|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5366 |
| Enzyme 1 Name |
Thioredoxin reductase 1, cytoplasmic precursor |
| Enzyme 1 Synonyms |
- TR
- TR1
|
| Enzyme 1 Gene Name |
TXNRD1 |
| Enzyme 1 Protein Sequence |
>Thioredoxin reductase 1, cytoplasmic precursor
MNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCV
NVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVAL
REKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISS
DDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHM
EEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKI
GLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLYAG
STVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNNK
CYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFT
TLSVTKRSGASILQAGCCG
|
| Enzyme 1 Number of Residues |
499 |
| Enzyme 1 Molecular Weight |
54707 |
| Enzyme 1 Theoretical pI |
6.43 |
| Enzyme 1 GO Classification |
| Function |
- FAD binding
- adenyl nucleotide binding
- binding
- catalytic activity
- disulfide oxidoreductase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on NADH or NADPH
- oxidoreductase activity, acting on NADH or NADPH, disulfide as acceptor
- purine nucleotide binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 1 General Function |
Energy production and conversion |
| Enzyme 1 Specific Function |
Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
1237038  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q16881  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
TRXR1_HUMAN  |
| Enzyme 1 PDB ID |
1H6V  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1494 bp
ATGAACGGCCCTGAAGATCTTCCCAAGTCCTATGACTATGACCTTATCATCATTGGAGGT
GGCTCAGGAGGTCTGGCAGCTGCTAAGGAGGCAGCCCAATATGGCAAGAAGGTGATGGTC
CTGGACTTTGTCACTCCCACCCCTCTTGGAACTAGATGGGGTCTTGGAGGAACATGTGTG
AATGTGGGTTGCATACCTAAAAAACTGATGCATCAAGCAGCTTTGTTAGGACAAGCCCTG
CAAGACTCTCGAAATTATGGATGGAAAGTCGAGGAGACAGTTAAGCATGATTGGGACAGA
ATGATAGAAGCTGTACAGAATCACATTGGCTCTTTGAATTGGGGCTACCGAGTAGCTCTG
CGGGAGAAAAAAGTCGTCTATGAGAATGCTTATGGGCAATTTATTGGTCCTCACAGGATT
AAGGCAACAAATAATAAAGGCAAAGAAAAAATTTATTCAGCAGAGAGTTTTCTCATTGCC
ACTGGTGAAAGACCACGTTACTTGGGCATCCCTGGTGACAAAGAATACTGCATCAGCAGT
GATGATCTTTTCTCCTTGCCTTACTGCCCGGGTAAGACCCTGGTTGTTGGAGCATCCTAT
GTCGCTTTGGAGTGCGCTGGATTTCTTGCTGGTATTGGTTTAGGCGTCACTGTTATGGTT
AGGTCCATTCTTCTTAGAGGATTTGACCAGGACATGGCCAACAAAATTGGTGAACACATG
GAAGAACATGGCATCAAGTTTATAAGACAGTTCGTACCAATTAAAGTTGAACAAATTGAA
GCAGGGACACCAGGCCGACTCAGAGTAGTAGCTCAGTCCACCAATAGTGAGGAAATCATT
GAAGGAGAATATAATACGGTGATGCTGGCAATAGGAAGAGATGCTTGCACAAGAAAAATT
GGCTTAGAAACCGTAGGGGTGAAGATAAATGAAAAGACTGGAAAAATACCTGTCACAGAT
GAAGAACAGACCAATGTGCCTTACATCTATGCCATTGGCGATATATTGGAGGATAAGGTG
GAGCTCACCCCAGTTGCAATCCAGGCAGGAAGATTGCTGGCTCAGAGGCTCTATGCAGGT
TCCACTGTCAAGTGTGACTATGAAAATGTTCCAACCACTGTATTTACTCCTTTGGAATAT
GGTGCTTGTGGCCTTTCTGAGGAGAAAGCTGTGGAGAAGTTTGGGGAAGAAAATATTGAG
GTTTACCATAGTTACTTTTGGCCATTGGAATGGACGATTCCGTCAAGAGATAACAACAAA
TGTTATGCAAAAATAATCTGTAATACTAAAGACAATGAACGTGTTGTGGGCTTTCACGTA
CTGGGTCCAAATGCTGGAGAAGTTACACAAGGCTTTGCAGCTGCGCTCAAATGTGGACTG
ACCAAAAAGCAGCTGGACAGCACAATTGGAATCCACCCTGTCTGTGCAGAGGTATTCACA
ACATTGTCTGTGACCAAGCGCTCTGGGGCAAGCATCCTCCAGGCTGGCTGCTGA
|
| Enzyme 1 GenBank Gene ID |
X91247  |
| Enzyme 1 GeneCard ID |
TXNRD1  |
| Enzyme 1 GenAtlas ID |
TXNRD1  |
| Enzyme 1 HGNC ID |
HGNC:12437  |
| Enzyme 1 Chromosome Location |
12 |
| Enzyme 1 Locus |
12q23-q24.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5390 |
| Enzyme 2 Name |
Thioredoxin reductase 2, mitochondrial precursor |
| Enzyme 2 Synonyms |
- TR3
- TR-beta
- Selenoprotein Z
- SelZ
|
| Enzyme 2 Gene Name |
TXNRD2 |
| Enzyme 2 Protein Sequence |
>Thioredoxin reductase 2, mitochondrial precursor
MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQ
LGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQP
VPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLS
ADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI
GLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDST
TGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDV
VEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHG
QEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALG
IKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCCG
|
| Enzyme 2 Number of Residues |
524 |
| Enzyme 2 Molecular Weight |
56460 |
| Enzyme 2 Theoretical pI |
7.53 |
| Enzyme 2 GO Classification |
| Function |
- FAD binding
- adenyl nucleotide binding
- binding
- catalytic activity
- disulfide oxidoreductase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on NADH or NADPH
- oxidoreductase activity, acting on NADH or NADPH, disulfide as acceptor
- purine nucleotide binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 2 General Function |
Energy production and conversion |
| Enzyme 2 Specific Function |
Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox- regulated cell signaling |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
5764541  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9NNW7  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
TRXR2_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
TXNRD2  |
| Enzyme 2 GenAtlas ID |
TXNRD2  |
| Enzyme 2 HGNC ID |
HGNC:18155  |
| Enzyme 2 Chromosome Location |
22 |
| Enzyme 2 Locus |
22q11.21 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5789 |
| Enzyme 3 Name |
Cystathionine gamma-lyase |
| Enzyme 3 Synonyms |
- Gamma-cystathionase
|
| Enzyme 3 Gene Name |
CTH |
| Enzyme 3 Protein Sequence |
>Cystathionine gamma-lyase
MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEY
SRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRY
FRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHG
DIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQ
NSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQH
ELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVL
KNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS
|
| Enzyme 3 Number of Residues |
405 |
| Enzyme 3 Molecular Weight |
44508 |
| Enzyme 3 Theoretical pI |
6.69 |
| Enzyme 3 GO Classification |
| Function |
| — |
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Amino acid transport and metabolism |
| Enzyme 3 Specific Function |
L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- L-cystathionine + H2O = L-cysteine + ammonia + 2-oxobutanoate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
262476  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P32929  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
CGL_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1218 bp
ATGCAGGAAAAAGACGCCTCCTCACAAGGTTTCCTGCCACACTTCCAACATTTCGCCACG
CAGGCGATCCATGTGGGCCAGGATCCGGAGCAATGGACCTCCAGGGCTGTAGTGCCCCCC
ATCTCACTGTCCACCACGTTCAAGCAAGGGGCGCCTGGCCAGCACTCGGGTTTTGAATAT
AGCCGTTCTGGAAATCCCACTAGGAATTGCCTTGAAAAAGCAGTGGCAGCACTGGATGGG
GCTAAGTACTGTTTGGCCTTTGCTTCAGGTTTAGCAGCCACTGTAACTATTACCCATCTT
TTAAAAGCAGGAGACCAAATTATTTGTATGGATGATGTGTATGGAGGTACAAACAGGTAC
TTCAGGCAAGTGGCATCTGAATTTGGATTAAAGATTTCTTTTGTTGATTGTTCCAAAATC
AAATTACTAGAGGCAGCAATTACACCAGAAACCAAGCTTGTTTGGATCGAAACCCCCACA
AACCCCACCCAGAAGGTGATTGACATTGAAGGCTGTGCACATATTGTCCATAAGCATGGA
GACATTATTTTGGTCGTGGATAACACTTTTATGTCACCATATTTCCAGCGCCCTTTGGCT
CTGGGAGCTGATATTTCTATGTATTCTGCAACAAAATACATGAATGGCCACAGTGATGTT
GTAATGGGCCTGGTGTCTGTTAATTGTGAAAGCCTTCATAATAGACTTCGTTTCTTGCAA
AACTCTCTTGGAGCAGTTCCATCTCCTATTGATTGTTACCTCTGCAATCGAGGTCTGAAG
ACTCTACATGTCCGAATGGAAAAGCATTTCAAAAACGGAATGGCAGTTGCCCAGTTCCTG
GAATCTAATCCTTGGGTAGAAAAGGTTATTTATCCTGGGCTGCCCTCTCATCCACAGCAT
GAGTTGGTGAAGCGTCAGTGTACAGGTTGTACAGGGATGGTCACCTTTTATATTAAGGGC
ACTCTTCAGCATGCTGAGATTTTCCTCAAGAACCTAAAGCTATTTACTCTGGCCGAGAGC
TTGGGAGGATTCGAAAGCCTTGCTGAGCTTCCGGCAATCATGACTCATGCATCAGTTCTT
AAGAATGACAGAGATGTCCTTGGAATTAGTGACACACTGATTCGACTTTCTGTGGGCTTA
GAGGATGAGGAAGACCTACTGGAAGATCTAGATCAAGCTTTGAAGGCAGCACACCCTCCA
AGTGGAATTCACAGCTAG
|
| Enzyme 3 GenBank Gene ID |
S52784  |
| Enzyme 3 GeneCard ID |
CTH  |
| Enzyme 3 GenAtlas ID |
CTH  |
| Enzyme 3 HGNC ID |
HGNC:2501  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p31.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5930 |
| Enzyme 4 Name |
Selenide, water dikinase 2 |
| Enzyme 4 Synonyms |
- Selenophosphate synthetase 2
- Selenium donor protein 2
|
| Enzyme 4 Gene Name |
SEPHS2 |
| Enzyme 4 Protein Sequence |
>Selenide, water dikinase 2
MAEASATGACGEAMAAAEGSSGPAGLTLGRSFSNYRPFEPQALGLSPSWRLTGFSGMKGC
GCKVPQEALLKLLAGLTRPDVRPPLGRGLVGGQEEASQEAGLPAGAGPSPTFPALGIGMD
SCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVS
QSMSEEEREKVTPLMVKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQPNEFIMPD
SAVVGDVLVLTKPLGTQVAVNAHQWLDNPERWNKVKMVVSREEVELAYQEAMFNMATLNR
TAAGLMHTFNAHAATDITGFGILGHSQNLAKQQRNEVSFVIHNLPIIAKMAAVSKASGRF
GLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKP
RVIEVLPRGATAAVLAPDSSNASSEPSS
|
| Enzyme 4 Number of Residues |
448 |
| Enzyme 4 Molecular Weight |
47259 |
| Enzyme 4 Theoretical pI |
5.69 |
| Enzyme 4 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- purine nucleotide binding
- selenide, water dikinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
Synthesizes selenophosphate from selenide and ATP |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + selenide + H2O = AMP + selenophosphate + phosphate
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
14717790  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q99611  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SPS2_HUMAN  |
| 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  |
| Enzyme 4 GeneCard ID |
SEPHS2  |
| Enzyme 4 GenAtlas ID |
SEPHS2  |
| Enzyme 4 HGNC ID |
HGNC:19686  |
| Enzyme 4 Chromosome Location |
16 |
| Enzyme 4 Locus |
16p11.2 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- 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
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6109 |
| Enzyme 5 Name |
Glutathione peroxidase 1 |
| Enzyme 5 Synonyms |
- GSHPx-1
- GPx-1
- Cellular glutathione peroxidase
|
| Enzyme 5 Gene Name |
GPX1 |
| Enzyme 5 Protein Sequence |
>Glutathione peroxidase 1
MCAARLAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLCGTTVRDYTQMNEL
QRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGA
HPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRR
FQTIDIEPDIEALLSQGPSCA
|
| Enzyme 5 Number of Residues |
201 |
| Enzyme 5 Molecular Weight |
21899 |
| Enzyme 5 Theoretical pI |
6.50 |
| Enzyme 5 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 5 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 5 Specific Function |
Protects the hemoglobin in erythrocytes from oxidative breakdown |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
577777  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P07203  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
GPX1_HUMAN  |
| 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  |
| Enzyme 5 GeneCard ID |
GPX1  |
| Enzyme 5 GenAtlas ID |
GPX1  |
| Enzyme 5 HGNC ID |
HGNC:4553  |
| Enzyme 5 Chromosome Location |
3 |
| Enzyme 5 Locus |
3p21.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6110 |
| Enzyme 6 Name |
Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor |
| Enzyme 6 Synonyms |
- PHGPx
- GPX-4
|
| Enzyme 6 Gene Name |
GPX4 |
| Enzyme 6 Protein Sequence |
>Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
MSLGRLCRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVNLDKYR
GFVCIVTNVASQCGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFA
AGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRY
GPMEEPLVIEKDLPHYF
|
| Enzyme 6 Number of Residues |
197 |
| Enzyme 6 Molecular Weight |
22128 |
| Enzyme 6 Theoretical pI |
8.41 |
| Enzyme 6 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 6 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 6 Specific Function |
Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
825667  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P36969  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
GPX4_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
GPX4  |
| Enzyme 6 GenAtlas ID |
GPX4  |
| Enzyme 6 HGNC ID |
HGNC:4556  |
| Enzyme 6 Chromosome Location |
19 |
| Enzyme 6 Locus |
19p13.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6111 |
| Enzyme 7 Name |
Glutathione peroxidase 3 precursor |
| Enzyme 7 Synonyms |
- GSHPx-3
- GPx-3
- Plasma glutathione peroxidase
- GSHPx-P
- Extracellular glutathione peroxidase
- GPx-P
|
| Enzyme 7 Gene Name |
GPX3 |
| Enzyme 7 Protein Sequence |
>Glutathione peroxidase 3 precursor
MARLLQASCLLSLLLAGFVSQSRGQEKSKMDCHGGISGTIYEYGALTIDGEEYIPFKQYA
GKYVLFVNVASYCGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPTLK
YVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTSELLGTSDRLFWEPMKVHDIR
WNFEKFLVGPDGIPIMRWHHRTTVSNVKMDILSYMRRQAALGVKRK
|
| Enzyme 7 Number of Residues |
226 |
| Enzyme 7 Molecular Weight |
25506 |
| Enzyme 7 Theoretical pI |
8.19 |
| Enzyme 7 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 7 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 7 Specific Function |
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
2160390  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P22352  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
GPX3_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>681 bp
ATGGCCCGGCTGCTGCAGGCGTCCTGCCTGCTTTCCCTGCTCCTGGCCGGCTTCGTCTCG
CAGAGCCGGGGACAAGAGAAGTCGAAGATGGACTGCCATGGTGGCATAAGTGGCACCATT
TACGAGTACGGAGCCCTCACCATTGATGGGGAGGAGTACATCCCCTTCAAGCAGTATGCT
GGCAAATACGTCCTCTTTGTCAACGTGGCCAGCTACTGAGGCCTGACGGGCCAGTACATT
GAACTGAATGCACTACAGGAAGAGCTTGCACCATTCGGTCTGGTCATTCTGGGCTTTCCC
TGCAACCAATTTGGAAAACAGGAACCAGGAGAGAACTCAGAGATCCTTCCTACCCTCAAG
TATGTCCGACCAGGTGGAGGCTTTGTCCCTAATTTCCAGCTCTTTGAGAAAGGGGATGTC
AATGGAGAGAAAGAGCAGAAATTCTACACTTTCCTAAAGAACTCCTGTCCTCCCACCTCG
GAGCTCCTGGGTACATCTGACCGCCTCTTCTGGGAACCCATGAAGGTTCACGACATCCGC
TGGAACTTTGAGAAGTTCCTGGTGGGGCCAGATGGTATACCCATCATGCGCTGGCACCAC
CGGACCACGGTCAGCAACGTCAAGATGGACATCCTGTCCTACATGAGGCGGCAGGCAGCC
CTGGGGGTCAAGAGGAAGTAA
|
| Enzyme 7 GenBank Gene ID |
D00632  |
| Enzyme 7 GeneCard ID |
GPX3  |
| Enzyme 7 GenAtlas ID |
GPX3  |
| Enzyme 7 HGNC ID |
HGNC:4555  |
| Enzyme 7 Chromosome Location |
5 |
| Enzyme 7 Locus |
5q23 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6114 |
| Enzyme 8 Name |
Glutathione peroxidase 2 |
| Enzyme 8 Synonyms |
- GSHPx-2
- GPx-2
- Glutathione peroxidase-gastrointestinal
- GSHPx-GI
- Glutathione peroxidase- related protein 2
- Gastrointestinal glutathione peroxidase
- GPRP
|
| Enzyme 8 Gene Name |
GPX2 |
| Enzyme 8 Protein Sequence |
>Glutathione peroxidase 2
MAFIAKSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLCGTTTRDFTQLNELQCRFPRR
LVVLGFPCNQFGHQENCQNEEILNSLKYVRPGGGYQPTFTLVQKCEVNGQNEHPVFAYLK
DKLPYPYDDPFSLMTDPKLIIWSPVRRSDVAWNFEKFLIGPEGEPFRRYSRTFPTINIEP
DIKRLLKVAI
|
| Enzyme 8 Number of Residues |
190 |
| Enzyme 8 Molecular Weight |
21907 |
| Enzyme 8 Theoretical pI |
7.84 |
| Enzyme 8 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 8 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 8 Specific Function |
Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
4902773  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P18283  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
GPX2_HUMAN  |
| 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  |
| Enzyme 8 GeneCard ID |
GPX2  |
| Enzyme 8 GenAtlas ID |
GPX2  |
| Enzyme 8 HGNC ID |
HGNC:4554  |
| Enzyme 8 Chromosome Location |
14 |
| Enzyme 8 Locus |
14q24.1 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6350 |
| Enzyme 9 Name |
Type I iodothyronine deiodinase |
| Enzyme 9 Synonyms |
- Type-I 5' deiodinase
- DIOI
- Type 1 DI
- 5DI
|
| Enzyme 9 Gene Name |
DIO1 |
| Enzyme 9 Protein Sequence |
>Type I iodothyronine deiodinase
MGLPQPGLWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMGEKTGMTRNPHFSHDN
WIPTFFSTQYFWFVLKVRWQRLEDTTELGGLAPNCPVVRLSGQRCNIWEFMQGNRPLVLN
FGSCTCPSFMFKFDQFKRLIEDFSSIADFLVIYIEEAHASDGWAFKNNMDIRNHQNLQDR
LQAAHLLLARSPQCPVVVDTMQNQSSQLYAALPERLYIIQEGRILYKGKSGPWNYNPEEV
RAVLEKLHS
|
| Enzyme 9 Number of Residues |
249 |
| Enzyme 9 Molecular Weight |
28878 |
| Enzyme 9 Theoretical pI |
8.72 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- thyroxine 5'-deiodinase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 (3,3'-diiodothyronine). Plays a role in providing a source of plasma T3 by deiodination of T4 in peripheral tissues such as liver and kidney |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
- 3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
Not Available |
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
13195755  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P49895  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
IOD1_HUMAN  |
| 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  |
| Enzyme 9 GeneCard ID |
DIO1  |
| Enzyme 9 GenAtlas ID |
DIO1  |
| Enzyme 9 HGNC ID |
HGNC:2883  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1p33-p32 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- 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
]
- 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
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6351 |
| Enzyme 10 Name |
Type II iodothyronine deiodinase |
| Enzyme 10 Synonyms |
- Type-II 5' deiodinase
- DIOII
- Type 2 DI
- 5DII
|
| Enzyme 10 Gene Name |
DIO2 |
| Enzyme 10 Protein Sequence |
>Type II iodothyronine deiodinase
MGILSVDLLITLQILPVFFSNCLFLALYDSVILLKHVVLLLSRSKSTRGEWRRMLTSEGL
RCVWKSFLLDAYKQVKLGEDAPNSSVVHVSSTEGGDNSGNGTQEKIAEGATCHLLDFASP
ERPLVVNFGSATCPPFTSQLPAFRKLVEEFSSVADFLLVYIDEAHPSDGWAIPGDSSLSF
EVKKHQNQEDRCAAAQQLLERFSLPPQCRVVADRMDNNANIAYGVAFERVCIVQRQKIAY
LGGKGPFSYNLQEVRHWLEKNFSKR
|
| Enzyme 10 Number of Residues |
265 |
| Enzyme 10 Molecular Weight |
29600 |
| Enzyme 10 Theoretical pI |
7.07 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- thyroxine 5'-deiodinase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for providing the brain with appropriate levels of T3 during the critical period of development |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
- 3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
Not Available |
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
1518542  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q92813  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
IOD2_HUMAN  |
| 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  |
| Enzyme 10 GeneCard ID |
DIO2  |
| Enzyme 10 GenAtlas ID |
DIO2  |
| Enzyme 10 HGNC ID |
HGNC:2884  |
| Enzyme 10 Chromosome Location |
14 |
| Enzyme 10 Locus |
14q24.2-q24.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- 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
]
- 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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
10418 |
| Enzyme 11 Name |
Selenocysteine lyase |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
SCLY |
| Enzyme 11 Protein Sequence |
>Selenocysteine lyase
MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGN
PSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTS
KGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQTEVDDI
LAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGK
QRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTP
MIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCN
FSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGR
STTRAEVDLVVQDLKQAVAQLEDQA
|
| Enzyme 11 Number of Residues |
445 |
| Enzyme 11 Molecular Weight |
48179 |
| Enzyme 11 Theoretical pI |
Not Available |
| Enzyme 11 GO Classification |
| Function |
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Amino acid transport and metabolism |
| Enzyme 11 Specific Function |
Not Available |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
- Pyridoxine 5'-phosphate + Selenocysteine --> L-Alanine + H+ + Pyridoxal 5'-phosphate + Selenide
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
14043901  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q96I15  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
Q96I15_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
Not Available |
| Enzyme 11 GenBank Gene ID |
BC007891  |
| Enzyme 11 GeneCard ID |
Not Available |
| Enzyme 11 GenAtlas ID |
SCLY  |
| Enzyme 11 HGNC ID |
HGNC:18161  |
| Enzyme 11 Chromosome Location |
Not Available |
| Enzyme 11 Locus |
Not Available |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
12722 |
| Enzyme 12 Name |
Thioredoxin reductase 3 |
| Enzyme 12 Synonyms |
- Thioredoxin reductase TR2
|
| Enzyme 12 Gene Name |
TXNRD3 |
| Enzyme 12 Protein Sequence |
>Thioredoxin reductase 3
GVRVASEGSVRRPSGPVPAPQPPAFRFVSRPGRARSESETLERSPPQSPGPGKAGDAPNR
RSGHVRGARVLSPPGRRARLSSPGPSRSSEAREELRRHLVGLIERSRVVIFSKSYCPHST
RVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAY
QSGLLQKLLQEDLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLG
GTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMTKAIQNHISSLNWGY
RLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGIQGDKEY
CITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKV
GSYMEQHGVKFLRKFIPVMVQQLEKGSPGKLKVLAKSTEGTETIEGVYNTVLLAIGRDSC
TRKIGLEKIGVKINEKSGKIPVNDVEQTNVPYVYAVGDILEDKPELTPVAIQSGKLLAQR
LFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYHTLFWPLEWTVAGR
ENNTCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCG
EVFTTLEITKSSGLDITQKGC
|
| Enzyme 12 Number of Residues |
681 |
| Enzyme 12 Molecular Weight |
74673 |
| Enzyme 12 Theoretical pI |
Not Available |
| Enzyme 12 GO Classification |
| Function |
- FAD binding
- adenyl nucleotide binding
- binding
- catalytic activity
- disulfide oxidoreductase activity
- electron transporter activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on NADH or NADPH
- oxidoreductase activity, acting on NADH or NADPH, disulfide as acceptor
- purine nucleotide binding
- transporter activity
|
| Process |
- cell homeostasis
- cell redox homeostasis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- homeostasis
- metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 12 General Function |
Energy production and conversion |
| Enzyme 12 Specific Function |
Not Available |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
- H+ + Nicotinamide adenine dinucleotide phosphate - reduced + Oxidized thioredoxin --> Nicotinamide adenine dinucleotide phosphate + Reduced thioredoxin
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
29476880  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q86VQ6  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
Q86VQ6_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
Not Available |
| Enzyme 12 GenBank Gene ID |
BC050032  |
| Enzyme 12 GeneCard ID |
Not Available |
| Enzyme 12 GenAtlas ID |
TXNRD3  |
| Enzyme 12 HGNC ID |
HGNC:20667  |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
12928 |
| Enzyme 13 Name |
Ethanolaminephosphotransferase 1 |
| Enzyme 13 Synonyms |
- hEPT1
- Selenoprotein I
|
| Enzyme 13 Gene Name |
SELI |
| Enzyme 13 Protein Sequence |
>Ethanolaminephosphotransferase 1
MAGYEYVSPEQLAGFDKYKYSAVDTNPLSLYVMHPFWNTIVKVFPTWLAPNLITFSGFLL
VVFNFLLMAYFDPDFYASAPGHKHVPDWVWIVVGILNFVAYTLDGVDGKQARRTNSSTPL
GELFDHGLDSWSCVYFVVTVYSIFGRGSTGVSVFVLYLLLWVVLFSFILSHWEKYNTGIL
FLPWGYDISQVTISFVYIVTAVVGVEAWYEPFLFNFLYRDLFTAMIIGCALCVTLPMSLL
NFFRSYKNNTLKLNSVYEAMVPLFSPCLLFILSTAWILWSPSDILELHPRVFYFMVGTAF
ANSTCQLIVCQMSSTRCPTLNWLLVPLFLVVLVVNLGVASYVESILLYTLTTAFTLAHIH
YGVRVVKQLSSHFQIYPFSLRKPNSDCLGMEEKNIGL
|
| Enzyme 13 Number of Residues |
397 |
| Enzyme 13 Molecular Weight |
45182 |
| Enzyme 13 Theoretical pI |
6.59 |
| Enzyme 13 GO Classification |
| Function |
| — |
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the foramtion of phosphatidylethanolamine via 'Kennedy' pathway |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- CDP-ethanolamine + 1,2-diacylglycerol = CMP + a phosphatidylethanolamine [RN:R02057] ALL_REAC R02057
- (other) R04920 R06364 R07384
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| 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  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9C0D9  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
SELI_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
Not Available |
| Enzyme 13 GenBank Gene ID |
BK001426  |
| Enzyme 13 GeneCard ID |
Q9C0D9  |
| Enzyme 13 GenAtlas ID |
Not Available |
| Enzyme 13 HGNC ID |
Not Available |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- 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
]
- 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
]
|
| 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 |
- Selenocysteine synthase
- Sec synthase
- Selenocysteinyl-tRNA(Secsynthase
- Sep-tRNA:Sec-tRNA synthase
- SepSecS
- UGA suppressor tRNA- associated protein
- tRNA(Ser/Sec-associated antigenic protein
- SLA/LP autoantigen
- Soluble liver antigen
- SLA
- Liver-pancreas antigen
- LP
- SLA-p35
|
| Enzyme 14 Gene Name |
SEPSECS |
| Enzyme 14 Protein Sequence |
>O-phosphoseryl-tRNA(Sec) selenium transferase
MNRESFAAGERLVSPAYVRQGCEARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAI
MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNS
LVLDIIKLAGVHTVANCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMI
TAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHSTTSCFAPRVPDRLEELAV
ICANYDIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND
SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYN
ERLLHTPHNPISLAMTLKTLDEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFR
GFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVRKERSKESDDNYDKTEDVD
IEEMALKLDNVLLDTYQDASS
|
| Enzyme 14 Number of Residues |
501 |
| Enzyme 14 Molecular Weight |
55727 |
| Enzyme 14 Theoretical pI |
8.13 |
| Enzyme 14 GO Classification |
Not Available |
| Enzyme 14 General Function |
Not Available |
| Enzyme 14 Specific Function |
Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl- tRNA(Sec) required for selenoprotein biosynthesis |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
7652498  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q9HD40  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
SPCS_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1269 bp
ATGAGCACCTCATACGGCTGCTTCTGGAGAAGGTTCATTCATGGCATTGGACGATCCGGT
GATATTTCTGCTGTGCAACCAAAAGCTGCAGGCTCTAGCCTTTTGAACAAAATTACCAAT
TCTTTGGTCCTGGACATTATAAAGCTGGCTGGTGTCCATACAGTAGCCAACTGCTTTGTA
GTTCCTATGGCAACTGGTATGAGTCTAACTCTGTGTTTCTTAACATTACGACACAAAAGA
CCAAAGGCAAAGTATATTATATGGCCACGAATAGACCAGAAGTCCTGCTTTAAATCCATG
ATCACTGCAGGTTTTGAGCCTGTGGTGATAGAAAATGTTTTGGAAGGTGACGAGCTGCGT
ACAGACCTGAAAGCAGTGGAGGCTAAAGTCCAGGAACTTGGGCCTGATTGCATTCTGTGT
ATTCATTCTACTACATCCTGTTTTGCTCCAAGGGTGCCTGATAGATTAGAAGAACTGGCT
GTGATTTGTGCTAATTATGACATTCCACATATAGTTAATAATGCTTATGGAGTGCAGTCT
TCAAAGTGTATGCATCTCATTCAGCAGGGGGCTCGAGTTGGTAGAATAGATGCTTTTGTT
CAGAGCTTGGACAAAAATTTTATGGTTCCAGTAGGTGGTGCTATAATTGCTGGCTTTAAT
GATTCATTCATTCAGGAAATCAGCAAGATGTATCCAGGAAGAGCTTCAGCTTCACCTTCT
TTAGATGTCCTTATTACTTTATTGTCACTTGGATCAAATGGCTATAAGAAGCTACTAAAA
GAAAGAAAGGAAATGTTTTCATATTTGTCCAACCAAATAAAGAAGTTGTCAGAAGCCTAC
AATGAAAGACTGTTGCATACACCTCACAATCCCATATCTTTAGCTATGACACTTAAAACA
CTAGATGAACACCGTGACAAAGCTGTCACTCAGCTTGGCTCGATGCTTTTTACCAAACAG
GTTTCTGGAGCCAGGGTTGTGCCTCTTGGGTCCATGCAAACTGTGAGTGGCTATACTTTC
AGAGGCTTTATGTCACATACAAATAATTACCCTTGTGCTTACCTCAATGCTGCATCAGCC
ATCGGAATGAAGATGCAGGATGTGGACCTGTTCATAAACAGACTTGACAGGTGTTTAAAG
GCAGTAAGAAAAGAACGAAGTAAAGAGAGTGATGACAATTATGACAAAACTGAAGATGTG
GATATTGAAGAAATGGCTTTAAAACTAGATAATGTACTTCTTGACACATACCAGGATGCT
TCTTCATGA
|
| Enzyme 14 GenBank Gene ID |
AF146396  |
| Enzyme 14 GeneCard ID |
Q9HD40  |
| Enzyme 14 GenAtlas ID |
SEPSECS  |
| Enzyme 14 HGNC ID |
HGNC:30605  |
| Enzyme 14 Chromosome Location |
Not Available |
| Enzyme 14 Locus |
Not Available |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- 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
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
14932 |
| Enzyme 15 Name |
Aflatoxin B1 aldehyde reductase member 4 |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
AKR7A4 |
| Enzyme 15 Protein Sequence |
>Aflatoxin B1 aldehyde reductase member 4
MSRQLSRARPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFLYSDGQSETILGG
LGLRMGSSDCRVKIATKANPWIGNSLKPDSVRSQLETSLKRLQCPUVDLFYLHAPDHSAP
VEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYSATTRQVE
TELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGTQWAEIYRNSFWKEH
HFEGIALVEKALQAAYGASAPSMTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLA
AAEEGPLEPAVVDAFNQAWHLFAHECPNYFI
|
| Enzyme 15 Number of Residues |
331 |
| Enzyme 15 Molecular Weight |
36914 |
| Enzyme 15 Theoretical pI |
6.70 |
| Enzyme 15 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 15 General Function |
Energy production and conversion |
| Enzyme 15 Specific Function |
Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
Not Available |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q8NHP1  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
ARK74_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
Not Available |
| Enzyme 15 GenBank Gene ID |
AL035413  |
| Enzyme 15 GeneCard ID |
Q8NHP1  |
| Enzyme 15 GenAtlas ID |
Not Available |
| Enzyme 15 HGNC ID |
Not Available |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- 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
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
16854 |
| Enzyme 16 Name |
Methionine-R-sulfoxide reductase B1 |
| Enzyme 16 Synonyms |
- Selenoprotein X
- SelX
|
| Enzyme 16 Gene Name |
SEPX1 |
| Enzyme 16 Protein Sequence |
>Methionine-R-sulfoxide reductase B1
MSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPE
HNRSEALKVSCGKCGNGLGHEFLNDGPKPGQSRFUIFSSSLKFVPKGKETSASQGH
|
| Enzyme 16 Number of Residues |
116 |
| Enzyme 16 Molecular Weight |
12760 |
| Enzyme 16 Theoretical pI |
8.50 |
| Enzyme 16 GO Classification |
Not Available |
| Enzyme 16 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 16 Specific Function |
L-methionine + oxidized thioredoxin = L- methionine R-oxide + reduced thioredoxin |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
Not Available |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9NZV6  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
MSRB1_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
Not Available |
| Enzyme 16 GenBank Gene ID |
AF166124  |
| Enzyme 16 GeneCard ID |
Q9NZV6  |
| Enzyme 16 GenAtlas ID |
SEPX1  |
| Enzyme 16 HGNC ID |
HGNC:14133  |
| Enzyme 16 Chromosome Location |
16 |
| Enzyme 16 Locus |
16p13.3 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
16978 |
| Enzyme 17 Name |
Selenoprotein P |
| Enzyme 17 Synonyms |
- SeP
|
| Enzyme 17 Gene Name |
SEPP1 |
| Enzyme 17 Protein Sequence |
>Selenoprotein P
MWRSLGLALALCLLPSGGTESQDQSSLCKQPPAWSIRDQDPMLNSNGSVTVVALLQASUY
LCILQASKLEDLRVKLKKEGYSNISYIVVNHQGISSRLKYTHLKNKVSEHIPVYQQEENQ
TDVWTLLNGSKDDFLIYDRCGRLVYHLGLPFSFLTFPYVEEAIKIAYCEKKCGNCSLTTL
KDEDFCKRVSLATVDKTVETPSPHYHHEHHHNHGHQHLGSSELSENQQPGAPNAPTHPAP
PGLHHHHKHKGQHRQGHPENRDMPASEDLQDLQKKLCRKRCINQLLCKLPTDSELAPRSU
CCHCRHLIFEKTGSAITUQCKENLPSLCSUQGLRAEENITESCQURLPPAAUQISQQLIP
TEASASURUKNQAKKUEUPSN
|
| Enzyme 17 Number of Residues |
381 |
| Enzyme 17 Molecular Weight |
43174 |
| Enzyme 17 Theoretical pI |
7.92 |
| Enzyme 17 GO Classification |
| Function |
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
Not Available |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P49908  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
SEPP1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
Not Available |
| Enzyme 17 GenBank Gene ID |
Z11793  |
| Enzyme 17 GeneCard ID |
P49908  |
| Enzyme 17 GenAtlas ID |
SEPP1  |
| Enzyme 17 HGNC ID |
HGNC:10751  |
| Enzyme 17 Chromosome Location |
Not Available |
| Enzyme 17 Locus |
Not Available |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- 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
]
- Akesson B, Bellew T, Burk RF: Purification of selenoprotein P from human plasma. Biochim Biophys Acta. 1994 Feb 16;1204(2):243-9. [PubMed
]
- 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
]
- Mostert V: Selenoprotein P: properties, functions, and regulation. Arch Biochem Biophys. 2000 Apr 15;376(2):433-8. [PubMed
]
- Burk RF, Hill KE: Selenoprotein P. A selenium-rich extracellular glycoprotein. J Nutr. 1994 Oct;124(10):1891-7. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
16979 |
| Enzyme 18 Name |
15 kDa selenoprotein |
| Enzyme 18 Synonyms |
Not Available |
| Enzyme 18 Gene Name |
SEP15 |
| Enzyme 18 Protein Sequence |
>15 kDa selenoprotein
MAAGPSGCLVPAFGLRLLLATVLQAVSAFGAEFSSEACRELGFSSNLLCSSCDLLGQFNL
LQLDPDCRGCCQEEAQFETKKLYAGAILEVCGUKLGRFPQVQAFVRSDKPKLFRGLQIKY
VRGSDPVLKLLDDNGNIAEELSILKWNTDSVEEFLSEKLERI
|
| Enzyme 18 Number of Residues |
162 |
| Enzyme 18 Molecular Weight |
17791 |
| Enzyme 18 Theoretical pI |
4.67 |
| Enzyme 18 GO Classification |
Not Available |
| Enzyme 18 General Function |
Not Available |
| Enzyme 18 Specific Function |
May be involved in redox reactions associated with the formation of disulfide bonds. May contribute to the quality control of protein folding in the endoplasmic reticulum |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
Not Available |
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
Not Available |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
O60613  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
SEP15_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
Not Available |
| Enzyme 18 GenBank Gene ID |
AF051894  |
| Enzyme 18 GeneCard ID |
O60613  |
| Enzyme 18 GenAtlas ID |
Not Available |
| Enzyme 18 HGNC ID |
Not Available |
| Enzyme 18 Chromosome Location |
Not Available |
| Enzyme 18 Locus |
Not Available |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- 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
]
- 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
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
16980 |
| Enzyme 19 Name |
Selenoprotein N |
| Enzyme 19 Synonyms |
- SelN
|
| Enzyme 19 Gene Name |
SEPN1 |
| Enzyme 19 Protein Sequence |
>Selenoprotein N
MGRARPGQRGPPSPGPAAQPPAPPRRRARSLALLGALLAAAAAAAVRVCARHAEAQAAAR
QELALKTLGTDGLFLFSSLDTDGDMYISPEEFKPIAEKLTGSCSVTQTGVQWCSHSSLQP
QLPWLNUSSCLSLLRSTPAASCEEEELPPDPSEETLTIEARFQPLLPETMTKSKDGFLGV
SRLALSGLRNWTAAASPSAVFATRHFQPFLPPPGQELGEPWWIIPSELSMFTGYLSNNRF
YPPPPKGKEVIIHRLLSMFHPRPFVKTRFAPQGAVACLTAISDFYYTVMFRIHAEFQLSE
PPDFPFWFSPAQFTGHIILSKDATHVRDFRLFVPNHRSLNVDMEWLYGASESSNMEVDIG
YIPQMELEATGPSVPSVILDEDGSMIDSHLPSGEPLQFVFEEIKWQQELSWEEAARRLEV
AMYPFKKVSYLPFTEAFDRAKAENKLVHSILLWGALDDQSCUGSGRTLRETVLESSPILT
LLNESFISTWSLVKELEELQNKQENSSHQKLAGLHLEKYSFPVEMMICLPNGTVVHHINA
NYFLDITSVKPEEIESNLFSFSSTFEDPSTATYMQFLKEGLRRGLPLLQP
|
| Enzyme 19 Number of Residues |
590 |
| Enzyme 19 Molecular Weight |
65827 |
| Enzyme 19 Theoretical pI |
5.27 |
| Enzyme 19 GO Classification |
| Function |
- binding
- calcium ion binding
- cation binding
- ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 19 General Function |
Not Available |
| Enzyme 19 Specific Function |
Not Available |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
Not Available |
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
Not Available |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9NZV5  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
SELN_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
Not Available |
| Enzyme 19 GenBank Gene ID |
AJ306399  |
| Enzyme 19 GeneCard ID |
Q9NZV5  |
| Enzyme 19 GenAtlas ID |
SEPN1  |
| Enzyme 19 HGNC ID |
HGNC:15999  |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- 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
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
16981 |
| Enzyme 20 Name |
Selenoprotein W |
| Enzyme 20 Synonyms |
- SelW
|
| Enzyme 20 Gene Name |
SEPW1 |
| Enzyme 20 Protein Sequence |
>Selenoprotein W
MALAVRVVYCGAUGYKSKYLQLKKKLEDEFPGRLDICGEGTPQATGFFEVMVAGKLIHSK
KKGDGYVDTESKFLKLVAAIKAALAQG
|
| Enzyme 20 Number of Residues |
87 |
| Enzyme 20 Molecular Weight |
9448 |
| Enzyme 20 Theoretical pI |
9.74 |
| Enzyme 20 GO Classification |
| Function |
|
| Process |
- cell homeostasis
- cell redox homeostasis
- homeostasis
- physiological process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Not Available |
| Enzyme 20 Specific Function |
May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
Not Available |
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
Not Available |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
P63302  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
SELW_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
U67171  |
| Enzyme 20 GeneCard ID |
P63302  |
| Enzyme 20 GenAtlas ID |
SEPW1  |
| Enzyme 20 HGNC ID |
HGNC:10752  |
| Enzyme 20 Chromosome Location |
19 |
| Enzyme 20 Locus |
19q13.3 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- 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
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
16982 |
| Enzyme 21 Name |
Selenoprotein S |
| Enzyme 21 Synonyms |
- SelS
- VCP-interacting membrane protein
|
| Enzyme 21 Gene Name |
SELS |
| Enzyme 21 Protein Sequence |
>Selenoprotein S
MERQEESLSARPALETEGLRFLHTTVGSLLATYGWYIVFSCILLYVVFQKLSARLRALRQ
RQLDRAAAAVEPDVVVKRQEALAAARLKMQEELNAQVEKHKEKLKQLEEEKRRQKIEMWD
SMQEGKSYKGNAKKPQEEDSPGPSTSSVLKRKSDRKPLRGGGYNPLSGEGGGACSWRPGR
RGPSSGGUG
|
| Enzyme 21 Number of Residues |
189 |
| Enzyme 21 Molecular Weight |
21163 |
| Enzyme 21 Theoretical pI |
10.30 |
| Enzyme 21 GO Classification |
| Function |
|
| Process |
- cellular physiological process
- intracellular protein transport
- physiological process
- protein transport
- transport
|
| Component |
- cell
- integral to endoplasmic reticulum membrane
- intrinsic to endoplasmic reticulum membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane
|
|
| Enzyme 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
Not Available |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9BQE4  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
SELS_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
Not Available |
| Enzyme 21 GenBank Gene ID |
AY324824  |
| Enzyme 21 GeneCard ID |
Q9BQE4  |
| Enzyme 21 GenAtlas ID |
Not Available |
| Enzyme 21 HGNC ID |
Not Available |
| Enzyme 21 Chromosome Location |
15 |
| Enzyme 21 Locus |
15q26.3 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- 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
]
- 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
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
16983 |
| Enzyme 22 Name |
Selenoprotein K |
| Enzyme 22 Synonyms |
- SelK
|
| Enzyme 22 Gene Name |
SELK |
| Enzyme 22 Protein Sequence |
>Selenoprotein K
MVYISNGQVLDSRSQSPWRLSLITDFFWGIAEFVVLFFKTLLQQDVKKRRSYGNSSDSRY
DDGRGPPGNPPRRMGRINHLRGPSPPPMAGGUGR
|
| Enzyme 22 Number of Residues |
94 |
| Enzyme 22 Molecular Weight |
10645 |
| Enzyme 22 Theoretical pI |
11.38 |
| Enzyme 22 GO Classification |
Not Available |
| Enzyme 22 General Function |
Not Available |
| Enzyme 22 Specific Function |
Not Available |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
Not Available |
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
Not Available |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q9Y6D0  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
SELK_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
Not Available |
| Enzyme 22 GenBank Gene ID |
AF537132  |
| Enzyme 22 GeneCard ID |
Q9Y6D0  |
| Enzyme 22 GenAtlas ID |
Not Available |
| Enzyme 22 HGNC ID |
Not Available |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- 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
]
- 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
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
16984 |
| Enzyme 23 Name |
Selenoprotein M |
| Enzyme 23 Synonyms |
- SelM
|
| Enzyme 23 Gene Name |
SELM |
| Enzyme 23 Protein Sequence |
>Selenoprotein M
MSLLLPPLALLLLLAALVAPATAATAYRPDWNRLSGLTRARVETCGGUQLNRLKEVKAFV
TQDIPFYHNLVMKHLPGADPELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAP
DAQVPPEYVWAPAKPPEETSDHADL
|
| Enzyme 23 Number of Residues |
145 |
| Enzyme 23 Molecular Weight |
16232 |
| Enzyme 23 Theoretical pI |
5.24 |
| Enzyme 23 GO Classification |
Not Available |
| Enzyme 23 General Function |
Not Available |
| Enzyme 23 Specific Function |
May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
Not Available |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q8WWX9  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
SELM_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
Not Available |
| Enzyme 23 GenBank Gene ID |
AY043487  |
| Enzyme 23 GeneCard ID |
Q8WWX9  |
| Enzyme 23 GenAtlas ID |
Not Available |
| Enzyme 23 HGNC ID |
Not Available |
| Enzyme 23 Chromosome Location |
22 |
| Enzyme 23 Locus |
22q12.2 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- 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
]
- 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
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
17183 |
| Enzyme 24 Name |
Selenoprotein T |
| Enzyme 24 Synonyms |
- SelT
|
| Enzyme 24 Gene Name |
SELT |
| Enzyme 24 Protein Sequence |
>Selenoprotein T
MRLLLLLLVAASAMVRSEASANLGGVPSKRLKMQYATGPLLKFQICVSUGYRRVFEEYMR
VISQRYPDIRIEGENYLPQPIYRHIASFLSVFKLVLIGLIIVGKDPFAFFGMQAPSIWQW
GQENKVYACMMVFFLSNMIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDNE
MKLNVHMDSIPHHRS
|
| Enzyme 24 Number of Residues |
195 |
| Enzyme 24 Molecular Weight |
22325 |
| Enzyme 24 Theoretical pI |
8.80 |
| Enzyme 24 GO Classification |
| Function |
|
| Process |
- cell homeostasis
- cell redox homeostasis
- homeostasis
- physiological process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Not Available |
| Enzyme 24 Specific Function |
Not Available |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
Not Available |
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
Not Available |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
P62341  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
SELT_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
Not Available |
| Enzyme 24 GenBank Gene ID |
AF195141  |
| Enzyme 24 GeneCard ID |
P62341  |
| Enzyme 24 GenAtlas ID |
Not Available |
| Enzyme 24 HGNC ID |
Not Available |
| Enzyme 24 Chromosome Location |
Not Available |
| Enzyme 24 Locus |
Not Available |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- 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
]
- 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
]
|
| Enzyme 24 Metabolite References |
Not Available |