We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Selenocysteine (HMDB03288)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 16:12:47
Update Date 2009-08-18 13:41:06
Accession Number HMDB03288
Secondary Accession Numbers Not Available
Common Name Selenocysteine
Description Amino Acids, Sulfur A naturally occurring amino acid in both eukaryotic and prokaryotic organisms. It is found in tRNAs and in the catalytic site of some enzymes. The genes for glutathione peroxidase and formate dehydrogenase contain the TGA codon, which codes for this amino acid. -- Pubchem; Selenocysteine is an amino acid that is present in several enzymes (for example glutathione peroxidases, tetraiodothyronine 5' deiodinases, thioredoxin reductases, formate dehydrogenases, glycine reductases and some hydrogenases). Selenocysteine has a structure similar to cysteine, but with an atom of selenium taking the place of the usual sulfur. Proteins that include a selenocysteine residue are called selenoproteins. -- Wikipedia
Synonyms
  1. (2R)-2-amino-3-selanylpropanoate
  2. (2R)-2-amino-3-selanylpropanoic acid
  3. 3-Selenoalanine
  4. 3-seleno-alanine
  5. 3-selenyl-L-Alanine
  6. L-Selenocystein
  7. L-Selenozystein
  8. L-selenocysteine
Chemical IUPAC Name Not Available
Chemical Formula C3H6NO2Se
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 167.045
Monoisotopic Molecular Weight 167.956375
Isomeric SMILES N[C@@H](C[SeH])C(O)=O
Canonical SMILES NC(C[SeH])C(O)=O
KEGG Compound ID C05688 Link Image
BioCyc ID L-SELENOCYSTEINE Link Image
BiGG ID 46290 Link Image
Wikipedia Link Selenocysteine Link Image
NuGOwiki Link HMDB03288 Link Image
Metagene Link HMDB03288 Link Image
METLIN ID 3292 Link Image
PubChem Compound 6326983 Link Image
PubChem Substance 167858 Link Image
ChEBI ID 9093 Link Image
CAS Registry Number 3614-08-2
InChI Identifier InChI=1/C3H7NO2Se/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 325.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -3.20 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts
Kidney
Testes
Thyroid Gland
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Selenoamino Acid Metabolism SMP00029 Link Image map00450 Link Image
General References
  1. Mostert V, Wolff S, Dreher I, Kohrle J, Abel J: Identification of an element within the promoter of human selenoprotein P responsive to transforming growth factor-beta. Eur J Biochem. 2001 Dec;268(23):6176-81. [PubMed Link Image]
  2. Zimmermann MB, Kohrle J: The impact of iron and selenium deficiencies on iodine and thyroid metabolism: biochemistry and relevance to public health. Thyroid. 2002 Oct;12(10):867-78. [PubMed Link Image]
  3. Sun QA, Su D, Novoselov SV, Carlson BA, Hatfield DL, Gladyshev VN: Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase. Biochemistry. 2005 Nov 8;44(44):14528-37. [PubMed Link Image]
  4. Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF: Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood. 1992 Jun 15;79(12):3233-8. [PubMed Link Image]
  5. Blotcky AJ, Ebrahim A, Rack EP: Determination of selenium metabolites in biological fluids using instrumental and molecular neutron activation analysis. Anal Chem. 1988 Dec 15;60(24):2734-7. [PubMed Link Image]
  6. Utomo A, Jiang X, Furuta S, Yun J, Levin DS, Wang YC, Desai KV, Green JE, Chen PL, Lee WH: Identification of a novel putative non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx) essential for alleviating oxidative stress generated from polyunsaturated fatty acids in breast cancer cells. J Biol Chem. 2004 Oct 15;279(42):43522-9. Epub 2004 Aug 4. [PubMed Link Image]
  7. Rooseboom M, Vermeulen NP, Andreadou I, Commandeur JN: Evaluation of the kinetics of beta-elimination reactions of selenocysteine Se-conjugates in human renal cytosol: possible implications for the use as kidney selective prodrugs. J Pharmacol Exp Ther. 2000 Aug;294(2):762-9. [PubMed Link Image]
  8. Wikipedia Link Image
Metabolic Enzymes
  1. Thioredoxin reductase 1, cytoplasmic precursor
  2. Thioredoxin reductase 2, mitochondrial precursor
  3. Cystathionine gamma-lyase
  4. Selenide, water dikinase 2
  5. Glutathione peroxidase 1
  6. Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
  7. Glutathione peroxidase 3 precursor
  8. Glutathione peroxidase 2
  9. Type I iodothyronine deiodinase
  10. Type II iodothyronine deiodinase
  11. Selenocysteine lyase
  12. Thioredoxin reductase 3
  13. Ethanolaminephosphotransferase 1
  14. O-phosphoseryl-tRNA(Sec) selenium transferase
  15. Aflatoxin B1 aldehyde reductase member 4
  16. Methionine-R-sulfoxide reductase B1
  17. Selenoprotein P
  18. 15 kDa selenoprotein
  19. Selenoprotein N
  20. Selenoprotein W
  21. Selenoprotein S
  22. Selenoprotein K
  23. Selenoprotein M
  24. Selenoprotein T
Enzyme 1 [top]
Enzyme 1 ID 5366
Enzyme 1 Name Thioredoxin reductase 1, cytoplasmic precursor
Enzyme 1 Synonyms
  1. TR
  2. TR1
Enzyme 1 Gene Name TXNRD1
Enzyme 1 Protein Sequence >Thioredoxin reductase 1, cytoplasmic precursor
MNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCV
NVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVAL
REKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISS
DDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHM
EEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKI
GLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLYAG
STVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNNK
CYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFT
TLSVTKRSGASILQAGCCG
Enzyme 1 Number of Residues 499
Enzyme 1 Molecular Weight 54707
Enzyme 1 Theoretical pI 6.43
Enzyme 1 GO Classification
Function
  • FAD binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • disulfide oxidoreductase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, disulfide as acceptor
  • purine nucleotide binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Energy production and conversion
Enzyme 1 Specific Function Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH
Enzyme 1 Pathways
Enzyme 1 Reactions
  • thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1237038 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q16881 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name TRXR1_HUMAN Link Image
Enzyme 1 PDB ID 1H6V Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1494 bp
ATGAACGGCCCTGAAGATCTTCCCAAGTCCTATGACTATGACCTTATCATCATTGGAGGT
GGCTCAGGAGGTCTGGCAGCTGCTAAGGAGGCAGCCCAATATGGCAAGAAGGTGATGGTC
CTGGACTTTGTCACTCCCACCCCTCTTGGAACTAGATGGGGTCTTGGAGGAACATGTGTG
AATGTGGGTTGCATACCTAAAAAACTGATGCATCAAGCAGCTTTGTTAGGACAAGCCCTG
CAAGACTCTCGAAATTATGGATGGAAAGTCGAGGAGACAGTTAAGCATGATTGGGACAGA
ATGATAGAAGCTGTACAGAATCACATTGGCTCTTTGAATTGGGGCTACCGAGTAGCTCTG
CGGGAGAAAAAAGTCGTCTATGAGAATGCTTATGGGCAATTTATTGGTCCTCACAGGATT
AAGGCAACAAATAATAAAGGCAAAGAAAAAATTTATTCAGCAGAGAGTTTTCTCATTGCC
ACTGGTGAAAGACCACGTTACTTGGGCATCCCTGGTGACAAAGAATACTGCATCAGCAGT
GATGATCTTTTCTCCTTGCCTTACTGCCCGGGTAAGACCCTGGTTGTTGGAGCATCCTAT
GTCGCTTTGGAGTGCGCTGGATTTCTTGCTGGTATTGGTTTAGGCGTCACTGTTATGGTT
AGGTCCATTCTTCTTAGAGGATTTGACCAGGACATGGCCAACAAAATTGGTGAACACATG
GAAGAACATGGCATCAAGTTTATAAGACAGTTCGTACCAATTAAAGTTGAACAAATTGAA
GCAGGGACACCAGGCCGACTCAGAGTAGTAGCTCAGTCCACCAATAGTGAGGAAATCATT
GAAGGAGAATATAATACGGTGATGCTGGCAATAGGAAGAGATGCTTGCACAAGAAAAATT
GGCTTAGAAACCGTAGGGGTGAAGATAAATGAAAAGACTGGAAAAATACCTGTCACAGAT
GAAGAACAGACCAATGTGCCTTACATCTATGCCATTGGCGATATATTGGAGGATAAGGTG
GAGCTCACCCCAGTTGCAATCCAGGCAGGAAGATTGCTGGCTCAGAGGCTCTATGCAGGT
TCCACTGTCAAGTGTGACTATGAAAATGTTCCAACCACTGTATTTACTCCTTTGGAATAT
GGTGCTTGTGGCCTTTCTGAGGAGAAAGCTGTGGAGAAGTTTGGGGAAGAAAATATTGAG
GTTTACCATAGTTACTTTTGGCCATTGGAATGGACGATTCCGTCAAGAGATAACAACAAA
TGTTATGCAAAAATAATCTGTAATACTAAAGACAATGAACGTGTTGTGGGCTTTCACGTA
CTGGGTCCAAATGCTGGAGAAGTTACACAAGGCTTTGCAGCTGCGCTCAAATGTGGACTG
ACCAAAAAGCAGCTGGACAGCACAATTGGAATCCACCCTGTCTGTGCAGAGGTATTCACA
ACATTGTCTGTGACCAAGCGCTCTGGGGCAAGCATCCTCCAGGCTGGCTGCTGA
Enzyme 1 GenBank Gene ID X91247 Link Image
Enzyme 1 GeneCard ID TXNRD1 Link Image
Enzyme 1 GenAtlas ID TXNRD1 Link Image
Enzyme 1 HGNC ID HGNC:12437 Link Image
Enzyme 1 Chromosome Location 12
Enzyme 1 Locus 12q23-q24.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Gasdaska PY, Gasdaska JR, Cochran S, Powis G: Cloning and sequencing of a human thioredoxin reductase. FEBS Lett. 1995 Oct 2;373(1):5-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5390
Enzyme 2 Name Thioredoxin reductase 2, mitochondrial precursor
Enzyme 2 Synonyms
  1. TR3
  2. TR-beta
  3. Selenoprotein Z
  4. SelZ
Enzyme 2 Gene Name TXNRD2
Enzyme 2 Protein Sequence >Thioredoxin reductase 2, mitochondrial precursor
MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQ
LGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQP
VPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLS
ADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI
GLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDST
TGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDV
VEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHG
QEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALG
IKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCCG
Enzyme 2 Number of Residues 524
Enzyme 2 Molecular Weight 56460
Enzyme 2 Theoretical pI 7.53
Enzyme 2 GO Classification
Function
  • FAD binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • disulfide oxidoreductase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, disulfide as acceptor
  • purine nucleotide binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox- regulated cell signaling
Enzyme 2 Pathways
Enzyme 2 Reactions
  • thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 5764541 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9NNW7 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name TRXR2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1575 bp
ATGGCGGCAATGGCGGTGGCGCTGCGGGGATTAGGAGGGCGCTTCCGGTGGCGGACGCAG
GCCGTGGCGGGCGGGGTGCGGGGCGCGGCGCGGGGCGCAGCAGCAGGTCAGCGGGACTAT
GATCTCCTGGTGGTCGGCGGGGGATCTGGTGGCCTGGCTTGTGCCAAGGAGGCCGCCCAG
CTGGGAAGGAAGGTGGCCGTGGTGGACTACGTGGAACCTTCTCCCCAAGGCACCCGGTGG
GGCCTCGGCGGCACCTGCGTCAACGTGGGCTGCATCCCCAAGAAGCTGATGCACCAGGCG
GCACTGCTGGGAGGCCTGATCCAAGATGCCCCCAACTATGGCTGGGAGGTGGCCCAGCCC
GTGCCGCATGACTGGAGGAAGATGGCAGAAGCTGTTCAAAATCACGTGAAATCCTTGAAC
TGGGGCCACCGTGTCCAGCTTCAGGACAGAAAAGTCAAGTACTTTAACATCAAAGCCAGC
TTTGTTGACGAGCACACGGTTTGCGGCGTTGCCAAAGGTGGGAAAGAGATTCTGCTGTCA
GCCGATCACATCATCATTGCTACTGGAGGGCGGCCGAGATACCCCACGCACATCGAAGGT
GCCTTGGAATATGGAATCACAAGTGATGACATCTTCTGGCTGAAGGAATCCCCTGGAAAA
ACGTTGGTGGTCGGGGCCAGCTATGTGGCCCTGGAGTGTGCTGGCTTCCTCACCGGGATT
GGGCTGGACACCACCATCATGATGCGCAGCATCCCCCTCCGCGGCTTCGACCAGCAAATG
TCCTCCATGGTCATAGAGCACATGGCATCTCATGGCACCCGGTTCCTGAGGGGCTGTGCC
CCCTCGCGGGTCAGGAGGCTCCCTGATGGCCAGCTGCAGGTCACCTGGGAGGACAGCACC
ACCGGCAAGGAGGACACGGGCACCTTTGACACCGTCCTGTGGGCCATAGGTCGAGTCCCA
GACACCAGAAGTCTGAATTTGGAGAAGGCTGGGGTAGATACTAGCCCCGACACTCAGAAG
ATCCTGGTGGACTCCCGGGAAGCCACCTCTGTGCCCCACATCTACGCCATTGGTGACGTG
GTGGAGGGGCGGCCTGAGCTGACACCCATAGCGATCATGGCCGGGAGGCTCCTGGTGCAG
CGGCTCTTCGGCGGGTCCTCAGATCTGATGGACTACGACAATGTTCCCACGACCGTCTTC
ACCCCGCTGGAGTATGGCTGTGTGGGGCTGTCCGAGGAGGAGGCAGTGGCTCGCCACGGG
CAGGAGCATGTTGAGGTCTATCACGCCCATTATAAACCACTGGAGTTCACGGTGGCTGGA
CGAGATGCATCCCAGTGTTATGTAAAGATGGTGTGCCTGAGGGAGCCCCCACAGCTGGTG
CTGGGCCTGCATTTCCTTGGCCCCAACGCAGGCGAAGTTACTCAAGGATTTGCTCTGGGG
ATCAAGTGTGGGGCTTCCTATGCGCAGGTGATGCGGACCGTGGGTATCCATCCCACATGC
TCTGAGGAGGTAGTCAAGCTGCGCATCTCCAAGCGCTCAGGCCTGGACCCCACGGTGACA
GGCTGCTGAGGGTAA
Enzyme 2 GenBank Gene ID AF171054 Link Image
Enzyme 2 GeneCard ID TXNRD2 Link Image
Enzyme 2 GenAtlas ID TXNRD2 Link Image
Enzyme 2 HGNC ID HGNC:18155 Link Image
Enzyme 2 Chromosome Location 22
Enzyme 2 Locus 22q11.21
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Sun QA, Wu Y, Zappacosta F, Jeang KT, Lee BJ, Hatfield DL, Gladyshev VN: Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases. J Biol Chem. 1999 Aug 27;274(35):24522-30. [PubMed Link Image]
  2. Gasdaska PY, Berggren MM, Berry MJ, Powis G: Cloning, sequencing and functional expression of a novel human thioredoxin reductase. FEBS Lett. 1999 Jan 8;442(1):105-11. [PubMed Link Image]
  3. Miranda-Vizuete A, Damdimopoulos AE, Pedrajas JR, Gustafsson JA, Spyrou G: Human mitochondrial thioredoxin reductase cDNA cloning, expression and genomic organization. Eur J Biochem. 1999 Apr;261(2):405-12. [PubMed Link Image]
  4. Lescure A, Gautheret D, Carbon P, Krol A: Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem. 1999 Dec 31;274(53):38147-54. [PubMed Link Image]
  5. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  6. Sun QA, Zappacosta F, Factor VM, Wirth PJ, Hatfield DL, Gladyshev VN: Heterogeneity within animal thioredoxin reductases. Evidence for alternative first exon splicing. J Biol Chem. 2001 Feb 2;276(5):3106-14. Epub 2000 Nov 1. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5789
Enzyme 3 Name Cystathionine gamma-lyase
Enzyme 3 Synonyms
  1. Gamma-cystathionase
Enzyme 3 Gene Name CTH
Enzyme 3 Protein Sequence >Cystathionine gamma-lyase
MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEY
SRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRY
FRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHG
DIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQ
NSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQH
ELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVL
KNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS
Enzyme 3 Number of Residues 405
Enzyme 3 Molecular Weight 44508
Enzyme 3 Theoretical pI 6.69
Enzyme 3 GO Classification
Function
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • L-cystathionine + H2O = L-cysteine + ammonia + 2-oxobutanoate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 262476 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P32929 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CGL_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1218 bp
ATGCAGGAAAAAGACGCCTCCTCACAAGGTTTCCTGCCACACTTCCAACATTTCGCCACG
CAGGCGATCCATGTGGGCCAGGATCCGGAGCAATGGACCTCCAGGGCTGTAGTGCCCCCC
ATCTCACTGTCCACCACGTTCAAGCAAGGGGCGCCTGGCCAGCACTCGGGTTTTGAATAT
AGCCGTTCTGGAAATCCCACTAGGAATTGCCTTGAAAAAGCAGTGGCAGCACTGGATGGG
GCTAAGTACTGTTTGGCCTTTGCTTCAGGTTTAGCAGCCACTGTAACTATTACCCATCTT
TTAAAAGCAGGAGACCAAATTATTTGTATGGATGATGTGTATGGAGGTACAAACAGGTAC
TTCAGGCAAGTGGCATCTGAATTTGGATTAAAGATTTCTTTTGTTGATTGTTCCAAAATC
AAATTACTAGAGGCAGCAATTACACCAGAAACCAAGCTTGTTTGGATCGAAACCCCCACA
AACCCCACCCAGAAGGTGATTGACATTGAAGGCTGTGCACATATTGTCCATAAGCATGGA
GACATTATTTTGGTCGTGGATAACACTTTTATGTCACCATATTTCCAGCGCCCTTTGGCT
CTGGGAGCTGATATTTCTATGTATTCTGCAACAAAATACATGAATGGCCACAGTGATGTT
GTAATGGGCCTGGTGTCTGTTAATTGTGAAAGCCTTCATAATAGACTTCGTTTCTTGCAA
AACTCTCTTGGAGCAGTTCCATCTCCTATTGATTGTTACCTCTGCAATCGAGGTCTGAAG
ACTCTACATGTCCGAATGGAAAAGCATTTCAAAAACGGAATGGCAGTTGCCCAGTTCCTG
GAATCTAATCCTTGGGTAGAAAAGGTTATTTATCCTGGGCTGCCCTCTCATCCACAGCAT
GAGTTGGTGAAGCGTCAGTGTACAGGTTGTACAGGGATGGTCACCTTTTATATTAAGGGC
ACTCTTCAGCATGCTGAGATTTTCCTCAAGAACCTAAAGCTATTTACTCTGGCCGAGAGC
TTGGGAGGATTCGAAAGCCTTGCTGAGCTTCCGGCAATCATGACTCATGCATCAGTTCTT
AAGAATGACAGAGATGTCCTTGGAATTAGTGACACACTGATTCGACTTTCTGTGGGCTTA
GAGGATGAGGAAGACCTACTGGAAGATCTAGATCAAGCTTTGAAGGCAGCACACCCTCCA
AGTGGAATTCACAGCTAG
Enzyme 3 GenBank Gene ID S52784 Link Image
Enzyme 3 GeneCard ID CTH Link Image
Enzyme 3 GenAtlas ID CTH Link Image
Enzyme 3 HGNC ID HGNC:2501 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p31.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  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 Link Image]
  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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5930
Enzyme 4 Name Selenide, water dikinase 2
Enzyme 4 Synonyms
  1. Selenophosphate synthetase 2
  2. Selenium donor protein 2
Enzyme 4 Gene Name SEPHS2
Enzyme 4 Protein Sequence >Selenide, water dikinase 2
MAEASATGACGEAMAAAEGSSGPAGLTLGRSFSNYRPFEPQALGLSPSWRLTGFSGMKGC
GCKVPQEALLKLLAGLTRPDVRPPLGRGLVGGQEEASQEAGLPAGAGPSPTFPALGIGMD
SCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVS
QSMSEEEREKVTPLMVKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQPNEFIMPD
SAVVGDVLVLTKPLGTQVAVNAHQWLDNPERWNKVKMVVSREEVELAYQEAMFNMATLNR
TAAGLMHTFNAHAATDITGFGILGHSQNLAKQQRNEVSFVIHNLPIIAKMAAVSKASGRF
GLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKP
RVIEVLPRGATAAVLAPDSSNASSEPSS
Enzyme 4 Number of Residues 448
Enzyme 4 Molecular Weight 47259
Enzyme 4 Theoretical pI 5.69
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • selenide, water dikinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
Component
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Synthesizes selenophosphate from selenide and ATP
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + selenide + H2O = AMP + selenophosphate + phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 14717790 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q99611 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SPS2_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1347 bp
ATGGCGGAAGCCTCGGCGACGGGCGCCTGCGGAGAGGCGATGGCAGCGGCGGAAGGCTCC
TCGGGCCCGGCGGGCTTGACTCTGGGCCGGAGCTTCTCGAACTACCGGCCCTTCGAGCCC
CAGGCGTTGGGCCTCAGCCCGAGCTGGCGGCTGACGGGCTTCTCCGGCATGAAGGGCTGA
GGCTGCAAGGTCCCGCAGGAGGCGCTGCTCAAACTCCTGGCGGGACTGACGCGGCCGGAC
GTGCGGCCCCCGCTGGGCCGGGGCCTGGTGGGTGGCCAGGAAGAGGCGTCCCAGGAAGCC
GGCCTGCCGGCAGGAGCGGGCCCCAGCCCCACCTTTCCAGCCCTGGGCATCGGGATGGAC
TCCTGCGTCATCCCCCTGAGGCACGGGGGCCTGTCACTGGTGCAGACCACGGACTTCTTT
TACCCCTTGGTAGAAGATCCCTACATGATGGGGCGCATAGCTTGTGCCAACGTGCTGAGT
GACCTCTACGCCATGGGGATTACTGAGTGTGACAACATGTTGATGTTACTCAGCGTCAGC
CAGAGTATGAGTGAGGAGGAACGCGAAAAGGTAACGCCACTCATGGTCAAAGGCTTTCGG
GATGCGGCTGAGGAAGGAGGGACGGCAGTGACCGGTGGGCAAACGGTGGTCAACCCTTGG
ATTATAATCGGTGGAGTTGCCACTGTAGTATGCCAACCAAATGAGTTCATAATGCCGGAC
AGCGCCGTCGTTGGGGACGTGCTGGTGTTAACCAAACCGTTAGGAACCCAGGTTGCTGTC
AATGCCCACCAATGGCTGGATAATCCTGAAAGATGGAATAAAGTAAAGATGGTGGTCTCC
AGAGAAGAGGTGGAGCTGGCCTATCAGGAAGCCATGTTCAATATGGCTACCCTCAACAGA
ACTGCTGCAGGTTTAATGCACACATTTAATGCCCATGCGGCCACAGATATCACAGGCTTT
GGCATTCTAGGACACTCCCAGAACCTTGCAAAACAACAAAGAAATGAAGTGTCCTTTGTT
ATTCATAATCTGCCAATAATTGCCAAGATGGCTGCCGTCAGCAAGGCCAGTGGACGGTTT
GGGCTTCTTCAAGGAACCTCAGCTGAAACCTCTGGGGGATTACTGATTTGTCTGCCAAGA
GAACAGGCGGCTCGCTTTTGTTCTGAAATCAAATCCTCCAAGTACGGAGAGGGTCACCAA
GCGTGGATCGTTGGCATTGTGGAAAAGGGAAACCGAACGGCCCGGATCATTGACAAGCCG
CGAGTTATTGAAGTCCTGCCTCGTGGGGCCACAGCTGCTGTTCTTGCTCCTGACAGTTCA
AATGCCTCCTCTGAGCCTAGCTCGTGA
Enzyme 4 GenBank Gene ID U43286 Link Image
Enzyme 4 GeneCard ID SEPHS2 Link Image
Enzyme 4 GenAtlas ID SEPHS2 Link Image
Enzyme 4 HGNC ID HGNC:19686 Link Image
Enzyme 4 Chromosome Location 16
Enzyme 4 Locus 16p11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Guimaraes MJ, Bazan JF, Zlotnik A, Wiles MV, Grimaldi JC, Lee F, McClanahan T: A new approach to the study of haematopoietic development in the yolk sac and embryoid bodies. Development. 1995 Oct;121(10):3335-46. [PubMed Link Image]
  2. Guimaraes MJ, Peterson D, Vicari A, Cocks BG, Copeland NG, Gilbert DJ, Jenkins NA, Ferrick DA, Kastelein RA, Bazan JF, Zlotnik A: Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism? Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15086-91. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6109
Enzyme 5 Name Glutathione peroxidase 1
Enzyme 5 Synonyms
  1. GSHPx-1
  2. GPx-1
  3. Cellular glutathione peroxidase
Enzyme 5 Gene Name GPX1
Enzyme 5 Protein Sequence >Glutathione peroxidase 1
MCAARLAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLCGTTVRDYTQMNEL
QRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGA
HPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRR
FQTIDIEPDIEALLSQGPSCA
Enzyme 5 Number of Residues 201
Enzyme 5 Molecular Weight 21899
Enzyme 5 Theoretical pI 6.50
Enzyme 5 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 5 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 5 Specific Function Protects the hemoglobin in erythrocytes from oxidative breakdown
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-16
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 577777 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P07203 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GPX1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >606 bp
ATGTGTGCTGCTCGGCTAGCGGCGGCGGCGGCCCAGTCGGTGTATGCCTTCTCGGCGCGC
CCGTTGGCCGGCGGGGAGCCTGTGAGCCTGGGCTCCCTGCGGGGCAAGGTACTACTTATC
GAGAATGTGGCGTCCCTCTGAGGCACCACGGTCCGGGACTACACCCAGATGAACGAGCTG
CAGCGGCGCCTCGGACCCCGGGGCCTGGTGGTGCTCGGCTTCCCGTGCAACCAGTTTGGG
CATCAGGAGAACGCCAAGAACGAAGAGATTCTGAATTCCCTCAAGTACGTCCGGCCTGGT
GGTGGGTTCGAGCCCAACTTCATGCTCTTCGAGAAGTGCGAGGTGAACGGTGCGGGGGCG
CACCCTCTCTTCGCCTTCCTGCGGGAGGCCCTGCCAGCTCCCAGCGACGACGCCACCGCG
CTTATGACCGACCCCAAGCTCATCACCTGGTCTCCGGTGTGTCGCAACGATGTTGCCTGG
AACTTTGAGAAGTTCCTGGTGGGCCCTGACGGTGTGCCCCTACGCAGGTACAGCCGCCGC
TTCCAGACCATTGACATCGAGCCTGACATCGAAGCCCTGCTGTCTCAAGGGCCCAGCTGT
GCCTAG
Enzyme 5 GenBank Gene ID Y00433 Link Image
Enzyme 5 GeneCard ID GPX1 Link Image
Enzyme 5 GenAtlas ID GPX1 Link Image
Enzyme 5 HGNC ID HGNC:4553 Link Image
Enzyme 5 Chromosome Location 3
Enzyme 5 Locus 3p21.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Sukenaga Y, Ishida K, Takeda T, Takagi K: cDNA sequence coding for human glutathione peroxidase. Nucleic Acids Res. 1987 Sep 11;15(17):7178. [PubMed Link Image]
  2. Ishida K, Morino T, Takagi K, Sukenaga Y: Nucleotide sequence of a human gene for glutathione peroxidase. Nucleic Acids Res. 1987 Dec 10;15(23):10051. [PubMed Link Image]
  3. Mullenbach GT, Tabrizi A, Irvine BD, Bell GI, Hallewell RA: Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine. Nucleic Acids Res. 1987 Jul 10;15(13):5484. [PubMed Link Image]
  4. Chada S, Le Beau MM, Casey L, Newburger PE: Isolation and chromosomal localization of the human glutathione peroxidase gene. Genomics. 1990 Feb;6(2):268-71. [PubMed Link Image]
  5. Moscow JA, Morrow CS, He R, Mullenbach GT, Cowan KH: Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J Biol Chem. 1992 Mar 25;267(9):5949-58. [PubMed Link Image]
  6. Forsberg L, de Faire U, Morgenstern R: Low yield of polymorphisms from EST blast searching: analysis of genes related to oxidative stress and verification of the P197L polymorphism in GPX1. Hum Mutat. 1999;13(4):294-300. [PubMed Link Image]
  7. Kote-Jarai Z, Durocher F, Edwards SM, Hamoudi R, Jackson RA, Ardern-Jones A, Murkin A, Dearnaley DP, Kirby R, Houlston R, Easton DF, Eeles R: Association between the GCG polymorphism of the selenium dependent GPX1 gene and the risk of young onset prostate cancer. Prostate Cancer Prostatic Dis. 2002;5(3):189-92. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6110
Enzyme 6 Name Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
Enzyme 6 Synonyms
  1. PHGPx
  2. GPX-4
Enzyme 6 Gene Name GPX4
Enzyme 6 Protein Sequence >Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
MSLGRLCRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVNLDKYR
GFVCIVTNVASQCGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFA
AGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRY
GPMEEPLVIEKDLPHYF
Enzyme 6 Number of Residues 197
Enzyme 6 Molecular Weight 22128
Enzyme 6 Theoretical pI 8.41
Enzyme 6 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 6 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 6 Specific Function Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage
Enzyme 6 Pathways
Enzyme 6 Reactions
  • 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-25
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 825667 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P36969 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name GPX4_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >594 bp
ATGAGCCTCGGCCGCCTTTGCCGCCTACTGAAGCCGGCGCTGCTCTGTGGGGCTCTGGCC
GCGCCTGGCCTGGCCGGGACCATGTGCGCGTCCCGGGACGACTGGCGCTGTGCGCGCTCC
ATGCACGAGTTTTCCGCCAAGGACATCGACGGGCACATGGTTAACCTGGACAAGTACCGG
GGCTTCGTGTGCATCGTCACCAACGTGGCCTCCCAGTGAGGCAAGACCGAAGTAAACTAC
ACTCAGCTCGTCGACCTGCACGCCCGATACGCTGAGTGTGGTTTGCGGATCCTGGCCTTC
CCGTGTAACCAGTTCGGGAAGCAGGAGCCAGGGAGTAACGAAGAGATCAAAGAGTTCGCC
GCGGGCTACAACGTCAAATTCGATATGTTCAGCAAGATCTGCGTGAACGGGGACGACGCC
CACCCGCTGTGGAAGTGGATGAAGATCCAACCCAAGGGCAAGGGCATCCTGGGAAATGCC
ATCAAGTGGAACTTCACCAAGTTCCTCATCGACAAGAACGGCTGCGTGGTGAAGCGCTAC
GGACCCATGGAGGAGCCCCTGGTGATAGAGAAGGACCTGCCCCACTATTTCTAG
Enzyme 6 GenBank Gene ID X71973 Link Image
Enzyme 6 GeneCard ID GPX4 Link Image
Enzyme 6 GenAtlas ID GPX4 Link Image
Enzyme 6 HGNC ID HGNC:4556 Link Image
Enzyme 6 Chromosome Location 19
Enzyme 6 Locus 19p13.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Esworthy RS, Doan K, Doroshow JH, Chu FF: Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase. Gene. 1994 Jul 8;144(2):317-8. [PubMed Link Image]
  2. Kelner MJ, Montoya MA: Structural organization of the human selenium-dependent phospholipid hydroperoxide glutathione peroxidase gene (GPX4): chromosomal localization to 19p13.3. Biochem Biophys Res Commun. 1998 Aug 10;249(1):53-5. [PubMed Link Image]
  3. Maiorino M, Bosello V, Ursini F, Foresta C, Garolla A, Scapin M, Sztajer H, Flohe L: Genetic variations of gpx-4 and male infertility in humans. Biol Reprod. 2003 Apr;68(4):1134-41. Epub 2002 Nov 27. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6111
Enzyme 7 Name Glutathione peroxidase 3 precursor
Enzyme 7 Synonyms
  1. GSHPx-3
  2. GPx-3
  3. Plasma glutathione peroxidase
  4. GSHPx-P
  5. Extracellular glutathione peroxidase
  6. GPx-P
Enzyme 7 Gene Name GPX3
Enzyme 7 Protein Sequence >Glutathione peroxidase 3 precursor
MARLLQASCLLSLLLAGFVSQSRGQEKSKMDCHGGISGTIYEYGALTIDGEEYIPFKQYA
GKYVLFVNVASYCGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPTLK
YVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTSELLGTSDRLFWEPMKVHDIR
WNFEKFLVGPDGIPIMRWHHRTTVSNVKMDILSYMRRQAALGVKRK
Enzyme 7 Number of Residues 226
Enzyme 7 Molecular Weight 25506
Enzyme 7 Theoretical pI 8.19
Enzyme 7 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 7 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 7 Specific Function Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione
Enzyme 7 Pathways
Enzyme 7 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-20
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 2160390 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P22352 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name GPX3_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >681 bp
ATGGCCCGGCTGCTGCAGGCGTCCTGCCTGCTTTCCCTGCTCCTGGCCGGCTTCGTCTCG
CAGAGCCGGGGACAAGAGAAGTCGAAGATGGACTGCCATGGTGGCATAAGTGGCACCATT
TACGAGTACGGAGCCCTCACCATTGATGGGGAGGAGTACATCCCCTTCAAGCAGTATGCT
GGCAAATACGTCCTCTTTGTCAACGTGGCCAGCTACTGAGGCCTGACGGGCCAGTACATT
GAACTGAATGCACTACAGGAAGAGCTTGCACCATTCGGTCTGGTCATTCTGGGCTTTCCC
TGCAACCAATTTGGAAAACAGGAACCAGGAGAGAACTCAGAGATCCTTCCTACCCTCAAG
TATGTCCGACCAGGTGGAGGCTTTGTCCCTAATTTCCAGCTCTTTGAGAAAGGGGATGTC
AATGGAGAGAAAGAGCAGAAATTCTACACTTTCCTAAAGAACTCCTGTCCTCCCACCTCG
GAGCTCCTGGGTACATCTGACCGCCTCTTCTGGGAACCCATGAAGGTTCACGACATCCGC
TGGAACTTTGAGAAGTTCCTGGTGGGGCCAGATGGTATACCCATCATGCGCTGGCACCAC
CGGACCACGGTCAGCAACGTCAAGATGGACATCCTGTCCTACATGAGGCGGCAGGCAGCC
CTGGGGGTCAAGAGGAAGTAA
Enzyme 7 GenBank Gene ID D00632 Link Image
Enzyme 7 GeneCard ID GPX3 Link Image
Enzyme 7 GenAtlas ID GPX3 Link Image
Enzyme 7 HGNC ID HGNC:4555 Link Image
Enzyme 7 Chromosome Location 5
Enzyme 7 Locus 5q23
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Takahashi K, Akasaka M, Yamamoto Y, Kobayashi C, Mizoguchi J, Koyama J: Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences. J Biochem (Tokyo). 1990 Aug;108(2):145-8. [PubMed Link Image]
  2. Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF: Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood. 1992 Jun 15;79(12):3233-8. [PubMed Link Image]
  3. Yoshimura S, Suemizu H, Taniguchi Y, Arimori K, Kawabe N, Moriuchi T: The human plasma glutathione peroxidase-encoding gene: organization, sequence and localization to chromosome 5q32. Gene. 1994 Aug 5;145(2):293-7. [PubMed Link Image]
  4. Comhair SA, Thomassen MJ, Erzurum SC: Differential induction of extracellular glutathione peroxidase and nitric oxide synthase 2 in airways of healthy individuals exposed to 100% O(2) or cigarette smoke. Am J Respir Cell Mol Biol. 2000 Sep;23(3):350-4. [PubMed Link Image]
  5. Esworthy RS, Chu FF, Paxton RJ, Akman S, Doroshow JH: Characterization and partial amino acid sequence of human plasma glutathione peroxidase. Arch Biochem Biophys. 1991 May 1;286(2):330-6. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6114
Enzyme 8 Name Glutathione peroxidase 2
Enzyme 8 Synonyms
  1. GSHPx-2
  2. GPx-2
  3. Glutathione peroxidase-gastrointestinal
  4. GSHPx-GI
  5. Glutathione peroxidase- related protein 2
  6. Gastrointestinal glutathione peroxidase
  7. GPRP
Enzyme 8 Gene Name GPX2
Enzyme 8 Protein Sequence >Glutathione peroxidase 2
MAFIAKSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLCGTTTRDFTQLNELQCRFPRR
LVVLGFPCNQFGHQENCQNEEILNSLKYVRPGGGYQPTFTLVQKCEVNGQNEHPVFAYLK
DKLPYPYDDPFSLMTDPKLIIWSPVRRSDVAWNFEKFLIGPEGEPFRRYSRTFPTINIEP
DIKRLLKVAI
Enzyme 8 Number of Residues 190
Enzyme 8 Molecular Weight 21907
Enzyme 8 Theoretical pI 7.84
Enzyme 8 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 8 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 8 Specific Function Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors
Enzyme 8 Pathways
Enzyme 8 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4902773 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P18283 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name GPX2_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >573 bp
ATGGCTTTCATTGCCAAGTCCTTCTATGACCTCAGTGCCATCAGCCTGGATGGGGAGAAG
GTAGATTTCAATACGTTCCGGGGCAGGGCCGTGCTGATTGAGAATGTGCGTTCGCTCTGA
GGCACAACCACCCGGGACTTCACCCAGCTCAACGAGCTGCAATGCCGCTTTCCCAGGCGC
CTGGTGGTCCTTGGCTTCCCTTGCAACCAATTTGGACATCAGGAGAACAGTCAGAATGAG
GAGATCCTGAACAGTCTCAAGTATGTCCGTCCTGGGGGTGGATACCAGCCCACCTTCACC
CTTGTCCAAAAATGTGAGGTGAATGGGCAGAACGAGCATCCTGTCTTCGCCTACCTGAAG
GACAAGCTCCCCTACCCTTATGATGACCCATTTTCCCTCATGACCGATCCCAAGCTCATC
ATTTGGAGCCCTGTGCGCCGCTCAGATGTGGCCTGGAACTTTGAGAAGTTCCTCATAGGG
CCGGAGGGAGAGCCCTTCCGACGCTACAGCCGCACCTTCCCAACCATCAACATTGAGCCT
GACATCAAGCGCCTCCTTAAAGTTGCCATATAG
Enzyme 8 GenBank Gene ID X53463 Link Image
Enzyme 8 GeneCard ID GPX2 Link Image
Enzyme 8 GenAtlas ID GPX2 Link Image
Enzyme 8 HGNC ID HGNC:4554 Link Image
Enzyme 8 Chromosome Location 14
Enzyme 8 Locus 14q24.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Akasaka M, Mizoguchi J, Takahashi K: A human cDNA sequence of a novel glutathione peroxidase-related protein. Nucleic Acids Res. 1990 Aug 11;18(15):4619. [PubMed Link Image]
  2. Chu FF, Doroshow JH, Esworthy RS: Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J Biol Chem. 1993 Feb 5;268(4):2571-6. [PubMed Link Image]
  3. Kelner MJ, Bagnell RD, Montoya MA, Lanham KA: Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents. Gene. 2000 May 2;248(1-2):109-16. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6350
Enzyme 9 Name Type I iodothyronine deiodinase
Enzyme 9 Synonyms
  1. Type-I 5' deiodinase
  2. DIOI
  3. Type 1 DI
  4. 5DI
Enzyme 9 Gene Name DIO1
Enzyme 9 Protein Sequence >Type I iodothyronine deiodinase
MGLPQPGLWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMGEKTGMTRNPHFSHDN
WIPTFFSTQYFWFVLKVRWQRLEDTTELGGLAPNCPVVRLSGQRCNIWEFMQGNRPLVLN
FGSCTCPSFMFKFDQFKRLIEDFSSIADFLVIYIEEAHASDGWAFKNNMDIRNHQNLQDR
LQAAHLLLARSPQCPVVVDTMQNQSSQLYAALPERLYIIQEGRILYKGKSGPWNYNPEEV
RAVLEKLHS
Enzyme 9 Number of Residues 249
Enzyme 9 Molecular Weight 28878
Enzyme 9 Theoretical pI 8.72
Enzyme 9 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • thyroxine 5'-deiodinase activity
Process
Component
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 (3,3'-diiodothyronine). Plays a role in providing a source of plasma T3 by deiodination of T4 in peripheral tissues such as liver and kidney
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • 3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-26
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 13195755 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P49895 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name IOD1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >750 bp
ATGGGGCTGCCCCAGCCAGGGCTGTGGCTGAAGAGGCTCTGGGTGCTCTTGGAGGTGGCT
GTGCATGTGGTCGTGGGTAAAGTGCTTCTGATATTGTTTCCAGACAGAGTCAAGCGGAAC
ATCCTGGCCATGGGCGAGAAGACGGGTATGACCAGGAACCCCCATTTCAGCCACGACAAC
TGGATACCAACCTTTTTCAGCACCCAGTATTTCTGGTTCGTCTTGAAGGTCCGTTGGCAG
CGACTAGAGGACACGACTGAGCTAGGGGGTCTGGCCCCAAACTGCCCGGTGGTCCGCCTC
TCAGGACAGAGGTGCAACATTTGGGAGTTTATGCAAGGTAATAGGCCACTGGTGCTGAAT
TTTGGAAGTTGTACCTGACCTTCATTTATGTTCAAATTTGACCAGTTCAAGAGGCTTATT
GAAGACTTTAGTTCCATAGCAGATTTTCTTGTCATTTACATTGAAGAAGCACATGCATCA
GATGGCTGGGCTTTTAAGAACAACATGGACATCAGAAATCACCAGAACCTTCAGGATCGC
CTGCAGGCAGCCCATCTACTGCTGGCCAGGAGCCCCCAGTGCCCTGTGGTGGTGGACACC
ATGCAGAACCAGAGCAGCCAGCTCTACGCAGCACTGCCTGAGAGGCTCTACATAATCCAG
GAGGGCAGGATCCTCTACAAGGGTAAATCTGGCCCTTGGAACTACAACCCAGAGGAAGTT
CGTGCTGTTCTGGAAAAGCTCCACAGTTAA
Enzyme 9 GenBank Gene ID S48220 Link Image
Enzyme 9 GeneCard ID DIO1 Link Image
Enzyme 9 GenAtlas ID DIO1 Link Image
Enzyme 9 HGNC ID HGNC:2883 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1p33-p32
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Mandel SJ, Berry MJ, Kieffer JD, Harney JW, Warne RL, Larsen PR: Cloning and in vitro expression of the human selenoprotein, type I iodothyronine deiodinase. J Clin Endocrinol Metab. 1992 Oct;75(4):1133-9. [PubMed Link Image]
  2. Toyoda N, Zavacki AM, Maia AL, Harney JW, Larsen PR: A novel retinoid X receptor-independent thyroid hormone response element is present in the human type 1 deiodinase gene. Mol Cell Biol. 1995 Sep;15(9):5100-12. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6351
Enzyme 10 Name Type II iodothyronine deiodinase
Enzyme 10 Synonyms
  1. Type-II 5' deiodinase
  2. DIOII
  3. Type 2 DI
  4. 5DII
Enzyme 10 Gene Name DIO2
Enzyme 10 Protein Sequence >Type II iodothyronine deiodinase
MGILSVDLLITLQILPVFFSNCLFLALYDSVILLKHVVLLLSRSKSTRGEWRRMLTSEGL
RCVWKSFLLDAYKQVKLGEDAPNSSVVHVSSTEGGDNSGNGTQEKIAEGATCHLLDFASP
ERPLVVNFGSATCPPFTSQLPAFRKLVEEFSSVADFLLVYIDEAHPSDGWAIPGDSSLSF
EVKKHQNQEDRCAAAQQLLERFSLPPQCRVVADRMDNNANIAYGVAFERVCIVQRQKIAY
LGGKGPFSYNLQEVRHWLEKNFSKR
Enzyme 10 Number of Residues 265
Enzyme 10 Molecular Weight 29600
Enzyme 10 Theoretical pI 7.07
Enzyme 10 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • thyroxine 5'-deiodinase activity
Process
Component
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for providing the brain with appropriate levels of T3 during the critical period of development
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • 3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-22
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 1518542 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q92813 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name IOD2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >822 bp
ATGGGCATCCTCAGCGTAGACTTGCTGATCACACTGCAAATTCTGCCAGTTTTTTTCTCC
AACTGCCTCTTCCTGGCTCTCTATGACTCGGTCATTCTGCTCAAGCACGTGGTGCTGCTG
TTGAGCCGCTCCAAGTCCACTCGCGGAGAGTGGCGGCGCATGCTGACCTCAGAGGGACTG
CGCTGCGTCTGGAAGAGCTTCCTCCTCGATGCCTACAAACAGGTGAAATTGGGTGAGGAT
GCCCCCAATTCCAGTGTGGTGCATGTCTCCAGTACAGAAGGAGGTGACAACAGTGGCAAT
GGTACCCAGGAGAAGATAGCTGAGGGAGCCACATGCCACCTTCTTGACTTTGCCAGCCCT
GAGCGCCCACTAGTGGTCAACTTTGGCTCAGCCACTTGACCTCCTTTCACGAGCCAGCTG
CCAGCCTTCCGCAAACTGGTGGAAGAGTTCTCCTCAGTGGCTGACTTCCTGCTGGTCTAC
ATTGATGAGGCTCATCCATCAGATGGCTGGGCGATACCGGGGGACTCCTCTTTGTCTTTT
GAGGTGAAGAAGCACCAGAACCAGGAAGATCGATGTGCAGCAGCCCAGCAGCTTCTGGAG
CGTTTCTCCTTGCCGCCCCAGTGCCGAGTTGTGGCTGACCGCATGGACAATAACGCCAAC
ATAGCTTACGGGGTAGCCTTTGAACGTGTGTGCATTGTGCAGAGACAGAAAATTGCTTAT
CTGGGAGGAAAGGGCCCCTTCTCCTACAACCTTCAAGAAGTCCGGCATTGGCTGGAGAAG
AATTTCAGCAAGAGATGAAAGAAAACTAGATTAGCTGGTTAA
Enzyme 10 GenBank Gene ID U53506 Link Image
Enzyme 10 GeneCard ID DIO2 Link Image
Enzyme 10 GenAtlas ID DIO2 Link Image
Enzyme 10 HGNC ID HGNC:2884 Link Image
Enzyme 10 Chromosome Location 14
Enzyme 10 Locus 14q24.2-q24.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Croteau W, Davey JC, Galton VA, St Germain DL: Cloning of the mammalian type II iodothyronine deiodinase. A selenoprotein differentially expressed and regulated in human and rat brain and other tissues. J Clin Invest. 1996 Jul 15;98(2):405-17. [PubMed Link Image]
  2. Buettner C, Harney JW, Larsen PR: The 3'-untranslated region of human type 2 iodothyronine deiodinase mRNA contains a functional selenocysteine insertion sequence element. J Biol Chem. 1998 Dec 11;273(50):33374-8. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 10418
Enzyme 11 Name Selenocysteine lyase
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name SCLY
Enzyme 11 Protein Sequence >Selenocysteine lyase
MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGN
PSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTS
KGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQTEVDDI
LAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGK
QRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTP
MIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCN
FSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGR
STTRAEVDLVVQDLKQAVAQLEDQA
Enzyme 11 Number of Residues 445
Enzyme 11 Molecular Weight 48179
Enzyme 11 Theoretical pI Not Available
Enzyme 11 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • metabolism
  • physiological process
Component
Enzyme 11 General Function Amino acid transport and metabolism
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • Pyridoxine 5'-phosphate + Selenocysteine --> L-Alanine + H+ + Pyridoxal 5'-phosphate + Selenide
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 14043901 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q96I15 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name Q96I15_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID BC007891 Link Image
Enzyme 11 GeneCard ID Not Available
Enzyme 11 GenAtlas ID SCLY Link Image
Enzyme 11 HGNC ID HGNC:18161 Link Image
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  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 Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 12722
Enzyme 12 Name Thioredoxin reductase 3
Enzyme 12 Synonyms
  1. Thioredoxin reductase TR2
Enzyme 12 Gene Name TXNRD3
Enzyme 12 Protein Sequence >Thioredoxin reductase 3
GVRVASEGSVRRPSGPVPAPQPPAFRFVSRPGRARSESETLERSPPQSPGPGKAGDAPNR
RSGHVRGARVLSPPGRRARLSSPGPSRSSEAREELRRHLVGLIERSRVVIFSKSYCPHST
RVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAY
QSGLLQKLLQEDLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLG
GTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMTKAIQNHISSLNWGY
RLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGIQGDKEY
CITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKV
GSYMEQHGVKFLRKFIPVMVQQLEKGSPGKLKVLAKSTEGTETIEGVYNTVLLAIGRDSC
TRKIGLEKIGVKINEKSGKIPVNDVEQTNVPYVYAVGDILEDKPELTPVAIQSGKLLAQR
LFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYHTLFWPLEWTVAGR
ENNTCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCG
EVFTTLEITKSSGLDITQKGC
Enzyme 12 Number of Residues 681
Enzyme 12 Molecular Weight 74673
Enzyme 12 Theoretical pI Not Available
Enzyme 12 GO Classification
Function
  • FAD binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • disulfide oxidoreductase activity
  • electron transporter activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, disulfide as acceptor
  • purine nucleotide binding
  • transporter activity
Process
  • cell homeostasis
  • cell redox homeostasis
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • homeostasis
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 12 General Function Energy production and conversion
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • H+ + Nicotinamide adenine dinucleotide phosphate - reduced + Oxidized thioredoxin --> Nicotinamide adenine dinucleotide phosphate + Reduced thioredoxin
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 29476880 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q86VQ6 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q86VQ6_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID BC050032 Link Image
Enzyme 12 GeneCard ID Not Available
Enzyme 12 GenAtlas ID TXNRD3 Link Image
Enzyme 12 HGNC ID HGNC:20667 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  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 Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 12928
Enzyme 13 Name Ethanolaminephosphotransferase 1
Enzyme 13 Synonyms
  1. hEPT1
  2. Selenoprotein I
Enzyme 13 Gene Name SELI
Enzyme 13 Protein Sequence >Ethanolaminephosphotransferase 1
MAGYEYVSPEQLAGFDKYKYSAVDTNPLSLYVMHPFWNTIVKVFPTWLAPNLITFSGFLL
VVFNFLLMAYFDPDFYASAPGHKHVPDWVWIVVGILNFVAYTLDGVDGKQARRTNSSTPL
GELFDHGLDSWSCVYFVVTVYSIFGRGSTGVSVFVLYLLLWVVLFSFILSHWEKYNTGIL
FLPWGYDISQVTISFVYIVTAVVGVEAWYEPFLFNFLYRDLFTAMIIGCALCVTLPMSLL
NFFRSYKNNTLKLNSVYEAMVPLFSPCLLFILSTAWILWSPSDILELHPRVFYFMVGTAF
ANSTCQLIVCQMSSTRCPTLNWLLVPLFLVVLVVNLGVASYVESILLYTLTTAFTLAHIH
YGVRVVKQLSSHFQIYPFSLRKPNSDCLGMEEKNIGL
Enzyme 13 Number of Residues 397
Enzyme 13 Molecular Weight 45182
Enzyme 13 Theoretical pI 6.59
Enzyme 13 GO Classification
Function
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the foramtion of phosphatidylethanolamine via 'Kennedy' pathway
Enzyme 13 Pathways
Enzyme 13 Reactions
  • CDP-ethanolamine + 1,2-diacylglycerol = CMP + a phosphatidylethanolamine [RN:R02057] ALL_REAC R02057
  • (other) R04920 R06364 R07384
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 47-69 84-103 123-145 150-172 179-201 221-243 256-278 291-310 317-339 344-366
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 52078126 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9C0D9 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name SELI_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID BK001426 Link Image
Enzyme 13 GeneCard ID Q9C0D9 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed Link Image]
  2. Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 14707
Enzyme 14 Name O-phosphoseryl-tRNA(Sec) selenium transferase
Enzyme 14 Synonyms
  1. Selenocysteine synthase
  2. Sec synthase
  3. Selenocysteinyl-tRNA(Secsynthase
  4. Sep-tRNA:Sec-tRNA synthase
  5. SepSecS
  6. UGA suppressor tRNA- associated protein
  7. tRNA(Ser/Sec-associated antigenic protein
  8. SLA/LP autoantigen
  9. Soluble liver antigen
  10. SLA
  11. Liver-pancreas antigen
  12. LP
  13. SLA-p35
Enzyme 14 Gene Name SEPSECS
Enzyme 14 Protein Sequence >O-phosphoseryl-tRNA(Sec) selenium transferase
MNRESFAAGERLVSPAYVRQGCEARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAI
MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNS
LVLDIIKLAGVHTVANCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMI
TAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHSTTSCFAPRVPDRLEELAV
ICANYDIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND
SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYN
ERLLHTPHNPISLAMTLKTLDEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFR
GFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVRKERSKESDDNYDKTEDVD
IEEMALKLDNVLLDTYQDASS
Enzyme 14 Number of Residues 501
Enzyme 14 Molecular Weight 55727
Enzyme 14 Theoretical pI 8.13
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl- tRNA(Sec) required for selenoprotein biosynthesis
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 7652498 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9HD40 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name SPCS_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1269 bp
ATGAGCACCTCATACGGCTGCTTCTGGAGAAGGTTCATTCATGGCATTGGACGATCCGGT
GATATTTCTGCTGTGCAACCAAAAGCTGCAGGCTCTAGCCTTTTGAACAAAATTACCAAT
TCTTTGGTCCTGGACATTATAAAGCTGGCTGGTGTCCATACAGTAGCCAACTGCTTTGTA
GTTCCTATGGCAACTGGTATGAGTCTAACTCTGTGTTTCTTAACATTACGACACAAAAGA
CCAAAGGCAAAGTATATTATATGGCCACGAATAGACCAGAAGTCCTGCTTTAAATCCATG
ATCACTGCAGGTTTTGAGCCTGTGGTGATAGAAAATGTTTTGGAAGGTGACGAGCTGCGT
ACAGACCTGAAAGCAGTGGAGGCTAAAGTCCAGGAACTTGGGCCTGATTGCATTCTGTGT
ATTCATTCTACTACATCCTGTTTTGCTCCAAGGGTGCCTGATAGATTAGAAGAACTGGCT
GTGATTTGTGCTAATTATGACATTCCACATATAGTTAATAATGCTTATGGAGTGCAGTCT
TCAAAGTGTATGCATCTCATTCAGCAGGGGGCTCGAGTTGGTAGAATAGATGCTTTTGTT
CAGAGCTTGGACAAAAATTTTATGGTTCCAGTAGGTGGTGCTATAATTGCTGGCTTTAAT
GATTCATTCATTCAGGAAATCAGCAAGATGTATCCAGGAAGAGCTTCAGCTTCACCTTCT
TTAGATGTCCTTATTACTTTATTGTCACTTGGATCAAATGGCTATAAGAAGCTACTAAAA
GAAAGAAAGGAAATGTTTTCATATTTGTCCAACCAAATAAAGAAGTTGTCAGAAGCCTAC
AATGAAAGACTGTTGCATACACCTCACAATCCCATATCTTTAGCTATGACACTTAAAACA
CTAGATGAACACCGTGACAAAGCTGTCACTCAGCTTGGCTCGATGCTTTTTACCAAACAG
GTTTCTGGAGCCAGGGTTGTGCCTCTTGGGTCCATGCAAACTGTGAGTGGCTATACTTTC
AGAGGCTTTATGTCACATACAAATAATTACCCTTGTGCTTACCTCAATGCTGCATCAGCC
ATCGGAATGAAGATGCAGGATGTGGACCTGTTCATAAACAGACTTGACAGGTGTTTAAAG
GCAGTAAGAAAAGAACGAAGTAAAGAGAGTGATGACAATTATGACAAAACTGAAGATGTG
GATATTGAAGAAATGGCTTTAAAACTAGATAATGTACTTCTTGACACATACCAGGATGCT
TCTTCATGA
Enzyme 14 GenBank Gene ID AF146396 Link Image
Enzyme 14 GeneCard ID Q9HD40 Link Image
Enzyme 14 GenAtlas ID SEPSECS Link Image
Enzyme 14 HGNC ID HGNC:30605 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Wies I, Brunner S, Henninger J, Herkel J, Kanzler S, Meyer zum Buschenfelde KH, Lohse AW: Identification of target antigen for SLA/LP autoantibodies in autoimmune hepatitis. Lancet. 2000 Apr 29;355(9214):1510-5. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 14932
Enzyme 15 Name Aflatoxin B1 aldehyde reductase member 4
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name AKR7A4
Enzyme 15 Protein Sequence >Aflatoxin B1 aldehyde reductase member 4
MSRQLSRARPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFLYSDGQSETILGG
LGLRMGSSDCRVKIATKANPWIGNSLKPDSVRSQLETSLKRLQCPUVDLFYLHAPDHSAP
VEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYSATTRQVE
TELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGTQWAEIYRNSFWKEH
HFEGIALVEKALQAAYGASAPSMTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLA
AAEEGPLEPAVVDAFNQAWHLFAHECPNYFI
Enzyme 15 Number of Residues 331
Enzyme 15 Molecular Weight 36914
Enzyme 15 Theoretical pI 6.70
Enzyme 15 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
Component
Enzyme 15 General Function Energy production and conversion
Enzyme 15 Specific Function Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID Q8NHP1 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name ARK74_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AL035413 Link Image
Enzyme 15 GeneCard ID Q8NHP1 Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Praml C, Savelyeva L, Schwab M: Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 in a region frequently altered in human tumour cells. Oncogene. 2003 Jul 24;22(30):4765-73. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 16854
Enzyme 16 Name Methionine-R-sulfoxide reductase B1
Enzyme 16 Synonyms
  1. Selenoprotein X
  2. SelX
Enzyme 16 Gene Name SEPX1
Enzyme 16 Protein Sequence >Methionine-R-sulfoxide reductase B1
MSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPE
HNRSEALKVSCGKCGNGLGHEFLNDGPKPGQSRFUIFSSSLKFVPKGKETSASQGH
Enzyme 16 Number of Residues 116
Enzyme 16 Molecular Weight 12760
Enzyme 16 Theoretical pI 8.50
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 16 Specific Function L-methionine + oxidized thioredoxin = L- methionine R-oxide + reduced thioredoxin
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID Q9NZV6 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name MSRB1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID AF166124 Link Image
Enzyme 16 GeneCard ID Q9NZV6 Link Image
Enzyme 16 GenAtlas ID SEPX1 Link Image
Enzyme 16 HGNC ID HGNC:14133 Link Image
Enzyme 16 Chromosome Location 16
Enzyme 16 Locus 16p13.3
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Lescure A, Gautheret D, Carbon P, Krol A: Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem. 1999 Dec 31;274(53):38147-54. [PubMed Link Image]
  2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 16978
Enzyme 17 Name Selenoprotein P
Enzyme 17 Synonyms
  1. SeP
Enzyme 17 Gene Name SEPP1
Enzyme 17 Protein Sequence >Selenoprotein P
MWRSLGLALALCLLPSGGTESQDQSSLCKQPPAWSIRDQDPMLNSNGSVTVVALLQASUY
LCILQASKLEDLRVKLKKEGYSNISYIVVNHQGISSRLKYTHLKNKVSEHIPVYQQEENQ
TDVWTLLNGSKDDFLIYDRCGRLVYHLGLPFSFLTFPYVEEAIKIAYCEKKCGNCSLTTL
KDEDFCKRVSLATVDKTVETPSPHYHHEHHHNHGHQHLGSSELSENQQPGAPNAPTHPAP
PGLHHHHKHKGQHRQGHPENRDMPASEDLQDLQKKLCRKRCINQLLCKLPTDSELAPRSU
CCHCRHLIFEKTGSAITUQCKENLPSLCSUQGLRAEENITESCQURLPPAAUQISQQLIP
TEASASURUKNQAKKUEUPSN
Enzyme 17 Number of Residues 381
Enzyme 17 Molecular Weight 43174
Enzyme 17 Theoretical pI 7.92
Enzyme 17 GO Classification
Function
  • binding
  • selenium binding
Process
Component
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-19
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein Not Available
Enzyme 17 UniProtKB/Swiss-Prot ID P49908 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name SEPP1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID Z11793 Link Image
Enzyme 17 GeneCard ID P49908 Link Image
Enzyme 17 GenAtlas ID SEPP1 Link Image
Enzyme 17 HGNC ID HGNC:10751 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Hill KE, Lloyd RS, Burk RF: Conserved nucleotide sequences in the open reading frame and 3' untranslated region of selenoprotein P mRNA. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):537-41. [PubMed Link Image]
  2. Akesson B, Bellew T, Burk RF: Purification of selenoprotein P from human plasma. Biochim Biophys Acta. 1994 Feb 16;1204(2):243-9. [PubMed Link Image]
  3. Mostert V, Lombeck I, Abel J: A novel method for the purification of selenoprotein P from human plasma. Arch Biochem Biophys. 1998 Sep 15;357(2):326-30. [PubMed Link Image]
  4. Mostert V: Selenoprotein P: properties, functions, and regulation. Arch Biochem Biophys. 2000 Apr 15;376(2):433-8. [PubMed Link Image]
  5. Burk RF, Hill KE: Selenoprotein P. A selenium-rich extracellular glycoprotein. J Nutr. 1994 Oct;124(10):1891-7. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 16979
Enzyme 18 Name 15 kDa selenoprotein
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name SEP15
Enzyme 18 Protein Sequence >15 kDa selenoprotein
MAAGPSGCLVPAFGLRLLLATVLQAVSAFGAEFSSEACRELGFSSNLLCSSCDLLGQFNL
LQLDPDCRGCCQEEAQFETKKLYAGAILEVCGUKLGRFPQVQAFVRSDKPKLFRGLQIKY
VRGSDPVLKLLDDNGNIAEELSILKWNTDSVEEFLSEKLERI
Enzyme 18 Number of Residues 162
Enzyme 18 Molecular Weight 17791
Enzyme 18 Theoretical pI 4.67
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function May be involved in redox reactions associated with the formation of disulfide bonds. May contribute to the quality control of protein folding in the endoplasmic reticulum
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-28
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID O60613 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name SEP15_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID AF051894 Link Image
Enzyme 18 GeneCard ID O60613 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Gladyshev VN, Jeang KT, Wootton JC, Hatfield DL: A new human selenium-containing protein. Purification, characterization, and cDNA sequence. J Biol Chem. 1998 Apr 10;273(15):8910-5. [PubMed Link Image]
  2. Kumaraswamy E, Malykh A, Korotkov KV, Kozyavkin S, Hu Y, Kwon SY, Moustafa ME, Carlson BA, Berry MJ, Lee BJ, Hatfield DL, Diamond AM, Gladyshev VN: Structure-expression relationships of the 15-kDa selenoprotein gene. Possible role of the protein in cancer etiology. J Biol Chem. 2000 Nov 10;275(45):35540-7. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16980
Enzyme 19 Name Selenoprotein N
Enzyme 19 Synonyms
  1. SelN
Enzyme 19 Gene Name SEPN1
Enzyme 19 Protein Sequence >Selenoprotein N
MGRARPGQRGPPSPGPAAQPPAPPRRRARSLALLGALLAAAAAAAVRVCARHAEAQAAAR
QELALKTLGTDGLFLFSSLDTDGDMYISPEEFKPIAEKLTGSCSVTQTGVQWCSHSSLQP
QLPWLNUSSCLSLLRSTPAASCEEEELPPDPSEETLTIEARFQPLLPETMTKSKDGFLGV
SRLALSGLRNWTAAASPSAVFATRHFQPFLPPPGQELGEPWWIIPSELSMFTGYLSNNRF
YPPPPKGKEVIIHRLLSMFHPRPFVKTRFAPQGAVACLTAISDFYYTVMFRIHAEFQLSE
PPDFPFWFSPAQFTGHIILSKDATHVRDFRLFVPNHRSLNVDMEWLYGASESSNMEVDIG
YIPQMELEATGPSVPSVILDEDGSMIDSHLPSGEPLQFVFEEIKWQQELSWEEAARRLEV
AMYPFKKVSYLPFTEAFDRAKAENKLVHSILLWGALDDQSCUGSGRTLRETVLESSPILT
LLNESFISTWSLVKELEELQNKQENSSHQKLAGLHLEKYSFPVEMMICLPNGTVVHHINA
NYFLDITSVKPEEIESNLFSFSSTFEDPSTATYMQFLKEGLRRGLPLLQP
Enzyme 19 Number of Residues 590
Enzyme 19 Molecular Weight 65827
Enzyme 19 Theoretical pI 5.27
Enzyme 19 GO Classification
Function
  • binding
  • calcium ion binding
  • cation binding
  • ion binding
Process
Component
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function Not Available
Enzyme 19 Signals
  • 1-43
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID Q9NZV5 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name SELN_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AJ306399 Link Image
Enzyme 19 GeneCard ID Q9NZV5 Link Image
Enzyme 19 GenAtlas ID SEPN1 Link Image
Enzyme 19 HGNC ID HGNC:15999 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Lescure A, Gautheret D, Carbon P, Krol A: Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem. 1999 Dec 31;274(53):38147-54. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 16981
Enzyme 20 Name Selenoprotein W
Enzyme 20 Synonyms
  1. SelW
Enzyme 20 Gene Name SEPW1
Enzyme 20 Protein Sequence >Selenoprotein W
MALAVRVVYCGAUGYKSKYLQLKKKLEDEFPGRLDICGEGTPQATGFFEVMVAGKLIHSK
KKGDGYVDTESKFLKLVAAIKAALAQG
Enzyme 20 Number of Residues 87
Enzyme 20 Molecular Weight 9448
Enzyme 20 Theoretical pI 9.74
Enzyme 20 GO Classification
Function
  • binding
  • selenium binding
Process
  • cell homeostasis
  • cell redox homeostasis
  • homeostasis
  • physiological process
Component
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function Not Available
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein Not Available
Enzyme 20 UniProtKB/Swiss-Prot ID P63302 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name SELW_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID U67171 Link Image
Enzyme 20 GeneCard ID P63302 Link Image
Enzyme 20 GenAtlas ID SEPW1 Link Image
Enzyme 20 HGNC ID HGNC:10752 Link Image
Enzyme 20 Chromosome Location 19
Enzyme 20 Locus 19q13.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Gu QP, Beilstein MA, Vendeland SC, Lugade A, Ream W, Whanger PD: Conserved features of selenocysteine insertion sequence (SECIS) elements in selenoprotein W cDNAs from five species. Gene. 1997 Jul 9;193(2):187-96. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 16982
Enzyme 21 Name Selenoprotein S
Enzyme 21 Synonyms
  1. SelS
  2. VCP-interacting membrane protein
Enzyme 21 Gene Name SELS
Enzyme 21 Protein Sequence >Selenoprotein S
MERQEESLSARPALETEGLRFLHTTVGSLLATYGWYIVFSCILLYVVFQKLSARLRALRQ
RQLDRAAAAVEPDVVVKRQEALAAARLKMQEELNAQVEKHKEKLKQLEEEKRRQKIEMWD
SMQEGKSYKGNAKKPQEEDSPGPSTSSVLKRKSDRKPLRGGGYNPLSGEGGGACSWRPGR
RGPSSGGUG
Enzyme 21 Number of Residues 189
Enzyme 21 Molecular Weight 21163
Enzyme 21 Theoretical pI 10.30
Enzyme 21 GO Classification
Function
  • binding
  • selenium binding
Process
  • cellular physiological process
  • intracellular protein transport
  • physiological process
  • protein transport
  • transport
Component
  • cell
  • integral to endoplasmic reticulum membrane
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 28-48
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID Q9BQE4 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name SELS_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID AY324824 Link Image
Enzyme 21 GeneCard ID Q9BQE4 Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location 15
Enzyme 21 Locus 15q26.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed Link Image]
  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 Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 16983
Enzyme 22 Name Selenoprotein K
Enzyme 22 Synonyms
  1. SelK
Enzyme 22 Gene Name SELK
Enzyme 22 Protein Sequence >Selenoprotein K
MVYISNGQVLDSRSQSPWRLSLITDFFWGIAEFVVLFFKTLLQQDVKKRRSYGNSSDSRY
DDGRGPPGNPPRRMGRINHLRGPSPPPMAGGUGR
Enzyme 22 Number of Residues 94
Enzyme 22 Molecular Weight 10645
Enzyme 22 Theoretical pI 11.38
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function Not Available
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID Q9Y6D0 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name SELK_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID AF537132 Link Image
Enzyme 22 GeneCard ID Q9Y6D0 Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed Link Image]
  2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 16984
Enzyme 23 Name Selenoprotein M
Enzyme 23 Synonyms
  1. SelM
Enzyme 23 Gene Name SELM
Enzyme 23 Protein Sequence >Selenoprotein M
MSLLLPPLALLLLLAALVAPATAATAYRPDWNRLSGLTRARVETCGGUQLNRLKEVKAFV
TQDIPFYHNLVMKHLPGADPELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAP
DAQVPPEYVWAPAKPPEETSDHADL
Enzyme 23 Number of Residues 145
Enzyme 23 Molecular Weight 16232
Enzyme 23 Theoretical pI 5.24
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-23
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID Q8WWX9 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name SELM_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence Not Available
Enzyme 23 GenBank Gene ID AY043487 Link Image
Enzyme 23 GeneCard ID Q8WWX9 Link Image
Enzyme 23 GenAtlas ID Not Available
Enzyme 23 HGNC ID Not Available
Enzyme 23 Chromosome Location 22
Enzyme 23 Locus 22q12.2
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Korotkov KV, Novoselov SV, Hatfield DL, Gladyshev VN: Mammalian selenoprotein in which selenocysteine (Sec) incorporation is supported by a new form of Sec insertion sequence element. Mol Cell Biol. 2002 Mar;22(5):1402-11. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 17183
Enzyme 24 Name Selenoprotein T
Enzyme 24 Synonyms
  1. SelT
Enzyme 24 Gene Name SELT
Enzyme 24 Protein Sequence >Selenoprotein T
MRLLLLLLVAASAMVRSEASANLGGVPSKRLKMQYATGPLLKFQICVSUGYRRVFEEYMR
VISQRYPDIRIEGENYLPQPIYRHIASFLSVFKLVLIGLIIVGKDPFAFFGMQAPSIWQW
GQENKVYACMMVFFLSNMIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDNE
MKLNVHMDSIPHHRS
Enzyme 24 Number of Residues 195
Enzyme 24 Molecular Weight 22325
Enzyme 24 Theoretical pI 8.80
Enzyme 24 GO Classification
Function
  • binding
  • selenium binding
Process
  • cell homeostasis
  • cell redox homeostasis
  • homeostasis
  • physiological process
Component
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function Not Available
Enzyme 24 Signals
  • 1-19
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID P62341 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name SELT_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID AF195141 Link Image
Enzyme 24 GeneCard ID P62341 Link Image
Enzyme 24 GenAtlas ID Not Available
Enzyme 24 HGNC ID Not Available
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Kryukov GV, Kryukov VM, Gladyshev VN: New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements. J Biol Chem. 1999 Nov 26;274(48):33888-97. [PubMed Link Image]
  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 Link Image]
Enzyme 24 Metabolite References Not Available