1. (+)-2-Amino-3-mercaptopropionic acid
2. (2R)-2-amino-3-mercaptopropanoic acid
3. (2R)-2-amino-3-sulfanylpropanoic acid
4. (R)-2-Amino-3-mercaptopropanoate
5. (R)-2-amino-3-mercapto-Propanoic acid
6. (R)-(+)-cysteine
7. (R)-cysteine
8. 2-Amino-3-mercaptopropanoic acid
9. 2-Amino-3-mercaptopropionate
10. 2-Amino-3-mercaptopropionic acid
11. 3-mercapto-L-Alanine
12. B-mercaptoalanine
13. Carbocysteine
14. Cisteina
15. Cisteinum
16. Cystein
17. Cysteine
18. Cysteinum
19. Half-cystine
20. Free cysteine
21. L cysteine
22. L-(+)-cysteine
23. L-2-Amino-3-mercaptopropanoic acid
24. L-2-Amino-3-mercaptopropionic acid
25. L-cystein
26. L-cysteine
27. Polycysteine
28. Thioserine
29. alpha-amino-beta-thiolpropionic acid
30. beta-mercaptoalanine
31. acetylcysteine
32. (2R)-2-amino-3-mercaptopropanoate
33. (2R)-2-amino-3-sulfanylpropanoate
34. (R)-2-Amino-3-mercaptopropanoic acid
35. (R)-2-amino-3-mercapto-Propanoate
36. 2-Amino-3-mercaptopropanoate
37. L-2-Amino-3-mercaptopropanoate

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• Cytoplasm
• Extracellular
• mitochondria

• Blood
• Cerebrospinal Fluid
• Urine

• 167320 (Dementia)
• 126200 (Multiple sclerosis)
• 540000 (Stroke)

1. Sandmann J, Schwedhelm KS, Tsikas D: Specific transport of S-nitrosocysteine in human red blood cells: Implications for formation of S-nitrosothiols and transport of NO bioactivity within the vasculature. FEBS Lett. 2005 Aug 1;579(19):4119-24. [PubMed ]
2. Paivalainen S, Suokas M, Lahti O, Heape AM: Degraded myelin-associated glycoprotein (dMAG) formation from pure human brain myelin-associated glycoprotein (MAG) is not mediated by calpain or cathepsin L-like activities. J Neurochem. 2003 Feb;84(3):533-45. [PubMed ]
3. Iyer S, Leonidas DD, Swaminathan GJ, Maglione D, Battisti M, Tucci M, Persico MG, Acharya KR: The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 A resolution. J Biol Chem. 2001 Apr 13;276(15):12153-61. Epub 2000 Nov 7. [PubMed ]
4. Nishiya Y, Yoshida Y, Yoshimura M, Fukamachi H, Nakano Y: Homogeneous enzymatic assay for L-cysteine with betaC-S lyase. Biosci Biotechnol Biochem. 2005 Nov;69(11):2244-6. [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. Santamaria I, Velasco G, Cazorla M, Fueyo A, Campo E, Lopez-Otin C: Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Res. 1998 Apr 15;58(8):1624-30. [PubMed ]
7. Eriksson A, Tohonen V, Wedell A, Nordqvist K: Isolation of the human testatin gene and analysis in patients with abnormal gonadal development. Mol Hum Reprod. 2002 Jan;8(1):8-15. [PubMed ]
8. Kaminska J, Wisniewska A, Koscielak J: Chemical modifications of alpha1,6-fucosyltransferase define amino acid residues of catalytic importance. Biochimie. 2003 Mar-Apr;85(3-4):303-10. [PubMed ]
9. Li Y, Gamper N, Shapiro MS: Single-channel analysis of KCNQ K+ channels reveals the mechanism of augmentation by a cysteine-modifying reagent. J Neurosci. 2004 Jun 2;24(22):5079-90. [PubMed ]
10. Lindzen M, Gottschalk KE, Fuzesi M, Garty H, Karlish SJ: Structural interactions between FXYD proteins and Na+,K+-ATPase: alpha/beta/FXYD subunit stoichiometry and cross-linking. J Biol Chem. 2006 Mar 3;281(9):5947-55. Epub 2005 Dec 21. [PubMed ]
11. Norris FA, Wilson MP, Wallis TS, Galyov EE, Majerus PW: SopB, a protein required for virulence of Salmonella dublin, is an inositol phosphate phosphatase. Proc Natl Acad Sci U S A. 1998 Nov 24;95(24):14057-9. [PubMed ]
12. Kersemans V, Cornelissen B, Kersemans K, Bauwens M, Achten E, Dierckx RA, Mertens J, Slegers G: In vivo characterization of 123/125I-2-iodo-L-phenylalanine in an R1M rhabdomyosarcoma athymic mouse model as a potential tumor tracer for SPECT. J Nucl Med. 2005 Mar;46(3):532-9. [PubMed ]
13. Foss CA, Mease RC, Fan H, Wang Y, Ravert HT, Dannals RF, Olszewski RT, Heston WD, Kozikowski AP, Pomper MG: Radiolabeled small-molecule ligands for prostate-specific membrane antigen: in vivo imaging in experimental models of prostate cancer. Clin Cancer Res. 2005 Jun 1;11(11):4022-8. [PubMed ]
14. 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 ]
15. Kozaki K, Miyaishi O, Asai N, Iida K, Sakata K, Hayashi M, Nishida T, Matsuyama M, Shimizu S, Kaneda T, et al.: Tissue distribution of ERp61 and association of its increased expression with IgG production in hybridoma cells. Exp Cell Res. 1994 Aug;213(2):348-58. [PubMed ]
16. Amberger VR, Hensel T, Ogata N, Schwab ME: Spreading and migration of human glioma and rat C6 cells on central nervous system myelin in vitro is correlated with tumor malignancy and involves a metalloproteolytic activity. Cancer Res. 1998 Jan 1;58(1):149-58. [PubMed ]
17. Zhang JT, Li QX, Wang D, Zhu ZL, Yang YH, Cui DS, Wang MW, Sun XF: Up-regulation of PINCH in the stroma of oral squamous cell carcinoma predicts nodal metastasis. Oncol Rep. 2005 Dec;14(6):1519-22. [PubMed ]
18. Taveau M, Bourg N, Sillon G, Roudaut C, Bartoli M, Richard I: Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components. Mol Cell Biol. 2003 Dec;23(24):9127-35. [PubMed ]
19. Yu FH, Westenbroek RE, Silos-Santiago I, McCormick KA, Lawson D, Ge P, Ferriera H, Lilly J, DiStefano PS, Catterall WA, Scheuer T, Curtis R: Sodium channel beta4, a new disulfide-linked auxiliary subunit with similarity to beta2. J Neurosci. 2003 Aug 20;23(20):7577-85. [PubMed ]
20. Naisbitt DJ, Vilar FJ, Stalford AC, Wilkins EG, Pirmohamed M, Park BK: Plasma cysteine deficiency and decreased reduction of nitrososulfamethoxazole with HIV infection. AIDS Res Hum Retroviruses. 2000 Dec 10;16(18):1929-38. [PubMed ]
21. Wikipedia

1. Aspartate aminotransferase, cytoplasmic
2. Aspartate aminotransferase, mitochondrial precursor
3. Aminopeptidase N
4. Glutamate--cysteine ligase catalytic subunit
5. Glutamate--cysteine ligase regulatory subunit
6. Cystathionine gamma-lyase
7. Glutaminyl-peptide cyclotransferase precursor
8. Cystathionine beta-synthase
9. Glutathione synthetase
10. Cytosol aminopeptidase
11. Cysteine sulfinic acid decarboxylase
12. Cysteine dioxygenase type 1
13. Methylated-DNA--protein-cysteine methyltransferase
14. Large neutral amino acids transporter small subunit 2
15. Cysteine desulfurase, mitochondrial precursor
16. Novel protein
17. 4F2 cell-surface antigen heavy chain
18. Phosphopantothenate--cysteine ligase
19. Probable cysteinyl-tRNA synthetase, mitochondrial precursor
20. Prenylcysteine oxidase 1 precursor
21. Putative uncharacterized protein DKFZp686F1612 (Cysteinyl-tRNA synthetase, isoform CRA_e)
22. Gamma-glutamylcyclotransferase
23. cDNA, FLJ94281, Homo sapiens cystathionine-beta-synthase (CBS), mRNA (Cystathionine-beta-synthase, isoform CRA_b)
24. cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
25. cDNA FLJ10608 fis, clone NT2RP2005239, highly similar to Cysteine desulfurase, mitochondrial (EC 2.8.1.7)
26. cDNA, FLJ94971, highly similar to Homo sapiens cysteine dioxygenase, type I (CDO1), mRNA (Cysteine dioxygenase, type I)
27. cDNA, FLJ95254, highly similar to Homo sapiens prenylcysteine lyase (PCL1), mRNA (Prenylcysteine oxidase 1)
28. Cysteine dioxygenase
29. Cysteinyl-tRNA synthetase, cytoplasmic

1. Transaminase A
2. Glutamate oxaloacetate transaminase 1

MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ

• Arginine and Proline Metabolism (map00330 )
• Carbon fixation (map00710 )
• Cysteine Metabolism (map00272 )
• Glutamate Metabolism (map00251 )
• Phenylalanine Metabolism (map00360 )
• Phenylalanine and Tyrosine Metabolism (map00400 )
• Tyrosine Metabolism (map00350 )
• Novobiocin biosynthesis (map00401 )

• L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

• Aminotran_1_2 (PF00155 )

• None

• None

ATGGCACCTCCGTCAGTCTTTGCCGAGGTTCCGCAGGCCCAGCCTGTCCTGGTCTTCAAG
CTCACTGCCGACTTCAGGGAGGATCCGGACCCCCGCAAGGTCAACCTGGGAGTGGGAGCA
TATCGCACGGATGACTGCCATCCCTGGGTTTTGCCAGTAGTGAAGAAAGTGGAGCAGAAG
ATTGCTAATGACAATAGCCTAAATCACGAGTATCTGCCAATCCTGGGCCTGGCTGAGTTC
CGGAGCTGTGCTTCTCGTCTTGCCCTTGGGGATGACAGCCCAGCACTCAAGGAGAAGCGG
GTAGGAGGTGTGCAATCTTTGGGGGGAACAGGTGCACTTCGAATTGGAGCTGATTTCTTA
GCGCGTTGGTACAATGGAACAAACAACAAGAACACACCTGTCTATGTGTCCTCACCAACC
TGGGAGAATCACAATGCTGTGTTTTCCGCTGCTGGTTTTAAAGACATTCGGTCCTATCGC
TACTGGGATGCAGAGAAGAGAGGATTGGACCTCCAGGGCTTCCTGAATGATCTGGAGAAT
GCTCCTGAGTTCTCCATTGTTGTCCTCCACGCCTGTGCACACAACCCAACTGGGATTGAC
CCAACTCCGGAGCAGTGGAAGCAGATTGCTTCTGTCATGAAGCACCGGTTTCTGTTCCCC
TTCTTTGACTCAGCCTATCAGGGCTTCGCATCTGGAAACCTGGAGAGAGATGCCTGGGCC
ATTCGCTATTTTGTGTCTGAAGGCTTCGAGTTCTTCTGTGCCCAGTCCTTCTCCAAGAAC
TTCGGGCTCTACAATGAGAGAGTCGGGAATCTGACTGTGGTTGGAAAAGAACCTGAGAGC
ATCCTGCAAGTCCTTTCCCAGATGGAGAAGATCGTGCGGATTACTTGGTCCAATCCCCCC
GCCCAGGGAGCACGAATTGTGGCCAGCACCCTCTCTAACCCTGAGCTCTTTGAGGAATGG
ACAGGTAATGTGAAGACAATGGCTGACCGGATTCTGACCATGAGATCTGAACTCAGGGCA
CGACTAGAAGCCCTCAAAACCCCTGGGACCTGGAACCACATCACTGATCAAATTGGCATG
TTCAGCTTCACTGGGTTGAACCCCAAGCAGGTTGAGTATCTGGTCAATGAAAAGCACATC
TACCTGCTGCCAAGTGGTCGAATCAACGTGAGTGGCTTAACCACCAAAAATCTAGATTAC
GTGGCCACCTCCATCCATGAAGCAGTCACCAAAATCCAGTGA

1. Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R: Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. Biochemistry. 1990 Jun 5;29(22):5293-9. [PubMed ]
2. Doyle JM, Schinina ME, Bossa F, Doonan S: The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem J. 1990 Sep 15;270(3):651-7. [PubMed ]

1. Transaminase A
2. Glutamate oxaloacetate transaminase 2

MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEV
LKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKGMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK

• Arginine and Proline Metabolism (map00330 )
• Carbon fixation (map00710 )
• Cysteine Metabolism (map00272 )
• Glutamate Metabolism (map00251 )
• Phenylalanine Metabolism (map00360 )
• Phenylalanine and Tyrosine Metabolism (map00400 )
• Tyrosine Metabolism (map00350 )
• Novobiocin biosynthesis (map00401 )

• L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

• Aminotran_1_2 (PF00155 )

• 1-24

ATGGCCCTGCTGCACTCCGGCCGCGTCCTCCCCGGGATCGCCGCCGCCTTCCACCCGGGC
CTCGCCGCCGCGGCCTCTGCCAGAGCCAGCTCCTGGTGGACCCATGTGGAAATGGGACCT
CCAGATCCCATTCTGGGAGTCACTGAAGCCTTTAAGAGGGACACCAATAGCAAAAAGATG
AATCTGGGAGTTGGTGCCTACCGGGATGATAATGGAAAGCCTTACGTTCTGCCTAGCGTC
CGCAAGGCAGAGGCCCAGATTGCCGCAAAAAATTTGGACAAGGAATACCTGCCCATTGGG
GGACTGGCTGAATTTTGCAAGGCATCTGCAGAACTAGCCCTGGGTGAGAACAGCGAAGTC
TTGAAGAGTGGCCGGTTTGTCACTGTGCAGACCATTTCTGGAACTGGAGCCTTAAGGATC
GGAGCCAGTTTTCTGCAAAGATTTTTTAAGTTCAGCCGAGATGTCTTTCTGCCCAAACCA
ACCTGGGGAAACCACACACCCATCTTCAGGGATGCTGGCATGCAGCTACAAGGTTATCGG
TATTATGACCCCAAGACTTGCGGTTTTGACTTCACAGGCGCTGTGGAGGATATTTCAAAA
ATACCAGAGCAGAGTGTTCTTCTTCTGCATGCCTGCGCCCACAATCCCACGGGAGTGGAC
CCGCGTCCGGAACAGTGGAAGGAAATAGCAACAGTGGTGAAGAAAAGGAATCTCTTTGCG
TTCTTTGACATGGCCTACCAAGGCTTTGCCAGTGGTGATGGTGATAAGGATGCCTGGGCT
GTGCGCCACTTCATCGAACAGGGCATTAATGTTTGCCTCTGCCAATCATATGCCAAGAAC
ATGGGCTTATATGGTGAGCGTGTAGGAGCCTTCACTATGGTCTGCAAAGATGCGGATGAA
GCCAAAAGGGTAGAGTCACAGTTGAAGATCTTGATCCGTCCCATGTATTCCAACCCTCCC
CTCAATGGGGCCCGGATTGCTGCTGCCATTCTGAACACCCCAGATTTGCGAAAACAATGG
CTGCAAGAAGTGAAAGGCATGGCTGACCGCATCATTGGCATGCGGACTCAACTGGTCTCC
AACCTCAAGAAGGAGGGTTCCACCCACAATTGGCAACACATCACCGACCAAATTGGCATG
TTCTGTTTCACAGGGCTAAAGCCTGAACAGGTGGAGCGGCTGATCAAGGAGTTCTCCATC
TACATGACAAAAGATGGCCGCATCTCTGTGGCAGGGGTCACCTCCAGCAACGTGGGCTAC
CTTGCCCATGCCATTCACCAGGTCACCAAGTAA

1. Pol S, Bousquet-Lemercier B, Pave-Preux M, Pawlak A, Nalpas B, Berthelot P, Hanoune J, Barouki R: Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. Biochem Biophys Res Commun. 1988 Dec 30;157(3):1309-15. [PubMed ]
2. Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F: The primary structure of mitochondrial aspartate aminotransferase from human heart. Biochim Biophys Acta. 1985 Nov 8;832(1):46-51. [PubMed ]

1. hAPN
2. Alanyl aminopeptidase
3. Microsomal aminopeptidase
4. Aminopeptidase M
5. gp150
6. Myeloid plasma membrane glycoprotein CD13
7. CD13 antigen

MAKGFYISKSLGILGILLGVAAVCTIIALSVVYSQEKNKNANSSPVASTTPSASATTNPA
SATTLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEATDVI
IIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLKGSLVKDSQYEMDS
EFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKAEFNITLIHP
KDLTALSNMLPKGPSTPLPEDPNWNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLI
RIWARPSAIAAGHGDYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLV
TYRENSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFASYVEYL
GADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINTPAQISELFDAISYSKG
ASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIYLNLWDHLQEAVNNRSIQLPTTVRDIM
NRWTLQMGFPVITVDTSTGTLSQEHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDY
WLIDVRAQNDLFSTSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQ
IINDAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGPMKN
YLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPECEEMVSGLFKQWM
ENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFRNATLVNEADKLRAALACSKELWI
LNRYLSYTLNPDLIRKQDATSTIISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSN
LIQAVTRRFSTEYELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQ
WFTENSK

• Glutathione Metabolism (map00480 )

• Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide

• 1-22

ATGGCCAAGGGCTTCTATATTTCCAAGTCCCTGGGCATCCTGGGGATCCTCCTGGGCGTG
GCAGCCGTGTGCACAATCATCGCACTGTCAGTGGTGTACTCCCAGGAGAAGAACAAGAAC
GCCAACAGCTCCCCCGTGGCCTCCACCACCCCGTCCGCCTCAGCCACCACCAACCCCGCC
TCGGCCACCACCTTGGACCAAAGTAAAGCGTGGAATCGTTACCGCCTCCCCAACACGCTG
AAACCCGATTCCTACCAGGTGACGCTGAGACCGTACCTCACCCCCAATGACAGGGGCCTG
TACGTTTTTAAGGGCTCCAGCACCGTCCGTTTCACCTGCAAGGAGGCCACTGACGTCATC
ATCATCCACAGCAAGAAGCTCAACTACACCCTCAGCCAGGGGCACAGGGTGGTCCTGCGT
GGTGTGGGAGGCTCCCAGCCCCCCGACATTGACAAGACTGAGCTGGTGGAGCCCACCGAG
TACCTGGTGGTGCACCTCAAGGGCTCCCTGGTGAAGGACAGCCAGTATGAGATGGACAGC
GAGTTCGAGGGGGAGTTGGCAGATGACCTGGCGGGCTTCTACCGCAGCGAGTACATGGAG
GGCAATGTCAGAAAGGTGGTGGCCACTACACAGATGCAGGCTGCAGATGCCCGGAAGTCC
TTCCCATGCTTCGATGAGCCGGCCATGAAGGCCGAGTTCAACATCACGCTTATCCACCCC
AAGGACCTGACAGCCCTGTCCAACATGCTTCCCAAAGGTCCCAGCACCCCACTTCCAGAA
GACCCCAACTGGAATGTCACTGAGTTCCACACCACGCCCAAGATGTCCACGTACTTGCTG
GCCTTCATTGTCAGTGAGTTCGACTACGTGGAGAAGCAGGCATCCAATGGTGTCTTGATC
CGGATCTGGGCCCGGCCCAGTGCCATTGCGGCGGGCCACGGCGATTATGCCCTGAACGTG
ACGGGCCCCATCCTTAACTTCTTTGCTGGTCATTATGACACACCCTACCCACTCCCAAAA
TCAGACCAGATTGGCCTGCCAGACTTCAACGCCGGCGCCATGGAGAACTGGGGACTGGTG
ACCTACCGGGAGAACTCCCTGCTGTTCGACCCCCTGTCCTCCTCCAGCAGCAACAAGGAG
CGGGTGGTCACTGTGATTGCTCATGAGCTGGCCCACCAGTGGTTCGGGAACCTGGTGACC
ATAGAGTGGTGGAATGACCTGTGGCTGAACGAGGGCTTCGCCTCCTACGTGGAGTACCTG
GGTGCTGACTATGCGGAGCCCACCTGGAACTTGAAAGACCTCATGGTGCTGAATGATGTG
TACCGCGTGATGGCAGTGGATGCACTGGCCTCCTCCCACCCGCTGTCCACACCCGCCTCG
GAGATCAACACGCCGGCCCAGATCAGTGAGCTGTTTGACGCCATCTCCTACAGCAAGGGC
GCCTCAGTCCTCAGGATGCTCTCCAGCTTCCTGTCCGAGGACGTATTCAAGCAGGGCCTG
GCGTCCTACCTCCACACCTTTGCCTACCAGAACACCATCTACCTGAACCTGTGGGACCAC
CTGCAGGAGGCTGTGAACAACCGGTCCATCCAACTCCCCACCACCGAGCGGGACATCATG
AACCGCTGGACCCTGCAGATGGGCTTCCCGGTCATCACGGTGGATACCAGCACGGGGACC
CTTTCCCAGGAGCACTTCCTCCTTGACCCCGATTCCAATGTTACCCGCCCCTCAGAATTC
AACTACGTGTGGATTGTGCCCATCACATCCATCAGAGATGGCAGACAGCAGCAGGACTAC
TGGCTGATGGATGTAAGAGCCCAGAACGATCTCTTCAGCACATCAGGCAATGAGTGGGTC
CTGCTGAACCTCAATGTGACGGGCTATTACCGGGTGAACTACGACGAAGAGAACTGGAGG
AAGATTCAGACTCAGCTGCAGAGAGACCACTCGGCCATCCCTGTCATCAATCGGGCACAG
ATCATTAATGACGCCTTCAACCTGGCCAGTGCCCATAAGGTCCCTGTCACTCTGGCGCTG
AACAACACCCTCTTCCTGATTGAAGAGAGACAGTACATGCCCTGGGAGGCCGCCCTGAGC
AGCCTGAGCTACTTCAAGCTCATGTTTGACCGCTCCGAGGTCTATGGCCCCATGAAGAAC
TACCTGAAGAAGCAGGTCACACCCCTCTTCATTCACTTCAGAAATAATACCAACAACTGG
AGGGAGATCCCAGAAAACCTGATGGACCAGTACAGCGAGGTTAATGCCATCAGCACCGCC
TGCTCCAACGGAGTTCCAGAGTGTGAGGAGATGGTCTCTGGCCTTTTCAAGCAGTGGATG
GAGAACCCCAATAATAACCCGATCCACCCCAACCTGCGGTCCACCGTCTACTGCAACGCT
ATCGCCCAGGGCGGGGAGGAGGAGTGGGACTTCGCCTGGGAGCAGTTCCGAAATGCCACA
CTGGTCAATGAGGCTGACAAGCTCCGGGCAGCCCTGGCCTGCAGCAAAGAGTTGTGGATC
CTGAACAGGTACCTGAGCTACACCCTGAACCCGGACTTAATCCGGAAGCAGGACGCCACC
TCTACCATCATCAGCATTACCAACAACGTCATTGGGCAAGGTCTGGTCTGGGACTTTGTC
CAGAGCAACTGGAAGAAGCCTTTTAACGATTATGGTGGTGGCTCGTTCTCCTTCTCCAAC
CTCATCCAGGCAGTGACACGACGATTCTCCACCGAGTATGAGCTGCAGCAGCTGGAGCAG
TTCAAGAAGGACAACGAGGAAACAGGCTTCGGCTCAGGCACCCGGGCCCTGGAGCAAGCC
CTGGAGAAGACGAAAGCCAACATCAAGTGGGTGAAGGAGAACAAGGAGGTGGTGCTCCAG
TGGTTCACAGAAAACAGCAAATAG

1. Olsen J, Cowell GM, Konigshofer E, Danielsen EM, Moller J, Laustsen L, Hansen OC, Welinder KG, Engberg J, Hunziker W, et al.: Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. FEBS Lett. 1988 Oct 10;238(2):307-14. [PubMed ]
2. Look AT, Ashmun RA, Shapiro LH, Peiper SC: Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N. J Clin Invest. 1989 Apr;83(4):1299-307. [PubMed ]
3. Shapiro LH, Ashmun RA, Roberts WM, Look AT: Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells. J Biol Chem. 1991 Jun 25;266(18):11999-2007. [PubMed ]
4. Watanabe Y, Iwaki-Egawa S, Mizukoshi H, Fujimoto Y: Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N. Biol Chem Hoppe Seyler. 1995 Jul;376(7):397-400. [PubMed ]
5. Nunez L, Amigo L, Rigotti A, Puglielli L, Mingrone G, Greco AV, Nervi F: Cholesterol crystallization-promoting activity of aminopeptidase-N isolated from the vesicular carrier of biliary lipids. FEBS Lett. 1993 Aug 23;329(1-2):84-8. [PubMed ]
6. Tokioka-Terao M, Hiwada K, Kokubu T: Purification and characterization of aminopeptidase N from human plasma. Enzyme. 1984;32(2):65-75. [PubMed ]
7. O'Connell PJ, Gerkis V, d'Apice AJ: Variable O-glycosylation of CD13 (aminopeptidase N). J Biol Chem. 1991 Mar 5;266(7):4593-7. [PubMed ]
8. Yeager CL, Ashmun RA, Williams RK, Cardellichio CB, Shapiro LH, Look AT, Holmes KV: Human aminopeptidase N is a receptor for human coronavirus 229E. Nature. 1992 Jun 4;357(6377):420-2. [PubMed ]
9. Favaloro EJ, Browning T, Facey D: CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated. Exp Hematol. 1993 Dec;21(13):1695-701. [PubMed ]
10. Soderberg C, Giugni TD, Zaia JA, Larsson S, Wahlberg JM, Moller E: CD13 (human aminopeptidase N) mediates human cytomegalovirus infection. J Virol. 1993 Nov;67(11):6576-85. [PubMed ]
11. Kolb AF, Maile J, Heister A, Siddell SG: Characterization of functional domains in the human coronavirus HCV 229E receptor. J Gen Virol. 1996 Oct;77 ( Pt 10):2515-21. [PubMed ]
12. Noren K, Hansen GH, Clausen H, Noren O, Sjostrom H, Vogel LK: Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13) is normally expressed at the cell surface and has full enzymatic activity. Exp Cell Res. 1997 Feb 25;231(1):112-8. [PubMed ]
13. Kolb AF, Hegyi A, Siddell SG: Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N. J Gen Virol. 1997 Nov;78 ( Pt 11):2795-802. [PubMed ]
14. Hegyi A, Kolb AF: Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N. J Gen Virol. 1998 Jun;79 ( Pt 6):1387-91. [PubMed ]
15. Dong X, An B, Salvucci Kierstead L, Storkus WJ, Amoscato AA, Salter RD: Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells. J Immunol. 2000 Jan 1;164(1):129-35. [PubMed ]
16. Pasqualini R, Koivunen E, Kain R, Lahdenranta J, Sakamoto M, Stryhn A, Ashmun RA, Shapiro LH, Arap W, Ruoslahti E: Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis. Cancer Res. 2000 Feb 1;60(3):722-7. [PubMed ]
17. Seli E, Senturk LM, Bahtiyar OM, Kayisli UA, Arici A: Expression of aminopeptidase N in human endometrium and regulation of its activity by estrogen. Fertil Steril. 2001 Jun;75(6):1172-6. [PubMed ]
18. Wentworth DE, Holmes KV: Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): influence of N-linked glycosylation. J Virol. 2001 Oct;75(20):9741-52. [PubMed ]
19. van Hensbergen Y, Broxterman HJ, Hanemaaijer R, Jorna AS, van Lent NA, Verheul HM, Pinedo HM, Hoekman K: Soluble aminopeptidase N/CD13 in malignant and nonmalignant effusions and intratumoral fluid. Clin Cancer Res. 2002 Dec;8(12):3747-54. [PubMed ]
20. Bonavia A, Zelus BD, Wentworth DE, Talbot PJ, Holmes KV: Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E. J Virol. 2003 Feb;77(4):2530-8. [PubMed ]
21. Lendeckel U, Wex T, Arndt M, Frank K, Franke A, Ansorge S: Identification of point mutations in the aminopeptidase N gene by SSCP analysis and sequencing. Hum Mutat. 1998;Suppl 1:S158-60. [PubMed ]

1. Gamma- glutamylcysteine synthetase
2. Gamma-ECS
3. GCS heavy chain

MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDH
ENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTV
EANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAI
NKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDA
MGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVI
SASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQ
EGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDI
GWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVL
QGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNS
YLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYS
LILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN

• Glutamate Metabolism (map00251 )
• Glutathione Metabolism (map00480 )

• ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine

• GCS (PF03074 )

• None

• None

ATGGGGCTGCTGTCCCAGGGCTCGCCGCTGAGCTGGGAGGAAACCAAGCGCCATGCCGAC
CACGTGCGGCGGCACGGGATCCTCCAGTTCCTGCACATCTACCACGCCGTCAAGGACCGG
CACAAGGACGTTCTCAAGTGGGGCGATGAGGTGGAATACATGTTGGTATCTTTTGATCAT
GAAAATAAAAAAGTCCGGTTGGTCCTGTCTGGGGAGAAAGTTCTTGAAACTCTGCAAGAG
AAGGGGGAAAGGACAAACCCAAACCATCCTACCCTTTGGAGACCAGAGTATGGGAGTTAC
ATGATTGAAGGGACACCAGGACAGCCCTACGGAGGAACAATGTCCGAGTTCAATACAGTT
GAGGCCAACATGCGAAAACGCCGGAAGGAGGCTACTTCTATATTAGAAGAAAATCAGGCT
CTTTGCACAATAACTTCATTTCCCAGATTAGGCTGTCCTGGGTTCACACTGCCCGAGGTC
AAACCCAACCCAGTGGAAGGAGGAGCTTCCAAGTCCCTCTTCTTTCCAGATGAAGCAATA
AACAAGCACCCTCGCTTCAGTACCTTAACAAGAAATATCCGACATAGGAGAGGAGAAAAG
GTTGTCATCAATGTACCAATATTTAAGGACAAGAATACACCATCTCCATTTATAGAAACA
TTTACTGAGGATGATGAAGCTTCAAGGGCTTCTAAGCCGGATCATATTTACATGGATGCC
ATGGGATTTGGAATGGGCAATTGCTGTCTCCAGGTGACATTCCAAGCCTGCAGTATATCT
GAGGCCAGATACCTTTATGATCAGTTGGCTACTATCTGTCCAATTGTTATGGCTTTGAGT
GCTGCATCTCCCTTTTACCGAGGCTATGTGTCAGACATTGATTGTCGCTGGGGAGTGATT
TCTGCATCTGTAGATGATAGAACTCGGGAGGAGCGAGGACTGGAGCCATTGAAGAACAAT
AACTATAGGATCAGTAAATCCCGATATGACTCAATAGACAGCTATTTATCTAAGTGTGGT
GAGAAATATAATGACATCGACTTGACGATAGATAAAGAGATCTACGAACAGCTGTTGCAG
GAAGGCATTGATCATCTCCTGGCCCAGCATGTTGCTCATCTCTTTATTAGAGACCCACTG
ACACTGTTTGAAGAGAAAATACACCTGGATGATGCTAATGAGTCTGACCATTTTGAGAAT
ATTCAGTCCACAAATTGGCAGACAATGAGATTTAAGCCCCCTCCTCCAAACTCAGACATT
GGATGGAGAGTAGAATTTCGACCCATGGAGGTGCAATTAACAGACTTTGAGAACTCTGCC
TATGTGGTGTTTGTGGTACTGCTCACCAGAGTGATCCTTTCCTACAAATTGGATTTTCTC
ATTCCACTGTCAAAGGTTGATGAGAACATGAAGGTAGCACAGAAAAGAGATGCTGTCTTG
CAGGGAATGTTTTATTTCAGGAAAGATATTTGCAAAGGTGGCAATGCAGTGGTGGATGGT
TGTGGCAAGGCCCAGAACAGCACGGAGCTCGCTGCAGAGGAGTACACCCTCATGAGCATA
GACACCATCATCAATGGGAAGGAAGGTGTGTTTCCTGGACTGATCCCAATTCTGAACTCT
TACCTTGAAAACATGGAAGTGGATGTGGACACCAGATGTAGTATTCTGAACTACCTAAAG
CTAATTAAGAAGAGAGCATCTGGAGAACTAATGACAGTTGCCAGATGGATGAGGGAGTTT
ATCGCAAACCATCCTGACTACAAGCAAGACAGTGTCATAACTGATGAAATGAATTATAGC
CTTATTTTGAAGTGTAACCAAATTGCAAATGAATTATGTGAATGCCCAGAGTTACTTGGA
TCAGCATTTAGGAAAGTAAAATATAGTGGAAGTAAAACTGACTCATCCAACTAG

1. Gipp JJ, Chang C, Mulcahy RT: Cloning and nucleotide sequence of a full-length cDNA for human liver gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 1992 May 29;185(1):29-35. [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. Mulcahy RT, Gipp JJ: Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun. 1995 Apr 6;209(1):227-33. [PubMed ]
4. Beutler E, Gelbart T, Kondo T, Matsunaga AT: The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood. 1999 Oct 15;94(8):2890-4. [PubMed ]
5. Ristoff E, Augustson C, Geissler J, de Rijk T, Carlsson K, Luo JL, Andersson K, Weening RS, van Zwieten R, Larsson A, Roos D: A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia. Blood. 2000 Apr 1;95(7):2193-6. [PubMed ]

1. Gamma- glutamylcysteine synthetase
2. Gamma-ECS
3. GCS light chain
4. Glutamate--cysteine ligase modifier subunit

MGTDSRAAKALLARARTLHLQTGNLLNWGRLRKKCPSTHSEELHDCIQKTLNEWSSQINP
DLVREFPDVLECTVSHAVEKINPDEREEMKVSAKLFIVESNSSSSTRSAVDMACSVLGVA
QLDSVIIASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQ
VKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIQAH
EWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS

• Glutamate Metabolism (map00251 )
• Glutathione Metabolism (map00480 )

• ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine

• None

• None

ATGGGCACCGACAGCCGCGCGGCCAAGGCGCTCCTGGCGCGGGCCCGCACCCTGCACCTG
CAGACGGGGAACCTGCTGAACTGGGGCCGCCTGCGGAAGAAGTGCCCGTCCACGCACAGC
GAGGAGCTTCATGATTGTATCCAAAAAACCTTGAATGAATGGAGTTCCCAAATCAACCCA
GATTTGGTCAGGGAGTTTCCAGATGTCTTGGAATGCACTGTATCTCATGCAGTAGAAAAG
ATAAATCCTGATGAAAGAGAAGAAATGAAAGTTTCTGCAAAACTGTTCATTGTAGAATCA
AACTCTTCATCATCAACTAGAAGTGCAGTTGACATGGCCTGTTCAGTCCTTGGAGTTGCA
CAGCTGGATTCTGTGATCATTGCTTCACCTCCTATTGAAGATGGAGTTAATCTTTCCTTG
GAGCATTTACAGCCTTACTGGGAGGAATTAGAAAACTTAGTTCAGAGCAAAAAGATTGTT
GCCATAGGTACCTCTGATCTAGACAAAACACAGTTGGAACAGCTGTATCAGTGGGCACAG
GTAAAACCAAATAGTAACCAAGTTAATCTTGCCTCCTGCTGTGTGATGCCACCAGATTTG
ACTGCATTTGCTAAACAATTTGACATACAGCTGTTGACTCACAATGATCCAAAAGAACTG
CTTTCTGAAGCAAGTTTCCAAGAAGCTCTTCAGGAAAGCATTCCTGACATTCAAGCGCAC
GAGTGGGTGCCGCTGTGGCTACTGCGGTATTCGGTCATTGTGAAAAGTAGAGGAATTATC
AAATCAAAAGGCTACATTTTACAAGCTAAAAGAAGGGGTTCTTAA

1. Gipp JJ, Bailey HH, Mulcahy RT: Cloning and sequencing of the cDNA for the light subunit of human liver gamma-glutamylcysteine synthetase and relative mRNA levels for heavy and light subunits in human normal tissues. Biochem Biophys Res Commun. 1995 Jan 17;206(2):584-9. [PubMed ]

1. Gamma-cystathionase

MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEY
SRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRY
FRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHG
DIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQ
NSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQH
ELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVL
KNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS

• Cysteine Metabolism (map00272 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Methionine Metabolism (map00271 )
• Nitrogen Metabolism (map00910 )
• Selenoamino Acid Metabolism (map00450 )

• L-cystathionine + H2O = L-cysteine + ammonia + 2-oxobutanoate

• Cys_Met_Meta_PP (PF01053 )

• None

• None

ATGCAGGAAAAAGACGCCTCCTCACAAGGTTTCCTGCCACACTTCCAACATTTCGCCACG
CAGGCGATCCATGTGGGCCAGGATCCGGAGCAATGGACCTCCAGGGCTGTAGTGCCCCCC
ATCTCACTGTCCACCACGTTCAAGCAAGGGGCGCCTGGCCAGCACTCGGGTTTTGAATAT
AGCCGTTCTGGAAATCCCACTAGGAATTGCCTTGAAAAAGCAGTGGCAGCACTGGATGGG
GCTAAGTACTGTTTGGCCTTTGCTTCAGGTTTAGCAGCCACTGTAACTATTACCCATCTT
TTAAAAGCAGGAGACCAAATTATTTGTATGGATGATGTGTATGGAGGTACAAACAGGTAC
TTCAGGCAAGTGGCATCTGAATTTGGATTAAAGATTTCTTTTGTTGATTGTTCCAAAATC
AAATTACTAGAGGCAGCAATTACACCAGAAACCAAGCTTGTTTGGATCGAAACCCCCACA
AACCCCACCCAGAAGGTGATTGACATTGAAGGCTGTGCACATATTGTCCATAAGCATGGA
GACATTATTTTGGTCGTGGATAACACTTTTATGTCACCATATTTCCAGCGCCCTTTGGCT
CTGGGAGCTGATATTTCTATGTATTCTGCAACAAAATACATGAATGGCCACAGTGATGTT
GTAATGGGCCTGGTGTCTGTTAATTGTGAAAGCCTTCATAATAGACTTCGTTTCTTGCAA
AACTCTCTTGGAGCAGTTCCATCTCCTATTGATTGTTACCTCTGCAATCGAGGTCTGAAG
ACTCTACATGTCCGAATGGAAAAGCATTTCAAAAACGGAATGGCAGTTGCCCAGTTCCTG
GAATCTAATCCTTGGGTAGAAAAGGTTATTTATCCTGGGCTGCCCTCTCATCCACAGCAT
GAGTTGGTGAAGCGTCAGTGTACAGGTTGTACAGGGATGGTCACCTTTTATATTAAGGGC
ACTCTTCAGCATGCTGAGATTTTCCTCAAGAACCTAAAGCTATTTACTCTGGCCGAGAGC
TTGGGAGGATTCGAAAGCCTTGCTGAGCTTCCGGCAATCATGACTCATGCATCAGTTCTT
AAGAATGACAGAGATGTCCTTGGAATTAGTGACACACTGATTCGACTTTCTGTGGGCTTA
GAGGATGAGGAAGACCTACTGGAAGATCTAGATCAAGCTTTGAAGGCAGCACACCCTCCA
AGTGGAATTCACAGCTAG

1. Lu Y, O'Dowd BF, Orrego H, Israel Y: Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase. Biochem Biophys Res Commun. 1992 Dec 15;189(2):749-58. [PubMed ]
2. Wang J, Hegele RA: Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH). Hum Genet. 2003 Apr;112(4):404-8. Epub 2003 Feb 6. [PubMed ]

1. QC
2. Glutaminyl-tRNA cyclotransferase
3. Glutaminyl cyclase

MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGT
SISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSF
SNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLS
LKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHG
MDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYG
GVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLH
L

• L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3

• Peptidase_M28 (PF04389 )

• 1-28

ATGGCAGGCGGAAGACACCGGCGCGTCGTGGGCACCCTCCACCTGCTGCTGCTGGTGGCC
GCCCTGCCCTGGGCATCCAGGGGGGTCAGTCCGAGTGCCTCAGCCTGGCCAGAGGAGAAG
AATTACCACCAGCCAGCCATTTTGAATTCATCGGCTCTTCGGCAAATTGCAGAAGGCACC
AGTATCTCTGAAATGTGGCAAAATGACTTACAGCCATTGCTGATAGAGCGATACCCGGGA
TCCCCTGGAAGCTATGCTGCTCGTCAGCACATCATGCAGCGAATTCAGAGGCTTCAGGCT
GACTGGGTCTTGGAAATAGACACCTTCTTGAGTCAGACACCCTATGGGTACCGGTCTTTC
TCAAATATCATCAGCACCCTCAATCCCACTGCTAAACGACATTTGGTCCTCGCCTGCCAC
TATGACTCCAAGTATTTTTCCCACTGGAACAACAGAGTGTTTGTAGGAGCCACTGATTCA
GCCGTGCCATGTGCAATGATGTTGGAACTTGCTCGTGCCTTAGACAAGAAACTCCTTTCC
TTAAAGACTGTTTCAGACTCCAAGCCAGATTTGTCACTCCAGCTGATCTTCTTTGATGGT
GAAGAGGCTTTTCTTCACTGGTCTCCTCAAGATTCTCTCTATGGGTCTCGACACTTAGCT
GCAAAGATGGCATCGACCCCGCACCCACCTGGAGCGAGAGGCACCAGCCAACTGCATGGC
ATGGATTTATTGGTCTTATTGGATTTGATTGGAGCTCCAAACCCAACGTTTCCCAATTTT
TTTCCAAACTCAGCCAGGTGGTTCGAAAGACTTCAAGCAATTGAACATGAACTTCATGAA
TTGGGTTTGCTCAAGGATCACTCTTTGGAGGGGCGGTATTTCCAGAATTACAGTTATGGA
GGTGTGATTCAGGATGACCATATTCCATTTTTAAGAAGAGGTGTTCCAGTTCTGCATCTG
ATACCGTCTCCTTTCCCTGAAGTCTGGCACACCATGGATGACAATGAAGAAAATTTGGAT
GAATCAACCATTGACAATCTAAACAAAATCCTACAAGTCTTTGTGTTGGAATATCTTCAT
TTGTAA

1. Song I, Chuang CZ, Bateman RC Jr: Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase. J Mol Endocrinol. 1994 Aug;13(1):77-86. [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. Glutathione synthase
2. GSH synthetase
3. GSH-S

MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSA
LLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVF
LGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKIL
SNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFE
DISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQ
LAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSR
FVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVV
QCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV

• Glutamate Metabolism (map00251 )
• Glutathione Metabolism (map00480 )

• ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione

• GSH_synth_ATP (PF03917 )
• GSH_synthase (PF03199 )

• None

• None

ATGGCCACCAACTGGGGGAGCCTCTTGCAGGATAAACAGCAGCTAGAGGAGCTGGCACGG
CAGGCCGTGGACCGGGCCCTGGCTGAGGGAGTATTGCTGAGGACCTCACAGGAGCCCACT
TCCTCGGAGGTGGTGAGCTATGCCCCATTCACGCTCTTCCCCTCACTGGTCCCCAGTGCC
CTGCTGGAGCAAGCCTATGCTGTGCAGATGGACTTCAACCTGCTAGTGGATGCTGTCAGC
CAGAACGCTGCCTTCCTGGAGCAAACTCTTTCCAGCACCATCAAACAGGATGACTTTACC
GCTCGTCTCTTTGACATCCACAAGCAAGTCCTAAAAGAGGGCATTGCCCAGACTGTGTTC
CTGGGCCTGAATCGCTCAGACTACATGTTCCAGCGCAGCGCAGATGGCTCCCCAGCCCTG
AAACAGATCGAAATCAACACCATCTCTGCCAGCTTTGGGGGCCTGGCCTCCCGGACCCCA
GCTGTGCACCGACATGTTCTCAGTGTCCTGAGTAAGACCAAAGAAGCTGGCAAGATCCTC
TCTAATAATCCCAGCAAGGGACTGGCCCTGGGAATTGCCAAAGCCTGGGAGCTCTACGGC
TCACCCAATGCTCTGGTGCTACTGATTGCTCAAGAGAAGGAAAGAAACATATTTGACCAG
CGTGCCATAGAGAATGAGCTACTGGCCAGGAACATCCATGTGATCCGACGAACATTTGAA
GATATCTCTGAAAAGGGGTCTCTGGACCAAGACCGAAGGCTGTTTGTGGATGGCCAGGAA
ATTGCTGTGGTTTACTTCCGGGATGGCTACATGCCTCGTCAGTACAGTCTACAGAATTGG
GAAGCACGTCTACTGCTGGAGAGGTCACATGCTGCCAAGTGCCCAGACATTGCCACCCAG
CTGGCTGGGACTAAGAAGGTGCAGCAGGAGCTAAGCAGGCCGGGCATGCTGGAGATGTTG
CTCCCTGGCCAGCCTGAGGCTGTGGCCCGCCTCCGCGCCACCTTTGCTGGCCTCTACTCA
CTGGATGTGGGTGAAGAAGGGGACCAGGCCATCGCCGAGGCCCTTGCTGCCCCTAGCCGG
TTTGTGCTAAAGCCCCAGAGAGAGGGTGGAGGTAACAACCTATATGGGGAGGAAATGGTA
CAGGCCCTGAAACAGCTGAAGGACAGTGAGGAGAGGGCCTCCTACATCCTCATGGAGAAG
ATCGAACCTGAGCCTTTTGAGAATTGCCTGCTACGGCCTGGCAGCCCTGCCCGAGTGGTC
CAGTGCATTTCAGAGCTGGGCATCTTTGGGGTCTATGTCAGGCAGGAAAAGACACTCGTG
ATGAACAAGCACGTGGGGCATCTACTTCGAACCAAAGCCATCGAGCATGCAGATGGTGGT
GTGGCAGCGGGAGTGGCAGTCCTGGACAACCCATACCCTGTGTGA

1. Gali RR, Board PG: Sequencing and expression of a cDNA for human glutathione synthetase. Biochem J. 1995 Aug 15;310 ( Pt 1):353-8. [PubMed ]
2. 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 ]
3. Shi ZZ, Habib GM, Rhead WJ, Gahl WA, He X, Sazer S, Lieberman MW: Mutations in the glutathione synthetase gene cause 5-oxoprolinuria. Nat Genet. 1996 Nov;14(3):361-5. [PubMed ]
4. Dahl N, Pigg M, Ristoff E, Gali R, Carlsson B, Mannervik B, Larsson A, Board P: Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Hum Mol Genet. 1997 Jul;6(7):1147-52. [PubMed ]

1. Leucine aminopeptidase
2. LAP
3. Leucyl aminopeptidase
4. Leucine aminopeptidase 3
5. Proline aminopeptidase
6. Prolyl aminopeptidase
7. Peptidase S

MFLLPLPAAGRVVVRRLAVRRFGSRSLSTADMTKGLVLGIYSKEKEDDVPQFTSAGENFD
KLLAGKLRETLNISGPPLKAGKTRTFYGLHQDFPSVVLVGLGKKAAGIDEQENWHEGKEN
IRAAVAAGCRQIQDLELSSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKMAVSAKLYGS
GDQEAWQKGVLFASGQNLARQLMETPANEMTPTRFAEIIEKNLKSASSKTEVHIRPKSWI
EEQAMGSFLSVAKGSDEPPVFLEIHYKGSPNANEPPLVFVGKGITFDSGGISIKASANMD
LMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRAKNGKTIQV
DNTDAEGRLILADALCYAHTFNPKVILNAATLTGAMDVALGSGATGVFTNSSWLWNKLFE
ASIETGDRVWRMPLFEHYTRQVVDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHL
DIAGVMTNKDEVPYLRKGMTGRPTRTLIEFLLRFSQDNA

• Arginine and Proline Metabolism (map00330 )

• Release of N-terminal proline from a peptide

• Peptidase_M17 (PF00883 )
• Peptidase_M17_N (PF02789 )

• 1-18

ATGTTCTTGCTGCCTCTTCCGGCTGCGGGGCGAGTAGTCGTCCGACGTCTGGCCGTAGTA
CGTTCTGGGAGCCGGAGTCTCTCCACCGCAGACATGACGAAGGGCCTTGTTTTAGGAATC
TATTCCAAAGAAAAAGAAGATGATGTGCCACAGTTCACAAGTGCAGGAGAGAATTTTGAT
AAATTGTTAGCTGGAAAGCTGAGAGAGACTTTGAACATATCTGGACCACCTCTGAAGGCA
GGGAAGACTCGAACCTTTTATGGTCTGCATCAGGACTTCCCCAGCGTGGTGCTAGTTGGC
CTCGGCAAAAAGGCAGCTGGAATCGACGAACAGGAAAACTGGCATGAAGGCAAAGAAAAC
ATCAGAGCTGCTGTTGCAGCGGGGTGCAGGCAGATTCAAGACCTGGAGCTCTCGTCTGTG
GAGGTGGATCCCTGTGGAGACGCTCAGGCTGCTGCGGAGGGAGCGGTGCTTGGTCTCTAT
GAATACGATGACCTAAAGCAAAAAAAGAAGATGGCTGTGTCGGCAAAGCTCTATGGAAGT
GGGGATCAGGAGGCCTGGCAGAAAGGAGTCCTGTTTGCTTCTGGGCAGAACTTGGCACGC
CAATTGATGGAGACGCCAGCCAATGAGATGACGCCAACCAGATTTGCCGAAATTATTGAG
AAGAATCTCAAAAGTGCTAGTAGTAAAACCGAGGTCCATATCAGACCCAAGTCTTGGATT
GAGGAACAGGCAATGGGATCATTCCTCAGTGTGGCCAAAGGATCTGACGAGCCCCCAGTC
TTCTTGGAAATTCACTACAAAGGCAGCCCCAATGCAAACGAACCACCCCTGGTGTTTGTT
GGGAAAGGAATTACCTTTGACAGTGGTGGTATCTCCATCAAGGCTTCTGCAAATATGGAC
CTCATGAGGGCTGACATGGGAGGAGCTGCAACTATATGCTCAGCCATCGTGTCTGCTGCA
AAGTTAAATTTGCCCATTAATATTATAGGTCTGGCCCCTCTTTGTGAAAATATGCCCAGC
GGCAAGGCCAACAAGCCGGGGGATGTTGTTAGAGCCAAAAACGGGAAGACCATCCAGGTT
GATAACACTGATGCTGAGGGGAGGCTCATACTGGCTGATGCGCTCTGTTACGCACACACG
TTTAACCCGAAGGTCATCCTCAATGCCGCCACCTTAACAGGTGCCATGGATGTAGCTTTG
GGATCAGGTGCCACTGGGGTCTTTACCAATTCATCCTGGCTCTGGAACAAACTCTTCGAG
GCCAGCATTGAAACAGGGGACCGTGTCTGGAGGATGCCTCTCTTCGAACATTATACAAGA
CAGGTTGTAGATTGCCAGCTTGCTGATGTTAACAACATTGGAAAATACAGATCTGCAGGA
GCATGTACAGCTGCAGCATTCCTGAAAGAATTCGTAACTCATCCTAAGTGGGCACATTTA
GACATAGCAGGCGTGATGACCAACAAAGATGAAGTTCCCTATCTACGGAAAGGCATGACT
GGGAGGCCCACAAGGACTCTCATTGAGTTCTTACTTCGTTTCAGTCAAGACAATGCTTAG

1. Matsushima M, Takahashi T, Ichinose M, Miki K, Kurokawa K, Takahashi K: Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1459-64. [PubMed ]

1. Sulfinoalanine decarboxylase
2. Cysteine-sulfinate decarboxylase

MADSEALPSLAGDPVAVEALLRAVFGVVVDEAIQKGTSVSQKVCEWKEPEELKQLLDLEL
RSQGESQKQILERCRAVIRYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEI
APVFVLMEEEVLRKLRALVGWSSGDGIFCPGGSISNMYAVNLARYQRYPDCKQRGLRTLP
PLALFTSKECHYSIQKGAAFLGLGTDSVRVVKADERGKMVPEDLERQIGMAEAEGAVPFL
VSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVA
WNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKFYDVALDTGDKVVQCGRRV
DCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFVPPS
LRGKQESPDYHERLSKVAPVLKERMVKEGSMMIGYQPHGTRGNFFRVVVANSALTCADMD
FLLNELERLGQDL

• Taurine and Hypotaurine Metabolism (map00430 )

• 3-sulfino-L-alanine = hypotaurine + CO2

• Pyridoxal_deC (PF00282 )

• None

• None

ATGGCTGACTCAGAAGCACTCCCCTCCCTTGCTGGGGACCCAGTGGCTGTGGAAGCCTTG
CTCCGGGCCGTGTTTGGGGTTGTTGTGGATGAGGCCATTCAGAAAGGAACCAGTGTCTCC
CAGAAGTGTCACTACTCCATCCAGAAGGGAGCTGCGTTTCTGGGACTTGGCACCGACAGT
GTCCGAGTGGTCAAGGCTGATGAGAGAGGGAAAATGGTCCCCGAGGATCTGGAGAGGCAG
ATTGGTATGGCCGAGGCTGAGGGTGCTGTGCCGTTCCTGGTCAGTGCCACCTCTGGCACC
ACTGTGCTAGGGGCCTTTGACCCCCTGGAGGCAATTGCTGATGTGTGCCAGCGTCATGGG
CTATGGCTGCATGTGGATGCTGCCTGGGGTGGGAGCGTCCTGCTGTCACAGACACACAGG
CATCTCCTGGATGGGATCCAGAGGGCTGACTCTGTGGCCTGGAATCCCCACAAGCTCCTC
GCAGCAGGCCTGCAATGCTCTGCACTTCTTCTCCAGGATACCTCGAACCTGCTCAAGCGC
TGCCATGGGTCCCAGGCCAGCTACCTTTTCCAGCAGGACAAGTTCTACGATGTGGCTCTG
GACACGGGAGACAAGGTGGTGCAGTGTGGCCGCCGTGTGGACTGTCTGAAGCTGTGGCTC
ATGTGGAAGGCACAGGGCGATCAAGGGCTGGAGCGGCGCATCGACCAGGCCTTTGTCCTT
GCCCGGTACCTGGTGGAGGAAATGAAGAAGCGGGAAGGGTTTGAGCTAGTCATGGAGCCT
GAGTTTGTCAATGTGTGTTTCTGGTTCGTACCCCCCAGCCTGCGAGGGAAGCAGGAGAGT
CCAGATTACCACGAAGGGCTGTCAAAGGTGGCCCCCGTGCTCAAGGAGCGCATGGTGAAG
GAGGGCTCCATGATGATTGGCTACCAGCCCCACGGGACCCGGGGCAACTTCTTCCGTGTG
GTTGTGGCCAACTCTGCACTGACCTGTGCTGATATGGACTTCCTCCTCAACGAGCTGGAG
CGGCTAGGCCAGGACCTGTGA

1. Cysteine dioxygenase type I
2. CDO
3. CDO-I

MEQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPTEWAMYAKFDQYRYTR
NLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKK
SERVLRENQCAYINDSIGLHRVENISHTEPAVSLHLYSPPFDTCHAFDQRTGHKNKVTMT
FHSKFGIRTPNATSGSLENN

• Cysteine Metabolism (map00272 )
• Taurine and Hypotaurine Metabolism (map00430 )

• L-cysteine + O2 = 3-sulfinoalanine

• CDO_I (PF05995 )

• None

• None

ATGGAACAGACCGAAGTGCTGAAGCCACGGACCCTGGCTGATCTGATCCGCATCCTGCAC
CAGCTCTTTGCCGGCGATGAGGTCAATGTAGAGGAGGTGCAGGCCATCATGGAAGCCTAC
GAGAGCGACCCCATCGAGTGGGCAATGTACGCCAAGTTCGACCAGTACAGGTATACCCGA
AATCTTGTGGATCAAGGAAATGGAAAATTTAATCTGATGATTCTCTGTTGGGGTGAAGGA
CATGGCAGCAGTATTCATGATCATACCAACTCCCACTGCTTTCTGAAGATGCTACAGGGA
AATCTAAAGGAGACATTATTTGCCTGGCCTGACAAAAAATCCAATGAGATGGTCAAGAAG
TCTGAAAGAGTCTTGAGGGAAAACCAGTGTGCCTACATCAATGATTCCATTGGCTTACAT
CGAGTAGAGAACATCAGCCATACGGAACCTGCTGTGAGCCTTCACTTGTACAGTCCACCT
TTTGATACATGCCATGCCTTTGATCAAAGAACAGGACATAAAAACAAAGTCACAATGACA
TTCCATAGTAAATTTGGAATCAGAACTCCAAATGCAACTTCGGGCTCGCTGGAGAACAAC
TAA

1. McCann KP, Akbari MT, Williams AC, Ramsden DB: Human cysteine dioxygenase type I: primary structure derived from base sequencing of cDNA. Biochim Biophys Acta. 1994 Nov 16;1209(1):107-10. [PubMed ]
2. Ramsden DB, Kapadi A, Fitch NJ, Farmer MJ, Bennett P, Williams AC: Human cysteine dioxygenase type I (CDO-I; EC 1.13.11.20): 5' flanking region and intron-exon structure of the gene. Mol Pathol. 1997 Oct;50(5):269-71. [PubMed ]

1. 6-O- methylguanine-DNA methyltransferase
2. MGMT
3. O-6-methylguanine-DNA- alkyltransferase

MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPAAVLGGPEPLM
QCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYQQLAAL
AGNPKAARAVGGAMRGNPVPILIPCHRVVCSSGAVGNYSGGLAVKEWLLAHEGHRLGKPG
LGGSSGLAGAWLKGAGATSGSPPAGRN

• DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine

• DNA_binding_1 (PF01035 )
• Methyltransf_1N (PF02870 )

• None

• None

ATGGACAAGGATTGTGAAATGAAACGCACCACACTGGACAGCCCTTTGGGGAAGCTGGAG
CTGTCTGGTTGTGAGCAGGGTCTGCACGAAATAAAGCTCCTGGGCAAGGGGACGTCTGCA
GCTGATGCCGTGGAGGTCCCAGCCCCCGCTGCGGTTCTCGGAGGTCCGGAGCCCCTGATG
CAGTGCACAGCCTGGCTGAATGCCTATTTCCACCAGCCCGAGGCTATCGAAGAGTTCCCC
GTGCCGGCACTTCACCATCCCGTTTTCCAGCAAGAGTCGTTCACCAGACAGGTGTTATGG
AAGCTGCTGAAGGTTGTGAAATTCGGAGAAGTGATTTCTTACCAGCAATTAGCAGCCCTG
GCAGGCAACCCCAAAGCCGCGCGAGCAGTGGGAGGAGCAATGAGAGGCAATCCTGTCCCC
ATCCTCATCCCGTGCCACAGAGTGGTCTGCAGCAGCGGAGCCGTGGGCAACTACTCCGGA
GGACTGGCCGTGAAGGAATGGCTTCTGGCCCATGAAGGCCACCGGTTGGGGAAGCCAGGC
TTGGGAGGGAGCTCAGGTCTGGCAGGGGCCTGGCTCAAGGGAGCGGGAGCTACCTCGGGC
TCCCCGCCTGCTGGCCGAAACTGA

1. Tano K, Shiota S, Collier J, Foote RS, Mitra S: Isolation and structural characterization of a cDNA clone encoding the human DNA repair protein for O6-alkylguanine. Proc Natl Acad Sci U S A. 1990 Jan;87(2):686-90. [PubMed ]
2. Rydberg B, Spurr N, Karran P: cDNA cloning and chromosomal assignment of the human O6-methylguanine-DNA methyltransferase. cDNA expression in Escherichia coli and gene expression in human cells. J Biol Chem. 1990 Jun 5;265(16):9563-9. [PubMed ]
3. Koike G, Maki H, Takeya H, Hayakawa H, Sekiguchi M: Purification, structure, and biochemical properties of human O6-methylguanine-DNA methyltransferase. J Biol Chem. 1990 Sep 5;265(25):14754-62. [PubMed ]
4. Hayakawa H, Koike G, Sekiguchi M: Expression and cloning of complementary DNA for a human enzyme that repairs O6-methylguanine in DNA. J Mol Biol. 1990 Jun 20;213(4):739-47. [PubMed ]
5. von Wronski MA, Shiota S, Tano K, Mitra S, Bigner DD, Brent TP: Structural and immunological comparison of indigenous human O6-methylguanine-DNA methyltransferase with that encoded by a cloned cDNA. J Biol Chem. 1991 Jan 15;266(2):1064-70. [PubMed ]
6. Liem LK, Lim A, Li BF: Specificities of human, rat and E. coli O6-methylguanine-DNA methyltransferases towards the repair of O6-methyl and O6-ethylguanine in DNA. Nucleic Acids Res. 1994 May 11;22(9):1613-9. [PubMed ]

1. L-type amino acid transporter 2
2. hLAT2

MEEGARHRNNTEKKHPGGGESDASPEAGSGGGGVALKKEIGLVSACGIIVGNIIGSGIFV
SPKGVLENAGSVGLALIVWIVTGFITVVGALCYAELGVTIPKSGGDYSYVKDIFGGLAGF
LRLWIAVLVIYPTNQAVIALTFSNYVLQPLFPTCFPPESGLRLLAAICLLLLTWVNCSSV
RWATRVQDIFTAGKLLALALIIIMGIVQICKGEYFWLEPKNAFENFQEPDIGLVALAFLQ
GSFAYGGWNFLNYVTEELVDPYKNLPRAIFISIPLVTFVYVFANVAYVTAMSPQELLASN
AVAVTFGEKLLGVMAWIMPISVALSTFGGVNGSLFTSSRLFFAGAREGHLPSVLAMIHVK
RCTPIPALLFTCISTLLMLVTSDMYTLINYVGFINYLFYGVTVAGQIVLRWKKPDIPRPI
KINLLFPIIYLLFWAFLLVFSLWSEPVVCGIGLAIMLTGVPVYFLGVYWQHKPKCFSDFI
ELLTLVSQKMCVVVYPEVERGSGTEEANEDMEEQQQPMYQPTPTKDKDVAGQPQP

• AA_permease (PF00324 )

• None

• 40-60 72-92 113-133 155-175 189-209 231-251 268-288 310-330 362-382 388-408 424-444 447-467

ATGGAAGAAGGAGCCAGGCACCGAAACAACACCGAAAAGAAACACCCAGGTGGGGGCGAG
TCGGACGCCAGCCCCGAGGCTGGTTCCGGAGGGGGCGGAGTAGCCCTGAAGAAAGAGATC
GGATTGGTCAGTGCCTGTGGTATCATCGTAGGGAACATCATCGGCTCTGGAATCTTTGTC
TCGCCAAAGGGAGTGCTGGAGAATGCTGGTTCTGTGGGCCTTGCTCTCATCGTCTGGATT
GTGACGGGCTTCATCACAGTTGTGGGAGCCCTCTGCTATGCTGAACTCGGGGTCACCATC
CCCAAATCTGGAGGTGACTACTCCTATGTCAAGGACATCTTCGGAGGACTGGCTGGGTTC
CTGAGGCTGTGGATTGCTGTGCTGGTGATCTACCCCACCAACCAGGCTGTCATCGCCCTC
ACCTTCTCCAACTACGTGCTGCAGCCGCTCTTCCCCACCTGCTTCCCCCCAGAGTCTGGC
CTTCGGCTCCTGGCTGCCATCTGCTTATTGCTCCTCACATGGGTCAACTGTTCCAGTGTG
CGGTGGGCCACCCGGGTTCAAGACATCTTCACAGCTGGGAAGCTCCTGGCCTTGGCCCTG
ATTATCATCATGGGGATTGTACAGATATGCAAAGGAGAGTACTTCTGGCTGGAGCCAAAG
AATGCATTTGAGAATTTCCAGGAACCTGACATCGGCCTCGTCGCACTGGCTTTCCTTCAG
GGCTCCTTTGCCTATGGAGGCTGGAACTTTCTGAATTACGTGACTGAGGAGCTTGTTGAT
CCCTACAAGAACCTTCCCAGAGCCATCTTCATCTCCATCCCACTGGTCACATTTGTGTAT
GTCTTTGCCAATGTCGCTTATGTCACTGCAATGTCCCCCCAGGAGCTGCTGGCATCCAAC
GCCGTCGCTGTGACTTTTGGAGAGAAGCTCCTAGGAGTCATGGCCTGGATCATGCCCATT
TCTGTTGCCCTGTCCACATTTGGAGGAGTTAATGGGTCTCTCTTCACCTCCTCTCGGCTG
TTCTTCGCTGGAGCCCGAGAGGGCCACCTTCCCAGTGTGTTGGCCATGATCCACGTGAAG
CGCTGCACCCCAATCCCAGCCCTGCTCTTCACATGCATCTCCACCCTGCTGATGCTGGTC
ACCAGCGACATGTACACACTCATCAACTACGTGGGCTTCATCAACTACCTCTTCTATGGG
GTCACGGTTGCTGGACAGATAGTCCTTCGCTGGAAGAAGCCTGATATCCCCCGCCCCATC
AAGATCAACCTGCTGTTCCCCATCATCTACTTGCTGTTCTGGGCCTTCCTGCTGGTCTTC
AGCCTGTGGTCAGAGCCGGTGGTGTGTGGCATTGGCCTGGCCATCATGCTGACAGGAGTG
CCTGTCTATTTCCTGGGTGTTTACTGGCAACACAAGCCCAAGTGTTTCAGTGACTTCATT
GAGCTGCTAACCCTGGTGAGCCAGAAGATGTGTGTGGTCGTGTACCCCGAGGTGGAGCGG
GGCTCAGGGACAGAGGAGGCTAATGAGGACATGGAGGAGCAGCAGCAGCCCATGTACCAA
CCCACTCCCACGAAGGACAAGGACGTGGCGGGGCAGCCCCAGCCCTGA

1. Rossier G, Meier C, Bauch C, Summa V, Sordat B, Verrey F, Kuhn LC: LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine. J Biol Chem. 1999 Dec 3;274(49):34948-54. [PubMed ]
2. Borsani G, Bassi MT, Sperandeo MP, De Grandi A, Buoninconti A, Riboni M, Manzoni M, Incerti B, Pepe A, Andria G, Ballabio A, Sebastio G: SLC7A7, encoding a putative permease-related protein, is mutated in patients with lysinuric protein intolerance. Nat Genet. 1999 Mar;21(3):297-301. [PubMed ]
3. Pineda M, Fernandez E, Torrents D, Estevez R, Lopez C, Camps M, Lloberas J, Zorzano A, Palacin M: Identification of a membrane protein, LAT-2, that Co-expresses with 4F2 heavy chain, an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids. J Biol Chem. 1999 Jul 9;274(28):19738-44. [PubMed ]

MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLY
MDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPRE
IIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQK
SGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKI
PLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPL
VVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAY
VEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD
YTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH

• L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine

• Aminotran_5 (PF00266 )

• 1-23

ATGCTGCTCCGAGTCGCTTGGAGGCGGGCGGCAGTGGCGGTGACAGCGGCTCCAGGGCCG
AAGCCCGCGGCGCCCACTCGGGGGCTGCGCCTGCGCGTTGGAGACCGTGCTCCTCAGTCT
GCGGTTCCCGCAGATACAACCGCTGCCCCGGAGGTGGGGCCAGTGCTGCGACCTCTCTAT
ATGGATGTGCAAGCTACAACTCCTCTGGACCCCCGGGTGCTTGATGCCATGCTCCCTTAC
CTAATCAACTACTATGGGAACCCACACTCCCGGACACATGCTTATGGCTGGGAGAGTGAG
GCAGCCATGGAACGTGCTCGTCAGCAAGTAGCATCTCTGATTGGAGCTGATCCTCGTGAG
ATCATTTTTACTAGTGGTGCTACTGAATCCAACAACATAGCAATTAAGGGGGTGGCCCGA
TTCTACAGGTCACGGAAAAAGCACTTGATCACCACCCAGACAGAACACAAATGTGTCTTG
GACTCCTGCCGTTCACTGGAAGCTGAGGGCTTTCAGGTCACCTACCTCCCAGTGCAGAAG
AGTGGGATCATTGACCTAAAGGAACTAGAGGCTGCTATCCAGCCAGATACTAGCCTGGTG
TCAGTCATGACTGTGAACAATGAGATTGGAGTGAAGCAGCCTATTGCAGAAATAGGGCGG
ATTTGCAGTTCCAGAAAGGTATATTTCCATACTGATGCAGCCCAGGCTGTTGGAAAAATC
CCACTTGATGTCAATGACATGAAAATTGATCTCATGAGCATTAGTGGTCACAAAATCTAC
GGTCCCAAAGGGGTTGGTGCCATCTACATCCGTCGCCGGCCCCGTGTGCGTGTGGAGGCC
CTGCAGAGTGGAGGGGGGCAGGAGCGGGGTATGCGGTCTGGGACAGTGCCCACACCCTTA
GTGGTGGGGTTGGGGGCTGCGTGTGAGGTGGCACAGCAAGAGATGGAGTATGACCACAAG
CGAATCTCAAAGTTGTCAGAGCGGCTGATACAGAATATAATGAAGAGCCTTCCAGATGTG
GTGATGAATGGGGACCCTAAGCACCATTATCCCGGCTGTATCAACCTCTCCTTTGCATAT
GTGGAAGGGGAAAGTCTGCTGATGGCACTGAAGGACGTTGCCTTATCCTCAGGGAGTGCC
TGCACCTCTGCATCCCTGGAGCCCTCTTATGTGCTTAGAGCAATTGGCACTGATGAGGAT
TTAGCGCACTCTTCTATCAGGTTTGGAATTGGCGCTTTCACTACAGAGGAGGAAGTGGAC
TACACAGTGGAGAAATGCATTCAGCATGTGAATCGTCTTCGAGAAATGAGCCCTCTCTGG
GAGATGGTTCAGGATGGCATTGACCTCAAGAGCATCAAGTGGACCCAACACTAG

1. Land T, Rouault TA: Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol Cell. 1998 Dec;2(6):807-15. [PubMed ]
2. 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 ]
3. Stanchi F, Bertocco E, Toppo S, Dioguardi R, Simionati B, Cannata N, Zimbello R, Lanfranchi G, Valle G: Characterization of 16 novel human genes showing high similarity to yeast sequences. Yeast. 2001 Jan 15;18(1):69-80. [PubMed ]
4. Tong WH, Rouault T: Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 2000 Nov 1;19(21):5692-700. [PubMed ]

MFYLAAAVSDFYVPVSEMPEHKIQSSGGPLQITMKMVPKLLSPLVKDWAPKAFIISFKLE
TDPAIVINRARKALEIYQHQVVVANILESRQSFVFIVTKDSETKLLLSEEEIEKGVEIEE
KIVDNLQSRHTAFIGDRN

• DFP (PF04127 )

ATGGCGGAAATGGATCCGGTAGCCGAGTTCCCCCAGCCTCCCGGTGCTGCGCGCTGGGCT
GAGGTTATGGCTCGCTTCGCGGCCAGGCTGGGCGCGCAGGGCCGGCGGGTGGTGTTGGTT
ACGTCAGGCGGCACCAAGGTCCCACTGGAAGCGCGGCCGGTGCGCTTCCTGGACAACTTC
AGCAGCGGGCGGCGCGGTGCAACCTCGGCCGAGGCCTTCCTAGCCGCCGGCTACGGGGTC
CTGTTCTTGTATCGCGCTCGCTCTGCCTTCCCCTATGCCCACCGCTTCCCACCCCAGACT
TGGCTGTCCGCTCTGCGGCCTTCGGGCCCAGCCCTTTCGGGCTTGCTGAGCCTGGAGGCC
GAGGAGAATGCACTTCCGGGTTTTGCTGAGGCTCTGAGGAGCTACCAGGAGGCTGCGGCT
GCAGGCACCTTCCTGGCAGTAGAGTTCACCACTTTGGCGGACTATTTGCATCTGTTGCAG
GCTGCGGCCCAGGCACTCAATCCGCTAGGCCCTTCTGCGATGTTTTACCTGGCTGCGGCT
GTGTCAGATTTCTATGTTCCTGTCTCTGAAATGCCTGAACACAAGATCCAGTCATCTGGG
GGCCCACTGCAGATAACAATGAAGATGGTGCCAAAACTGCTTTCTCCTTTGGTTAAAGAT
TGGGCTCCCAAAGCATTTATAATTTCCTTTAAGTTGGAGACTGACCCCGCCATTGTAATT
AATCGAGCTCGGAAGGCTTTGGAAATTTATCAGCATCAAGTGGTGGTGGCTAATATCCTT
GAGTCACGACAGTCCTTTGTGTTTATTGTAACCAAAGACTCGGAAACCAAGTTATTGCTA
TCAGAGGAAGAAATAGAAAAAGGCGTAGAGATAGAAGAGAAGATAGTGGATAATCTTCAG
TCTCGACACACAGCTTTTATAGGTGACAGAAACTGA

1. 4F2hc
2. Lymphocyte activation antigen 4F2 large subunit
3. 4F2 heavy chain antigen
4. CD98 antigen

MSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKF
TGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHT
GALYRIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQID
PNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAG
VDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLT
SSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLP
GTPVFSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLS
LFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQAS
DLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA

• Alpha-amylase (PF00128 )

• 1-98

• 82-104

ATGAGCCAGGACACCGAGGTGGATATGAAGGAGGTGGAGCTGAATGAGTTAGAGCCCGAG
AAGCAGCCGATGAACGCGGCGTCTGGGGCGGCCATGTCCCTGGCGGGAGCCGAGAAGAAT
GGTCTGGTGAAGATCAAGGTGGCGGAAGACGAGGCGGAGGCGGCAGCCGCGGCTAAGTTC
ACGGGCCTGTCCAAGGAGGAGCTGCTGAAGGTGGCAGGCAGCCCCGGCTGGGTACGCACC
CGCTGGGCACTGCTGCTGCTCTTCTGGCTCGGCTGGCTCGGCATGCTTGCTGGTGCCGTG
GTCATAATCGTGCGAGCGCCGCGTTGTCGCGAGCTACCGGCGCAGAAGTGGTGGCACACG
GGCGCCCTCTACCGCATCGGCGACCTTCAGGCCTTCCAGGGCCACGGCGCGGGCAACCTG
GCGGGTCTGAAGGGGCGTCTCGATTACCTGAGCTCTCTGAAGGTGAAGGGCCTTGTGCTG
GGTCCAATTCACAAGAACCAGAAGGATGATGTCGCTCAGACTGACTTGCTGCAGATCGAC
CCCAATTTTGGCTCCAAGGAAGATTTTGACAGTCTCTTGCAATCGGCTAAAAAAAAGAGC
ATCCGTGTCATTCTGGACCTTACTCCCAACTACCGGGGTGAGAACTCGTGGTTCTCCACT
CAGGTTGACACTGTGGCCACCAAGGTGAAGGATGCTCTGGAGTTTTGGCTGCAAGCTGGC
GTGGATGGGTTCCAGGTTCGGGACATAGAGAATCTGAAGGATGCATCCTCATTCTTGGCT
GAGTGGCAAAATATCACCAAGGGCTTCAGTGAAGACAGGCTCTTGATTGCGGGGACTAAC
TCCTCCGACCTTCAGCAGATCCTGAGCCTACTCGAATCCAACAAAGACTTGCTGTTGACT
AGCTCATACCTGTCTGATTCTGGTTCTACTGGGGAGCATACAAAATCCCTAGTCACACAG
TATTTGAATGCCACTGGCAATCGCTGGTGCAGCTGGAGTTTGTCTCAGGCAAGGCTCCTG
ACTTCCTTCTTGCCGGCTCAACTTCTCCGACTCTACCAGCTGATGCTCTTCACCCTGCCA
GGGACCCCTGTTTTCAGCTACGGGGATGAGATTGGCCTGGATGCAGCTGCCCTTCCTGGA
CAGCCTATGGAGGCTCCAGTCATGCTGTGGGATGAGTCCAGCTTCCCTGACATCCCAGGG
GCTGTAAGTGCCAACATGACTGTGAAGGGCCAGAGTGAAGACCCTGGCTCCCTCCTTTCC
TTGTTCCGGCGGCTGAGTGACCAGCGGAGTAAGGAGCGCTCCCTACTGCATGGGGACTTC
CACGCGTTCTCCGCTGGGCCTGGACTCTTCTCCTATATCCGCCACTGGGACCAGAATGAG
CGTTTTCTGGTAGTGCTTAACTTTGGGGATGTGGGCCTCTCGGCTGGACTGCAGGCCTCC
GACCTGCCTGCCAGCGCCAGCCTCCCAGCCAAGGCTGACCTCCTGCTCAGCACCCAGCCA
GGCCGTGAGGAGGGCTCCCCTCTTGAGCTGGAACGCCTGAAACTGGAGCCTCACGAAGGG
CTGCTGCTCCGCTTCCCCTACGCGGCCTGA

1. Quackenbush E, Clabby M, Gottesdiener KM, Barbosa J, Jones NH, Strominger JL, Speck S, Leiden JM: Molecular cloning of complementary DNAs encoding the heavy chain of the human 4F2 cell-surface antigen: a type II membrane glycoprotein involved in normal and neoplastic cell growth. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6526-30. [PubMed ]
2. Teixeira S, Di Grandi S, Kuhn LC: Primary structure of the human 4F2 antigen heavy chain predicts a transmembrane protein with a cytoplasmic NH2 terminus. J Biol Chem. 1987 Jul 15;262(20):9574-80. [PubMed ]
3. Lumadue JA, Glick AB, Ruddle FH: Cloning, sequence analysis, and expression of the large subunit of the human lymphocyte activation antigen 4F2. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9204-8. [PubMed ]
4. Gottesdiener KM, Karpinski BA, Lindsten T, Strominger JL, Jones NH, Thompson CB, Leiden JM: Isolation and structural characterization of the human 4F2 heavy-chain gene, an inducible gene involved in T-lymphocyte activation. Mol Cell Biol. 1988 Sep;8(9):3809-19. [PubMed ]
5. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed ]
6. Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ: Cluster analysis of an extensive human breast cancer cell line protein expression map database. Proteomics. 2002 Feb;2(2):212-23. [PubMed ]
7. He X, Di Y, Li J, Xie Y, Tang Y, Zhang F, Wei L, Zhang Y, Qin W, Huo K, Li Y, Wan D, Gu J: Molecular cloning and characterization of CT120, a novel membrane-associated gene involved in amino acid transport and glutathione metabolism. Biochem Biophys Res Commun. 2002 Sep 27;297(3):528-36. [PubMed ]

1. Phosphopantothenoylcysteine synthetase
2. PPC synthetase

MAEMDPVAEFPQPPGAARWAEVMARFAARLGAQGRRVVLVTSGGTKVPLEARPVRFLDNF
SSGRRGATSAEAFLAAGYGVLFLYRARSAFPYAHRFPPQTWLSALRPSGPALSGLLSLEA
EENALPGFAEALRSYQEAAAAGTFLAVEFTTLADYLHLLQAAAQALNPLGPSAMFYLAAA
VSDFYVPVSEMPEHKIQSSGGPLQITMKMVPKLLSPLVKDWAPKAFIISFKLETDPAIVI
NRARKALEIYQHQVVVANILESRQSFVFIVTKDSETKLLLSEEEIEKGVEIEEKIVDNLQ
SRHTAFIGDRN

• Pantothenate and CoA Biosynthesis (map00770 )

• D-4'-Phosphopantothenate + ATP + L-Cysteine --> N-((R)-4-Phosphopantothenoyl)-L-cysteine + AMP + H+ + Diphosphate

• DFP (PF04127 )

• None

• None

1. Daugherty M, Polanuyer B, Farrell M, Scholle M, Lykidis A, de Crecy-Lagard V, Osterman A: Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics. J Biol Chem. 2002 Jun 14;277(24):21431-9. Epub 2002 Mar 28. [PubMed ]

1. Cysteine--tRNA ligase
2. CysRS

MLRTTRGPGLGPPLLQAALGLGRAGWHWPAGRAASGGRGRAWLQPTGRETGVQVYNSLTG
RKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKVFGCSIVMVMGITD
VDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGII
ARGNAYSTAKGNVYFDLKSRGDKYGKLVGVVPGPVGEPADSDKRHASDFALWKAAKPQEV
FWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWG
NYFLHSGHLHAKGKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAM
LQAQQLLLGLGSFLEDARAYMKGQLACGSVREAMLWERLSSTKRAVKAALADDFDTPRVV
DAILGLAHHGNGQLRASLKEPEGPRSPAVFGAIISYFEQFFETVGISLANQQYVSGDGSE
ATLHGVVDELVRFRQKVRQFALAMPEATGDARRQQLLERQPLLEACDTLRRGLTAHGINI
KDRSSTTSTWELLDQRTKDQKSAG

• Aminoacyl-tRNA biosynthesis (map00970 )
• Cysteine Metabolism (map00272 )

• ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys [RN:R03650] ALL_REAC R03650

• tRNA-synt_1e (PF01406 )

• None

• None

1. Prenylcysteine lyase

MGRVVAELVSSLLGLWLLLCSCGCPEGAELRAPPDKIAIIGAGIGGTSAAYYLRQKFGKD
VKIDLFEREEVGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLSAVQASGGLLGI
YNGETLVFEESNWFIINVIKLVWRYGFQSLRMHMWVEDVLDKFMRIYRYQSHDYAFSSVE
KLLHALGGDDFLGMLNRTLLETLQKAGFSEKFLNEMIAPVMRVNYGQSTDINAFVGAVSL
SCSDSGLWAVEGGNKLVCSGLLQASKSNLISGSVMYIEEKTKTKYTGNPTKMYEVVYQIG
TETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLVKGELNTSIFSSR
PIDKFGLNTVLTTDNSDLFINSIGIVPSVREKEDPEPSTDGTYVWKIFSQETLTKAQILK
LFLSYDYAVKKPWLAYPHYKPPEKCPSIILHDRLYYLNGIECAASAMEMSAIAAHNAALL
AYHRWNGHTDMIDQDGLYEKLKTEL

• an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2 [RN:R07360] ALL_REAC R07360

• Prenylcys_lyase (PF07156 )
• Pyr_redox_2 (PF07992 )

• 1-27

• None

ATGGGGCGCGTCGTCGCGGAGCTCGTCTCCTCGCTGCTGGGGTTGTGGCTGTTGCTGTGC
AGCTGCGGATGCCCCGAGGGTGCCGAGCTGCGTGCTCCGCCAGATAAAATCGCGATTATT
GGAGCCGGAATTGGTGGCACTTCAGCAGCCTATTACCTGCGGCAGAAATTTGGGAAAGAT
GTGAAGATAGACCTGTTTGAAAGAGAAGAGGTCGGGGGCCGCCTGGCTACCATGATGGTG
CAGGGGCAAGAATACGAGGCAGGAGGTTCTGTCATCCATCCTTTAAATCTGCACATGAAA
CGTTTTGTCAAAGACCTGGGTCTCTCTGCTGTTCAGGCCTCTGGTGGCCTACTGGGGATA
TATAATGGAGAGACTCTGGTATTTGAGGAGAGCAACTGGTTCATAATTAACGTGATTAAA
TTAGTTTGGCGCTATGGATTTCAATCCCTCCGTATGCACATGTGGGTAGAGGACGTGTTA
GACAAGTTCATGAGGATCTACCGCTACCAGTCTCATGACTATGCCTTCAGTAGTGTCGAA
AAATTACTTCATGCTCTAGGAGGAGATGACTTCCTTGGAATGCTTAATCGAACACTTCTT
GAAACCTTGCAAAAGGCCGGCTTTTCTGAGAAGTTCCTCAATGAAATGATTGCTCCTGTT
ATGAGGGTCAATTATGGCCAAAGCACGGACATCAATGCCTTTGTGGGGGCGGTGTCACTG
TCCTGTTCTGATTCTGGCCTTTGGGCAGTAGAAGGTGGCAATAAACTTGTTTGCTCAGGG
CTTCTGCAGGCATCCAAAAGCAATCTTATATCTGGCTCAGTAATGTACATCGAGGAGAAA
ACAAAGACCAAGTACACAGGAAATCCAACAAAGATGTATGAAGTGGTCTACCAAATTGGA
ACTGAGACTCGTTCAGACTTCTATGACATCGTCTTGGTGGCCACTCCGTTGAATCGAAAA
ATGTCGAATATTACTTTTCTCAACTTTGATCCTCCAATTGAGGAATTCCATCAATATTAT
CACCATATAGTGACAACTTTAGTTAAGGGGGAATTGAATACATCTATCTTTAGCTCTAGA
CCCATAGATAAATTTGGCCTTAATACAGTTTTAACCACTGATAATTCAGATTTGTTCATT
AACAGTATTGGGATTGTGCCCTCTGTGAGAGAAAAGGAAGATCCTGAGCCATCAACAGAT
GGAACATATGTTTGGAAGATCTTTTCCCAAGAAACTCTTACTAAAGCACAAATTTTAAAG
CTCTTTCTGTCCTATGATTATGCTGTGAAGAAGCCATGGCTTGCATATCCTCACTATAAG
CCCCCGGAGAAATGCCCCTCTATCATTCTCCATGATCGACTTTATTACCTCAATGGCATA
GAGTGTGCAGCAAGTGCCATGGAGATGAGTGCCATTGCAGCCCACAACGCTGCACTCCTT
GCCTATCACCGCTGGAACGGGCACACAGACATGATTGATCAGGATGGCTTATATGAGAAA
CTTAAAACTGAACTATGA

1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed ]
2. 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 ]

MADSSGQQAPDYRSILSISDEAARAQALNEHLSTRSYVQGYSLSQADVDAFRQLSAPPAD
PQLFHVARWFRHIEALLGSPCGKGQPCRLQASKGRRVQPQWSPPAGTQPCRLHLYNSLTR
NKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYFKFDVFYCMNITD
IDDKIIKRARQNHLFEQYREKRPEAAQLLEDVQAALKPFSVKLNETTDPDKKQMLERIQH
AVQLATEPLEKAVQSRLTGEEVNSCVEVLLEEAKDLLSDWLDSTLGCDVTDNSIFSKLPK
FWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSVYFDTAKFAS
SEKHSYGKLVPEAVGDQKALQEGEGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPW
GKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHT
GHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEK
FLNEFFLNVKDILRAPVDITGQFEKWGEEEAELNKNFYDKKTAIHKALCDNVDTRTVMEE
MRALVSQCNLYMAARKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTS
LSLEATVMPYLQVLSEFREGVRKIAREQKVPEILQLSDALRDNILPELGVRFEDHEGLPT
VVKLVDRNTLLKEREEKRRVEEEKRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDK
YSKFDENGLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ

• tRNA-synt_1e (PF01406 )

• None

• None

ATGGCAGATTCCTCCGGGCAGCAGGCTCCTGACTACAGGTCCATTCTGAGCATTAGTGAC
GAGGCAGCCAGGGCACAAGCCCTGAACGAGCACCTCAGCACGCGTAGCTATGTCCAGGGG
TACTCACTGTCCCAGGCAGACGTGGACGCGTTCAGGCAGCTCTCGGCCCCGCCCGCTGAC
CCCCAGCTCTTCCACGTGGCTCGGTGGTTCAGGCACATAGAAGCGCTCCTGGGTAGCCCC
TGTGGCAAAGGCCAGCCCTGCAGGCTCCAAGCAAGCAAAGGCCGGCGTGTGCAGCCCCAG
TGGTCCCCTCCTGCTGGGACCCAGCCATGCAGACTCCACCTTTACAACAGCCTCACCAGG
AACAAGGAAGTGTTCATACCTCAAGATGGGAAAAAGGTGACGTGGTATTGCTGTGGGCCA
ACCGTCTATGACGCATCTCACATGGGGCACGCCAGGTCCTACATCTCTTTTGATATCTTG
AGAAGAGTGTTGAAGGATTACTTCAAATTTGATGTCTTTTATTGCATGAACATTACGGAT
ATTGATGACAAGATCATCAAGAGGGCCCGGCAGAACCACCTGTTCGAGCAGTATCGGGAG
AAGAGGCCTGAAGCGGCACAGCTCTTGGAGGATGTTCAGGCCGCCCTGAAGCCATTTTCA
GTAAAATTAAATGAGACCACGGATCCCGATAAAAAGCAGATGCTCGAACGGATTCAGCAC
GCAGTGCAGCTTGCCACAGAGCCACTTGAGAAAGCTGTGCAGTCCAGACTCACGGGAGAG
GAAGTCAACAGCTGTGTGGAGGTGTTGCTGGAAGAAGCCAAGGATTTGCTCTCTGACTGG
CTGGATTCTACACTTGGCTGTGATGTCACTGACAATTCCATCTTCTCCAAGCTGCCCAAG
TTCTGGGAGGGGGACTTCCACAGAGACATGGAAGCTCTGAATGTTCTCCCTCCAGATGTC
TTAACCCGGGTTAGTGAGTATGTGCCAGAAATTGTGAACTTTGTCCAGAAGATTGTGGAC
AACGGTTACGGCTATGTCTCCAATGGGTCTGTCTACTTTGATACAGCGAAGTTTGCTTCT
AGCGAGAAGCACTCCTATGGGAAGCTGGTGCCTGAGGCCGTTGGAGATCAGAAAGCCCTT
CAAGAAGGGGAAGGTGACCTGAGCATCTCTGCAGACCGCCTGAGTGAGAAGCGCTCTCCC
AACGACTTTGCCTTATGGAAGGCCTCTAAGCCCGGAGAACCGTCCTGGCCGTGCCCTTGG
GGAAAGGGTCGTCCGGGCTGGCATATCGAGTGCTCGGCCATGGCAGGCACCCTCCTAGGG
GCTTCGATGGACATTCACGGAGGTGGGTTCGACCTCCGGTTCCCCCACCATGACAATGAG
CTGGCACAGTCGGAGGCCTACTTTGAAAACGACTGCTGGGTCAGGTACTTCCTGCACACA
GGCCACCTGACCATTGCAGGCTGCAAAATGTCAAAGTCACTAAAAAACTTCATCACCATT
AAAGATGCCTTGAAAAAGCACTCAGCACGGCAGTTGCGGCTGGCCTTCCTCATGCACTCG
TGGAAGGACACCCTGGACTACTCCAGCAACACCATGGAGTCAGCGCTTCAATATGAGAAG
TTCTTGAATGAGTTTTTCTTAAATGTGAAAGATATCCTTCGCGCTCCTGTTGACATCACT
GGTCAGTTTGAGAAGTGGGGAGAAGAAGAAGCAGAACTGAATAAGAACTTTTATGACAAG
AAGACAGCAATTCACAAAGCCCTCTGTGACAATGTTGACACCCGCACCGTCATGGAAGAG
ATGCGGGCCTTGGTCAGTCAGTGCAACCTCTATATGGCAGCCCGGAAAGCCGTGAGGAAG
AGGCCCAACCAGGCTCTGCTGGAGAACATCGCCCTGTACCTCACCCATATGCTGAAGATC
TTTGGGGCCGTAGAAGAGGACAGCTCCCTGGGATTCCCGGTCGGAGGGCCTGGAACCAGC
CTCAGTCTCGAGGCCACAGTCATGCCCTACCTTCAGGTGTTATCAGAATTCCGAGAAGGA
GTGCGGAAGATTGCCCGAGAGCAAAAAGTCCCTGAGATTCTGCAGCTCAGCGATGCCCTG
CGGGACAACATCCTGCCCGAGCTTGGGGTGCGGTTTGAAGACCACGAAGGACTGCCCACA
GTGGTGAAACTGGTAGACAGAAACACCTTATTAAAAGAGAGAGAAGAAAAGAGACGGGTT
GAAGAGGAGAAGAGGAAGAAGAAAGAGGAGGCGGCCCGGAGGAAACAGGAACAAGAAGCA
GCAAAGCTGGCCAAGATGAAGATTCCCCCCAGTGAGATGTTCTTGTCAGAAACCGACAAA
TACTCCAAGTTTGATGAAAATGGTCTGCCCACACATGACATGGAGGGCAAAGAGCTCAGC
AAAGGGCAAGCCAAGAAGCTGAAGAAGCTCTTCGAGGCTCAGGAGAAGCTCTACAAGGAA
TATCTGCAGATGGCCCAGAATGGAAGCTTCCAGTGA

1. Cytochrome c-releasing factor 21

MANSGCKDVTGPDEESFLYFAYGSNLLTERIHLRNPSAAFFCVARLQDFKLDFGNSQGKT
SQTWHGGIATIFQSPGDEVWGVVWKMNKSNLNSLDEQEGVKSGMYVVIEVKVATQEGKEI
TCRSYLMTNYESAPPSPQYKKIICMGAKENGLPLEYQEKLKAIEPNDYTGKVSEEIEDII
KKGETQTL

• None

• None

ATGGCCAACTCGGGCTGCAAGGACGTCACGGGTCCAGATGAGGAGAGTTTTCTGTACTTT
GCCTACGGCAGCAACCTGCTGACAGAGAGGATCCACCTCCGAAACCCCTCGGCGGCGTTC
TTCTGTGTGGCCCGCCTGCAGGATTTTAAGCTTGACTTTGGCAATTCCCAAGGCAAAACA
AGTCAAACTTGGCATGGAGGGATAGCCACCATTTTTCAGAGTCCTGGCGATGAAGTGTGG
GGAGTAGTATGGAAAATGAACAAAAGCAATTTAAATTCTCTGGATGAGCAAGAAGGGGTT
AAAAGTGGAATGTATGTTGTAATAGAAGTTAAAGTTGCAACTCAAGAAGGAAAAGAAATA
ACCTGTCGAAGTTATCTGATGACAAATTACGAAAGTGCTCCCCCATCCCCACAGTATAAA
AAGATTATTTGCATGGGTGCAAAAGAAAATGGTTTGCCGCTGGAGTATCAAGAGAAGTTA
AAAGCAATAGAACCAAATGACTATACAGGAAAGGTCTCAGAAGAAATTGAAGACATCATC
AAAAAGGGGGAAACACAAACTCTTTAG

MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK

• CBS (PF00571 )
• PALP (PF00291 )

• None

• None

MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ

• Aminotran_1_2 (PF00155 )

• None

• None

1. SubName: NFS1 nitrogen fixation 1 (S. cerevisiae), isoform CRA_a

MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLY
MDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPRE
IIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQK
SGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKI
PLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPL
VVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAY
VEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD
YTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH

• L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine ALL_REAC (other) R07460

• Aminotran_5 (PF00266 )

• None

• None

MEQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPTEWAMYAKFDQYRYTR
NLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKK
SERVLRENQCAYINDSIGLHRVENISHTEPAVSLHLYSPPFDTCHAFDQRTGHKNKVTMT
FHSKFGIRTPNATSGSLENN

• CDO_I (PF05995 )

• None

• None

MGRVVAELVSSLLGLWLLLCSCGCPEGAELRAPPDKIAIIGAGIGGTSAAYYLRQKFGKD
VKIDLFEREEVGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLSAVQASGGLLGI
YNGETLVFEESNWFIINVIKLVWRYGFQSLRMHMWVEDVLDKFMRIYRYQSHDYAFSSVE
KLLHALGGDDFLGMLNRTLLETLQKAGFSEKFLNEMIAPVMRVNYGQSTDINAFVGAVSL
SCSDSGLWAVEGGNKLVCSGLLQASKSNLISGSVMYIEEKTKTKYTGNPTKMYEVVYQIG
TETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLVKGELNTSIFSSR
PIDKFGLNTVLTTDNSDLFINSIGIVPSVREKEDPEPSTDGTYVWKIFSQETLTKAQILK
LFLSYDYAVKKPWLAYPHYKPPEKCPSIILHDRLYYLNGIECAASAMEMSAIAAHNAALL
AYHRWNGHTDMIDQDGLYEKLKTEL

• Prenylcys_lyase (PF07156 )
• Pyr_redox_2 (PF07992 )

• None

• None

MEQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPIEWAMYAKFDQY

• CDO_I (PF05995 )

• None

• None

1. Cysteine--tRNA ligase
2. CysRS

MADSSGQQGKGRRVQPQWSPPAGTQPCRLHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVY
DASHMGHARSYISFDILRRVLKDYFKFDVFYCMNITDIDDKIIKRARQNHLFEQYREKRP
EAAQLLEDVQAALKPFSVKLNETTDPDKKQMLERIQHAVQLATEPLEKAVQSRLTGEEVN
SCVEVLLEEAKDLLSDWLDSTLGCDVTDNSIFSKLPKFWEGDFHRDMEALNVLPPDVLTR
VSEYVPEIVNFVQKIVDNGYGYVSNGSVYFDTAKFASSEKHSYGKLVPEAVGDQKALQEG
EGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASM
DIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDA
LKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFLNEFFLNVKDILRAPVDITGQF
EKWGEEEAELNKNFYDKKTAIHKALCDNVDTRTVMEEMRALVSQCNLYMAARKAVRKRPN
QALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTSLSLEATVMPYLQVLSEFREGVRK
IAREQKVPEILQLSDALRDNILPELGVRFEDHEGLPTVVKLVDRNTLLKEREEKRRVEEE
KRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDKYSKFDENGLPTHDMEGKELSKGQ
AKKLKKLFEAQEKLYKEYLQMAQNGSFQ

• tRNA-synt_1e (PF01406 )

• None

• None

1. Cruzen ME, Arfin SM: Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA synthetase. DNA Seq. 1994;4(4):243-8. [PubMed ]
2. Davidson E, Caffarella J, Vitseva O, Hou YM, King MP: Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase. Biol Chem. 2001 Mar;382(3):399-406. [PubMed ]
3. Cools J, Wlodarska I, Somers R, Mentens N, Pedeutour F, Maes B, De Wolf-Peeters C, Pauwels P, Hagemeijer A, Marynen P: Identification of novel fusion partners of ALK, the anaplastic lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic tumor. Genes Chromosomes Cancer. 2002 Aug;34(4):354-62. [PubMed ]