| Enzyme 43 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
327747  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P69723  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1H2  |
| 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  |
| Enzyme 43 GeneCard ID |
vif  |
| 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  |
| Enzyme 43 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Camaur D, Trono D: Characterization of human immunodeficiency virus type 1 Vif particle incorporation. J Virol. 1996 Sep;70(9):6106-11. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
17753 |
| Enzyme 44 Name |
Virion infectivity factor |
| Enzyme 44 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
328570  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
P05900  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1RH  |
| 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  |
| Enzyme 44 GeneCard ID |
vif  |
| 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  |
| Enzyme 44 General References |
- 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
]
- 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
]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
17754 |
| Enzyme 45 Name |
Virion infectivity factor |
| Enzyme 45 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
3403228  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
O89941  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1SE  |
| 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  |
| Enzyme 45 GeneCard ID |
vif  |
| 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  |
| Enzyme 45 General References |
- 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
]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
17755 |
| Enzyme 46 Name |
Virion infectivity factor |
| Enzyme 46 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
328445  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
P20890  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1OY  |
| 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  |
| Enzyme 46 GeneCard ID |
vif  |
| 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  |
| Enzyme 46 General References |
- 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
]
- 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
]
|
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
17756 |
| Enzyme 47 Name |
Virion infectivity factor |
| Enzyme 47 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
459459  |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
P31820  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1NA  |
| 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  |
| Enzyme 47 GeneCard ID |
vif  |
| 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  |
| Enzyme 47 General References |
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
193783819  |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
B3KVI9  |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
B3KVI9_HUMAN  |
| 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  |
| Enzyme 48 GeneCard ID |
Not Available |
| Enzyme 48 GenAtlas ID |
Not Available |
| Enzyme 48 HGNC ID |
HGNC:17728  |
| Enzyme 48 Chromosome Location |
Not Available |
| Enzyme 48 Locus |
Not Available |
| Enzyme 48 SNPs |
Not Available |
| Enzyme 48 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
17758 |
| Enzyme 49 Name |
Virion infectivity factor |
| Enzyme 49 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 49 Transmembrane Regions |
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
4336332  |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
Q9WC55  |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1S2  |
| 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  |
| Enzyme 49 GeneCard ID |
vif  |
| 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  |
| Enzyme 49 General References |
- 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
]
|
| Enzyme 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
17759 |
| Enzyme 50 Name |
Virion infectivity factor |
| Enzyme 50 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
6580987  |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
Q9Q719  |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1V9  |
| 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  |
| Enzyme 50 GeneCard ID |
vif  |
| 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  |
| Enzyme 50 General References |
- 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
]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
17760 |
| Enzyme 51 Name |
Virion infectivity factor |
| Enzyme 51 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 51 Transmembrane Regions |
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
327816  |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
P20877  |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1JR  |
| 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  |
| Enzyme 51 GeneCard ID |
vif  |
| 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  |
| Enzyme 51 General References |
- 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
]
|
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
17761 |
| Enzyme 52 Name |
Virion infectivity factor |
| Enzyme 52 Synonyms |
- Vif
- SOR protein
- Virion infectivity factor p17
- 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 |
|
| Enzyme 52 Transmembrane Regions |
|
| Enzyme 52 Essentiality |
Not Available |
| Enzyme 52 GenBank ID Protein |
328420  |
| Enzyme 52 UniProtKB/Swiss-Prot ID |
P12504  |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1N5  |
| 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  |
| Enzyme 52 GeneCard ID |
vif  |
| 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  |
| Enzyme 52 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 52 Metabolite References |
Not Available |
|
Enzyme 53
[top]
|
| Enzyme 53 ID |
17762 |
| Enzyme 53 Name |
Virion infectivity factor |
| Enzyme 53 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
Not Available |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
P35964  |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1Y2  |
| 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  |
| 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  |
| Enzyme 53 General References |
- 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
]
- 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
]
|
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
17763 |
| Enzyme 54 Name |
Virion infectivity factor |
| Enzyme 54 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 54 Transmembrane Regions |
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
328454  |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
P69722  |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
VIF_HV112  |
| 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  |
| Enzyme 54 GeneCard ID |
vif  |
| 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  |
| Enzyme 54 General References |
- 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
]
- 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
]
|
| Enzyme 54 Metabolite References |
Not Available |
|
Enzyme 55
[top]
|
| Enzyme 55 ID |
17764 |
| Enzyme 55 Name |
Truncated virion infectivity factor |
| Enzyme 55 Synonyms |
- Vif
- SOR protein
- 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 |
|
| Enzyme 55 Transmembrane Regions |
|
| Enzyme 55 Essentiality |
Not Available |
| Enzyme 55 GenBank ID Protein |
665535  |
| Enzyme 55 UniProtKB/Swiss-Prot ID |
Q70623  |
| Enzyme 55 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1LW  |
| 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  |
| Enzyme 55 GeneCard ID |
vif  |
| 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  |
| Enzyme 55 General References |
- 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
]
|
| Enzyme 55 Metabolite References |
Not Available |
|
Enzyme 56
[top]
|
| Enzyme 56 ID |
17765 |
| Enzyme 56 Name |
Virion infectivity factor |
| Enzyme 56 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 56 Transmembrane Regions |
|
| Enzyme 56 Essentiality |
Not Available |
| Enzyme 56 GenBank ID Protein |
469242  |
| Enzyme 56 UniProtKB/Swiss-Prot ID |
Q79667  |
| Enzyme 56 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1MV  |
| 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  |
| Enzyme 56 GeneCard ID |
vif  |
| 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  |
| Enzyme 56 General References |
- 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
]
|
| Enzyme 56 Metabolite References |
Not Available |
|
Enzyme 57
[top]
|
| Enzyme 57 ID |
17766 |
| Enzyme 57 Name |
Virion infectivity factor |
| Enzyme 57 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 57 Transmembrane Regions |
|
| Enzyme 57 Essentiality |
Not Available |
| Enzyme 57 GenBank ID Protein |
328907  |
| Enzyme 57 UniProtKB/Swiss-Prot ID |
P24737  |
| Enzyme 57 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1U4  |
| 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  |
| Enzyme 57 GeneCard ID |
vif  |
| 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  |
| Enzyme 57 General References |
- 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
]
- 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
]
|
| Enzyme 57 Metabolite References |
Not Available |
|
Enzyme 58
[top]
|
| Enzyme 58 ID |
17767 |
| Enzyme 58 Name |
Virion infectivity factor |
| Enzyme 58 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 58 Transmembrane Regions |
|
| Enzyme 58 Essentiality |
Not Available |
| Enzyme 58 GenBank ID Protein |
2194189  |
| Enzyme 58 UniProtKB/Swiss-Prot ID |
O12159  |
| Enzyme 58 UniProtKB/Swiss-Prot Entry Name |
VIF_HV192  |
| 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  |
| Enzyme 58 GeneCard ID |
vif  |
| 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  |
| Enzyme 58 General References |
- 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
]
|
| Enzyme 58 Metabolite References |
Not Available |
|
Enzyme 59
[top]
|
| Enzyme 59 ID |
17768 |
| Enzyme 59 Name |
Virion infectivity factor |
| Enzyme 59 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 59 Transmembrane Regions |
|
| Enzyme 59 Essentiality |
Not Available |
| Enzyme 59 GenBank ID Protein |
326680  |
| Enzyme 59 UniProtKB/Swiss-Prot ID |
P04597  |
| Enzyme 59 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1EL  |
| 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  |
| Enzyme 59 GeneCard ID |
vif  |
| 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  |
| Enzyme 59 General References |
- 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
]
- 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
]
|
| Enzyme 59 Metabolite References |
Not Available |
|
Enzyme 60
[top]
|
| Enzyme 60 ID |
17769 |
| Enzyme 60 Name |
Virion infectivity factor |
| Enzyme 60 Synonyms |
- Vif
- 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 |
|
| Enzyme 60 Transmembrane Regions |
|
| Enzyme 60 Essentiality |
Not Available |
| Enzyme 60 GenBank ID Protein |
2570331  |
| Enzyme 60 UniProtKB/Swiss-Prot ID |
O41799  |
| Enzyme 60 UniProtKB/Swiss-Prot Entry Name |
VIF_HV19N  |
| 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  |
| Enzyme 60 GeneCard ID |
vif  |
| 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  |
| Enzyme 60 General References |
- 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
]
|
| Enzyme 60 Metabolite References |
Not Available |
|
Enzyme 61
[top]
|
| Enzyme 61 ID |
17770 |
| Enzyme 61 Name |
Virion infectivity factor |
| Enzyme 61 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 61 Transmembrane Regions |
|
| Enzyme 61 Essentiality |
Not Available |
| Enzyme 61 GenBank ID Protein |
3114550  |
| Enzyme 61 UniProtKB/Swiss-Prot ID |
O70887  |
| Enzyme 61 UniProtKB/Swiss-Prot Entry Name |
VIF_HV193  |
| 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  |
| Enzyme 61 GeneCard ID |
vif  |
| 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  |
| Enzyme 61 General References |
- 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
]
|
| Enzyme 61 Metabolite References |
Not Available |
|
Enzyme 62
[top]
|
| Enzyme 62 ID |
17771 |
| Enzyme 62 Name |
Virion infectivity factor |
| Enzyme 62 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 62 Transmembrane Regions |
|
| Enzyme 62 Essentiality |
Not Available |
| Enzyme 62 GenBank ID Protein |
328634  |
| Enzyme 62 UniProtKB/Swiss-Prot ID |
P05899  |
| Enzyme 62 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1SC  |
| 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  |
| Enzyme 62 GeneCard ID |
vif  |
| 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  |
| Enzyme 62 General References |
- 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
]
|
| Enzyme 62 Metabolite References |
Not Available |
|
Enzyme 63
[top]
|
| Enzyme 63 ID |
17772 |
| Enzyme 63 Name |
Virion infectivity factor |
| Enzyme 63 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 63 Transmembrane Regions |
|
| Enzyme 63 Essentiality |
Not Available |
| Enzyme 63 GenBank ID Protein |
Not Available |
| Enzyme 63 UniProtKB/Swiss-Prot ID |
P0C1L8  |
| Enzyme 63 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1MP  |
| 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  |
| 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  |
| Enzyme 63 General References |
- 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
]
|
| Enzyme 63 Metabolite References |
Not Available |
|
Enzyme 64
[top]
|
| Enzyme 64 ID |
17773 |
| Enzyme 64 Name |
Virion infectivity factor |
| Enzyme 64 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 64 Transmembrane Regions |
|
| Enzyme 64 Essentiality |
Not Available |
| Enzyme 64 GenBank ID Protein |
4336341  |
| Enzyme 64 UniProtKB/Swiss-Prot ID |
Q9WC64  |
| Enzyme 64 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1S9  |
| 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  |
| Enzyme 64 GeneCard ID |
vif  |
| 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  |
| Enzyme 64 General References |
- 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
]
|
| Enzyme 64 Metabolite References |
Not Available |
|
Enzyme 65
[top]
|
| Enzyme 65 ID |
17774 |
| Enzyme 65 Name |
Virion infectivity factor |
| Enzyme 65 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 65 Transmembrane Regions |
|
| Enzyme 65 Essentiality |
Not Available |
| Enzyme 65 GenBank ID Protein |
1353863  |
| Enzyme 65 UniProtKB/Swiss-Prot ID |
Q75003  |
| Enzyme 65 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1ET  |
| 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  |
| Enzyme 65 GeneCard ID |
vif  |
| 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  |
| Enzyme 65 General References |
- 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
]
|
| Enzyme 65 Metabolite References |
Not Available |
|
Enzyme 66
[top]
|
| Enzyme 66 ID |
17775 |
| Enzyme 66 Name |
Virion infectivity factor |
| Enzyme 66 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 66 Transmembrane Regions |
|
| Enzyme 66 Essentiality |
Not Available |
| Enzyme 66 GenBank ID Protein |
328663  |
| Enzyme 66 UniProtKB/Swiss-Prot ID |
P03402  |
| Enzyme 66 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1A2  |
| 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  |
| Enzyme 66 GeneCard ID |
vif  |
| 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  |
| Enzyme 66 General References |
- 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
]
|
| Enzyme 66 Metabolite References |
Not Available |
|
Enzyme 67
[top]
|
| Enzyme 67 ID |
17776 |
| Enzyme 67 Name |
Virion infectivity factor |
| Enzyme 67 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 67 Transmembrane Regions |
|
| Enzyme 67 Essentiality |
Not Available |
| Enzyme 67 GenBank ID Protein |
Not Available |
| Enzyme 67 UniProtKB/Swiss-Prot ID |
P0C1K5  |
| Enzyme 67 UniProtKB/Swiss-Prot Entry Name |
VIF_HV196  |
| 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  |
| 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  |
| Enzyme 67 General References |
- 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
]
|
| Enzyme 67 Metabolite References |
Not Available |
|
Enzyme 68
[top]
|
| Enzyme 68 ID |
17777 |
| Enzyme 68 Name |
Virion infectivity factor |
| Enzyme 68 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 68 Transmembrane Regions |
|
| Enzyme 68 Essentiality |
Not Available |
| Enzyme 68 GenBank ID Protein |
329382  |
| Enzyme 68 UniProtKB/Swiss-Prot ID |
P12503  |
| Enzyme 68 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1Z2  |
| 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  |
| Enzyme 68 GeneCard ID |
vif  |
| 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  |
| Enzyme 68 General References |
- 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
]
|
| Enzyme 68 Metabolite References |
Not Available |
|
Enzyme 69
[top]
|
| Enzyme 69 ID |
17778 |
| Enzyme 69 Name |
Virion infectivity factor |
| Enzyme 69 Synonyms |
- Vif
- SOR protein
- p17
- 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 |
|
| Enzyme 69 Transmembrane Regions |
|
| Enzyme 69 Essentiality |
Not Available |
| Enzyme 69 GenBank ID Protein |
463060  |
| Enzyme 69 UniProtKB/Swiss-Prot ID |
Q77374  |
| Enzyme 69 UniProtKB/Swiss-Prot Entry Name |
VIF_HV1AN  |
| 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  |
| Enzyme 69 GeneCard ID |
vif  |
| 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  |
| Enzyme 69 General References |
- 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
]
|
| Enzyme 69 Metabolite References |
Not Available |