1. 1,3-Diamino-n-propane
2. 1,3-Propylenediamine
3. 1,3-Trimethylenediamine
4. 1,3-propanediamine
5. 3-Aminopropylamine
6. Propane-1,3-diamine
7. Trimethylenediamine
8. a,w-Propanediamine

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• Cytoplasm

• Blood
• Urine

1. van den Berg GA, Muskiet FA, Kingma AW, van der Slik W, Halie MR: Simultaneous gas-chromatographic determination of free and acetyl-conjugated polyamines in urine. Clin Chem. 1986 Oct;32(10):1930-7. [PubMed ]
2. Kim KR, Paik MJ, Kim JH, Dong SW, Jeong DH: Rapid gas chromatographic profiling and screening of biologically active amines. J Pharm Biomed Anal. 1997 Jun;15(9-10):1309-18. [PubMed ]
3. Bremer HJ, Kohne E: The excretion of diamines in human urine. II. Cadaverine, putrescine, 1,3-diaminopropane, 2,2'-dithiobis(ethylamine) and spermidine in urine of patients with cystinuria and cystinlysinuria. Clin Chim Acta. 1971 May;32(3):407-18. [PubMed ]
4. Fleisher JH, Russell DH: Estimation of urinary diamines and polyamines by thin-layer chromatography. J Chromatogr. 1975 Jul 16;110(2):335-40. [PubMed ]
5. Blackburn P, Peterson CM: Thiol-disulfide interchange between cystine and N-2-mercaptoethyl-1, 3-diaminopropane as a potential treatment for cystinuria. Anal Biochem. 1984 Jan;136(1):31-8. [PubMed ]
6. Aigner-Held R, Campbell RA, Daves GD Jr: Polyamine-pyridoxal Schiff bases in urine. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6652-5. [PubMed ]
7. Somayaji VV, Guay V, Peng Z, Sykes TR, Noujaim AA: Synthesis and evaluation of a new bifunctional chelating agent for the preparation of radioimmunoconjugates. Q J Nucl Med. 1995 Dec;39(4):300-10. [PubMed ]
8. van den Berg GA, Schaaf JM, Nagel GT, Teelken AW, Muskiet FA: Determination of polyamines and metabolites in cerebrospinal fluid by isotope dilution mass fragmentography, and a clinical application. Clin Chim Acta. 1987 Jun 15;165(2-3):147-54. [PubMed ]
9. Muskiet FA, van den Berg GA, Kingma AW, Fremouw-Ottevangers DC, Halie MR: Total polyamines and their non-alpha-amino acid metabolites simultaneously determined in urine by capillary gas chromatography, with nitrogen-phosphorus detector; and some clinical applications. Clin Chem. 1984 May;30(5):687-95. [PubMed ]
10. Lee SH, Suh JW, Chung BC, Kim SO: Polyamine profiles in the urine of patients with leukemia. Cancer Lett. 1998 Jan 9;122(1-2):1-8. [PubMed ]

1. Spermine synthase
2. Deoxyhypusine synthase
3. Amiloride-sensitive amine oxidase [copper-containing] precursor
4. Membrane copper amine oxidase
5. Retina-specific copper amine oxidase precursor
6. S-adenosylmethionine decarboxylase proenzyme
7. Ornithine decarboxylase
8. cDNA FLJ75710, highly similar to Homo sapiens deoxyhypusine synthase (DHPS), transcript variant 1, mRNA (Deoxyhypusine synthase, isoform CRA_b)

1. Spermidine aminopropyltransferase
2. SPMSY

MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFAN
LRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAI
DRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRA
IMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDV
LDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILD
LSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTV
WKKAKP

• Arginine and Proline Metabolism (map00330 )
• Beta Alanine Metabolism (map00410 )

• S-adenosylmethioninamine + spermidine = 5'-methylthioadenosine + spermine

• Spermine_synth (PF01564 )

• None

• None

ATGCCTGGGGCAGCAGCACGGCACAGCACGCTCGACTTCATGCTCGGCGCCAAAGCTGAT
GGTGAGACCATTCTAAAAGGCCTCCAGTCCATTTTCCAGGAGCAGGGGATGGCGGAGTCG
GTGCACACCTGGCAGGACCATGGCTATTTAGCAACCTACACAAACAAGAACGGCAGCTTT
GCCAATTTGAGAATTTACCCACATGGATTGGTGTTGCTGGACCTTCAGAGTTATGATGGT
GATGCGCAAGGCAAAGAAGAGATCGACAGTATTTTGAACAAAGTAGAGGAAAGAATGAAA
GAATTGAGTCAGGACAGTACTGGGCGGGTGAAACGATTACCACCCATAGTGCGAGGAGGA
GCCATCGACAGATACTGGCCCACCGCCGACGGGCGCCTGGTTGAATATGACATAGATGAA
GTGGTATATGACGAAGATTCACCTTATCAAAATATAAAAATTCTACACTCGAAGCAGTTT
GGAAATATTCTCATCCTTAGTGGGGATGTTAATTTGGCAGAGAGTGATTTGGCATATACC
CGGGCCATCATGGGCAGTGGCAAAGAAGATTACACTGGCAAAGATGTACTCATTCTGGGA
GGTGGAGACGGAGGCATATTGTGTGAAATAGTCAAACTAAAACCAAAGATGGTCACTATG
GTAGAGATTGACCAAATGGTGATTGATGGGTGTAAGAAATACATGCGAAAAACGTGTGGC
GATGTCTTAGACAATCTTAAAGGAGACTGCTATCAGGTTCTAATAGAAGACTGTATCCCG
GTACTGAAGAGGTACGCCAAAGAAGGGAGAGAATTTGATTATGTGATTAATGATTTGACA
GCTGTTCCAATCTCCACGTCTCCAGAAGAAGATTCCACATGGGAGTTTCTCAGACTGATT
CTTGACCTCTCAATGAAAGTGTTGAAACAGGATGGGAAATATTTTACACAGGGGAACTGT
GTCAATCTGACAGAAGCACTGTCGCTCTATGAAGAACAGCTGGGGCGCCTGTATTGTCCT
GTGGAATTTTCAAAGGAGATCGTCTGTGTCCCTTCATACTTGGAATTGTGGGTATTTTAC
ACTGTTTGGAAGAAAGCTAAACCCTGA

1. Korhonen VP, Halmekyto M, Kauppinen L, Myohanen S, Wahlfors J, Keinanen T, Hyvonen T, Alhonen L, Eloranta T, Janne J: Molecular cloning of a cDNA encoding human spermine synthase. DNA Cell Biol. 1995 Oct;14(10):841-7. [PubMed ]
2. Grieff M, Whyte MP, Thakker RV, Mazzarella R: Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX. Genomics. 1997 Sep 1;44(2):227-31. [PubMed ]
3. 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 ]

1. Oredsson SM, Anehus S, Heby O: Reversal of the growth inhibitory effect of alpha-difluoromethylornithine by putrescine but not by other divalent cations. Mol Cell Biochem. 1984 Sep;64(2):163-72. [PubMed ]

1. DHS

MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFG
RAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLV
QHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFE
DWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGS
LGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGA
DYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMD
AFMHEKNED

• [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine

• DS (PF01916 )

• None

• None

ATGGAAGGTTCCCTGGAACGGGAGGCGCCAGCGGGGGCGCTGGCCGCCGTGCTAAAGCAC
AGCTCGACGTTGCCGCCCGAAAGCACCCAGGTCCGGGGCTACGACTTCAACCGCGGTGTG
AATTACCGCGCACTGCTGGAGGCCTTCGGCACCACCGGCTTCCAAGCAACCAACTTCGGG
CGCGCTGTACAGCAAGTCAATGCCATGATCGAGAAGAAGCTGGAACCACTGTCACAGGAT
GAAGACCAGCACGCGGACCTGACCCAGAGCCGCCGCCCACTTACCAGCTGCACCATTTTC
CTGGGATATACATCCAACCTCATCAGTTCAGGCATCCGTGAGACCATTCGCTACCTTGTG
CAGCACAACATGGTGGACGTATTGGTGACCACAGCTGGCGGCGTGGAGGAAGACCTCATC
AAGTGCCTGGCGCCCACATACTTGGGCGAGTTTAGCCTCAGGGGGAAGGAGCTCCGGGAG
AACGGGATCAATAGGATCGGAAACCTGCTGGTGCCCAATGAGAATTACTGCAAGTTTGAG
GACTGGCTGATGCCCATTCTGGACCAGATGGTGATGGAGCAGAACACAGAGGGTGTAAAG
TGGACGCCTTCTAAGATGATCGCCCGGCTGGGCAAGGAGATCAACAACCCAGAGTCCGTG
TATTACTGGGCCCAGAAGAACCACATCCCTGTGTTTAGTCCCGCACTTACAGACGGCTCG
CTGGGCGACATGATCTTCTTCCATTCCTACAAGAACCCGGGCCTGGTCCTGGACATCGTT
GAGGACCTGAGGCTCATCAACACACAGGCCATCTTTGCCAAGTGCACTGGGATGATCATT
CTGGGCGGGGGCGTGGTCAAGCACCACATTGCCAATGCCAACCTCATGCGGAACGGGGCC
GACTACGCTGTTTACATCAACACAGCCCAGGAGTTTGATGGCTCTGACTCAGGTGCCCGA
CCAGACGAGGCTGTCTCCTGGGGCAAGATCCGGGTGGATGCACAGCCCGTCAAGGTCTAT
GCTGACGCCTCCCTGGTCTTCCCCCTGCTTGTGGCTGAAACCTTTGCCCAGAAGATGGAT
GCCTTCATGCATGAGAAGAACGAGGACTGA

1. Joe YA, Wolff EC, Park MH: Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins. J Biol Chem. 1995 Sep 22;270(38):22386-92. [PubMed ]
2. Bevec D, Kappel B, Jaksche H, Csonga R, Hauber J, Klier H, Steinkasserer A: Molecular characterization of a cDNA encoding functional human deoxyhypusine synthase and chromosomal mapping of the corresponding gene locus. FEBS Lett. 1996 Jan 8;378(2):195-8. [PubMed ]
3. Yan YP, Tao Y, Chen KY: Molecular cloning and functional expression of human deoxyhypusine synthase cDNA based on expressed sequence tag information. Biochem J. 1996 Apr 15;315 ( Pt 2):429-34. [PubMed ]
4. Mantuano E, Trettel F, Olsen AS, Lennon G, Frontali M, Jodice C: Localization and genomic structure of human deoxyhypusine synthase gene on chromosome 19p13.2-distal 19p13.1. Gene. 1998 Jul 17;215(1):153-7. [PubMed ]
5. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed ]
6. Klier H, Csonga R, Steinkasserer A, Wohl T, Lottspeich F, Eder J: Purification and characterization of human deoxyhypusine synthase from HeLa cells. FEBS Lett. 1995 May 8;364(2):207-10. [PubMed ]
7. Liao DI, Wolff EC, Park MH, Davies DR: Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site. Structure. 1998 Jan 15;6(1):23-32. [PubMed ]

1. Park JH, Wolff EC, Folk JE, Park MH: Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase. J Biol Chem. 2003 Aug 29;278(35):32683-91. Epub 2003 Jun 4. [PubMed ]

1. Diamine oxidase
2. DAO
3. Amiloride-binding protein
4. ABP
5. Histaminase
6. Kidney amine oxidase
7. KAO

MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSS
TTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLP
GPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNG
KFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGP
RLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYG
GHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMH
ATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENIT
NPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRSYRLQIHSM
ADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWDPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRD
NGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV

• Alkaloid biosynthesis II (map00960 )
• Arginine and Proline Metabolism (map00330 )
• Beta Alanine Metabolism (map00410 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Histidine Metabolism (map00340 )
• Phenylalanine Metabolism (map00360 )
• Tryptophan Metabolism (map00380 )
• Tyrosine Metabolism (map00350 )

• RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2

• Cu_amine_oxid (PF01179 )
• Cu_amine_oxidN2 (PF02727 )
• Cu_amine_oxidN3 (PF02728 )

• 1-19

ATGCCGGCCCTGGGCTGGGCCGTGGCTGCCATCCTGATGCTGCAGACGGCCATGGCGGAG
CCCTCCCCGGGGACTCTGCCCAGGAAGGCAGGGGTGTTTTCAGACCTAAGCAACCAAGAG
CTGAAGGCAGTGCACAGCTTCCTCTGGTCCAAGAAGGAGCTGAGGCTGCAGCCCTCCAGT
ACCACCACCATGGCCAAGAACACCGTGTTTCTCATCGAGATGCTGCTGCCCAAGAAGTAC
CATGTGCTGAGGTTTCTGGATAAAGGTGAAAGGCATCCTGTGCGGGAAGCCCGTGCCGTC
ATCTTCTTTGGTGACCAGGAGCATCCCAATGTCACCGAGTTTGCTGTGGGGCCCCTGCCA
GGGCCCTGCTACATGCGAGCACTGTCCCCCAGGCCTGGGTACCAGTCCTCCTGGGCATCG
AGGCCCATCTCCACAGCAGAGTATGCCCTCCTCTACCACACCCTGCAGGAAGCCACCAAG
CCCCTGCATCAGTTCTTCCTCAATACCACAGGCTTCTCATTCCAAGACTGCCATGACAGA
TGCCTGGCCTTCACCGATGTGGCCCCCCGGGGTGTGGCTTCTGGCCAGCGCCGCAGTTGG
CTTATCATACAGCGCTATGTAGAAGGCTACTTTCTGCACCCCACTGGGCTGGAGCTCCTC
GTGGATCATGGGAGCACAGATGCTGGGCACTGGGCCGTGGAGCAGGTGTGGTACAACGGG
AAGTTCTATGGGAGCCCAGAGGAACTGGCACGGAAGTATGCAGATGGAGAGGTGGACGTG
GTGGTCCTGGAGGACCGCTGCCTGGGGGCAAGGGGCATGACAGCACAGAGGAGCCGGCCC
TCTTCTCCTCCACAAGCCCCGCGGGACTTTCCCCAGCCCCATCCATGTGAGCGGCCCCCG
CTTGGTCCAGCCCCACGGCCCTCGCTTCAGGCTGGAGGGCAACGCTGTGCTCTACGGCGG
CTGGAGCTTTGCCTTCCGGTGCGCTCCTCCTCCGGGCTGCAGGTCCTGAACGTGCACTTC
GGCGGAGAGCGCATTGCCTATGAGGTCAGCGTGCAAGAGGCAGTGGCGCTGTATGGAGGA
CACACACCTGCAGGCATGCAGACCAAGTACCTCGATGTCGGCTGGGGCCTGGGCAGCGTC
ACTCATGAGTTAGCCCCCGGCATCGACTGCCCGGAGACCGCCACCTTCCTGGACACTTTC
CACTACTATGATGCCGATGACCCGGTCCATTATCCCCGAGCCCTCTGCCTCTTTGAAATG
CCCACAGGGGTGCCCCTTCGGCGGCACTTTAATTCCAACTTTAAAGGTGGCTTCAACTTC
TATGCAGGGCTGAAGGGCCAGGTGCTGGTGCTGCGGACAACTTCAACTGTCTACAATTAT
GATTACATTTGGGACTTTATCTTCTACCCCAACGGGGTGATGGAGGCCAAGATGCATGCC
ACTGGCTACGTCCACGCCACCTTCTACACCCCCGAGGGCTGCGCACGGCACTCGCCTGCA
CACCCACCTGATTGGCAACATACACACTCACTTGTGCACTACCGCGTAGACCTGGATGTG
GCAGGCACCAAGAACAGCTTCCAGACACTGCAGATGAAGCTAGAAAACATCACCAACCCC
TGGAGCCCGAGACACCGCGTGGTCCAGCCAACTCTGGAGCAGACGCAGTACTCCTGGGAG
CGCCAGGCGGCCTTCCGCTTCAAAAGGAGGCTGCCCAAGTACCTGCTCTTTACCAGCCCC
CAGGAGAACCCCTGGGGCCACAAGCGCAGCTACCGCCTGCAGATCCACTCCATGGCCGAC
CAGGTGCTGCCCCCAGGCTGGCAGGAGGAGCAGGCCATCACCTGGGCAAGGTACCCCCTG
GCAGTGACCAAGTACCGGGAGTCAGAGCTGTGCAGCAGCAGCATCTACCACCAGAACGAC
CCCTGGGACCCGCCCGTGGTCTTTGAGCAGTTTCTTCACAACAACGAGAACATTGAAAAT
GAGGACCTGGTGGCCTGGGTGACGGTGGGCTTCCTGCACATCCCCCACTCAGAGGACATT
CCCAACACAGCCACACCTGGGAACTCCGTGGGCTTCCTGCTCCGGCCATTCAACTTCTTC
CCAGAGGACCCCTCCCCTCCCTGGCATCCAGAGACACTGTGA

1. Barbry P, Champe M, Chassande O, Munemitsu S, Champigny G, Lingueglia E, Maes P, Frelin C, Tartar A, Ullrich A, et al.: Human kidney amiloride-binding protein: cDNA structure and functional expression. Proc Natl Acad Sci U S A. 1990 Oct;87(19):7347-51. [PubMed ]
2. Chassande O, Renard S, Barbry P, Lazdunski M: The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter. J Biol Chem. 1994 May 20;269(20):14484-9. [PubMed ]
3. Zhang X, Kim J, McIntire WS: cDNA sequences of variant forms of human placenta diamine oxidase. Biochem Genet. 1995 Aug;33(7-8):261-8. [PubMed ]
4. 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 ]

1. 6790686;3085656

1. Semicarbazide-sensitive amine oxidase
2. SSAO
3. Vascular adhesion protein 1
4. VAP-1
5. HPAO

MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLF
ADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPP
AREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDID
QMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFL
HHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSW
SLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLV
YEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQ
APKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFH
PSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVW
AEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHP
RGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDF
SDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSA
DSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN

• Alkaloid biosynthesis II (map00960 )
• Arginine and Proline Metabolism (map00330 )
• Beta Alanine Metabolism (map00410 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Histidine Metabolism (map00340 )
• Phenylalanine Metabolism (map00360 )
• Tryptophan Metabolism (map00380 )
• Tyrosine Metabolism (map00350 )

• RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2

• Cu_amine_oxid (PF01179 )
• Cu_amine_oxidN2 (PF02727 )
• Cu_amine_oxidN3 (PF02728 )

• 1-19

ATGAACCAGAAGACAATCCTCGTGCTCCTCATTCTGGCCGTCATCACCATCTTTGCCTTG
GTTTGTGTCCTGCTGGTGGGCAGGGGTGGAGATGGGGGTGAACCCAGCCAGCTTCCCCAT
TGCCCCTCTGTATCTCCCAGTGCCCAGCCTTGGACACACCCTGGCCAGAGCCAGCTGTTT
GCAGACCTGAGCCGAGAGGAGCTGACGGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGG
CCAGGGCTGGTGGATGCAGCCCAGGCCCGGCCCTCGGACAACTGTGTCTTCTCAGTGGAG
TTGCAGCTGCCTCCCAAGGCTGCAGCCCTGGCTCACTTGGACAGGGGGAGCCCCCCACCT
GCCCGGGAGGCACTGGCCATCGTCTTCTTTGGCAGGCAACCCCAGCCCAACGTGAGTGAG
CTGGTGGTGGGGCCACTGCCTCACCCCTCCTACATGCGGGACGTGACTGTGGAGCGTCAT
GGAGGCCCCCTGCCCTATCACCGACGCCCCGTGCTGTTCCAAGAGTACCTGGACATAGAC
CAGATGATCTTCAACAGAGAGCTGCCCCAGGCTTCTGGGCTTCTCCACCACTGTTGCTTC
TACAAGCACCGGGGACGGAACCTGGTGACAATGACCACGGCTCCCCGTGGTCTGCAATCA
GGGGACCGGGCCACCTGGTTTGGCCTCTACTACAACATCTCGGGCGCTGGGTTCTTCCTG
CACCACGTGGGCTTGGAGCTGCTAGTGAACCACAAGGCCCTTGACCCTGCCCGCTGGACT
ATCCAGAAGGTGTTCTATCAAGGCCGCTACTACGACAGCCTGGCCCAGCTGGAGGCCCAG
TTTGAGGCCGGCCTGGTGAATGTGGTGCTGATCCCAGACAATGGCACAGGTGGGTCCTGG
TCCCTGAAGTCCCCTGTGCCCCCGGGTCCAGCTCCCCCTCTACAGTTCTATCCCCAAGGC
CCCCGCTTCAGTGTCCAGGGAAGTCGAGTGGCCTCCTCACTGTGGACTTTCTCCTTTGGC
CTCGGAGCATTCAGTGGCCCAAGGATCTTTGACGTTCGCTTCCAAGGAGAAAGACTAGTT
TATGAGATAAGCCTCCAAGAGGCCTTGGCCATCTATGGTGGAAATTCCCCAGCAGCAATG
ACGACCCGCTATGTGGATGGAGGCTTTGGCATGGGCAAGTACACCACGCCCCTGACCCGT
GGGGTGGACTGCCCCTACTTGGCCACCTACGTGGACTGGCACTTCCTTTTGGAGTCCCAG
GCCCCCAAGACAATACGTGATGCCTTTTGTGTGTTTGAACAGAACCAGGGCCTCCCCCTG
CGGCGACACCACTCAGATCTCTACTCGCACTACTTTGGGGGTCTTGCGGAAACGGTGCTG
GTCGTCAGATCTATGTCCACCTTGCTCAACTATGACTATGTGTGGGATACGGTCTTCCAC
CCCAGTGGGGCCATAGAAATACGATTCTATGCCACGGGCTACATCAGCTCGGCATTCCTC
TTTGGTGCTACTGGGAAGTACGGGAACCAAGTGTCAGAGCACACCCTGGGCACGGTCCAC
ACCCACAGCGCCCACTTCAAGGTGGATCTGGATGTAGCAGGACTGGAGAACTGGGTCTGG
GCCGAGGATATGGTCTTTGTCCCCATGGCTGTGCCCTGGAGCCCTGAGCACCAGCTGCAG
AGGCTGCAGGTGACCCGGAAGCTGCTGGAGATGGAGGAGCAGGCCGCCTTCCTCGTGGGA
AGCGCCACCCCTCGCTACCTGTACCTGGCCAGCAACCACAGCAACAAGTGGGGTCACCCC
CGGGGCTACCGCATCCAGATGCTCAGCTTTGCTGGAGAGCCGCTGCCCCAAAACAGCTCC
ATGGCGAGAGGCTTCAGCTGGGAGAGGTACCAGCTGGCTGTGACCCAGCGGAAGGAGGAG
GAGCCCAGTAGCAGCAGCGTTTTCAATCAGAATGACCCTTGGGCCCCCACTGTGGATTTC
AGTGACTTCATCAACAATGAGACCATTGCTGGAAAGGATTTGGTGGCCTGGGTGACAGCT
GGTTTTCTGCATATCCCACATGCAGAGGACATTCCTAACACAGTGACTGTGGGGAACGGC
GTGGGCTTCTTCCTCCGACCCTATAACTTCTTTGACGAAGACCCCTCCTTCTACTCTGCC
GACTCCATCTACTTCCGAGGGGACCAGGATGCTGGGGCCTGCGAGGTCAACCCCCTAGCT
TGCCTGCCCCAGGCTGCTGCCTGTGCCCCCGACCTCCCTGCCTTCTCCCACGGGGGCTTC
TCTCACAACTAG

1. Zhang X, McIntire WS: Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta. Gene. 1996 Nov 14;179(2):279-86. [PubMed ]
2. Smith DJ, Salmi M, Bono P, Hellman J, Leu T, Jalkanen S: Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J Exp Med. 1998 Jul 6;188(1):17-27. [PubMed ]

1. RAO
2. Amine oxidase [copper-containing]

MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLS
REELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREA
LAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLK
EVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLE
LLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRN
SPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQ
ECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLP
GAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALE
GRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDV
VFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYR
IQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFI
NNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVY
FEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF

• Alkaloid biosynthesis II (map00960 )
• Arginine and Proline Metabolism (map00330 )
• Beta Alanine Metabolism (map00410 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Histidine Metabolism (map00340 )
• Phenylalanine Metabolism (map00360 )
• Tryptophan Metabolism (map00380 )
• Tyrosine Metabolism (map00350 )

• RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2

• Cu_amine_oxid (PF01179 )
• Cu_amine_oxidN2 (PF02727 )
• Cu_amine_oxidN3 (PF02728 )

• 1-32

ATGCATCTCAAGATAGTCCTGGCGTTCCTGGCACTGTCCCTCATTACCATCTTTGCCCTG
GCCTATGTTTTGCTGACCAGCCCAGGTGGTTCCAGCCAGCCTCCCCACTGCCCCTCTGTA
TCCCATAGGGCCCAGCCCTGGCCACACCCTGGCCAGAGCCAGCTGTTTGCAGACCTGAGC
CGAGAGGAGTTGACAGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGGCCAGGGCTGGTG
GACGCAGCCCAGGCTCAGCCCTCGGACAACTGCATCTTCTCAGTGGAGCTGCAGCTGCCC
CCCAAGGCTGCAGCCCTGGCCCACCTGGACAGGGGGAGCCCCCCACCTGCCCGGGAGGCA
CTGGCCATCGTCCTCTTTGGTGGACAACCCCAACCCAATGTGAGTGAGCTGGTGGTGGGG
CCGCTGCCTCACCCCTCGTACATGCGGGATGTGACTGTGGAGCGTCACGGCGGGCCCCTG
CCCTATCACCGTCGCCCGGTGCTGAGAGCTGAGTTTACACAGATGTGGAGGCATCTGAAA
GATGTGGAGCTACCCAAGGCACCCATCTTCCTGTCGTCCACCTTCAACTACAATGGCTCT
ACCCTGGCAGCTGTGCATGCCACCCCTCGGGGCTTGCGCTCAAGGGAACGAACTACCTGG
ATTGGCCTCTACCATAACATCTCAGGGGTTGGTCTTTTCCTTCACCCCGTGGGGCTGGAG
CTACTACTGGACCACAGGGCCCTGGACCCTGCCCACTGGACTGTCCAGCAGGTCTTCTAC
CTTGGGCACTACTATGCAGACTTGGGCCAGTTGGAACGGGAGTTTAAGTCTGGCCGGTTG
GAAGTGGTTAGAGTCCCTCTACCTCCACCAAATGGAGCTTCATCCCTGAGGTCTCGGAAC
TCTCCAGGTCCTCTTCCCCCTCTTCAGTTCTCGCCCCAGGGTTCCCAGTACAGTGTGCAA
GGAAACCTGGTGGTATCCTCCCTCTGGTCATTTACCTTTGGCCATGGGGTGTTCAGCGGC
CTGAGGATTTTTGATGTTCGGTTCCAGGGTGAGCGAATAGCCTATGAAGTCAGTGTCCAG
GAGTGTGTATCTATCTATGGTGCCGATTCACCCAAGACGATGCTGACTCGCTATTTGGAT
AGCAGCTTTGGACTCGGCCGTAACAGCCGAGGCTTGGTGCGGGGAGTGGACTGCCCCTAT
CAAGCCACGATGGTGGACATCCATATATTAGTGGGCAAAGGGGCAGTCCAGCTGCTTCCA
GGGGCTGTGTGTGTATTTGAGGAAGCCCAGGGACTGCCCCTTCGAAGGCACCACAATTAC
CTTCAAAATCATTTCTATGGTGGTTTGGCCAGCTCAGCCCTTGTGGTCAGGTCTGTGTCA
TCTGTGGGCAACTATGACTACATTTGGGACTTTGTGTTGTACCCAAATGGGGCACTTGAA
GGGCGGGTCCATGCCACGGGTTATATCAACACAGCTTTCCTGAAAGGGGGAGAGGAGGGC
CTCCTCTTTGGGAACCGTGTGGGGGAAAGAGTGCTGGGAACGGTGCACACACATGCCTTC
CACTTCAAGCTGGACCTGGATGTGGCAGGGCTGAAAAACTGGGTGGTAGCTGAAGACGTG
GTGTTTAAACCTGTGGCTGCCCCCTGGAACCCGGAGCACTGGCTACAGCGCCCACAGCTG
ACTCGGCAGGTCCTGGGAAAGGAGGACCTGACAGCTTTTTCCTTGGGAAGCCCCCTACCC
CGCTACCTCTACCTGGCTAGCAACCAGACTAATGCGTGGGGTCACCAGCGCGGATACCAG
CTTGTGGTGACCCAGAGAAAGGAGGAGGAGTCACAGAGCAGTAGCATCTATCACCAGAAT
GACATCTGGACACCCACAGTTACCTTTGCTGACTTCATCAACAATGAAACCCTCTTAGGA
GAGGATCTGGTGGCTTGGGTCACAGCCAGCTTCCTGCACATTCCCCATGCCGAGGACATC
CCAAACACAGTGACTCTGGGGAACAGAGTTGGCTTCTTGCTCCGACCCTATAACTTCTTT
GATGAGGACCCCTCCATCTTCTCCCCTGGCAGTGTGTACTTTGAGAAGGGCCAGGATGCT
GGGCTCTGCAGCATCAATCCTGTGGCCTGCCTCCCCGACCTGGCAGCCTGTGTCCCGGAC
TTACCCCCTTTCTCTTACCACGGCTTCTAG

1. Imamura Y, Kubota R, Wang Y, Asakawa S, Kudoh J, Mashima Y, Oguchi Y, Shimizu N: Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping. Genomics. 1997 Mar 1;40(2):277-83. [PubMed ]
2. Imamura Y, Noda S, Mashima Y, Kudoh J, Oguchi Y, Shimizu N: Human retina-specific amine oxidase: genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina. Genomics. 1998 Jul 15;51(2):293-8. [PubMed ]

1. AdoMetDC
2. SamDC[Contains: S-adenosylmethionine decarboxylase alpha chain
3. S- adenosylmethionine decarboxylase beta chain]

MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQ
EAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKP
SHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEIL
MSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYW
TIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQ
KIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS

• Arginine and Proline Metabolism (map00330 )

• S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2

• SAM_decarbox (PF01536 )

• None

• None

ATGGAAGCTGCACATTTTTTCGAAGGGACCGAGAAGCTGCTGGAGGTTTGGTTCTCCCGG
CAGCAGCCCGACGCAAACCAAGGATCTGGGGATCTTCGCACTATCCCAAGATCTGAGTGG
GACATACTTTTGAAGGATGTGCAATGTTCAATCATAAGTGTGACAAAAACTGACAAGCAG
GAAGCTTATGTACTCAGTGAGAGTAGCATGTTTGTCTCCAAGAGACGTTTCATTTTGAAG
ACATGTGGTACCACCCTCTTGCTGAAAGCACTGGTTCCCCTGTTGAAGCTTGCTAGGGAT
TACAGTGGGTTTGACTCAATTCAAAGCTTCTTTTATTCTCGTAAGAATTTCATGAAGCCT
TCTCACCAAGGGTACCCACACCGGAATTTCCAGGAAGAAATAGAGTTTCTTAATGCAATT
TTCCCAAATGGAGCAGGATATTGTATGGGACGTATGAATTCTGACTGTTGGTACTTATAT
ACTCTGGATTTCCCAGAGAGTCGGGTAATCAGTCAGCCAGATCAAACCTTGGAAATTCTG
ATGAGTGAGCTTGACCCAGCAGTTATGGACCAGTTCTACATGAAAGATGGTGTTACTGCA
AAGGATGTCACTCGTGAGAGTGGAATTCGTGACCTGATACCAGGTTCTGTCATTGATGCC
ACAATGTTCAATCCTTGTGGGTATTCGATGAATGGAATGAAATCGGATGGAACTTATTGG
ACTATTCACATCACTCCAGAACCAGAATTTTCTTATGTTAGCTTTGAAACAAACTTAAGT
CAGACCTCCTATGATGACCTGATCAGGAAAGTTGTAGAAGTCTTCAAGCCAGGAAAATTT
GTGACCACCTTGTTTGTTAATCAGAGTTCTAAATGTCGCACAGTGCTTGCTTCGCCCCAG
AAGATTGAAGGTTTTAAGCGTCTTGATTGCCAGAGTGCTATGTTCAATGATTACAATTTT
GTTTTTACCAGTTTTGCTAAGAAGCAGCAACAACAGCAGAGTTGA

1. Pajunen A, Crozat A, Janne OA, Ihalainen R, Laitinen PH, Stanley B, Madhubala R, Pegg AE: Structure and regulation of mammalian S-adenosylmethionine decarboxylase. J Biol Chem. 1988 Nov 15;263(32):17040-9. [PubMed ]
2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
3. 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 ]
4. 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 ]
5. 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 ]
6. 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 ]
7. 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 ]

1. Pegg AE, Shuttleworth K, Hibasami H: Specificity of mammalian spermidine synthase and spermine synthase. Biochem J. 1981 Aug 1;197(2):315-20. [PubMed ]

1. ODC

MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALP
RVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQI
KYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLL
LERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPG
SEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQ
TGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTC
DGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQF
QNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV

• Arginine and Proline Metabolism (map00330 )

• L-ornithine = putrescine + CO2

• Orn_Arg_deC_N (PF02784 )
• Orn_DAP_Arg_deC (PF00278 )

• None

• None

ATGAACAACTTTGGTAATGAAGAGTTTGACTGCCACTTCCTCGATGAAGGTTTTACTGCC
AAGGACATTCTGGACCAGAAAATTAATGAAGTTTCTTCTTCTGATGATAAGGATGCCTTC
TATGTGGCAGACCTGGGAGACATTCTAAAGAAACATCTGAGGTGGTTAAAAGCTCTCCCT
CGTGTCACCCCCTTTTATGCAGTCAAATGTAATGATAGCAAAGCCATCGTGAAGACCCTT
GCTGCTACCGGGACAGGATTTGACTGTGCTAGCAAGACTGAAATACAGTTGGTGCAGAGT
CTGGGGGTGCCTCCAGAGAGGATTATCTATGCAAATCCTTGTAAACAAGTATCTCAAATT
AAGTATGCTGCTAATAATGGAGTCCAGATGATGACTTTTGATAGTGAAGTTGAGTTGATG
AAAGTTGCCAGAGCACATCCCAAAGCAAAGTTGGTTTTGCGGATTGCCACTGATGATTCC
AAAGCAGTCTGTCGTCTCAGTGTGAAATTCGGTGCCACGCTCAGAACCAGCAGGCTCCTT
TTGGAACGGGCGAAAGAGCTAAATATCGATGTTGTTGGTGTCAGCTTCCATGTAGGAAGC
GGCTGTACCGATCCTGAGACCTTCGTGCAGGCAATCTCTGATGCCCGCTGTGTTTTTGAC
ATGGGGGCTGAGGTTGGTTTCAGCATGTATCTGCTTGATATTGGCGGTGGCTTTCCTGGA
TCTGAGGATGTGAAACTTAAATTTGAAGAGATCACCGGCGTAATCAACCCAGCGTTGGAC
AAATACTTTCCGTCAGACTCTGGAGTGAGAATCATAGCTGAGCCCGGCAGATACTATGTT
GCATCAGCTTTCACGCTTGCAGTTAATATCATTGCCAAGAAAATTGTATTAAAGGAACAG
ACGGGCTCTGATGACGAAGATGAGTCGAGTGAGCAGACCTTTATGTATTATGTGAATGAT
GGCGTCTATGGATCATTTAATTGCATACTCTATGACCACGCACATGTAAAGCCCCTTCTG
CAAAAGAGACCTAAACCAGATGAGAAGTATTATTCATCCAGCATATGGGGACCAACATGT
GATGGCCTCGATCGGATTGTTGAGCGCTGTGACCTGCCTGAAATGCATGTGGGTGATTGG
ATGCTCTTTGAAAACATGGGCGCTTACACTGTTGCTGCTGCCTCTACGTTCAATGGCTTC
CAGAGGCCGACGATCTACTATGTGATGTCAGGGCCTGCGTGGCAACTCATGCAGCAATTC
CAGAACCCCGACTTCCCACCCGAAGTAGAGGAACAGGATGCCAGCACCCTGCCTGTGTCT
TGTGCCTGGGAGAGTGGGATGAAACGCCACAGAGCAGCCTGTGCTTCGGCTAGTATTAAT
GTGTAG

1. Hickok NJ, Seppanen PJ, Gunsalus GL, Janne OA: Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA. DNA. 1987 Jun;6(3):179-87. [PubMed ]
2. Fitzgerald MC, Flanagan MA: Characterization and sequence analysis of the human ornithine decarboxylase gene. DNA. 1989 Nov;8(9):623-34. [PubMed ]
3. van Steeg H, van Oostrom CT, Martens JW, van Kreyl C, Schepens J, Wieringa B: Nucleotide sequence of the human ornithine decarboxylase gene. Nucleic Acids Res. 1989 Nov 11;17(21):8855-6. [PubMed ]
4. Hickok NJ, Wahlfors J, Crozat A, Halmekyto M, Alhonen L, Janne J, Janne OA: Human ornithine decarboxylase-encoding loci: nucleotide sequence of the expressed gene and characterization of a pseudogene. Gene. 1990 Sep 14;93(2):257-63. [PubMed ]
5. Moshier JA, Gilbert JD, Skunca M, Dosescu J, Almodovar KM, Luk GD: Isolation and expression of a human ornithine decarboxylase gene. J Biol Chem. 1990 Mar 25;265(9):4884-92. [PubMed ]
6. Moshier JA, Osborne DL, Skunca M, Dosescu J, Gilbert JD, Fitzgerald MC, Polidori G, Wagner RL, Friezner Degen SJ, Luk GD, et al.: Multiple promoter elements govern expression of the human ornithine decarboxylase gene in colon carcinoma cells. Nucleic Acids Res. 1992 May 25;20(10):2581-90. [PubMed ]
7. 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 ]
8. 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 ]
9. 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 ]

1. 497233;14707

MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFG
RAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLV
QHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFE
DWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGS
LGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGA
DYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMD
AFMHEKNED

• None

• None

ATGGAAGGTTCCCTGGAACGGGAGGCGCCAGCGGGGGCGCTGGCCGCCGTGCTAAAGCAC
AGCTCGACGTTGCCGCCCGAAAGCACCCAGGTCCGGGGCTACGACTTCAACCGCGGTGTG
AATTACCGCGCACTGCTGGAGGCCTTCGGCACCACCGGCTTCCAAGCAACCAACTTCGGG
CGCGCTGTACAGCAAGTCAATGCCATGATCGAGAAGAAGCTGGAACCACTGTCACAGGAT
GAAGACCAGCACGCGGACCTGACCCAGAGCCGCCGCCCACTTACCAGCTGCACCATTTTC
CTGGGATATACATCCAACCTCATCAGTTCAGGCATCCGTGAGACCATTCGCTACCTTGTG
CAGCACAACATGGTGGACGTATTGGTGACCACAGCTGGCGGCGTGGAGGAAGACCTCATC
AAGTGCCTGGCGCCCACATACTTGGGCGAGTTTAGCCTCAGGGGGAAGGAGCTCCGGGAG
AACGGGATCAATAGGATCGGAAACCTGCTGGTGCCCAATGAGAATTACTGCAAGTTTGAG
GACTGGCTGATGCCCATTCTGGACCAGATGGTGATGGAGCAGAACACAGAGGGTGTAAAG
TGGACGCCTTCTAAGATGATCGCCCGGCTGGGCAAGGAGATCAACAACCCAGAGTCCGTG
TATTACTGGGCCCAGAAGAACCACATCCCTGTGTTTAGTCCCGCACTTACAGACGGCTCG
CTGGGCGACATGATCTTCTTCCATTCCTACAAGAACCCGGGCCTGGTCCTGGACATCGTT
GAGGACCTGAGGCTCATCAACACACAGGCCATCTTTGCCAAGTGCACTGGGATGATCATT
CTGGGCGGGGGCGTGGTCAAGCACCACATTGCCAATGCCAACCTCATGCGGAACGGGGCC
GACTACGCTGTTTACATCAACACAGCCCAGGAGTTTGATGGCTCTGACTCAGGTGCCCGA
CCAGACGAGGCTGTCTCCTGGGGCAAGATCCGGGTGGATGCACAGCCCGTCAAGGTCTAT
GCTGACGCCTCCCTGGTCTTCCCCCTGCTTGTGGCTGAAACCTTTGCCCAGAAGATGGAT
GCCTTCATGCATGAGAAGAACGAGGACTGA