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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 Link Image
SDF File Show Link Image
PDB File Show Link Image
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
  2. Thioredoxin reductase 2, mitochondrial
  3. Cystathionine gamma-lyase
  4. Selenide, water dikinase 2
  5. Glutathione peroxidase 1
  6. Phospholipid hydroperoxide glutathione peroxidase, mitochondrial
  7. Glutathione peroxidase 3
  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
Enzyme 1 Synonyms
  1. TR
  2. Gene associated with retinoic and interferon-induced mortality 12 protein
  3. GRIM-12
  4. Gene associated with retinoic and IFN-induced mortality 12 protein
  5. KM-102-derived reductase-like factor
  6. Thioredoxin reductase TR1
Enzyme 1 Gene Name TXNRD1
Enzyme 1 Protein Sequence >Thioredoxin reductase 1, cytoplasmic
MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLPENPAGFTSTATADSRALLQ
AYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVPYFVLELDQTEDGRALEGTLSELAAETDL
PVVFVKQRKIGGHGPTLKAYQEGRLQKLLKMNGPEDLPKSYDYDLIIIGGGSGGLAAAKE
AAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKV
EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEK
IYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLA
GIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLRVV
AQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIY
AIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKA
VEKFGEENIEVYHSYFWPLEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQ
GFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQAGCUG
Enzyme 1 Number of Residues 649
Enzyme 1 Molecular Weight 70905.6
Enzyme 1 Theoretical pI 7.42
Enzyme 1 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • antioxidant activity
  • binding
  • catalytic activity
  • disulfide oxidoreductase activity
  • electron carrier activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on a sulfur group of donors
  • oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
  • protein disulfide oxidoreductase activity
  • purine nucleoside binding
  • thioredoxin-disulfide reductase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid
Enzyme 1 Pathways
Enzyme 1 Reactions
  • thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ [RN:R02016]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 148277071 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 >1950 bp
ATGGGCTGCGCCGAGGGCAAGGCAGTGGCGGCGGCCGCCCCAACGGAGCTGCAGACGAAA
GGCAAGAACGGCGATGGCCGCCGTAGGTCAGCTAAAGATCATCACCCTGGTAAAACTTTG
CCAGAGAACCCAGCAGGATTCACCAGCACGGCCACTGCAGACTCCAGAGCCCTGCTTCAG
GCCTATATAGATGGTCACTCTGTGGTCATCTTCAGTAGGTCCACATGCACACGCTGTACT
GAGGTAAAGAAGTTATTTAAATCTCTGTGTGTTCCTTATTTTGTGCTTGAACTTGATCAA
ACAGAGGACGGTCGGGCCCTGGAAGGAACGCTCTCGGAATTGGCCGCGGAAACCGATCTG
CCCGTTGTGTTTGTGAAACAGAGAAAGATAGGCGGCCATGGTCCAACCTTGAAGGCTTAT
CAGGAGGGCAGACTTCAAAAGCTACTAAAAATGAACGGCCCTGAAGATCTTCCCAAGTCC
TATGACTATGACCTTATCATCATTGGAGGTGGCTCAGGAGGTCTGGCAGCTGCTAAGGAG
GCAGCCCAATATGGCAAGAAGGTGATGGTCCTGGACTTTGTCACTCCCACCCCTCTTGGA
ACTAGATGGGGTCTCGGAGGAACATGTGTGAATGTGGGTTGCATACCTAAAAAACTGATG
CATCAAGCAGCTTTGTTAGGACAAGCCCTGCAAGACTCTCGAAATTATGGATGGAAAGTC
GAGGAGACAGTTAAGCATGATTGGGACAGAATGATAGAAGCTGTACAGAATCACATTGGC
TCTTTGAATTGGGGCTACCGAGTAGCTCTGCGGGAGAAAAAAGTCGTCTATGAGAATGCT
TATGGGCAATTTATTGGTCCTCACAGGATTAAGGCAACAAATAATAAAGGCAAAGAAAAA
ATTTATTCAGCAGAGAGATTTCTCATTGCCACTGGTGAAAGACCACGTTACTTGGGCATC
CCTGGTGACAAAGAATACTGCATCAGCAGTGATGATCTTTTCTCCTTGCCTTACTGCCCG
GGTAAGACCCTGGTTGTTGGAGCATCCTATGTCGCTTTGGAGTGCGCTGGATTTCTTGCT
GGTATTGGTTTAGACGTCACTGTTATGGTTAGGTCCATTCTTCTTAGAGGATTTGACCAG
GACATGGCCAACAAAATTGGTGAACACATGGAAGAACATGGCATCAAGTTTATAAGACAG
TTCGTACCAATTAAAGTTGAACAAATTGAAGCAGGGACACCAGGCCGACTCAGAGTAGTA
GCTCAGTCCACCAATAGTGAGGAAATCATTGAAGGAGAATATAATACGGTGATGCTGGCA
ATAGGAAGAGATGCTTGCACAAGAAAAATTGGCTTAGAAACCGTAGGGGTGAAGATAAAT
GAAAAGACTGGAAAAATACCTGTCACAGATGAAGAACAGACCAATGTGCCTTACATCTAT
GCCATTGGCGATATATTGGAGGATAAGGTGGAGCTCACCCCAGTTGCAATCCAGGCAGGA
AGATTGCTGGCTCAGAGGCTCTATGCAGGTTCCACTGTCAAGTGTGACTATGAAAATGTT
CCAACCACTGTATTTACTCCTTTGGAATATGGTGCTTGTGGCCTTTCTGAGGAGAAAGCT
GTGGAGAAGTTTGGGGAAGAAAATATTGAGGTTTACCATAGTTACTTTTGGCCATTGGAA
TGGACGATTCCGTCAAGAGATAACAACAAATGTTATGCAAAAATAATCTGTAATACTAAA
GACAATGAACGTGTTGTGGGCTTTCACGTACTGGGTCCAAATGCTGGAGAAGTTACACAA
GGCTTTGCAGCTGCGCTCAAATGTGGACTGACCAAAAAGCAGCTGGACAGCACAATTGGA
ATCCACCCTGTCTGTGCAGAGGTATTCACAACATTGTCTGTGACCAAGCGCTCTGGGGCA
AGCATCCTCCAGGCTGGCTGCTGAGGTTAA
Enzyme 1 GenBank Gene ID NM_001093771.1 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 1
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]
  2. Koishi R, Kawashima I, Yoshimura C, Sugawara M, Serizawa N: Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102. J Biol Chem. 1997 Jan 24;272(4):2570-7. [PubMed Link Image]
  3. Hofmann ER, Boyanapalli M, Lindner DJ, Weihua X, Hassel BA, Jagus R, Gutierrez PL, Kalvakolanu DV: Thioredoxin reductase mediates cell death effects of the combination of beta interferon and retinoic acid. Mol Cell Biol. 1998 Nov;18(11):6493-504. [PubMed Link Image]
  4. Rundlof AK, Janard M, Miranda-Vizuete A, Arner ES: Evidence for intriguingly complex transcription of human thioredoxin reductase 1. Free Radic Biol Med. 2004 Mar 1;36(5):641-56. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gladyshev VN, Jeang KT, Stadtman TC: Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):6146-51. [PubMed Link Image]
  7. Tamura T, Stadtman TC: A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1006-11. [PubMed Link Image]
  8. Su D, Gladyshev VN: Alternative splicing involving the thioredoxin reductase module in mammals: a glutaredoxin-containing thioredoxin reductase 1. Biochemistry. 2004 Sep 28;43(38):12177-88. [PubMed Link Image]
  9. Damdimopoulos AE, Miranda-Vizuete A, Treuter E, Gustafsson JA, Spyrou G: An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling. J Biol Chem. 2004 Sep 10;279(37):38721-9. Epub 2004 Jun 14. [PubMed Link Image]
  10. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  11. Wong JJ, Pung YF, Sze NS, Chin KC: HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets. Proc Natl Acad Sci U S A. 2006 Jul 11;103(28):10735-40. Epub 2006 Jun 30. [PubMed Link Image]
  12. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  13. Dammeyer P, Damdimopoulos AE, Nordman T, Jimenez A, Miranda-Vizuete A, Arner ES: Induction of cell membrane protrusions by the N-terminal glutaredoxin domain of a rare splice variant of human thioredoxin reductase 1. J Biol Chem. 2008 Feb 1;283(5):2814-21. Epub 2007 Nov 27. [PubMed Link Image]
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  15. Fritz-Wolf K, Urig S, Becker K: The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis. J Mol Biol. 2007 Jun 29;370(1):116-27. Epub 2007 Apr 24. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5390
Enzyme 2 Name Thioredoxin reductase 2, mitochondrial
Enzyme 2 Synonyms
  1. Selenoprotein Z
  2. SelZ
  3. TR-beta
  4. Thioredoxin reductase TR3
Enzyme 2 Gene Name TXNRD2
Enzyme 2 Protein Sequence >Thioredoxin reductase 2, mitochondrial
MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQ
LGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQP
VPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLS
ADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI
GLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDST
TGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDV
VEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHG
QEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALG
IKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG
Enzyme 2 Number of Residues 524
Enzyme 2 Molecular Weight 56506.3
Enzyme 2 Theoretical pI 7.55
Enzyme 2 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • antioxidant activity
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
  • purine nucleoside binding
  • thioredoxin-disulfide reductase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 2 General Function Involved in oxidoreductase activity
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+ [RN:R02016]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
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 2
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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed 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 44507.6
Enzyme 3 Theoretical pI 6.69
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 3 General Function Involved in pyridoxal phosphate binding
Enzyme 3 Specific Function Catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (1) L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate (overall reaction) [RN:R01001]
  • (2) (1a) L-cystathionine = L-cysteine + 2-ammoniobut-2-enoate [RN:R08632]
  • (3) (1b) 2-ammoniobut-2-enoate + H2O = 2-oxobutanoate + NH3 (spontaneous) [RN:R08637]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 62898313 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
CAGGCGATCCATGTGGGCCAGGATCCAGAGCAATGGACCTCCAGGGCTGTAGTGCCCCCC
ATCTCACTGTCCACCACGTTCAAGCAAGGGGCGCCTGGCCAGCACTCGGGTTTTGAATAT
AGCCGTTCTGGAAATCCCACTAGGAATTGCCTTGAAAAAGCAGTGGCAGCACTGGATGGG
GCTAAGTACTGTTTGGCCTTTGCTTCAGGTTTAGCAGCCACTGTAACTATTACCCATCTT
TTAAAAGCAGGAGACCAAATTATTTGTATGGATGATGTGTATGGAGGTACAAACAGGTAC
TTCAGGCAAGTGGCATCTGAATTTGGATTAAAGATTTCTTTTGTTGATTGTTCCAAAATC
AAATTACTAGAGGCAGCAATTACACCAGAAACCAAGCTTGTTTGGATCGAAACCCCCACA
AACCCCACCCAGAAGGTGATTGACATTGAAGGCTGTGCACATATTGTCCATAAGCATGGA
GACATTATTTTGGTCGTGGATAACACTTTTATGTCACCATATTTCCAGCGCCCTTTGGCT
CTGGGAGCTGATATTTCTATGTATTCTGCAACAAAATACATGAATGGCCACAGTGATGTT
GTAATGGGCCTGGTGTCTGTTAATTGTGAAAGCCTTCATAATAGACTTCGTTTCTTGCAA
AACTCTCTTGGAGCAGTTCCATCTCCTATTGATTGTTACCTCTGCAATCGAGGTCTGAAG
ACTCTACATGTCCGAATGGAAAAGCATTTCAAAAACGGAATGGCAGTTGCCCAGTTCCTG
GAATCTAATCCTTGGGTAGAAAAGGTTATTTATCCTGGGCTGCCCTCTCATCCACAGCAT
GAGTTGGTGAAGCGTCAGTGTACAGGTTGTACAGGGATGGTCACCTTTTATATTAAGGGC
ACTCTTCAGCATGCTGAGATTTTCCTCAAGAACCTAAAGCTATTTACTCTGGCCGAGAGC
TTGGGAGGATTCGAAAGCCTTGCTGAGCTTCCGGCAATCATGACTCATGCATCAGTTCTT
AAGAATGACAGAGATGTCCTTGGAATTAGTGACACACTGATTCGACTTTCTGTGGGCTTA
GAGGATGAGGAAGACCTACTGGAAGATCTAGATCAAGCTTTGAAGGCAGCACACCCTCCA
AGTGGAATTCACAGCTAG
Enzyme 3 GenBank Gene ID AK223376 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. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Steegborn C, Clausen T, Sondermann P, Jacob U, Worbs M, Marinkovic S, Huber R, Wahl MC: Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration. J Biol Chem. 1999 Apr 30;274(18):12675-84. [PubMed Link Image]
  5. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  6. Chiku T, Padovani D, Zhu W, Singh S, Vitvitsky V, Banerjee R: H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia. J Biol Chem. 2009 Apr 24;284(17):11601-12. Epub 2009 Mar 4. [PubMed Link Image]
  7. Sun Q, Collins R, Huang S, Holmberg-Schiavone L, Anand GS, Tan CH, van-den-Berg S, Deng LW, Moore PK, Karlberg T, Sivaraman J: Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S. J Biol Chem. 2009 Jan 30;284(5):3076-85. Epub 2008 Nov 19. [PubMed Link Image]
  8. 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]
  9. Zhu W, Lin A, Banerjee R: Kinetic properties of polymorphic variants and pathogenic mutants in human cystathionine gamma-lyase. Biochemistry. 2008 Jun 10;47(23):6226-32. Epub 2008 May 14. [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. Selenium donor protein 2
  2. Selenophosphate synthase 2
Enzyme 4 Gene Name SEPHS2
Enzyme 4 Protein Sequence >Selenide, water dikinase 2
MAEASATGACGEAMAAAEGSSGPAGLTLGRSFSNYRPFEPQALGLSPSWRLTGFSGMKGU
GCKVPQEALLKLLAGLTRPDVRPPLGRGLVGGQEEASQEAGLPAGAGPSPTFPALGIGMD
SCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVS
QSMSEEEREKVTPLMVKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQPNEFIMPD
SAVVGDVLVLTKPLGTQVAVNAHQWLDNPERWNKVKMVVSREEVELAYQEAMFNMATLNR
TAAGLMHTFNAHAATDITGFGILGHSQNLAKQQRNEVSFVIHNLPIIAKMAAVSKASGRF
GLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKP
RVIEVLPRGATAAVLAPDSSNASSEPSS
Enzyme 4 Number of Residues 448
Enzyme 4 Molecular Weight 47304.7
Enzyme 4 Theoretical pI 5.69
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • purine nucleoside binding
  • selenide, water dikinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
Component
Enzyme 4 General Function Involved in catalytic activity
Enzyme 4 Specific Function Synthesizes selenophosphate from selenide and ATP
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + selenide + H2O = AMP + selenophosphate + phosphate [RN:R03595]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
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 1
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]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed 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. GPx-1
  2. GSHPx-1
  3. Cellular glutathione peroxidase
Enzyme 5 Gene Name GPX1
Enzyme 5 Protein Sequence >Glutathione peroxidase 1
MCAARLAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNEL
QRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGA
HPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRR
FQTIDIEPDIEALLSQGPSCA
Enzyme 5 Number of Residues 201
Enzyme 5 Molecular Weight 21945.8
Enzyme 5 Theoretical pI 6.51
Enzyme 5 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 5 General Function Involved in glutathione peroxidase activity
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 [RN:R00274]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
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. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. 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]
  9. 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]
  10. Hamanishi T, Furuta H, Kato H, Doi A, Tamai M, Shimomura H, Sakagashira S, Nishi M, Sasaki H, Sanke T, Nanjo K: Functional variants in the glutathione peroxidase-1 (GPx-1) gene are associated with increased intima-media thickness of carotid arteries and risk of macrovascular diseases in japanese type 2 diabetic patients. Diabetes. 2004 Sep;53(9):2455-60. [PubMed Link Image]
  11. Ichimura Y, Habuchi T, Tsuchiya N, Wang L, Oyama C, Sato K, Nishiyama H, Ogawa O, Kato T: Increased risk of bladder cancer associated with a glutathione peroxidase 1 codon 198 variant. J Urol. 2004 Aug;172(2):728-32. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6110
Enzyme 6 Name Phospholipid hydroperoxide glutathione peroxidase, mitochondrial
Enzyme 6 Synonyms
  1. PHGPx
  2. Glutathione peroxidase 4
  3. GPx-4
  4. GSHPx-4
Enzyme 6 Gene Name GPX4
Enzyme 6 Protein Sequence >Phospholipid hydroperoxide glutathione peroxidase, mitochondrial
MSLGRLCRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVNLDKYR
GFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFA
AGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRY
GPMEEPLVIEKDLPHYF
Enzyme 6 Number of Residues 197
Enzyme 6 Molecular Weight 22174.5
Enzyme 6 Theoretical pI 8.48
Enzyme 6 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 6 General Function Involved in glutathione peroxidase activity
Enzyme 6 Specific Function Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. 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 [RN:R03167]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
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 1
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. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. Scheerer P, Borchert A, Krauss N, Wessner H, Gerth C, Hohne W, Kuhn H: Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4). Biochemistry. 2007 Aug 7;46(31):9041-9. Epub 2007 Jul 13. [PubMed Link Image]
  7. 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
Enzyme 7 Synonyms
  1. GPx-3
  2. GSHPx-3
  3. Extracellular glutathione peroxidase
  4. Plasma glutathione peroxidase
  5. GPx-P
  6. GSHPx-P
Enzyme 7 Gene Name GPX3
Enzyme 7 Protein Sequence >Glutathione peroxidase 3
MARLLQASCLLSLLLAGFVSQSRGQEKSKMDCHGGISGTIYEYGALTIDGEEYIPFKQYA
GKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPTLK
YVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTSELLGTSDRLFWEPMKVHDIR
WNFEKFLVGPDGIPIMRWHHRTTVSNVKMDILSYMRRQAALGVKRK
Enzyme 7 Number of Residues 226
Enzyme 7 Molecular Weight 25552.2
Enzyme 7 Theoretical pI 8.29
Enzyme 7 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 7 General Function Involved in glutathione peroxidase activity
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 [RN:R00274]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-20
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 6006001 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 NM_002084.3 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. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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. GPx-2
  2. GSHPx-2
  3. Gastrointestinal glutathione peroxidase
  4. Glutathione peroxidase-gastrointestinal
  5. GPx-GI
  6. GSHPx-GI
  7. Glutathione peroxidase-related protein 2
  8. GPRP-2
Enzyme 8 Gene Name GPX2
Enzyme 8 Protein Sequence >Glutathione peroxidase 2
MAFIAKSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRDFTQLNELQCRFPRR
LVVLGFPCNQFGHQENCQNEEILNSLKYVRPGGGYQPTFTLVQKCEVNGQNEHPVFAYLK
DKLPYPYDDPFSLMTDPKLIIWSPVRRSDVAWNFEKFLIGPEGEPFRRYSRTFPTINIEP
DIKRLLKVAI
Enzyme 8 Number of Residues 190
Enzyme 8 Molecular Weight 21953.8
Enzyme 8 Theoretical pI 7.93
Enzyme 8 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 8 General Function Involved in glutathione peroxidase activity
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 [RN:R00274]
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 1
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]
  4. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed 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. 5DI
  2. DIOI
  3. Type 1 DI
  4. Type-I 5'-deiodinase
Enzyme 9 Gene Name DIO1
Enzyme 9 Protein Sequence >Type I iodothyronine deiodinase
MGLPQPGLWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMGEKTGMTRNPHFSHDN
WIPTFFSTQYFWFVLKVRWQRLEDTTELGGLAPNCPVVRLSGQRCNIWEFMQGNRPLVLN
FGSCTUPSFMFKFDQFKRLIEDFSSIADFLVIYIEEAHASDGWAFKNNMDIRNHQNLQDR
LQAAHLLLARSPQCPVVVDTMQNQSSQLYAALPERLYIIQEGRILYKGKSGPWNYNPEEV
RAVLEKLHS
Enzyme 9 Number of Residues 249
Enzyme 9 Molecular Weight 28924.2
Enzyme 9 Theoretical pI 8.90
Enzyme 9 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • thyroxine 5'-deiodinase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 9 General Function Involved in thyroxine 5'-deiodinase activity
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 [RN:R03734]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 13-33
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
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. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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. 5DII
  2. DIOII
  3. Type 2 DI
  4. Type-II 5'-deiodinase
Enzyme 10 Gene Name DIO2
Enzyme 10 Protein Sequence >Type II iodothyronine deiodinase
MGILSVDLLITLQILPVFFSNCLFLALYDSVILLKHVVLLLSRSKSTRGEWRRMLTSEGL
RCVWKSFLLDAYKQVKLGEDAPNSSVVHVSSTEGGDNSGNGTQEKIAEGATCHLLDFASP
ERPLVVNFGSATUPPFTSQLPAFRKLVEEFSSVADFLLVYIDEAHPSDGWAIPGDSSLSF
EVKKHQNQEDRCAAAQQLLERFSLPPQCRVVADRMDNNANIAYGVAFERVCIVQRQKIAY
LGGKGPFSYNLQEVRHWLEKNFSKRUKKTRLAG
Enzyme 10 Number of Residues 273
Enzyme 10 Molecular Weight 30551.5
Enzyme 10 Theoretical pI 8.13
Enzyme 10 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • thyroxine 5'-deiodinase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 10 General Function Involved in thyroxine 5'-deiodinase activity
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 [RN:R03734]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 10-34
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
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 1
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]
  3. Ohba K, Yoshioka T, Muraki T: Identification of two novel splicing variants of human type II iodothyronine deiodinase mRNA. Mol Cell Endocrinol. 2001 Feb 14;172(1-2):169-75. [PubMed Link Image]
  4. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Curcio-Morelli C, Zavacki AM, Christofollete M, Gereben B, de Freitas BC, Harney JW, Li Z, Wu G, Bianco AC: Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation. J Clin Invest. 2003 Jul;112(2):189-96. [PubMed Link Image]
  7. Zavacki AM, Arrojo E Drigo R, Freitas BC, Chung M, Harney JW, Egri P, Wittmann G, Fekete C, Gereben B, Bianco AC: The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase. Mol Cell Biol. 2009 Oct;29(19):5339-47. Epub 2009 Aug 3. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 10418
Enzyme 11 Name Selenocysteine lyase
Enzyme 11 Synonyms
  1. hSCL
Enzyme 11 Gene Name SCLY
Enzyme 11 Protein Sequence >Selenocysteine lyase
MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGN
PSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTS
KGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQAEVDDI
LAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGK
QRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTP
MIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCN
FSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGR
STTRAEVDLVVQDLKQAVAQLEDQA
Enzyme 11 Number of Residues 445
Enzyme 11 Molecular Weight 48148.4
Enzyme 11 Theoretical pI 7.13
Enzyme 11 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
Process
  • metabolic process
Component
Enzyme 11 General Function Involved in metabolic process
Enzyme 11 Specific Function Catalyzes the decomposition of L-selenocysteine to L- alanine and elemental selenium
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor [RN:R03598]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 156713448 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q96I15 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name SCLY_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1338 bp
ATGGAGGCGGCCGTGGCGCCGGGGAGGGATGCGCCGGCACCCGCGGCGAGTCAGCCCAGC
GGCTGCGGGAAACACAACTCGCCGGAGAGGAAAGTTTATATGGACTATAATGCAACGACT
CCCCTGGAGCCAGAAGTTATCCAGGCCATGACCAAGGCCATGTGGGAAGCCTGGGGAAAT
CCCAGCAGCCCGTATTCAGCAGGAAGAAAGGCCAAGGATATTATAAATGCAGCTCGGGAA
AGCCTCGCGAAGATGATAGGGGGGAAACCTCAAGATATAATCTTCACTTCCGGGGGCACT
GAGTCAAATAATTTAGTAATCCATTCTGTGGTGAAACATTTCCACGCAAACCAGACCTCA
AAGGGACACACAGGTGGGCACCACAGCCCAGTGAAGGGGGCCAAGCCCCATTTCATTACT
TCCTCGGTGGAACACGACTCCATCCGGCTGCCCCTGGAGCACCTGGTGGAAGAACAAGTG
GCAGCGGTCACCTTTGTCCCGGTGTCCAAGGTGAGCGGGCAGGCAGAGGTGGACGACATC
CTCGCGGCAGTCCGCCCGACCACACGCCTCGTGACCATCATGCTGGCCAACAATGAGACT
GGCATTGTCATGCCTGTCCCTGAAATCAGTCAGCGCATTAAAGCCCTGAACCAGGAACGG
GTGGCAGCTGGGCTACCTCCCATCCTCGTGCACACGGATGCTGCACAGGCCTTGGGGAAG
CAGCGCGTGGATGTGGAGGACCTGGGCGTGGACTTCCTTACAATCGTGGGGCACAAGTTT
TATGGTCCCAGGATTGGCGCACTTTATATACGAGGACTTGGTGAATTTACCCCTCTCTAC
CCTATGCTATTTGGAGGTGGACAAGAACGGAATTTCAGGCCAGGGACAGAGAACACCCCA
ATGATTGCTGGCCTTGGGAAGGCCGCGGAGCTGGTGACCCAGAACTGCGAGGCTTATGAG
GCCCACATGAGGGACGTCCGCGACTACCTGGAAGAGAGGCTGGAAGCTGAATTCGGTCAG
AAGAGAATCCATCTGAATAGCCAGTTTCCAGGCACCCAGCGGCTTCCCAATACCTGTAAC
TTTTCCATCCGGGGACCCCGGCTTCAAGGCCACGTGGTGCTTGCGCAGTGCCGAGTGCTG
ATGGCCAGTGTGGGGGCCGCGTGCCACTCGGACCACGGGGACCAGCCGTCCCCAGTGCTG
CTGAGCTACGGTGTCCCCTTCGACGTGGCCAGGAACGCGCTCCGGCTCAGCGTGGGCCGC
AGCACCACCAGGGCCGAGGTGGACCTCGTCGTGCAGGACCTGAAGCAGGCCGTGGCGCAG
CTGGAGGACCAGGCCTAG
Enzyme 11 GenBank Gene ID NM_016510.4 Link Image
Enzyme 11 GeneCard ID SCLY Link Image
Enzyme 11 GenAtlas ID SCLY Link Image
Enzyme 11 HGNC ID HGNC:18161 Link Image
Enzyme 11 Chromosome Location 2
Enzyme 11 Locus 2q37.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Mihara H, Kurihara T, Watanabe T, Yoshimura T, Esaki N: cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis. J Biol Chem. 2000 Mar 3;275(9):6195-200. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Jafari C, Panzer U, Steinmetz OM, Zahner G, Stahl RA, Harendza S: Enhanced expression of selenocysteine lyase in acute glomerulonephritis and its regulation by AP-1. Cell Mol Biol Lett. 2006;11(3):424-37. [PubMed Link Image]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed 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 and glutathione reductase
  2. Thioredoxin reductase TR2
Enzyme 12 Gene Name TXNRD3
Enzyme 12 Protein Sequence >Thioredoxin reductase 3
VRVASEGSVRRPSGPVPAPQPPAFRFVSRPGRARSESETLERSPPQSPGPGKAGDAPNRR
SGHVRGARVLSPPGRRARLSSPGPSRSSEAREELRRHLVGLIERSRVVIFSKSYCPHSTR
VKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQ
SGLLQKLLQEDLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLGG
TCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMTKAIQNHISSLNWGYR
LSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGIQGDKEYC
ITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVG
SYMEQHGVKFLRKFIPVMVQQLEKGSPGKLKVLAKSTEGTETIEGVYNTVLLAIGRDSCT
RKIGLEKIGVKINEKSGKIPVNDVEQTNVPYVYAVGDILEDKPELTPVAIQSGKLLAQRL
FGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYHTLFWPLEWTVAGRE
NNTCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGE
VFTTLEITKSSGLDITQKGCUG
Enzyme 12 Number of Residues 682
Enzyme 12 Molecular Weight 74822.1
Enzyme 12 Theoretical pI 8.30
Enzyme 12 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • antioxidant activity
  • binding
  • catalytic activity
  • disulfide oxidoreductase activity
  • electron carrier activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on a sulfur group of donors
  • oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
  • protein disulfide oxidoreductase activity
  • purine nucleoside binding
  • thioredoxin-disulfide reductase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 12 General Function Involved in oxidoreductase activity
Enzyme 12 Specific Function Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ [RN:R02016]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 291045266 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q86VQ6 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name TRXR3_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1932 bp
CTGGAGCGGTCGCCGCCGCAGTCGCCCGGGCCGGGAAAGGCGGGCGATGCCCCCAACCGC
CGCTCGGGCCATGTCCGAGGGGCGCGCGTGTTGTCGCCGCCGGGGCGCCGTGCCCGCCTG
TCGTCCCCCGGGCCCAGCCGCTCGTCCGAGGCCCGCGAGGAGCTGCGCCGCCACCTCGTG
GGCCTCATCGAGCGCAGCCGGGTGGTGATCTTCAGCAAGAGCTACTGTCCCCATAGTACT
CGGGTGAAAGAACTCTTTTCTTCTTTGGGAGTCGAATGTAATGTCTTGGAACTTGATCAA
GTTGATGATGGGGCCAGGGTTCAAGAAGTGCTGTCAGAAATCACTAATCAGAAAACTGTG
CCCAATATTTTCGTGAATAAAGTGCATGTAGGTGGATGTGACCAAACTTTCCAGGCATAT
CAGAGTGGTTTGTTACAGAAGCTCCTTCAGGAAGATTTGGCATATGATTATGATCTCATC
ATCATCGGTGGTGGTTCTGGAGGCCTTTCATGTGCGAAGGAAGCTGCCATTTTGGGAAAG
AAAGTTATGGTGCTAGACTTTGTTGTCCCGTCACCTCAGGGCACATCCTGGGGTCTTGGT
GGCACTTGTGTAAATGTAGGTTGTATTCCTAAGAAATTGATGCATCAGGCTGCCCTTTTG
GGGCAGGCATTATGTGACTCAAGGAAATTTGGCTGGGAATATAATCAACAAGTGAGGCAC
AACTGGGAGACAATGACAAAAGCGATTCAGAACCACATCAGCTCTCTAAACTGGGGCTAC
AGGTTGTCTCTGAGGGAAAAGGCTGTGGCCTATGTCAATTCCTATGGAGAATTTGTTGAA
CATCATAAAATAAAGGCAACCAATAAAAAAGGACAGGAGACTTATTATACTGCTGCACAG
TTTGTCATAGCAACGGGTGAAAGGCCACGGTATTTAGGAATCCAAGGAGATAAAGAATAC
TGTATTACTAGTGATGACCTTTTTTCTCTGCCTTATTGCCCTGGCAAAACATTAGTGGTG
GGTGCCTCTTATGTTGCCCTGGAGTGTGCAGGGTTTCTGGCTGGCTTTGGCCTAGATGTC
ACAGTTATGGTACGCTCAATCCTTCTCCGTGGCTTCGACCAAGAAATGGCAGAAAAAGTG
GGTTCCTACATGGAGCAGCATGGTGTGAAGTTCCTACGGAAATTCATACCTGTGATGGTT
CAACAGTTGGAGAAAGGTTCACCTGGAAAGCTGAAAGTGTTGGCTAAATCCACTGAAGGA
ACAGAAACAATTGAAGGAGTCTATAACACAGTTTTGTTAGCTATTGGTCGTGACTCCTGT
ACAAGGAAAATAGGCTTGGAGAAGATTGGTGTCAAAATTAATGAGAAGAGTGGAAAAATA
CCTGTAAATGATGTGGAACAGACCAATGTGCCATATGTCTATGCTGTTGGTGATATTTTG
GAGGATAAGCCAGAGCTCACTCCTGTCGCCATACAGTCAGGCAAGCTGCTAGCTCAGAGA
CTTTTTGGGGCCTCTTTAGAAAAGTGTGATTATATTAATGTTCCGACTACAGTGTTTACT
CCTCTGGAGTATGGTTGCTGTGGATTATCTGAAGAGAAAGCTATTGAAGTATATAAAAAA
GAGAATCTAGAAATATATCATACTTTGTTCTGGCCTCTTGAATGGACAGTAGCTGGCAGA
GAGAACAACACTTGTTACGCAAAGATAATCTGCAATAAATTCGACCATGATCGGGTGATA
GGATTTCATATTCTTGGACCAAACGCCGGTGAGGTTACCCAAGGATTTGCAGCTGCAATG
AAATGTGGGCTCACAAAACAGCTACTTGATGACACCATTGGAATTCACCCCACATGTGGG
GAGGTGTTCACGACTTTGGAAATCACAAAGTCGTCAGGACTAGACATCACTCAGAAAGGC
TGCTGAGGCTAG
Enzyme 12 GenBank Gene ID Not Available
Enzyme 12 GeneCard ID TXNRD3 Link Image
Enzyme 12 GenAtlas ID TXNRD3 Link Image
Enzyme 12 HGNC ID HGNC:20667 Link Image
Enzyme 12 Chromosome Location 3
Enzyme 12 Locus 3q21.3
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. 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]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed 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
  3. SelI
Enzyme 13 Gene Name EPT1
Enzyme 13 Protein Sequence >Ethanolaminephosphotransferase 1
MAGYEYVSPEQLAGFDKYKYSAVDTNPLSLYVMHPFWNTIVKVFPTWLAPNLITFSGFLL
VVFNFLLMAYFDPDFYASAPGHKHVPDWVWIVVGILNFVAYTLDGVDGKQARRTNSSTPL
GELFDHGLDSWSCVYFVVTVYSIFGRGSTGVSVFVLYLLLWVVLFSFILSHWEKYNTGIL
FLPWGYDISQVTISFVYIVTAVVGVEAWYEPFLFNFLYRDLFTAMIIGCALCVTLPMSLL
NFFRSYKNNTLKLNSVYEAMVPLFSPCLLFILSTAWILWSPSDILELHPRVFYFMVGTAF
ANSTCQLIVCQMSSTRCPTLNWLLVPLFLVVLVVNLGVASYVESILLYTLTTAFTLAHIH
YGVRVVKQLSSHFQIYPFSLRKPNSDULGMEEKNIGL
Enzyme 13 Number of Residues 397
Enzyme 13 Molecular Weight 45228.4
Enzyme 13 Theoretical pI 6.59
Enzyme 13 GO Classification
Function
  • catalytic activity
  • phosphotransferase activity, for other substituted phosphate groups
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
Component
  • cell part
  • membrane
Enzyme 13 General Function Involved in phosphotransferase activity, for other substituted phosphate groups
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 formation of phosphatidylethanolamine via 'Kennedy' pathway
Enzyme 13 Pathways
Enzyme 13 Reactions
  • CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine [RN:R02057]
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 EPT1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1194 bp
ATGGCTGGCTACGAATACGTGAGCCCGGAGCAGCTGGCTGGCTTTGATAAGTACAAGTAC
AGTGCTGTGGATACCAATCCACTTTCTCTGTATGTCATGCATCCATTCTGGAACACTATA
GTAAAGGTATTTCCTACTTGGCTGGCGCCCAATCTGATAACTTTTTCTGGCTTTCTGCTG
GTCGTATTCAATTTTCTGCTAATGGCATACTTTGATCCTGACTTTTATGCCTCAGCACCA
GGTCACAAGCACGTGCCTGACTGGGTTTGGATTGTAGTGGGCATCCTCAACTTCGTAGCC
TACACTCTAGATGGTGTGGACGGAAAGCAAGCTCGCAGAACCAATTCTAGCACTCCCTTA
GGGGAGCTTTTTGATCATGGCCTGGATAGTTGGTCATGTGTTTACTTTGTTGTGACTGTT
TATTCCATCTTTGGAAGAGGATCAACTGGTGTCAGTGTTTTTGTTCTTTATCTCCTGCTA
TGGGTAGTTTTGTTTTCTTTCATCCTGTCCCACTGGGAAAAGTATAACACAGGGATTCTT
TTCCTGCCATGGGGATATGACATTAGCCAGGTGACTATTTCTTTTGTCTACATAGTGACT
GCAGTTGTGGGAGTTGAGGCCTGGTATGAACCTTTCCTGTTTAATTTCTTATATAGAGAC
CTATTCACTGCAATGATTATTGGTTGTGCATTATGTGTGACTCTTCCAATGAGTTTATTA
AACTTTTTCAGAAGCTATAAAAATAACACCTTGAAACTCAATTCAGTCTATGAAGCTATG
GTTCCCTTATTTTCTCCATGCTTGCTGTTCATTTTGTCTACAGCGTGGATCCTTTGGTCA
CCTTCAGATATTTTAGAGCTACATCCTAGAGTATTCTACTTTATGGTTGGAACAGCCTTT
GCCAACAGTACATGTCAGCTGATTGTTTGCCAAATGAGTAGTACCCGGTGTCCAACTTTG
AATTGGTTGCTGGTTCCTCTCTTCTTGGTTGTCTTAGTGGTAAACCTAGGAGTAGCCTCT
TACGTTGAGAGCATTCTCCTGTATACATTAACAACTGCTTTTACTCTGGCCCACATCCAT
TATGGAGTACGAGTGGTAAAGCAGCTGAGCAGCCATTTTCAGATTTACCCCTTCTCATTG
AGGAAACCAAACTCAGATTGACTAGGAATGGAAGAAAAGAATATTGGCCTGTAA
Enzyme 13 GenBank Gene ID BK001426 Link Image
Enzyme 13 GeneCard ID EPT1 Link Image
Enzyme 13 GenAtlas ID EPT1 Link Image
Enzyme 13 HGNC ID HGNC:29361 Link Image
Enzyme 13 Chromosome Location 2
Enzyme 13 Locus 2p23.3
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]
  3. Horibata Y, Hirabayashi Y: Identification and characterization of human ethanolaminephosphotransferase1. J Lipid Res. 2007 Mar;48(3):503-8. Epub 2006 Nov 28. [PubMed Link Image]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed 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. Liver-pancreas antigen
  2. LP
  3. SLA-p35
  4. SLA/LP autoantigen
  5. Selenocysteine synthase
  6. Sec synthase
  7. Selenocysteinyl-tRNA(Sec) synthase
  8. Sep-tRNA:Sec-tRNA synthase
  9. SepSecS
  10. Soluble liver antigen
  11. SLA
  12. UGA suppressor tRNA-associated protein
  13. tRNA(Ser/Sec)-associated antigenic protein
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 55725.7
Enzyme 14 Theoretical pI 8.13
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Involved in catalytic activity
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
  • O-phospho-L-seryl-tRNASec + selenophosphate = L-selenocysteinyl-tRNASec + phosphate [RN:R08224]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 267844904 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 >1506 bp
ATGAACCGCGAGAGCTTCGCGGCGGGAGAGCGGCTGGTGTCGCCGGCTTACGTGCGGCAG
GGCTGTGAGGCCCGCCGCTCGCATGAGCACCTCATACGGCTGCTTCTGGAGAAGGGCAAG
TGTCCAGAGAATGGCTGGGATGAAAGTACACTTGAACTCTTTTTACATGAACTTGCAATC
ATGGACAGCAACAATTTCTTAGGCAATTGTGGTGTGGGAGAAAGGGAAGGGAGAGTGGCA
TCCGCACTGGTTGCTCGTCGTCATTACAGGTTCATTCATGGCATTGGACGATCCGGTGAT
ATTTCTGCTGTGCAACCAAAAGCTGCAGGCTCTAGCCTTTTGAACAAAATTACCAATTCT
TTGGTCCTGGACATTATAAAGCTGGCTGGTGTCCATACAGTAGCCAACTGCTTTGTAGTT
CCTATGGCAACTGGTATGAGTCTAACTCTGTGTTTCTTAACATTACGACACAAAAGACCA
AAGGCAAAGTATATTATATGGCCACGAATAGACCAGAAGTCCTGCTTTAAATCCATGATC
ACTGCAGGTTTTGAGCCTGTGGTGATAGAAAATGTTTTGGAAGGTGACGAGCTGCGTACA
GACCTGAAAGCAGTGGAGGCTAAAGTCCAGGAACTTGGGCCTGATTGCATTCTGTGTATT
CATTCTACTACATCCTGTTTTGCTCCAAGGGTGCCTGATAGATTAGAAGAACTGGCTGTG
ATTTGTGCTAATTATGACATTCCACATATAGTTAATAATGCTTATGGAGTGCAGTCTTCA
AAGTGTATGCATCTCATTCAGCAGGGGGCTCGAGTTGGTAGAATAGATGCTTTTGTTCAG
AGCTTGGACAAAAATTTTATGGTTCCAGTAGGTGGTGCTATAATTGCTGGCTTTAATGAT
TCATTCATTCAGGAAATCAGCAAGATGTATCCAGGAAGAGCTTCAGCTTCACCTTCTTTA
GATGTCCTTATTACTTTATTGTCACTTGGATCAAATGGCTATAAGAAGCTACTAAAAGAA
AGAAAGGAAATGTTTTCATATTTGTCCAACCAAATAAAGAAGTTGTCAGAAGCCTACAAT
GAAAGACTGTTGCATACACCTCACAATCCCATATCTTTAGCTATGACACTTAAAACACTA
GATGAACACCGTGACAAAGCTGTCACTCAGCTTGGCTCGATGCTTTTTACCAGACAGGTT
TCTGGAGCCAGGGTTGTGCCTCTTGGGTCCATGCAAACTGTGAGTGGCTATACTTTCAGA
GGCTTTATGTCACATACAAATAATTACCCTTGTGCTTACCTCAATGCTGCATCAGCCATC
GGAATGAAGATGCAGGATGTGGACCTGTTCATAAAGAGACTTGACAGGTGTTTAAAGGCA
GTAAGAAAAGAACGAAGTAAAGAGAGTGATGACAATTATGACAAAACTGAAGATGTGGAT
ATTGAAGAAATGGCTTTAAAACTAGATAATGTACTTCTTGACACATACCAGGATGCTTCT
TCATGA
Enzyme 14 GenBank Gene ID NM_016955.3 Link Image
Enzyme 14 GeneCard ID SEPSECS Link Image
Enzyme 14 GenAtlas ID SEPSECS Link Image
Enzyme 14 HGNC ID HGNC:30605 Link Image
Enzyme 14 Chromosome Location 4
Enzyme 14 Locus 4p15.2
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Costa M, Rodriguez-Sanchez JL, Czaja AJ, Gelpi C: Isolation and characterization of cDNA encoding the antigenic protein of the human tRNP(Ser)Sec complex recognized by autoantibodies from patients withtype-1 autoimmune hepatitis. Clin Exp Immunol. 2000 Aug;121(2):364-74. [PubMed Link Image]
  7. Volkmann M, Martin L, Baurle A, Heid H, Strassburg CP, Trautwein C, Fiehn W, Manns MP: Soluble liver antigen: isolation of a 35-kd recombinant protein (SLA-p35) specifically recognizing sera from patients with autoimmune hepatitis. Hepatology. 2001 Mar;33(3):591-6. [PubMed Link Image]
  8. Herkel J, Heidrich B, Nieraad N, Wies I, Rother M, Lohse AW: Fine specificity of autoantibodies to soluble liver antigen and liver/pancreas. Hepatology. 2002 Feb;35(2):403-8. [PubMed Link Image]
  9. Yuan J, Palioura S, Salazar JC, Su D, O'Donoghue P, Hohn MJ, Cardoso AM, Whitman WB, Soll D: RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea. Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):18923-7. Epub 2006 Dec 1. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed 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
  1. AFB1 aldehyde reductase 3
  2. AFB1-AR 3
  3. Aldoketoreductase 7-like
Enzyme 15 Gene Name AKR7L
Enzyme 15 Protein Sequence >Aflatoxin B1 aldehyde reductase member 4
MSRQLSRARPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFLYSDGQSETILGG
LGLRMGSSDCRVKIATKANPWIGNSLKPDSVRSQLETSLKRLQCPUVDLFYLHAPDHSAP
VEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYSATTRQVE
TELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGTQWAEIYRNHFWKEH
HFEGIALVEKALQAAYGASAPSMTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLA
AAEEGPLEPAVVDAFNQAWHLFAHECPNYFI
Enzyme 15 Number of Residues 331
Enzyme 15 Molecular Weight 36963.5
Enzyme 15 Theoretical pI 6.75
Enzyme 15 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 15 General Function Involved in oxidoreductase activity
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 223718702 Link Image
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 >996 bp
ATGTCCCGGCAGCTGTCGCGGGCCCGGCCAGCCACGGTGCTGGGCGCCATGGAGATGGGG
CGCCGCATGGACGCGCCCACCAGCGCCGCAGTCACGCGCGCCTTCCTGGAGCGCGGCCAC
ACCGAGATAGACACGGCCTTCCTGTACAGCGACGGCCAGTCCGAGACCATCCTTGGCGGC
CTGGGGCTCCGAATGGGCAGCAGCGACTGCAGAGTGAAAATTGCTACCAAGGCCAATCCA
TGGATTGGGAACTCCCTGAAGCCTGACAGTGTCCGATCCCAGCTGGAGACGTCACTGAAG
CGGCTGCAGTGTCCCTGAGTGGACCTCTTCTATCTACATGCACCTGACCACAGCGCCCCG
GTGGAAGAGACACTGCGTGCCTGCCACCAGCTGCACCAGGAGGGCAAGTTCGTGGAGCTT
GGCCTCTCCAACTATGCCGCCTGGGAAGTGGCCGAGATCTGTACCCTCTGCAAGAGCAAC
GGCTGGATCCTGCCCACTGTGTACCAGGGCATGTACAGCGCCACCACCCGGCAGGTGGAA
ACGGAGCTCTTCCCCTGCCTCAGGCACTTTGGACTGAGGTTCTATGCCTACAACCCTCTG
GCTGGGGGCCTGCTGACCGGCAAGTACAAGTATGAGGACAAGGACGGGAAACAGCCCGTG
GGCCGCTTCTTTGGGACTCAGTGGGCAGAGATCTACAGGAATCACTTCTGGAAGGAGCAC
CACTTCGAGGGCATTGCCCTGGTGGAGAAGGCCCTGCAGGCCGCGTATGGCGCCAGCGCT
CCCAGCATGACCTCGGCCGCCCTCCGGTGGATGTACCACCACTCACAGCTGCAGGGTGCC
CACGGGGACGCGGTCATCCTGGGCATGTCCAGCCTGGAGCAGCTGGAGCAGAACTTGGCA
GCGGCAGAGGAAGGGCCCCTGGAGCCGGCTGTCGTGGACGCCTTTAATCAAGCCTGGCAT
TTGTTTGCCCACGAATGTCCCAACTACTTCATCTAA
Enzyme 15 GenBank Gene ID NM_201252.3 Link Image
Enzyme 15 GeneCard ID AKR7L Link Image
Enzyme 15 GenAtlas ID AKR7L Link Image
Enzyme 15 HGNC ID HGNC:24056 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 1p36.13|1p35-p36.1
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. 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. MsrB1
  2. Selenoprotein X
  3. 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 12760.1
Enzyme 16 Theoretical pI 8.50
Enzyme 16 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
  • peptide-methionine-(S)-S-oxide reductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 16 General Function Involved in peptide-methionine-(S)-S-oxide reductase activity
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 14336773 Link Image
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 >351 bp
ATGTCGTTCTGCAGCTTCTTCGGGGGCGAGGTTTTCCAGAATCACTTTGAACCTGGCGTT
TACGTGTGTGCCAAGTGTGGCTATGAGCTGTTCTCCAGCCGCTCGAAGTATGCACACTCG
TCTCCATGGCCGGCGTTCACCGAGACCATTCACGCCGACAGCGTGGCCAAGCGTCCGGAG
CACAATAGATCTGAAGCCTTGAAGGTGTCCTGTGGCAAGTGTGGCAATGGGTTGGGCCAC
GAGTTCCTGAACGACGGCCCCAAGCCGGGGCAGTCCCGATTCTGAATATTCAGCAGCTCG
CTGAAGTTTGTCCCTAAAGGCAAAGAAACTTCTGCCTCACAGGGTCACTAG
Enzyme 16 GenBank Gene ID AE006640 Link Image
Enzyme 16 GeneCard ID SEPX1 Link Image
Enzyme 16 GenAtlas ID SEPX1 Link Image
Enzyme 16 HGNC ID HGNC:14133 Link Image
Enzyme 16 Chromosome Location 1
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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed 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 43173.4
Enzyme 17 Theoretical pI 7.92
Enzyme 17 GO Classification
Function
  • binding
  • selenium binding
Process
Component
Enzyme 17 General Function Involved in selenium binding
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 148277018 Link Image
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 >1146 bp
ATGTGGAGAAGCCTGGGGCTTGCCCTGGCTCTCTGTCTCCTCCCATCGGGAGGAACAGAG
AGCCAGGACCAAAGCTCCTTATGTAAGCAACCCCCAGCCTGGAGCATAAGAGATCAAGAT
CCAATGCTAAACTCCAATGGTTCAGTGACTGTGGTTGCTCTTCTTCAAGCCAGCTGATAC
CTGTGCATACTGCAGGCATCTAAATTAGAAGACCTGCGAGTAAAACTGAAGAAAGAAGGA
TATTCTAATATTTCTTATATTGTTGTTAATCATCAAGGAATCTCTTCTCGATTAAAATAC
ACACATCTTAAGAATAAGGTTTCAGAGCATATTCCTGTTTATCAACAAGAAGAAAACCAA
ACAGATGTCTGGACTCTTTTAAATGGAAGCAAAGATGACTTCCTCATATATGATAGATGT
GGCCGTCTTGTATATCATCTTGGTTTGCCTTTTTCCTTCCTAACTTTCCCATATGTAGAA
GAAGCCATTAAGATTGCTTACTGTGAAAAGAAATGTGGAAACTGCTCTCTCACGACTCTC
AAAGATGAAGACTTTTGTAAACGTGTATCTTTGGCTACTGTGGATAAAACAGTTGAAACT
CCATCGCCTCATTACCATCATGAGCATCATCACAATCATGGACATCAGCACCTTGGCAGC
AGTGAGCTTTCAGAGAATCAGCAACCAGGAGCACCAAATGCTCCTACTCATCCTGCTCCT
CCAGGCCTTCATCACCACCATAAGCACAAGGGTCAGCATAGGCAGGGTCACCCAGAGAAC
CGAGATATGCCAGCAAGTGAAGATTTACAAGATTTACAAAAGAAGCTCTGTCGAAAGAGA
TGTATAAATCAATTACTCTGTAAATTGCCCACAGATTCAGAGTTGGCTCCTAGGAGCTGA
TGCTGCCATTGTCGACATCTGATATTTGAAAAAACAGGGTCTGCAATCACCTGACAGTGT
AAAGAAAACCTCCCATCTTTATGTAGCTGACAGGGACTTCGGGCAGAGGAGAACATAACT
GAATCTTGTCAGTGACGTTTGCCTCCAGCTGCCTGACAAATAAGTCAGCAGCTTATACCC
ACAGAAGCCAGTGCCAGTTGACGCTGAAAGAATCAGGCAAAAAAGTGAGAATGACCTTCA
AACTAA
Enzyme 17 GenBank Gene ID NM_001085486.1 Link Image
Enzyme 17 GeneCard ID SEPP1 Link Image
Enzyme 17 GenAtlas ID SEPP1 Link Image
Enzyme 17 HGNC ID HGNC:10751 Link Image
Enzyme 17 Chromosome Location 5
Enzyme 17 Locus 5q31
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. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. 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]
  6. Mostert V: Selenoprotein P: properties, functions, and regulation. Arch Biochem Biophys. 2000 Apr 15;376(2):433-8. [PubMed Link Image]
  7. Burk RF, Hill KE: Selenoprotein P. A selenium-rich extracellular glycoprotein. J Nutr. 1994 Oct;124(10):1891-7. [PubMed Link Image]
  8. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  10. Zhou W, Ross MM, Tessitore A, Ornstein D, Vanmeter A, Liotta LA, Petricoin EF 3rd: An initial characterization of the serum phosphoproteome. J Proteome Res. 2009 Dec;8(12):5523-31. [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 17790.2
Enzyme 18 Theoretical pI 4.67
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Involved in selenium binding
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 3095111 Link Image
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 >489 bp
ATGGCGGCTGGGCCGAGTGGGTGTCTGGTGCCGGCGTTTGGGCTACGGTTGTTGTTGGCG
ACTGTGCTTCAAGCGGTGTCTGCTTTTGGGGCAGAGTTTTCATCGGAGGCATGCAGAGAG
TTAGGCTTTTCTAGCAACTTGCTTTGCAGCTCTTGTGATCTTCTCGGACAGTTCAACCTG
CTTCAGCTGGATCCTGATTGCAGAGGATGCTGTCAGGAGGAAGCACAATTTGAAACCAAA
AAGCTGTATGCAGGAGCTATTCTTGAAGTTTGTGGATGAAAATTGGGAAGGTTCCCTCAA
GTCCAAGCTTTTGTTAGGAGTGATAAACCCAAACTGTTCAGAGGACTGCAAATCAAGTAT
GTCCGTGGTTCAGACCCTGTATTAAAGCTTTTGGACGACAATGGGAACATTGCTGAAGAA
CTGAGCATTCTCAAATGGAACACAGACAGTGTAGAAGAATTCCTGAGTGAAAAGTTGGAA
CGCATATAA
Enzyme 18 GenBank Gene ID AF051894 Link Image
Enzyme 18 GeneCard ID SEP15 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1p31
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]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Korotkov KV, Kumaraswamy E, Zhou Y, Hatfield DL, Gladyshev VN: Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells. J Biol Chem. 2001 May 4;276(18):15330-6. Epub 2001 Feb 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 65826.1
Enzyme 19 Theoretical pI 5.27
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Involved in protein binding
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 47578099 Link Image
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 >1773 bp
ATGGGCCGGGCCCGGCCGGGCCAACGCGGGCCGCCCAGCCCCGGCCCCGCCGCGCAGCCT
CCCGCGCCACCGCGCCGCCGCGCCCGTTCCCTGGCGCTGCTCGGAGCCCTGCTGGCCGCC
GCCGCTGCCGCCGCCGTCCGGGTCTGCGCCCGCCACGCCGAGGCCCAGGCGGCCGCGCGG
CAGGAACTGGCGCTGAAGACCCTGGGGACAGATGGCCTTTTTCTCTTTTCCTCCTTGGAC
ACTGACGGGGATATGTACATCAGCCCTGAGGAGTTCAAACCCATTGCTGAGAAGCTAACA
GGGTCTTGTTCTGTCACCCAGACTGGAGTGCAGTGGTGCAGTCACAGCTCACTGCAGCCT
CAACTTCCCTGGCTCAATTGATCCTCCTGCCTCAGCCTCCTGAGGTCAACTCCCGCGGCC
AGCTGCGAGGAGGAGGAGTTGCCCCCTGACCCTAGCGAGGAGACGCTCACCATAGAAGCC
CGATTCCAGCCTCTGCTCCCGGAGACCATGACCAAGAGCAAAGATGGCTTCCTAGGGGTC
TCCCGCCTCGCCCTGTCCGGCCTCCGAAACTGGACAGCCGCCGCCTCACCAAGTGCAGTG
TTTGCCACCCGCCACTTCCAGCCCTTCCTTCCCCCGCCAGGCCAGGAGCTGGGTGAGCCC
TGGTGGATCATCCCCAGTGAGCTGAGCATGTTCACTGGCTACCTGTCCAACAACCGCTTC
TATCCACCGCCGCCCAAGGGCAAGGAGGTCATCATCCACCGGCTCCTGAGCATGTTCCAC
CCTCGGCCCTTTGTGAAGACCCGCTTTGCCCCTCAGGGAGCTGTGGCCTGCCTGACTGCC
ATCAGCGACTTCTACTACACTGTGATGTTCCGGATCCATGCCGAGTTCCAGCTCAGTGAG
CCGCCCGACTTCCCCTTTTGGTTCTCCCCTGCTCAGTTCACCGGCCACATCATCCTCTCC
AAAGACGCCACCCACGTCCGCGACTTCCGGCTCTTCGTGCCCAACCACAGGTCTCTGAAT
GTGGACATGGAGTGGCTTTACGGGGCCAGTGAAAGCAGCAACATGGAGGTGGACATCGGC
TACATACCCCAGATGGAGCTGGAGGCCACGGGCCCCTCTGTGCCCTCCGTGATCCTGGAT
GAGGATGGCAGCATGATCGACAGCCACCTGCCTTCAGGGGAGCCCCTGCAGTTTGTGTTT
GAGGAGATCAAGTGGCAGCAGGAGCTGAGCTGGGAGGAGGCTGCCCGGCGCCTGGAGGTG
GCCATGTACCCCTTCAAGAAGGTCTCCTACTTGCCGTTCACTGAGGCCTTCGACCGAGCC
AAGGCTGAGAACAAGCTGGTGCACTCAATCCTGCTGTGGGGGGCCCTGGATGACCAGTCC
TGCTGAGGTTCAGGGCGGACTCTCCGGGAGACTGTCCTGGAAAGTTCGCCCATCCTCACC
CTGCTCAACGAGAGCTTCATCAGCACCTGGTCCCTGGTGAAGGAGCTGGAGGAACTGCAG
AACAACCAGGAGAACTCGTCCCACCAGAAGCTGGCTGGCCTGCACCTGGAGAAGTACAGC
TTCCCCGTGGAGATGATGATCTGCCTGCCCAATGGCACCGTGGTCCATCACATCAATGCC
AACTACTTCTTGGACATCACCTCCGTGAAGCCCGAGGAAATCGAGAGCAATCTCTTCAGC
TTCTCATCCACCTTTGAAGACCCGTCCACGGCCACCTACATGCAGTTCCTGAAGGAGGGA
CTCCGGCGTGGCCTGCCCCTCCTCCAGCCCTAG
Enzyme 19 GenBank Gene ID NM_020451.2 Link Image
Enzyme 19 GeneCard ID SEPN1 Link Image
Enzyme 19 GenAtlas ID SEPN1 Link Image
Enzyme 19 HGNC ID HGNC:15999 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 1p36.13
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Moghadaszadeh B, Petit N, Jaillard C, Brockington M, Roy SQ, Merlini L, Romero N, Estournet B, Desguerre I, Chaigne D, Muntoni F, Topaloglu H, Guicheney P: Mutations in SEPN1 cause congenital muscular dystrophy with spinal rigidity and restrictive respiratory syndrome. Nat Genet. 2001 Sep;29(1):17-8. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Petit N, Lescure A, Rederstorff M, Krol A, Moghadaszadeh B, Wewer UM, Guicheney P: Selenoprotein N: an endoplasmic reticulum glycoprotein with an early developmental expression pattern. Hum Mol Genet. 2003 May 1;12(9):1045-53. [PubMed Link Image]
  6. Ferreiro A, Quijano-Roy S, Pichereau C, Moghadaszadeh B, Goemans N, Bonnemann C, Jungbluth H, Straub V, Villanova M, Leroy JP, Romero NB, Martin JJ, Muntoni F, Voit T, Estournet B, Richard P, Fardeau M, Guicheney P: Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease: reassessing the nosology of early-onset myopathies. Am J Hum Genet. 2002 Oct;71(4):739-49. Epub 2002 Aug 21. [PubMed Link Image]
  7. Ferreiro A, Ceuterick-de Groote C, Marks JJ, Goemans N, Schreiber G, Hanefeld F, Fardeau M, Martin JJ, Goebel HH, Richard P, Guicheney P, Bonnemann CG: Desmin-related myopathy with Mallory body-like inclusions is caused by mutations of the selenoprotein N gene. Ann Neurol. 2004 May;55(5):676-86. [PubMed Link Image]
  8. Maiti B, Arbogast S, Allamand V, Moyle MW, Anderson CB, Richard P, Guicheney P, Ferreiro A, Flanigan KM, Howard MT: A mutation in the SEPN1 selenocysteine redefinition element (SRE) reduces selenocysteine incorporation and leads to SEPN1-related myopathy. Hum Mutat. 2009 Mar;30(3):411-6. [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 9447.9
Enzyme 20 Theoretical pI 9.74
Enzyme 20 GO Classification
Function
  • binding
  • selenium binding
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
Component
Enzyme 20 General Function Involved in selenium binding
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
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 4506887 Link Image
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 >264 bp
ATGGCTCTCGCCGTCCGAGTCGTTTATTGTGGCGCTTGAGGCTACAAGTCCAAGTATCTT
CAGCTCAAGAAGAAGTTAGAAGATGAGTTCCCCGGCCGCCTGGACATCTGCGGCGAGGGA
ACTCCCCAGGCCACCGGGTTCTTTGAAGTGATGGTAGCCGGGAAGTTGATTCACTCTAAG
AAGAAAGGCGATGGCTACGTGGACACAGAAAGCAAGTTTCTGAAGTTGGTGGCCGCCATC
AAAGCCGCCTTGGCTCAGGGCTAA
Enzyme 20 GenBank Gene ID NM_003009.2 Link Image
Enzyme 20 GeneCard ID SEPW1 Link Image
Enzyme 20 GenAtlas ID SEPW1 Link Image
Enzyme 20 HGNC ID HGNC:10752 Link Image
Enzyme 20 Chromosome Location 1
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]
  2. Bellingham J, Gregory-Evans K, Fox MF, Gregory-Evans CY: Gene structure and tissue expression of human selenoprotein W, SEPW1, and identification of a retroprocessed pseudogene, SEPW1P. Biochim Biophys Acta. 2003 Jun 19;1627(2-3):140-6. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed 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 21162.8
Enzyme 21 Theoretical pI 10.30
Enzyme 21 GO Classification
Function
  • binding
  • selenium binding
Process
  • establishment of localization
  • intracellular protein transport
  • protein transport
  • transport
Component
  • cell part
  • integral to endoplasmic reticulum membrane
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 21 General Function Involved in selenium binding
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 33285002 Link Image
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 >570 bp
ATGGAACGCCAAGAGGAGTCTCTGTCCGCGCGGCCGGCCCTGGAGACCGAGGGGCTGCGC
TTCCTGCACACCACGGTGGGCTCCCTGCTGGCCACCTATGGCTGGTACATCGTCTTCAGC
TGCATCCTTCTCTACGTGGTCTTTCAGAAGCTTTCCGCCCGGCTAAGAGCCTTGAGGCAG
AGGCAGCTGGACCGAGCTGCGGCTGCTGTGGAACCTGATGTTGTTGTTAAACGACAAGAA
GCTTTAGCAGCTGCTCGACTGAAAATGCAAGAAGAACTAAATGCGCAAGTTGAAAAGCAT
AAGGAAAAACTGAAACAACTTGAAGAAGAAAAAAGGAGACAGAAGATTGAAATGTGGGAC
AGCATGCAAGAAGGAAAAAGTTACAAAGGAAATGCAAAGAAGCCCCAGGAGGAAGACAGT
CCTGGGCCTTCCACTTCATCTGTCCTGAAACGGAAATCGGACAGAAAGCCTTTGCGGGGA
GGAGGTTATAACCCGTTGTCTGGTGAAGGAGGCGGAGCTTGCTCCTGGAGACCTGGACGC
AGAGGCCCGTCATCTGGCGGATGAGGCTAA
Enzyme 21 GenBank Gene ID NM_018445.4 Link Image
Enzyme 21 GeneCard ID SELS Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location 1
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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ye Y, Shibata Y, Yun C, Ron D, Rapoport TA: A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature. 2004 Jun 24;429(6994):841-7. [PubMed Link Image]
  5. Ye Y, Shibata Y, Kikkert M, van Voorden S, Wiertz E, Rapoport TA: Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14132-8. Epub 2005 Sep 26. [PubMed Link Image]
  6. Lilley BN, Ploegh HL: Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14296-301. Epub 2005 Sep 26. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed 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 10644.9
Enzyme 22 Theoretical pI 11.38
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Involved in response to oxidative stress
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 24431324 Link Image
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 >285 bp
ATGGTTTACATCTCGAACGGACAAGTGTTGGACAGCCGGAGTCAGTCTCCATGGAGATTA
TCTTTGATAACAGATTTCTTCTGGGGAATAGCTGAGTTTGTGGTTTTGTTTTTCAAAACT
CTGCTTCAGCAAGATGTGAAAAAAAGAAGAAGCTATGGAAACTCATCTGATTCCAGATAT
GATGATGGAAGAGGGCCACCAGGAAACCCTCCCCGAAGAATGGGTAGAATCAATCATCTG
CGTGGCCCTAGTCCCCCTCCAATGGCTGGTGGATGAGGAAGGTAA
Enzyme 22 GenBank Gene ID AF537132 Link Image
Enzyme 22 GeneCard ID SELK Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location 3
Enzyme 22 Locus 3p21.31
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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed 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 16231.5
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 17975597 Link Image
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 >438 bp
ATGAGCCTCCTGTTGCCTCCGCTGGCGCTGCTGCTGCTTCTCGCGGCGCTTGTGGCCCCA
GCCACAGCCGCCACTGCCTACCGGCCGGACTGGAACCGTCTGAGCGGCCTAACCCGCGCC
CGGGTAGAGACCTGCGGGGGATGACAGCTGAACCGCCTAAAGGAGGTGAAGGCTTTCGTC
ACGCAGGACATTCCATTCTATCACAACCTGGTGATGAAACACCTCCCTGGGGCCGACCCT
GAGCTCGTGCTGCTGGGCCGCCGCTACGAGGAACTAGAGCGCATCCCACTCAGTGAAATG
ACCCGCGAAGAGATCAATGCGCTAGTGCAGGAGCTCGGCTTCTACCGCAAGGCGGCGCCC
GACGCGCAGGTGCCCCCCGAGTACGTGTGGGCGCCCGCGAAGCCCCCAGAGGAAACTTCG
GACCACGCTGACCTGTAG
Enzyme 23 GenBank Gene ID NM_080430.2 Link Image
Enzyme 23 GeneCard ID SELM Link Image
Enzyme 23 GenAtlas ID Not Available
Enzyme 23 HGNC ID Not Available
Enzyme 23 Chromosome Location 2
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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed 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 22324.0
Enzyme 24 Theoretical pI 8.80
Enzyme 24 GO Classification
Function
  • binding
  • selenium binding
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
Component
Enzyme 24 General Function Involved in selenium binding
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-19
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 42789380 Link Image
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 >588 bp
ATGAGGCTTCTGCTGCTTCTCCTAGTGGCGGCGTCTGCGATGGTCCGGAGCGAGGCCTCG
GCCAATCTGGGCGGCGTGCCCAGCAAGAGATTAAAGATGCAGTACGCCACGGGGCCGCTG
CTCAAGTTCCAGATTTGTGTTTCCTGAGGTTATAGGCGGGTGTTTGAGGAGTACATGCGG
GTTATTAGCCAGCGGTACCCAGACATCCGCATTGAAGGAGAGAATTACCTCCCTCAACCA
ATATATAGACACATAGCATCTTTCCTGTCAGTCTTCAAACTAGTATTAATAGGCTTAATA
ATTGTTGGCAAGGATCCTTTTGCTTTCTTTGGCATGCAAGCTCCTAGCATCTGGCAGTGG
GGCCAAGAAAATAAGGTTTATGCATGTATGATGGTTTTCTTCTTGAGCAACATGATTGAG
AACCAGTGTATGTCAACAGGTGCATTTGAGATAACTTTAAATGATGTACCTGTGTGGTCT
AAGCTGGAATCTGGTCACCTTCCATCCATGCAACAACTTGTTCAAATTCTTGACAATGAA
ATGAAGCTCAATGTGCATATGGATTCAATCCCACACCATCGATCATAG
Enzyme 24 GenBank Gene ID NM_016275.3 Link Image
Enzyme 24 GeneCard ID SELT Link Image
Enzyme 24 GenAtlas ID Not Available
Enzyme 24 HGNC ID Not Available
Enzyme 24 Chromosome Location 3
Enzyme 24 Locus 3q25.1
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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available