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Identification
HMDB Protein ID HMDBP00653
Secondary Accession Numbers
  • 5925
Name Selenide, water dikinase 1
Synonyms
  1. Selenium donor protein 1
  2. Selenophosphate synthase 1
Gene Name SEPHS1
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Synthesizes selenophosphate from selenide and ATP.
Pathways
  • Selenocompound metabolism
Reactions
Adenosine triphosphate + Hydrogen selenide + Water → Adenosine monophosphate + Phosphoroselenoic acid + Phosphate details
GO Classification
Biological Process
cellular protein modification process
Function
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
selenide, water dikinase activity
Molecular Function
selenide, water dikinase activity
ATP binding
GTP binding
Cellular Location Not Available
Gene Properties
Chromosome Location 10
Locus 10p14
SNPs SEPHS1
Gene Sequence
>1179 bp
ATGTCTACGCGGGAGTCCTTTAACCCGGAAAGTTACGAATTGGACAAAAGCTTCCGGCTA
ACCAGATTCACTGAACTGAAGGGCACAGGCTGCAAAGTGCCCCAAGATGTCCTGCAAAAA
TTGCTGGAATCTTTACAGGAGAACCACTTCCAAGAAGATGAGCAGTTTCTGGGAGCCGTT
ATGCCAAGGCTTGGCATTGGAATGGATACTTGTGTCATTCCTTTGAGGCACGGTGGGCTT
TCCTTGGTTCAAACCACAGATTACATTTACCCGATCGTAGACGACCCTTACATGATGGGC
AGGATAGCGTGTGCCAATGTCCTCAGTGACCTCTATGCAATGGGGGTCACGGAATGTGAC
AATATGCTGATGCTCCTTGGAGTCAGTAATAAAATGACCGACAGGGAAAGGGATAAAGTG
ATGCCTCTGATTATCCAAGGTTTTAAAGACGCAGCTGAGGAAGCAGGAACATCTGTAACA
GGCGGCCAAACAGTACTAAACCCCTGGATTGTCCTGGGAGGAGTGGCTACCACTGTCTGC
CAACCCAATGAATTTATCATGCCAGACAATGCAGTGCCAGGGGACGTGCTGGTGCTGACA
AAACCCCTGGGGACACAGGTGGCAGTGGCTGTGCACCAGTGGCTGGATATCCCTGAGAAA
TGGAATAAGATTAAACTAGTGGTCACCCAAGAAGATGTAGAGCTGGCCTACCAGGAGGCG
ATGATGAACATGGCGAGGCTCAACAGGACAGCTGCAGGACTCATGCACACGTTCAATGCC
CACGCCGCCACTGACATCACGGGCTTCGGGATTTTGGGCCATGCGCAGAACCTGGCCAAG
CAGCAGAGGAACGAGGTGTCGTTTGTAATTCACAACCTCCCGGTGCTGGCCAAGATGGCT
GCGGTGAGCAAGGCCTGCGGAAACATGTTCGGCCTCATGCACGGGACCTGCCCGGAGACT
TCAGGCGGCCTTCTGATCTGTTTACCACGTGAGCAAGCAGCTCGGTTCTGTGCAGAGATA
AAGTCCCCCAAATATGGTGAAGGCCACCAAGCATGGATTATTGGGATTGTAGAGAAGGGC
AACCGCACAGCCAGAATCATAGACAAACCCCGGATCATCGAGGTCGCACCACAAGTGGCC
ACTCAAAATGTGAATCCCACACCCGGGGCCACCTCTTAA
Protein Properties
Number of Residues 392
Molecular Weight 42910.325
Theoretical pI 5.972
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Selenide, water dikinase 1
MSTRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAV
MPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECD
NMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVC
QPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMA
AVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKG
NRTARIIDKPRIIEVAPQVATQNVNPTPGATS
GenBank ID Protein 55957750
UniProtKB/Swiss-Prot ID P49903
UniProtKB/Swiss-Prot Entry Name SPS1_HUMAN
PDB IDs
GenBank Gene ID AL138764
GeneCard ID SEPHS1
GenAtlas ID SEPHS1
HGNC ID HGNC:19685
References
General References
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  2. 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. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed:15164054 ]
  4. Low SC, Harney JW, Berry MJ: Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis. J Biol Chem. 1995 Sep 15;270(37):21659-64. [PubMed:7665581 ]
  5. Wang KT, Wang J, Li LF, Su XD: Crystal structures of catalytic intermediates of human selenophosphate synthetase 1. J Mol Biol. 2009 Jul 24;390(4):747-59. doi: 10.1016/j.jmb.2009.05.032. Epub 2009 May 25. [PubMed:19477186 ]