1. (-)-Serine
2. (S)-2-Amino-3-hydroxypropanoate
3. (S)-2-Amino-3-hydroxypropanoic acid
4. (S)-2-amino-3-hydroxy-Propanoate
5. (S)-2-amino-3-hydroxy-Propanoic acid
6. (S)-Serine
7. (S)-a-Amino-b-hydroxypropionate
8. (S)-a-Amino-b-hydroxypropionic acid
9. (S)-alpha-Amino-beta-hydroxypropionate
10. (S)-alpha-Amino-beta-hydroxypropionic acid
11. (S)-b-Amino-3-hydroxypropionate
12. (S)-b-Amino-3-hydroxypropionic acid
13. 2-Amino-3-hydroxypropanoate
14. 2-Amino-3-hydroxypropanoic acid
15. 3-hydroxy-L-Alanine
16. L-(-)-Serine
17. L-3-Hydroxy-2-aminopropionate
18. L-3-Hydroxy-2-aminopropionic acid
19. L-3-Hydroxy-alanine
20. L-Ser
21. b-Hydroxy-L-alanine
22. beta-Hydroxy-L-alanine
23. beta-Hydroxyalanine
24. (S)-beta-Amino-3-hydroxypropionate
25. (S)-beta-Amino-3-hydroxypropionic acid
26. Serine

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• Cytoplasm
• Extracellular
• mitochondria
• peroxisome

• Blood
• Cerebrospinal Fluid
• Urine

• 104300 (Alzheimer's disease)
• 606904 (Juvenile myoclonic epilepsy)
• 181500 (Schizophrenia)

1. Furuya S, Watanabe M: Novel neuroglial and glioglial relationships mediated by L-serine metabolism. Arch Histol Cytol. 2003 May;66(2):109-21. [PubMed ]
2. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed ]
3. Kaumeyer JF, Polazzi JO, Kotick MP: The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC). Nucleic Acids Res. 1986 Oct 24;14(20):7839-50. [PubMed ]
4. Haas W, Grabe K, Geis C, Pach T, Stoll K, Fuchs M, Haberl B, Loy C: Recognition and invasion of human skin by Schistosoma mansoni cercariae: the key-role of L-arginine. Parasitology. 2002 Feb;124(Pt 2):153-67. [PubMed ]
5. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed ]
6. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed ]
7. Hashimoto K, Engberg G, Shimizu E, Nordin C, Lindstrom LH, Iyo M: Reduced D-serine to total serine ratio in the cerebrospinal fluid of drug naive schizophrenic patients. Prog Neuropsychopharmacol Biol Psychiatry. 2005 Jun;29(5):767-9. [PubMed ]
8. Castedo M, Ferri KF, Blanco J, Roumier T, Larochette N, Barretina J, Amendola A, Nardacci R, Metivier D, Este JA, Piacentini M, Kroemer G: Human immunodeficiency virus 1 envelope glycoprotein complex-induced apoptosis involves mammalian target of rapamycin/FKBP12-rapamycin-associated protein-mediated p53 phosphorylation. J Exp Med. 2001 Oct 15;194(8):1097-110. [PubMed ]
9. Liu T, Zhu E, Wang L, Okada T, Yamaguchi A, Okada N: Abnormal expression of Rb pathway-related proteins in salivary gland acinic cell carcinoma. Hum Pathol. 2005 Sep;36(9):962-70. [PubMed ]
10. Franchi-Gazzola R, Gazzola GC, Dall'Asta V, Guidotti GG: The transport of alanine, serine, and cysteine in cultured human fibroblasts. J Biol Chem. 1982 Aug 25;257(16):9582-7. [PubMed ]
11. Fontaine M, Porchet N, Largilliere C, Marrakchi S, Lhermitte M, Aubert JP, Degand P: Biochemical contribution to diagnosis and study of a new case of D-glyceric acidemia/aciduria. Clin Chem. 1989 Oct;35(10):2148-51. [PubMed ]
12. Yamamoto T, Nishizaki I, Nukada T, Kamegaya E, Furuya S, Hirabayashi Y, Ikeda K, Hata H, Kobayashi H, Sora I, Yamamoto H: Functional identification of ASCT1 neutral amino acid transporter as the predominant system for the uptake of L-serine in rat neurons in primary culture. Neurosci Res. 2004 May;49(1):101-11. [PubMed ]
13. Mackie S, Aitken A: Novel brain 14-3-3 interacting proteins involved in neurodegenerative disease. FEBS J. 2005 Aug;272(16):4202-10. [PubMed ]
14. Kobza K, Camporeale G, Rueckert B, Kueh A, Griffin JB, Sarath G, Zempleni J: K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase. FEBS J. 2005 Aug;272(16):4249-59. [PubMed ]
15. Whittemore AS, Cirillo PM, Feldman D, Cohn BA: Prostate specific antigen levels in young adulthood predict prostate cancer risk: results from a cohort of Black and White Americans. J Urol. 2005 Sep;174(3):872-6; discussion 876. [PubMed ]
16. Schulz I, Zeitschel U, Rudolph T, Ruiz-Carrillo D, Rahfeld JU, Gerhartz B, Bigl V, Demuth HU, Rossner S: Subcellular localization suggests novel functions for prolyl endopeptidase in protein secretion. J Neurochem. 2005 Aug;94(4):970-9. [PubMed ]
17. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. [PubMed ]
18. Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed ]
19. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed ]
20. Wikipedia

1. Seryl-tRNA synthetase, mitochondrial precursor
2. Seryl-tRNA synthetase, cytoplasmic
3. L-serine dehydratase
4. Cystathionine beta-synthase
5. Serine--pyruvate aminotransferase
6. Serine hydroxymethyltransferase, mitochondrial precursor
7. Serine hydroxymethyltransferase, cytosolic
8. Serine palmitoyltransferase 1
9. Phosphoserine phosphatase
10. Serine palmitoyltransferase 2
11. Neutral amino acid transporter A
12. cDNA FLJ75824, highly similar to Homo sapiens serine dehydratase
13. cDNA FLJ75707, highly similar to Homo sapiens serine palmitoyltransferase, long chain base subunit 1
14. Serine palmitoyltransferase 3
15. Serine racemase
16. Uncharacterized protein SHMT1
17. Serine hydroxymethyltransferase
18. Serine hydroxymethyltransferase
19. Serine hydroxymethyltransferase
20. cDNA, FLJ93186, Homo sapiens seryl-tRNA synthetase (SARS), mRNA (Seryl-tRNA synthetase, isoform CRA_e)
21. cDNA, FLJ94281, Homo sapiens cystathionine-beta-synthase (CBS), mRNA (Cystathionine-beta-synthase, isoform CRA_b)
22. cDNA, FLJ96235, Homo sapiens phosphoserine phosphatase (PSPH), mRNA (Phosphoserine phosphatase, isoform CRA_a)
23. Serine incorporator 1

1. Seryl- tRNA(Ser/Secsynthetase
2. Serine--tRNA ligase
3. SerRSmt

MAASMARRLWPLLTRRGFRPRGGCISNDSPRRSFTTEKRNRNLLYEYAREGYSALPQLDI
ERFCACPEEAAHALELRKGELRSADLPAIISTWQELRQLQEQIRSLEEEKAAVTEAVRAL
LANQDSGEVQQDPKYQGLRARGREIRKELVHLYPREAQLEEQFYLQALKLPNQTHPDVPV
GDESQARVLHMVGDKPVFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQH
GLVNFTFNKLLRRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPARFKDLNLAGTA
EVGLAGYFMDHTVAFRDLPVRMVCSSTCYRAETNTGQEPRGLYRVHHFTKVEMFGVTGPG
LEQSSQLLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVT
SASNCTDFQSRRLHIMFQTEAGELQFAHTVNATACAVPRLLIALLESNQQKDGSVLVPPA
LQSYLGTDRITAPTHVPLQYIGPNQPRKPGLPGQPAVS

• Aminoacyl-tRNA biosynthesis (map00970 )
• Glycine, Serine and Threonine Metabolism (map00260 )

• ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser)

• Seryl_tRNA_N (PF02403 )
• tRNA-synt_2b (PF00587 )

• 1-24

ATGGCTGCGTCCATGGCGCGGCGCTTGTGGCCTTTGCTGACTCGTCGGGGGTTCCGGCCC
CGGGGAGGCTGCATCTCCAACGATAGTCCAAGGAGAAGTTTCACTACAGAGAAACGAAAC
CGGAACCTCCTGTACGAGTATGCGCGCGAGGGCTACAGCGCACTCCCTCAGCTGGACATA
GAGCGGTTCTGCGCATGCCCAGAAGAGGCCGCACACGCCCTGGAGCTCCGCAAGGGGGAG
CTGCGCTCGGCGGACCTGCCCGCGATCATCTCGACATGGCAGGAGCTGAGGCAGCTGCAG
GAGCAGATCCGGAGCCTGGAGGAAGAGAAGGCAGCTGTGACTGAGGCAGTGCGGGCCCTG
CTGGCAAACCAGGACAGTGGTGAAGTGCAGCAGGACCCCAAGTACCAGGGTCTGCGGGCA
CGTGGCCGGGAGATCCGGAAGGAGCTTGTTCACCTGTACCCCAGGGAGGCCCAGCTTGAG
GAGCAGTTCTACCTGCAGGCGCTGAAGCTGCCCAACCAGACCCACCCAGACGTGCCCGTC
GGGGATGAGAGCCAGGCTCGAGTGCTCCACATGGTCGGAGACAAGCCAGTTTTCTCCTTC
CAACCTCGGGGCCACCTGGAAATTGGCGAGAAACTCGACATCATCCGTCAGAAGCGCCTG
TCCCACGTGTCTGGCCACCGGTCCTATTACCTGCGCGGGGCTGGAGCCCTCCTGCAGCAC
GGCCTGGTCAACTTCACATTCAACAAGCTTCTCCGCCGGGGCTTCACCCCCATGACGGTG
CCAGACCTTCTCCGCGGAGCAGTGTTTGAAGGCTGTGGGATGACACCAAATGCCAACCCA
TCCCAAATTTACAACATCGACCCTGCCCGCTTCAAAGATCTCAACCTGGCTGGAACAGCG
GAGGTGGGGCTTGCAGGCTACTTCATGGACCACACCGTGGCCTTCAGGGACCTGCCAGTC
AGGATGGTTTGCTCCAGCACCTGCTACCGGGCAGAGACAAACACGGGACAGGAACCCCGG
GGGCTGTATCGAGTACACCACTTCACCAAGGTGGAGATGTTTGGGGTGACAGGCCCTGGG
CTGGAGCAGAGCTCACAGCTGCTGGAGGAGTTCCTGTCCCTTCAGATGGAGATCTTGACA
GAGCTGGGCTTGCACTTCCGGGTCCTGGATATGCCCACCCAAGAACTGGGCCTCCCCGCC
TACCGCAAGTTTGACATTGAGGCCTGGATGCCAGGCCGAGGCCGCTTTGGAGAGGTCACC
AGTGCTTCCAACTGCACAGACTTCCAGAGCCGCCGCCTCCACATCATGTTCCAGACCGAG
GCTGGGGAGCTGCAGTTTGCCCACACGGTGAACGCCACCGCCTGTGCTGTCCCCCGCCTT
CTCATCGCGCTCCTGGAGAGTAACCAGCAGAAGGACGGCTCAGTGCTCGTGCCCCCTGCC
CTCCAGTCCTACCTCGGCACTGATCGGATCACAGCCCCTACCCACGTGCCTCTCCAGTAC
ATCGGCCCCAACCAGCCCCGGAAGCCTGGGCTGCCTGGCCAGCCTGCTGTAAGCTAA

1. Yokogawa T, Shimada N, Takeuchi N, Benkowski L, Suzuki T, Omori A, Ueda T, Nishikawa K, Spremulli LL, Watanabe K: Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase. J Biol Chem. 2000 Jun 30;275(26):19913-20. [PubMed ]

1. Seryl-tRNA(Ser/Secsynthetase
2. Serine--tRNA ligase
3. SerRS

MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLC
SKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAE
RIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGF
EGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQL
SQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTC
FRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYH
IVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKV
EFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEP
SKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA

• Aminoacyl-tRNA biosynthesis (map00970 )
• Glycine, Serine and Threonine Metabolism (map00260 )

• ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser)

• Seryl_tRNA_N (PF02403 )
• tRNA-synt_2b (PF00587 )

• None

• None

ATGGTGCTGGATCTGGATTTGTTTCGGGTGGATAAAGGAGGGGACCCAGCCCTCATCCGA
GAGACGCAGGAGAAGCGCTTCAAGGACCCGGGACTAGTGGACCAGCTGGTGAAGGCAGAC
AGCGAGTGGCGACGATGTAGATTTCGGGCAGACAACTTGAGCAAGCTGAAGAACCTATGC
AGCAAGACAATCGGAGAGAAAATGAAGAAAAAAGAGCCAGTGGGAGATGATGAGTCTGTC
CCAGAGAATGTGCTGAGTTTCGATGACCTTACTGCAGACGCTTTAGCTAACCTGAAAGTC
TCACAAATCAAAAAAGTCCGACTCCTCATTGATGAAGCCATCCTGAAGTGTGACGCGGAG
CGGATAAAGTTGGAAGCAGAGCGGTTTGAGAACCTCCGAGAGATTGGGAACCTTCTGCAC
CCTTCTGTACCCATCAGTAACGATGAGGATGTGGACAACAAAGTAGAGAGGATTTGGGGC
GATTGTACAGTCAGGAAGAAGTACTCTCATGTGGACCTGGTGGTGATGGTAGATGGCTTT
GAAGGCGAAAAGGGGGCCGTGGTGGCTGGGAGTCGAGGGTACTTCTTGAAGGGGGTCCTG
GTGTTCCTGGAACAGGCTCTCATCCAGTATGCCCTTCGCACCTTGGGAAGTCGGGGCTAC
ATTCCCATTTATACCCCCTTTTTCATGAGGAAGGAGGTCATGCAGGAGGTGGCACAGCTC
AGCCAGTTTGATGAAGAACTTTATAAGGTGATTGGCAAAGGCAGTGAAAAGTCTGATGAC
AACTCCTATGATGAGAAGTACCTGATTGCCACCTCAGAGCAGCCCATTGCTGCCCTGCAC
CGGGATGAGTGGCTCCGGCCGGAGGACCTGCCCATCAAGTATGCTGGCCTGTCTACCTGC
TTCCGTCAGGAGGTGGGCTCCCATGGCCGTGACACCCGTGGCATCTTCCGAGTCCATCAG
TTTGAGAAGATTGAACAGTTTGTGTACTCATCACCCCATGACAACAAGTCATGGGAGATG
TTTGAAGAGATGATTACCACCGCAGAGGAGTTCTACCAGTCCCTGGGGATTCCTTACCAC
ATTGTGAATATTGTCTCAGGTTCTTTGAATCATGCTGCCAGTAAGAAGCTTGACCTGGAG
GCCTGGTTTCCGGGCTCAGGAGCCTTCCGTGAGTTGGTCTCCTGTTCTAATTGCACGGAT
TACCAGGCTCGCCGGCTTCGAATCCGATATGGGCAAACCAAGAAGATGATGGACAAGGTG
GAGTTTGTCCATATGCTCAATGCTACCATGTGCGCCACTACCCGTACCATCTGCGCCATC
CTGGAGAACTACCAGACAGAGAAGGGCATCACTGTGCCTGAGAAATTGAAGGAGTTCATG
CCGCCAGGACTGCAAGAACTGATCCCCTTTGTGAAGCCTGCGCCCATTGAGCAGGAGCCA
TCAAAGAAGCAGAAGAAGCAACATGAGGGCAGCAAAAAGAAAGCAGCAGCAAGAGACGTC
ACCCTAGAAAACAGGCTGCAGAACATGGAGGTCACCGATGCTTGA

1. Vincent C, Tarbouriech N, Hartlein M: Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase. Eur J Biochem. 1997 Nov 15;250(1):77-84. [PubMed ]

1. L-serine deaminase

MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHF
VCSSAGNAGMAAAYAARQLGVPATIVVPGTTPALTIERLKNEGATCKVVGELLDEAFELA
KALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGL
QECGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGSQALKLFQEHP
IFSEVISDQEAVAAIEKFVDDEKILVEPAWGAALAAVYSHVIQKLQLEGNLRTPLPSLVV
IVCGGSNISLAQLRALKEQLGMTNRLPK

• Cysteine Metabolism (map00272 )
• Glycine, Serine and Threonine Metabolism (map00260 )

• L-serine = pyruvate + NH3

• PALP (PF00291 )

• None

• None

ATGATGTCTGGAGAACCCCTGCACGTGAAGACCCCCATCCGTGACAGCATGGCCCTGTCC
AAAATGGCCGGCACCAGCGTCTACCTCAAGATGGACAGTGCCCAGCCCTCCGGCTCCTTC
AAGATCCGGGGCATTGGGCACTTCTGCAAGAGGTGGGCCAAGCAAGGCTGTGCACATTTT
GTCTGCTCCTCGGCGGGCAACGCAGGCATGGCGGCTGCATATGCGGCCAGGCAACTCGGC
GTCCCCGCCACCATCGTAGTGCCCGGCACCACACCTGCTCTCACCATTGAGCGCCTCAAG
AATGAAGGTGCCACATGCAAGGTGGTGGGTGAGTTATTGGATGAAGCCTTCGAGCTGGCC
AAGGCCCTAGCGAAGAACAACCCGGGTTGGGTCTACATTCCCCCCTTTGATGACCCCCTC
ATCTGGGAAGGCCACGCTTCCATCGTGAAAGAGCTGAAGGAGACACTGTGGGAAAAGCCG
GGGGCCATCGCGCTGTCAGTGGGCGGCGGGGGCCTGCTGTGTGGAGTGGTCCAGGGGCTG
CAGGAGTGTGGCTGGGGGGACGTGCCTGTCATCGCCATGGAGACTTTTGGTGCCCACAGC
TTCCACGCTGCCACCACCGCAGGCAAACTTGTCTCCCTGCCCAAGATCACCAGTGTTGCC
AAGGCCCTGGGCGTGAAGACTGTGGGGTCTCAGGCCCTGAAGCTGTTTCAGGAACACCCC
ATTTTCTCTGAAGTTATCTCGGACCAGGAGGCTGTGGCCGCCATTGAGAAGTTCGTGGAT
GATGAGAAGATCCTGGTGGAGCCCGCCTGGGGCGCAGCCCTGGCCGCTGTCTATAGCCAC
GTGATCCAGAAGCTCCAACTGGAGGGGAATCTCCGAACCCCGCTGCCATCCCTCGTGGTC
ATCGTCTGCGGGGGCAGCAACATCAGCCTGGCCCAGCTGCGGGCGCTCAAGGAACAGCTG
GGCATGACAAATAGGTTGCCCAAGTGA

1. Ogawa H, Gomi T, Konishi K, Date T, Nakashima H, Nose K, Matsuda Y, Peraino C, Pitot HC, Fujioka M: Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources. J Biol Chem. 1989 Sep 25;264(27):15818-23. [PubMed ]

1. Serine sulfhydrase
2. Beta- thionase

MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK

• Glycine, Serine and Threonine Metabolism (map00260 )
• Methionine Metabolism (map00271 )
• Selenoamino Acid Metabolism (map00450 )

• L-serine + L-homocysteine = cystathionine + H2O

• CBS (PF00571 )
• PALP (PF00291 )

• None

• None

ATGCCTTCTGAGACCCCCCAGGCAGAAGTGGGGCCCACAGGCTGCCCCCACCGCTCAGGG
CCACACTCGGCGAAGGGGAGCCTGGAGAAGGGGTCCCCAGAGGATAAGGAAGCCAAGGAG
CCCCTGTGGATCCGGCCCGATGCTCCGAGCAGGTGCACCTGGCAGCTGGGCCGGCCTGCC
TCCGAGTCCCCACATCACCACACTGCCCCGGCAAAATCTCCAAAAATCTTGCCAGATATT
CTGAAGAAAATCGGGGACACCCCTATGGTCAGAATCAACAAGATTGGGAAGAAGTTCGGC
CTGAAGTGTGAGCTCTTGGCCAAGTGTGAGTTCTTCAACGCGGGCGGGAGCGTGAAGGAC
CGCATCAGCCTGCGGATGATTGAGGATGCTGAGCGCGACGGGACGCTGAAGCCCGGGGAC
ACGATTATCGAGCCGACATCCGGGAACACCGGGATCGGGCTGGCCCTGGCTGCGGCAGTG
AGGGGCTATCGCTGCATCATCGTGATGCCAGAGAAGATGAGCTCCGAGAAGGTGGACGTG
CTGCGGGCACTGGGGGCTGAGATTGTGAGGACGCCCACCAATGCCAGGTTCGACTCCCCG
GAGTCACACGTGGGGGTGGCCTGGCGGCTGAAGAACGAAATCCCCAATTCTCACATCCTA
GACCAGTACCGCAACGCCAGCAACCCCCTGGCTCACTACGACACCACCGCTGATGAGATC
CTGCAGCAGTGTGATGGGAAGCTGGACATGCTGGTGGCTTCAGTGGGCACGGGCGGCACC
ATCACGGGCATTGCCAGGAAGCTGAAGGAGAAGTGTCCTGGATGCAGGATCATTGGGGTG
GATCCCGAAGGGTCCATCCTCGCAGAGCCGGAGGAGCTGAACCAGACGGAGCAGACAACC
TACGAGGTGGAAGGGATCGGCTACGACTTCATCCCCACGGTGCTGGACAGGACGGTGGTG
GACAAGTGGTTCAAGAGCAACGATGAGGAGGCGTTCACCTTTGCCCGCATGCTGATCGCG
CAAGAGGGGCTGCTGTGCGGTGGCAGTGCTGGCAGCACGGTGGCGGTGGCCGTGAAGGCT
GCGCAGGAGCTGCAGGAGGGCCAGCGCTGCGTGGTCATTCTGCCCGACTCAGTGCGGAAC
TACATGACCAAGTTCCTGAGCGACAGGTGGATGCTGCAGAAGGGCTTTCTGAAGGAGGAG
GACCTCACGGAGAAGAAGCCCTGGTGGTGGCACCTCCGTGTTCAGGAGCTGGGCCTGTCA
GCCCCGCTGACCGTGCTCCCGACCATCACCTGTGGGCACACCATCGAGATCCTCCGGGAG
AAGGGCTTCGACCAGGCGCCCGTGGTGGATGAGGCGGGGGTAATCCTGGGAATGGTGACG
CTTGGGAACATGCTCTCGTCCCTGCTTGCCGGGAAGGTGCAGCCGTCAGACCAAGTTGGC
AAAGTCATCTACAAGCAGTTCAAACAGATCCGCCTCACGGACACGCTGGGCAGGCTCTCG
CACATCCTGGAGATGGACCACTTCGCCCTGGTGGTGCACGAGCAGATCCAGTACCACAGC
ACCGGGAAGTCCAGTCAGCGGCAGATGGTGTTCGGGGTGGTCACCGCCATTGACTTGCTG
AACTTCGTGGCCGCCCAGGAGCGGGACCAGAAGTGA

1. Kraus JP, Le K, Swaroop M, Ohura T, Tahara T, Rosenberg LE, Roper MD, Kozich V: Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells. Hum Mol Genet. 1993 Oct;2(10):1633-8. [PubMed ]
2. Chasse JF, Paly E, Paris D, Paul V, Sinet PM, Kamoun P, London J: Genomic organization of the human cystathionine beta-synthase gene: evidence for various cDNAs. Biochem Biophys Res Commun. 1995 Jun 26;211(3):826-32. [PubMed ]
3. Kruger WD, Cox DR: A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6614-8. [PubMed ]
4. Chasse JF, Paul V, Escanez R, Kamoun P, London J: Human cystathionine beta-synthase: gene organization and expression of different 5' alternative splicing. Mamm Genome. 1997 Dec;8(12):917-21. [PubMed ]
5. Kraus JP, Oliveriusova J, Sokolova J, Kraus E, Vlcek C, de Franchis R, Maclean KN, Bao L, Bukovsk, Patterson D, Paces V, Ansorge W, Kozich V: The human cystathionine beta-synthase (CBS) gene: complete sequence, alternative splicing, and polymorphisms. Genomics. 1998 Sep 15;52(3):312-24. [PubMed ]
6. Kraus J, Packman S, Fowler B, Rosenberg LE: Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits. J Biol Chem. 1978 Sep 25;253(18):6523-8. [PubMed ]
7. Meier M, Janosik M, Kery V, Kraus JP, Burkhard P: Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. EMBO J. 2001 Aug 1;20(15):3910-6. [PubMed ]
8. Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R: Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 2002 Aug 20;41(33):10454-61. [PubMed ]
9. Kraus JP, Janosik M, Kozich V, Mandell R, Shih V, Sperandeo MP, Sebastio G, de Franchis R, Andria G, Kluijtmans LA, Blom H, Boers GH, Gordon RB, Kamoun P, Tsai MY, Kruger WD, Koch HG, Ohura T, Gaustadnes M: Cystathionine beta-synthase mutations in homocystinuria. Hum Mutat. 1999;13(5):362-75. [PubMed ]
10. Kozich V, Kraus JP: Screening for mutations by expressing patient cDNA segments in E. coli: homocystinuria due to cystathionine beta-synthase deficiency. Hum Mutat. 1992;1(2):113-23. [PubMed ]
11. Kozich V, de Franchis R, Kraus JP: Molecular defect in a patient with pyridoxine-responsive homocystinuria. Hum Mol Genet. 1993 Jun;2(6):815-6. [PubMed ]
12. Hu FL, Gu Z, Kozich V, Kraus JP, Ramesh V, Shih VE: Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria. Hum Mol Genet. 1993 Nov;2(11):1857-60. [PubMed ]
13. de Franchis R, Kozich V, McInnes RR, Kraus JP: Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. Hum Mol Genet. 1994 Jul;3(7):1103-8. [PubMed ]
14. Marble M, Geraghty MT, de Franchis R, Kraus JP, Valle D: Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria. Hum Mol Genet. 1994 Oct;3(10):1883-6. [PubMed ]
15. Kraus JP: Komrower Lecture. Molecular basis of phenotype expression in homocystinuria. J Inherit Metab Dis. 1994;17(4):383-90. [PubMed ]
16. Shih VE, Fringer JM, Mandell R, Kraus JP, Berry GT, Heidenreich RA, Korson MS, Levy HL, Ramesh V: A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype. Am J Hum Genet. 1995 Jul;57(1):34-9. [PubMed ]
17. Sebastio G, Sperandeo MP, Panico M, de Franchis R, Kraus JP, Andria G: The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations. Am J Hum Genet. 1995 Jun;56(6):1324-33. [PubMed ]
18. Kluijtmans LA, Blom HJ, Boers GH, van Oost BA, Trijbels FJ, van den Heuvel LP: Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients. Hum Genet. 1995 Aug;96(2):249-50. [PubMed ]
19. Kruger WD, Cox DR: A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61. [PubMed ]
20. Sperandeo MP, Panico M, Pepe A, Candito M, de Franchis R, Kraus JP, Andria G, Sebastio G: Molecular analysis of patients affected by homocystinuria due to cystathionine beta-synthase deficiency: report of a new mutation in exon 8 and a deletion in intron 11. J Inherit Metab Dis. 1995;18(2):211-4. [PubMed ]
21. Kluijtmans LA, Boers GH, Stevens EM, Renier WO, Kraus JP, Trijbels FJ, van den Heuvel LP, Blom HJ: Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient. J Clin Invest. 1996 Jul 15;98(2):285-9. [PubMed ]
22. Sperandeo MP, Candito M, Sebastio G, Rolland MO, Turc-Carel C, Giudicelli H, Dellamonica P, Andria G: Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations. J Inherit Metab Dis. 1996;19(3):351-6. [PubMed ]
23. Dawson PA, Cox AJ, Emmerson BT, Dudman NP, Kraus JP, Gordon RB: Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria. Eur J Hum Genet. 1997 Jan-Feb;5(1):15-21. [PubMed ]
24. Kim CE, Gallagher PM, Guttormsen AB, Refsum H, Ueland PM, Ose L, Folling I, Whitehead AS, Tsai MY, Kruger WD: Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria. Hum Mol Genet. 1997 Dec;6(13):2213-21. [PubMed ]
25. Aral B, Coude M, London J, Aupetit J, Chasse JF, Zabot MT, Chadefaux-Vekemans B, Kamoun P: Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients. Hum Mutat. 1997;9(1):81-2. [PubMed ]
26. Kozich V, Janosik M, Sokolova J, Oliveriusova J, Orendac M, Kraus JP, Elleder D: Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99. J Inherit Metab Dis. 1997 Jul;20(3):363-6. [PubMed ]
27. de Franchis R, Kraus E, Kozich V, Sebastio G, Kraus JP: Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype. Hum Mutat. 1999;13(6):453-7. [PubMed ]

1. SPT
2. Alanine-- glyoxylate aminotransferase
3. AGT

MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEI
KEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIG
ARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLL
LVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF
YLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHG
RLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLR
IGLLGCNATRENVDRVTEALRAALQHCPKKKL

• Glycine, Serine and Threonine Metabolism (map00260 )

• L-serine + pyruvate = 3-hydroxypyruvate + L-alanine

• Aminotran_5 (PF00266 )

• None

• None

ATGGCCTCTCACAAGCTGCTGGTGACCCCCCCCAAGGCCCTGCTCAAGCCCCTCTCCATC
CCCAACCAGCTCCTGCTGGGGCCTGGTCCTTCCAACCTGCCTCCTCGCATCATGGCAGCC
GGGGGGCTGCAGATGATCGGGTCCATGAGCAAGGATATGTACCAGATCATGGACGAGATC
AAGGAAGGCATCCAGTACGTGTTCCAGACCAGGAACCCACTCACACTGGTCATCTCTGGC
TCGGGACACTGTGCCCTGGAGGCCGCCCTGGTCAATGTGCTGGAGCCTGGGGACTCCTTC
CTGGTTGGGGCCAATGGCATTTGGGGGCAGCGAGCCGTGGACATCGGGGAGCGCATAGGA
GCCCGAGTGCACCCGATGACCAAGGACCCTGGAGGCCACTACACACTGCAGGAGGTGGAG
GAGGGCCTGGCCCAGCACAAGCCAGTGCTGCTGTTCTTAACCCACGGGGAGTCGTCCACC
GGCGTGCTGCAGCCCCTTGATGGCTTCGGGGAACTCTGCCACAGGTACAAGTGCCTGCTC
CTGGTGGATTCGGTGGCATCCCTGGGCGGGACCCCCCTTTACATGGACCGGCAAGGCATC
GACATCCTGTACTCGGGCTCCCAGAAGGCCCTGAACGCCCCTCCAGGGACCTCGCTCATC
TCCTTCAGTGACAAGGCCAAAAAGAAGATGTACTCCCGCAAGACGAAGCCCTTCTCCTTC
TACCTGGACATCAAGTGGCTGGCCAACTTCTGGGGCTGTGACGACCAGCCCAGGATGTAC
CATCACACAATCCCCGTCATCAGCCTGTACAGCCTGAGAGAGAGCCTGGCCCTCATTGCG
GAACAGGGCCTGGAGAACAGCTGGCGCCAGCACCGCGAGGCCGCGGCGTATCTGCATGGG
CGCCTGCAGGCACTGGGGCTGCAGCTCTTCGTGAAGGACCCGGCGCTCCGGCTTCCCACA
GTCACCACTGTGGCTGTACCCGCTGGCTATGACTGGAGAGACATCGTCAGCTACGTCATA
GACCACTTCGACATTGAGATCATGGGTGGCCTTGGGCCCTCCACGGGGAAGGTGCTGCGG
ATCGGCCTGCTGGGCTGCAATGCCACCCGCGAGAATGTGGACCGCGTGACGGAGGCCCTG
AGGGCGGCCCTGCAGCACTGCCCCAAGAAGAAGCTGTGA

1. Nishiyama K, Berstein G, Oda T, Ichiyama A: Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. Eur J Biochem. 1990 Nov 26;194(1):9-18. [PubMed ]
2. Purdue PE, Takada Y, Danpure CJ: Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. J Cell Biol. 1990 Dec;111(6 Pt 1):2341-51. [PubMed ]
3. Takada Y, Kaneko N, Esumi H, Purdue PE, Danpure CJ: Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. Biochem J. 1990 Jun 1;268(2):517-20. [PubMed ]
4. Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ: Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. Genomics. 1991 May;10(1):34-42. [PubMed ]
5. Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A: Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. Biochem Biophys Res Commun. 1991 May 15;176(3):1093-9. [PubMed ]
6. Purdue PE, Lumb MJ, Allsop J, Minatogawa Y, Danpure CJ: A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. Genomics. 1992 May;13(1):215-8. [PubMed ]
7. Minatogawa Y, Tone S, Allsop J, Purdue PE, Takada Y, Danpur CJ, Kido R: A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. Hum Mol Genet. 1992 Nov;1(8):643-4. [PubMed ]
8. Danpure CJ, Purdue PE, Fryer P, Griffiths S, Allsop J, Lumb MJ, Guttridge KM, Jennings PR, Scheinman JI, Mauer SM, et al.: Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. Am J Hum Genet. 1993 Aug;53(2):417-32. [PubMed ]
9. Danpure CJ: Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. Biochimie. 1993;75(3-4):309-15. [PubMed ]
10. von Schnakenburg C, Rumsby G: Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. J Med Genet. 1997 Jun;34(6):489-92. [PubMed ]
11. Amoroso A, Pirulli D, Puzzer D, Ferri L, Crovella S, Ferrettini C, Marangella M, Mazzola G, Florian F: Gene symbol: AGXT. Disease: primary hyperoxaluria type I. Hum Genet. 1999 May;104(5):441. [PubMed ]
12. Basmaison O, Rolland MO, Cochat P, Bozon D: Identification of 5 novel mutations in the AGXT gene. Hum Mutat. 2000 Jun;15(6):577. [PubMed ]

1. Serine methylase
2. Glycine hydroxymethyltransferase
3. SHMT

MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH

• Cyanoamino acid metabolism (map00460 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Lysine Degradation (map00310 )
• Methane metabolism (map00680 )
• One Carbon Pool By Folate (map00670 )

• 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine

• SHMT (PF00464 )

• 1-18

ATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAACAGG
GGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTGCAG
AGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGCAGC
CGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTATCCT
GGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGC
CGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTAC
TCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATC
ATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAG
CGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACT
GGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATC
ATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGT
GATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCC
AAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACT
CTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCC
AAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCA
TCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAG
GCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATG
GCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTG
GTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAG
CTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCG
GGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTC
CGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAG
ACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGT
CTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTT
GATGAGCATTGA

1. Stover PJ, Chen LH, Suh JR, Stover DM, Keyomarsi K, Shane B: Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene. J Biol Chem. 1997 Jan 17;272(3):1842-8. [PubMed ]
2. Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, Korenberg JR, Shane B: Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem. 1993 Jun 5;268(16):11910-6. [PubMed ]
3. Snell K, Baumann U, Byrne PC, Chave KJ, Renwick SB, Sanders PG, Whitehouse SK: The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase. Adv Enzyme Regul. 2000;40:353-403. [PubMed ]

1. Serine methylase
2. Glycine hydroxymethyltransferase
3. SHMT

MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL
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• Cyanoamino acid metabolism (map00460 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Lysine Degradation (map00310 )
• Methane metabolism (map00680 )
• One Carbon Pool By Folate (map00670 )

• 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine

• SHMT (PF00464 )

• None

• None

ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTCTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA

1. Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, Korenberg JR, Shane B: Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem. 1993 Jun 5;268(16):11910-6. [PubMed ]
2. Chave KJ, Snell K, Sanders PG: Isolation and characterisation of human genomic sequences encoding cytosolic serine hydroxymethyltransferase. Biochem Soc Trans. 1997 Feb;25(1):53S. [PubMed ]
3. Renwick SB, Snell K, Baumann U: The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy. Structure. 1998 Sep 15;6(9):1105-16. [PubMed ]

1. Long chain base biosynthesis protein 1
2. LCB 1
3. Serine-palmitoyl-CoA transferase 1
4. SPT 1
5. SPT1

MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEEL
IEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAA
ALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSK
RGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRR
FIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDI
DLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENP
GIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCM
NRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL

• Sphingolipid Metabolism (map00600 )

• palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2

• Aminotran_1_2 (PF00155 )

• None

• 16-36

ATGGCGACCGCCACGGAGCAGTGGGTTCTGGTGGAGATGGTACAGGCGCTTTACGAGGCT
CCTGCTTACCATCTTATTTTGGAAGGGATTCTGATCCTCTGGATAATCAGACTTCTTTTC
TCTAAGACTTACAAATTACAAGAACGATCTGATCTTACAGTCAAGGAAAAAGAAGAACTG
ATTGAAGAGTGGCAACCAGAACCTCTTGTTCCTCCTGTCCCAAAAGACCATCCTGCTCTC
AACTACAACATCGTTTCAGGCCCTCCAAGCCACAAAACTGTGGTGAATGGAAAAGAATGT
ATAAACTTCGCCTCATTTAATTTTCTTGGATTGTTGGATAACCCTAGGGTTAAGGCAGCA
GCTTTAGCATCTCTAAAGAAGTATGGCGTGGGGACTTGTGGACCCAGAGGATTTTATGGC
ACATTTGATGTTCATTTGGATTTGGAAGACCGCCTGGCAAAATTTATGAAGACAGAAGAA
GCCATTATATACTCATATGGATTTGCCACCATAGCCAGTGCTATTCCTGCTTACTCTAAA
AGAGGGGACATTGTTTTTGTAGATAGAGCTGCCTGCTTTGCTATTCAGAAAGGATTACAG
GCATCCCGTAGTGACATTAAGTTATTTAAGCATAATGACATGGCTGACCTCGAGCGACTA
CTAAAAGAACAAGAGATCGAAGATCAAAAGAATCCTCGCAAGGCTCGTGTAACTCGGCGT
TTCATTGTAGTAGAAGGATTGTATATGAATACTGGAACTATTTGTCCTCTTCCAGAATTG
GTTAAGTTAAAATACAAATACAAAGCAAGAATCTTCCTGGAGGAAAGCCTTTCATTTGGA
GTCCTAGGAGAGCATGGCCGAGGAGTCACTGAACACTATGGAATCAATATTGATGATATT
GATCTTATCAGTGCCAACATGGAGAATGCACTTGCTTCTATTGGAGGTTTCTGCTGTGGC
AGGTCTTTTGTAATTGACCATCAGCGACTTTCCGGCCAGGGATACTGCTTTTCAGCTTCG
TTACCTCCCCTGTTAGCTGCTGCAGCAATTGAGGCCCTCAACATCATGGAAGAGAATCCA
GGTATTTTTGCAGTGTTGAAGGAAAAGTGCGGACAAATTCATAAAGCTTTACAAGGCATT
TCTGGATTAAAAGTGGTGGGGGAGTCCCTTTCTCCAGCCTTTCACCTACAACTGGAAGAG
AGCACTGGGTCTCGCGAGCAAGATGTCAGACTGCTTCAGGAAATTGTAGATCAATGCATG
AACAGAAGTATTGCATTAACTCAGGCGCGCTACTTGGAGAAAGAAGAGAAGTGTCTCCCT
CCTCCCAGCATTCGGGTTGTGGTCACGGTGGAACAAACAGAGGAAGAACTGGAGAGAGCT
GCGTCCACCATCAAGGAGGTAGCCCAGGCCGTCCTGCTCTAG

1. Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed ]
2. Dawkins JL, Hulme DJ, Brahmbhatt SB, Auer-Grumbach M, Nicholson GA: Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I. Nat Genet. 2001 Mar;27(3):309-12. [PubMed ]

1. PSP
2. O-phosphoserine phosphohydrolase
3. PSPase
4. L-3-phosphoserine phosphatase

MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKA
ALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVA
SKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDG
ATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE

• Glycine, Serine and Threonine Metabolism (map00260 )

• L(or D)-O-phosphoserine + H2O = L(or D)-serine + phosphate

• Hydrolase (PF00702 )

• None

• None

ATGGTCTCCCACTCAGAGCTGAGGAAGCTTTTCTACTCAGCAGATGCTGTGTGTTTTGAT
GTTGACAGCACGGTCATCAGAGAAGAAGGAATCGATGAGCTAGCCAAAATCTGTGGCGTT
GAGGACGCGGTGTCAGAAATGACACGGCGAGCCATGGGCGGGGCAGTGCCTTTCAAAGCT
GCTCTCACAGAGCGCTTAGCCCTCATCCAGCCCTCCAGGGAGCAGGTGCAGAGACTCATA
GCAGAGCAACCCCCACACCTGACCCCCGGCATAAGGGAGCTGGTAAGTCGCCTACAGGAG
CGAAATGTTCAGGTTTTCCTAATATCTGGTGGCTTTAGGAGTATTGTAGAGCATGTTGCT
TCAAAGCTCAATATCCCAGCAACCAATGTATTTGCCAATAGGCTGAAATTCTACTTTAAC
GGTGAATATGCAGGTTTTGATGAGACGCAGCCAACAGCTGAATCTGGTGGAAAAGGAAAA
GTGATTAAACTTTTAAAGGAAAAATTTCATTTTAAGAAAATAATCATGATTGGAGATGGT
GCCACAGATATGGAAGCCTGTCCTCCTGCTGATGCTTTCATTGGATTTGGAGGAAATGTG
ATCAGGCAACAAGTCAAGGATAACGCCAAATGGTATATCACTGATTTTGTAGAGCTGCTG
GGAGAACTGGAAGAATAA

1. Collet JF, Gerin I, Rider MH, Veiga-da-Cunha M, Van Schaftingen E: Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate. FEBS Lett. 1997 May 26;408(3):281-4. [PubMed ]

1. Long chain base biosynthesis protein 2
2. LCB 2
3. Serine-palmitoyl-CoA transferase 2
4. SPT 2

MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFN
EAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFEN
FYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLG
FARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFA
TNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQ
PRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVV
EYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQII
TSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIG
AFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYS
RHRLVPLLDRPFDETTYEETED

• Sphingolipid Metabolism (map00600 )

• palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2

• Aminotran_1_2 (PF00155 )

• None

• 67-87

ATGCGGCCGGAGCCCGGAGGCTGCTGCTGCCGCCGCACGGTGCGGGCGAATGGCTGCGTG
GCGAACGGGGAAGTACGGAACGGGTACGTGAGGAGCAGCGCTGCAGCCGCAGCCGCAGCC
GCCGCCGGCCAGATCCATCATGTTACACAAAATGGAGGACTATATAAAAGACCGTTTAAT
GAAGCTTTTGAAGAAACACCAATGCTGGTTGCTGTGCTCACGTATGTGGGGTATGGCGTA
CTCACCCTCTTTGGATATCTTCGAGATTTCTTGAGGTATTGGAGAATTGAAAAGTGTCAC
CATGCAACAGAAAGAGAAGAACAAAAGGACTTTGTGTCATTGTATCAAGATTTTGAAAAC
TTTTATACAAGGAATCTGTACATGAGGATAAGAGACAACTGGAATCGGCCAATCTGTAGT
GTGCCTGGAGCCAGGGTGGACATCATGGAGAGACAGTCTCATGATTATAACTGGTCCTTC
AAGTATACAGGGAATATAATAAAGGGTGTTATAAACATGGGTTCCTACAACTATCTTGGA
TTTGCACGGAATACTGGATCATGTCAAGAAGCAGCCGCCAAAGTCCTTGAGGAGTATGGA
GCTGGAGTGTGCAGTACTCGGCAGGAAATTGGAAACCTGGACAAGCATGAAGAACTAGAG
GAGCTTGTAGCAAGGTTCTTAGGAGTAGAAGCTGCTATGGCGTATGGCATGGGATTTGCA
ACGAATTCAATGAACATTCCTGCTCTTGTTGGCAAAGGTTGCCTGATTCTGAGTGATGAA
CTGAACCATGCATCACTGGTTCTGGGAGCCAGACTGTCAGGAGCAACCATTAGAATCTTC
AAACACAACAATATGCAAAGCCTAGAGAAGCTATTGAAAGATGCCATTGTTTATGGTCAG
CCTCGGACACGAAGGCCCTGGAAGAAAATTCTCATCCTTGTGGAAGGAATATATAGCATG
GAGGGATCTATTGTTCGTCTTCCTGAAGTGATTGCCCTCAAGAAGAAATACAAGGCATAC
TTGTATCTGGATGAGGCTCACAGCATTGGCGCCCTGGGCCCCACAGGCCGGGGTGTGGTG
GAGTACTTTGGCCTGGATCCCGAGGATGTGGATGTTATGATGGGAACGTTCACAAAGAGT
TTTGGTGCTTCTGGAGGATATATTGGAGGCAAGAAGGAGCTGATAGACTACCTGCGAACA
CATTCTCATAGTGCAGTGTATGCCACGTCATTGTCACCTCCTGTAGTGGAGCAGATCATC
ACCTCCATGAAGTGCATCATGGGGCAGGATGGCACCAGCCTTGGTAAAGAGTGTGTACAA
CAGTTAGCTGAAAACACCAGGTATTTCAGGAGACGCCTGAAAGAGATGGGCTTCATCATC
TATGGAAATGAAGACTCTCCAGTAGTGCCTTTGATGCTCTACATGCCTGCCAAAATTGGC
GCCTTTGGACGGGAGATGCTGAAGCGGAACATCGGTGTCGTTGTGGTTGGATTTCCTGCC
ACCCCAATTATTGAGTCCAGAGCCAGGTTTTGCCTGTCAGCAGCTCATACCAAAGAAATA
CTTGATACTGCTTTAAAGGAGATAGATGAAGTTGGGGACCTATTGCAGCTGAAGTATTCC
CGTCATCGGTTGGTACCTCTACTGGACAGGCCCTTTGACGAGACGACGTATGAAGAAACA
GAAGACTGA

1. Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed ]
2. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed ]
3. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]
4. Nagiec MM, Lester RL, Dickson RC: Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase. Gene. 1996 Oct 24;177(1-2):237-41. [PubMed ]
5. Takeda J, Yano H, Eng S, Zeng Y, Bell GI: A molecular inventory of human pancreatic islets: sequence analysis of 1000 cDNA clones. Hum Mol Genet. 1993 Nov;2(11):1793-8. [PubMed ]

1. SATT
2. Solute carrier family 1 member 4
3. Alanine/serine/cysteine/ threonine transporter
4. ASCT1

MEKSNETNGYLDSAQAGPAAGPGAPGTAAGRARRCAGFLRRQALVLLTVSGVLAGAGLGA
ALRGLSLSRTQVTYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASCLGRLGGIAVAY
FGLTTLSASALAVALAFIIKPGSGAQTLQSSDLGLEDSGPPPVPKETVDSFLDLARNLFP
SNLVVAAFRTYATDYKVVTQNSSSGNVTHEKIPIGTEIEGMNILGLVLFALVLGVALKKL
GSEGEDLIRFFNSLNEATMVLVSWIMWYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFA
SILGHVIHGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSSSATLPSMMKCIEENN
GVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVELNAGQIFTILVTATASSVGA
AGVPAGGVLTIAIILEAIGLPTHDLPLILAVDWIVDRTTTVVNVEGDALGAGILHHLNQK
ATKKGEQELAEVKVEAIPNCKSEEETSPLVTHQNPAGPVASAPELESKESVL

• SDF (PF00375 )

• 1-104

• 42-62 88-108 119-139 217-237 257-277 298-318 328-348 373-393 418-438

ATGGAGAAGAGCAACGAGACCAACGGCTACCTTGACAGCGCTCAGGCGGGGCCTGCGGCC
GGGCCCGGAGCTCCGGGGACCGCGGCGGGACGCGCACGGCGTTGCGCGCGCTTCCTGCGG
CGCCAAGCGCTGGTGCTGCTCACCGTGTCCGGGGTGCTGGCGGGCGCGGGCCTGGGCGCG
GCGTTGCGCGGGCTCAGCCTGAGCCGCACGCAGGTCACCTACCTGGCCTTCCCCGGCGAG
ATGCTGCTCCGCATGCTGCGCATGATCATCCTGCCGCTGGTGGTCTGCAGCCTGGTGTCG
GGCGCCGCCTCGCTCGATGCCAGCTGCCTCGGGCGTCTGGGCGGCATCCGTGTCGCCTAC
TTTGGCCTCACCACACTGAGTGCCTCGGCGCTCGCCGTGGCCTTGGCGTTCATCATCAAG
CCAGGATCCGGTGCGCAGACCCTTCAGTCCAGCGACCTGGGGCTGGAGGACTCGGGGCCT
CCTCCTGTCCCCAAAGAGACGGTGGACTCTTTCCTCGACCTGGCCAGAAACCTGTTTCCC
TCCAATCTTGTGGTTGCAGCTTTCCGTACGTATGCAACCGATTATAAAGTCGTGACCCAG
AACAGCAGCTCTGGAAATGTAACCCATGAAAAGATCCCCATAGGCACTGAGATAGAAGGG
ATGAACATTTTAGGATTGGTCCTGTTTGCTCTGGTGTTAGGAGTGGCCTTAAAGAAACTA
GGCTCCGAAGGAGAAGACCTCATCCGTTTCTTCAATTCCCTCAACGAGGCGACGATGGTG
CTGGTGTCCTGGATTATGTGGTACGTACCTGTGGGCATCATGTTCCTTGTTGGAAGCAAG
ATCGTGGAAATGAAAGACATCATCGTGCTGGTGACCAGCCTGGGGAAATACATCTTCGCA
TCTATATTGGGCCATGTTATTCATGGAGGAATTGTTCTGCCACTTATTTATTTTGTTTTC
ACACGAAAAAACCCATTCAGATTCCTCCTGGGCCTCCTCGCCCCATTTGCGACAGCATTT
GCTACCTGCTCCAGCTCAGCGACCCTTCCCTCTATGATGAAGTGCATTGAAGAGAACAAT
GGTGTGGACAAGAGGATCAGCAGGTTTATTCTCCCCATCGGGGCCACCGTGAACATGGAC
GGAGCAGCCATCTTCCAGTGTGTGGCCGCGGTGTTCATTGCGCAACTCAACAACATAGAG
CTCAACGCAGGACAGATTTTCACCATTCTAGTGACTGCCACAGCGTCCAGTGTTGGAGCA
GCAGGCGTGCCAGCTGGAGGGGTCCTCACCATTGCCATTATCCTGGAGGCCATTGGGCTG
CCTACTCATGACCTGCCTCTGATCCTGGCTGTGGACTGGATTGTGGACCGGACCACCACG
GTGGTGAATGTGGAAGGGGATGCCCTGGGTGCAGGCATTCTCCACCACCTGAATCAGAAG
GCAACAAAGAAAGGCGAGCAGGAACTTGCTGAGGTGAAAGTGGAAGCCATCCCCAACTGC
AAGTCTGAGGAGGAGACATCGCCCCTGGTGACACACCAGAACCCCGCTGGCCCCGTGGCC
AGTGCCCCAGAACTGGAATCCAAGGAGTCGGTTCTGTGA

1. Arriza JL, Kavanaugh MP, Fairman WA, Wu YN, Murdoch GH, North RA, Amara SG: Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J Biol Chem. 1993 Jul 25;268(21):15329-32. [PubMed ]
2. Shafqat S, Tamarappoo BK, Kilberg MS, Puranam RS, McNamara JO, Guadano-Ferraz A, Fremeau RT Jr: Cloning and expression of a novel Na(+)-dependent neutral amino acid transporter structurally related to mammalian Na+/glutamate cotransporters. J Biol Chem. 1993 Jul 25;268(21):15351-5. [PubMed ]
3. Hofmann K, Duker M, Fink T, Lichter P, Stoffel W: Human neutral amino acid transporter ASCT1: structure of the gene (SLC1A4) and localization to chromosome 2p13-p15. Genomics. 1994 Nov 1;24(1):20-6. [PubMed ]

1. SDS, mRNA
2. Serine dehydratase, isoform CRA_a

MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHF
VCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELA
KALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGL
QEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHP
IFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVV
IVCGGSNISLAQLRALKEQLGMTNRLPK

• None

• None

1. SPTLC1, transcript variant 1, mRNA
2. Serine palmitoyltransferase, long chain base subunit 1, isoform CRA_a

MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEEL
IEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAA
ALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSK
RGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRR
FIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDI
DLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENP
GIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCM
NRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL

• None

• None

1. Long chain base biosynthesis protein 3
2. LCB 3
3. Serine-palmitoyl-CoA transferase 3
4. SPT 3

MANPGGGAVCNGKLHNHKKQSNGSQSRNCTKNGIVKEAQQNGKPHFYDKLIVESFEEAPL
HVMVFTYMGYGIGTLFGYLRDFLRNWGIEKCNAAVERKEQKDFVPLYQDFENFYTRNLYM
RIRDNWNRPICSAPGPLFDLMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAAKYDES
MRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPA
LVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTRRAWK
KILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPH
EVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMG
LDGTTQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLE
KKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKKSARP
ELYDETSFELED

• Sphingolipid Metabolism (map00600 )

• palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 [RN:R01281] ALL_REAC R01281

• None

• 59-79

ATGGCTAACCCTGGAGGTGGTGCTGTTTGCAACGGGAAACTTCACAATCACAAGAAACAG
AGCAATGGCTCACAAAGCAGAAACTGCACAAAGAATGGAATAGTGAAGGAAGCCCAGCAA
AATGGGAAGCCACATTTTTATGATAAGCTCATTGTTGAATCGTTTGAGGAAGCACCCCTT
CATGTTATGGTTTTCACTTACATGGGATATGGAATTGGAACCCTGTTTGGCTATCTCAGA
GACTTTTTAAGAAACTGGGGAATAGAAAAATGCAACGCAGCTGTGGAACGAAAAGAACAA
AAAGTACGTATGCGCACCTCCCTGGATCTTTGTCAATGCCTACTCCTCTCTAAAGTGTTC
TCAGAAGTGGTGATGCAGGTGCAGATTCTAGAAAGCATGAGGTGCTCAGGAACTATTCAG
GGCAAATTTCATTCATCTCCACCTGCTAAACCCCATTACCCATGGGCTTATGGACCTGTT
TTTACAAACATCTCATGGGCAACTACTATTTGCCACATACCAAACTAA

1. 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 ]

MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGA
LNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQA
YGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDAL
VVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGV
KSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQT
VSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV

• PALP (PF00291 )

• None

• None

ATGTGTGCTCAGTATTGCATCTCCTTTGCTGATGTTGAAAAAGCTCATATCAACATTCGA
GATTCTATCCACCTCACACCAGTGCTAACAAGCTCCATTTTGAATCAACTAACAGGGCGC
AATCTTTTCTTCAAATGTGAACTCTTCCAGAAAACAGGATCTTTTAAGATTCGTGGTGCT
CTCAATGCCGTCAGAAGCTTGGTTCCTGATGCTTTAGAAAGGAAGCCGAAAGCTGTTGTT
ACTCACAGCAGTGGAAACCATGGCCAGGCTCTCACCTATGCTGCCAAATTGGAAGGAATT
CCTGCTTATATTGTGGTGCCCCAGACAGCTCCAGACTGTAAAAAACTTGCAATACAAGCC
TACGGAGCGTCAATTGTATACTGTGAACCTAGTGATGAGTCCAGAGAAAATGTTGCAAAA
AGAGTTACAGAAGAAACAGAAGGCATCATGGTACATCCCAACCAGGAGCCTGCAGTGATA
GCTGGACAAGGGACAATTGCCCTGGAAGTGCTGAACCAGGTTCCTTTGGTGGATGCACTG
GTGGTACCTGTAGGTGGAGGAGGAATGCTTGCTGGAATAGCAATTACAGTTAAGGCTCTG
AAACCTAGTGTGAAGGTATATGCTGCTGAACCCTCAAATGCAGATGACTGCTACCAGTCC
AAGCTGAAGGGGAAACTGATGCCCAATCTTTATCCTCCAGAAACCATAGCAGATGGTGTC
AAATCCAGCATTGGCTTGAACACCTGGCCTATTATCAGGGACCTTGTGGATGATATCTTC
ACTGTCACAGAGGATGAAATTAAGTGTGCAACCCAGCTGGTGTGGGAGAGGATGAAACTA
CTCATTGAACCTACAGCTGGTGTTGGAGTGGCTGCTGTGCTGTCTCAACATTTTCAAACT
GTTTCCCCAGAAGTAAAGAACATTTGTATTGTGCTCAGTGGTGGAAATGTAGACTTAACC
TCCTCCATAACTTGGGTGAAGCAGGCTGAAAGGCCAGCTTCTTATCAGTCTGTTTCTGTT
TAA

1. De Miranda J, Santoro A, Engelender S, Wolosker H: Human serine racemase: moleular cloning, genomic organization and functional analysis. Gene. 2000 Oct 3;256(1-2):183-8. [PubMed ]

MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGIELTLQIQSDTGVRATLKEFKERLAGDKY
QAAVQALREEVESFASLFPLPGLPDF

• None

• None

ELRCCTSLCFGRLGLCRDVGSWSGWPFGLSTATQPRLRLGKQTGAGQARRACRTVILRCG
SCCRGRRTGSVVAWSSLPQRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGS
PANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLI
DYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVI
PSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFPSLQ
GGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLV
DLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV
VDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFDEH

• Cyanoamino acid metabolism (map00460 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Lysine Degradation (map00310 )
• Methane metabolism (map00680 )
• One Carbon Pool By Folate (map00670 )

• 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945] ALL_REAC R00945
• (other) R03284

• SHMT (PF00464 )

• None

• None

CCGAGTTGCGATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGG
GCAGCTGGTCAGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGG
GGAAGCAAACAGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTG
GGAGTTGCTGCAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGA
GATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGCCGGGCCT
TGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTACTCCGGGT
CCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATCATGGGGC
TGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAGCGGATAT
CAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACTGGCCTCA
TTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATCATAGCTG
GCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGTGATGAAG
TCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCCAAGGTGA
TTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACTCTTCGAG
GGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCCAAGACTG
GCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCATCCCTGC
AGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAGGCCTGCA
CCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATGGCAGATG
CCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTGGTGCTGG
TGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAGCTTGTAT
CCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCGGGCGGCC
TGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTCCGGAGAG
TTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAGACTGCCA
AGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGTCTGGCCA
ACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTTGATGAGC
ATTGA

1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed ]

MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLA
DMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYT
FEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGY
SLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPA
LTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVE
QFARAFPMPGFDEH

• Cyanoamino acid metabolism (map00460 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Lysine Degradation (map00310 )
• Methane metabolism (map00680 )
• One Carbon Pool By Folate (map00670 )

• 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945] ALL_REAC R00945
• (other) R03284

• SHMT (PF00464 )

• 1-18

• None

ATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGGGCAGCTGGTC
AGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAAC
AGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTG
CAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGC
AGCCGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTAT
CCTGGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAG
CGCCGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCC
TACTCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGG
ATCATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTC
AAGCGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCTGGCA
CTGACTGCTCGACTTTTCCGGCCACGGCTCATCATAGCTGGCACCAGCGCCTATGCTCGC
CTCATTGACTACGCCCGCATGAGAGAGGTGTGTGATGAAGTCAAAGCACACCTGCTGGCA
GACATGGCCCACATCAGTGGCCTGGTGGCTGCCAAGGTGATTCCCTCGCCTTTCAAGCAC
GCGGACATCGTCACCACCACTACTCACAAGACTCTTCGAGGGGCCAGGTCAGGGCTCATC
TTCTACCGGAAAGGGGTGAAGGCTGTGGACCCCAAGACTGGCCGGGAGATCCCTTACACA
TTTGAGGACCGAATCAACTTTGCCGTGTTCCCATCCCTGCAGGGGGGCCCCCACAATCAT
GCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAGGCCTGCACCCCCATGTTCCGGGAGTAC
TCCCTGCAGGTTCTGAAGAATGCTCGGGCCATGGCAGATGCCCTGCTAGAGCGAGGCTAC
TCACTGGTATCAGGTGGTACTGACAACCACCTGGTGCTGGTGGACCTGCGGCCCAAGGGC
CTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAGCTTGTATCCATCACTGCCAACAAGAAC
ACCTGTCCTGGAGACCGAAGTGCCATCACACCGGGCGGCCTGCGGCTTGGGGCCCCAGCC
TTAACTTCTCGACAGTTCCGTGAGGATGACTTCCGGAGAGTTGTGGACTTTATAGATGAA
GGGGTCAACATTGGCTTAGAGGTGAAGAGCAAGACTGCCAAGCTCCAGGATTTCAAATCC
TTCCTGCTTAAGGACTCAGAAACAAGTCAGCGTCTGGCCAACCTCAGGCAACGGGTGGAG
CAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTTGATGAGCATTGA

1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed ]

MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASFFPLPGL
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• Cyanoamino acid metabolism (map00460 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Lysine Degradation (map00310 )
• Methane metabolism (map00680 )
• One Carbon Pool By Folate (map00670 )

• 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945] ALL_REAC R00945
• (other) R03284

• SHMT (PF00464 )

• None

• None

ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTTTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA

1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed ]

MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLC
SKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAE
RIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGF
EGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQL
SQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTC
FRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYH
IVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKV
EFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEP
SKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA

• Seryl_tRNA_N (PF02403 )
• tRNA-synt_2b (PF00587 )

• None

• None

MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK

• CBS (PF00571 )
• PALP (PF00291 )

• None

• None

MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKA
ALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVA
SKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDG
ATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE

• Hydrolase (PF00702 )

• None

• None

1. Tumor differentially expressed protein 2
2. Tumor differentially expressed 1 protein-like

MGSVLGLCSMASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPG
MEEQLNKIPGFCENEKGVVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAA
VHNGFWFFKFAAAIAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNE
SWVEKMEEGNSRCWYAALLSATALNYLLSLVAIVLFFVYYTHPASCSENKAFISVNMLLC
VGASVMSILPKIQESQPRSGLLQSSVITVYTMYLTWSAMTNEPETNCNPSLLSIIGYNTT
STVPKEGQSVQWWHAQGIIGLILFLLCVFYSSIRTSNNSQVNKLTLTSDESTLIEDGGAR
SDGSLEDGDDVHRAVDNERDGVTYSYSFFHFMLFLASLYIMMTLTNWYRYEPSREMKSQW
TAVWVKISSSWIGIVLYVWTLVAPLVLTNRDFD

• Serinc (PF03348 )

• None

• 89-109 124-144 152-172 198-218 232-252 260-280 310-330 388-408 427-447

1. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed ]
2. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]
3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]
4. 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 ]