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Selenide, water dikinase 1 (EC 2.7.9.3) (Selenium donor protein 1) (Selenophosphate synthase 1)

 SPS1_HUMAN              Reviewed;         392 AA.
P49903; B4DWK0; D3DRS9; D6PSQ9; Q5T5U8; Q5T5U9; Q9BVT4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
13-DEC-2002, sequence version 2.
25-OCT-2017, entry version 155.
RecName: Full=Selenide, water dikinase 1;
EC=2.7.9.3;
AltName: Full=Selenium donor protein 1;
AltName: Full=Selenophosphate synthase 1;
Name=SEPHS1; Synonyms=SELD, SPS, SPS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ATP-BINDING, AND
MUTAGENESIS OF GLY-268; GLY-270; GLY-273 AND HIS-274.
TISSUE=Liver;
PubMed=7665581; DOI=10.1074/jbc.270.37.21659;
Low S.C., Harney J.W., Berry M.J.;
"Cloning and functional characterization of human selenophosphate
synthetase, an essential component of selenoprotein synthesis.";
J. Biol. Chem. 270:21659-21664(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBUNIT,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20471958; DOI=10.1016/j.bbrc.2010.05.055;
Kim J.Y., Lee K.H., Shim M.S., Shin H., Xu X.M., Carlson B.A.,
Hatfield D.L., Lee B.J.;
"Human selenophosphate synthetase 1 has five splice variants with
unique interactions, subcellular localizations and expression
patterns.";
Biochem. Biophys. Res. Commun. 397:53-58(2010).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
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 T.-O., 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. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., 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 A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 5-16 AND 64-76, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADP; MAGNESIUM
IONS AND PHOSPHATE, SUBUNIT, ENZYME REGULATION, AND MUTAGENESIS OF
THR-85.
PubMed=19477186; DOI=10.1016/j.jmb.2009.05.032;
Wang K.T., Wang J., Li L.F., Su X.D.;
"Crystal structures of catalytic intermediates of human
selenophosphate synthetase 1.";
J. Mol. Biol. 390:747-759(2009).
-!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
{ECO:0000269|PubMed:7665581}.
-!- CATALYTIC ACTIVITY: ATP + selenide + H(2)O = AMP + selenophosphate
+ phosphate.
-!- ENZYME REGULATION: Activated by phosphate ions and by potassium
ions. {ECO:0000269|PubMed:19477186}.
-!- SUBUNIT: Homodimer (isoform 1, isoform 2, isoform 3 and isoform
4). Heterodimer of isoform 1 and isoform 3. Heterodimer of isoform
2 and isoform 4. {ECO:0000269|PubMed:19477186,
ECO:0000269|PubMed:20471958}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-714091, EBI-714091;
Q2TAL8:QRICH1; NbExp=9; IntAct=EBI-714091, EBI-2798044;
P24278:ZBTB25; NbExp=8; IntAct=EBI-714091, EBI-739899;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane. Nucleus membrane.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Major type, MT;
IsoId=P49903-1; Sequence=Displayed;
Name=2; Synonyms=Delta E8;
IsoId=P49903-2; Sequence=VSP_046702;
Name=3; Synonyms=Delta E2;
IsoId=P49903-3; Sequence=VSP_046701;
Name=4; Synonyms=E9 and E9a;
IsoId=P49903-4; Sequence=VSP_047451;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are gradually
expressed during the cell cycle until G2/M phase and then
decreased. Isoform 3 is gradually expressed during the cell cycle
until S phase and then decreased. {ECO:0000269|PubMed:20471958}.
-!- SIMILARITY: Belongs to the selenophosphate synthase 1 family.
Class II subfamily. {ECO:0000305}.
-!- CAUTION: The conserved active site Cys (or selenocysteine) residue
in position 29 is replaced by a Thr. However, as function in
selenoprotein synthesis is proven, it is possible Cys-31 is the
active site. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA87567.1; Type=Frameshift; Positions=377; Evidence={ECO:0000305};
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EMBL; U34044; AAA87567.1; ALT_FRAME; mRNA.
EMBL; GU954545; ADF78120.1; -; mRNA.
EMBL; GU954546; ADF78121.1; -; mRNA.
EMBL; GU954547; ADF78122.1; -; mRNA.
EMBL; GU954548; ADF78123.1; -; mRNA.
EMBL; GU954549; ADF78124.1; -; mRNA.
EMBL; AK301568; BAG63062.1; -; mRNA.
EMBL; AL138764; CAI12907.1; -; Genomic_DNA.
EMBL; AL355870; CAI12907.1; JOINED; Genomic_DNA.
EMBL; AL355870; CAI14198.1; -; Genomic_DNA.
EMBL; AL138764; CAI14198.1; JOINED; Genomic_DNA.
EMBL; CH471072; EAW86289.1; -; Genomic_DNA.
EMBL; CH471072; EAW86290.1; -; Genomic_DNA.
EMBL; CH471072; EAW86291.1; -; Genomic_DNA.
EMBL; CH471072; EAW86292.1; -; Genomic_DNA.
EMBL; CH471072; EAW86293.1; -; Genomic_DNA.
EMBL; BC000941; AAH00941.1; -; mRNA.
EMBL; BC063816; AAH63816.1; -; mRNA.
CCDS; CCDS55702.1; -. [P49903-3]
CCDS; CCDS55703.1; -. [P49903-2]
CCDS; CCDS7098.1; -. [P49903-1]
RefSeq; NP_001182531.1; NM_001195602.1. [P49903-3]
RefSeq; NP_001182533.1; NM_001195604.1. [P49903-2]
RefSeq; NP_036379.2; NM_012247.4. [P49903-1]
RefSeq; XP_016871431.1; XM_017015942.1. [P49903-1]
RefSeq; XP_016871432.1; XM_017015943.1. [P49903-1]
RefSeq; XP_016871434.1; XM_017015945.1. [P49903-3]
UniGene; Hs.124027; -.
PDB; 3FD5; X-ray; 1.90 A; A/B=1-392.
PDB; 3FD6; X-ray; 1.95 A; A/B=1-392.
PDBsum; 3FD5; -.
PDBsum; 3FD6; -.
ProteinModelPortal; P49903; -.
SMR; P49903; -.
BioGrid; 116589; 51.
IntAct; P49903; 15.
STRING; 9606.ENSP00000367893; -.
iPTMnet; P49903; -.
PhosphoSitePlus; P49903; -.
BioMuta; SEPHS1; -.
DMDM; 27151792; -.
EPD; P49903; -.
MaxQB; P49903; -.
PaxDb; P49903; -.
PeptideAtlas; P49903; -.
PRIDE; P49903; -.
DNASU; 22929; -.
Ensembl; ENST00000327347; ENSP00000367893; ENSG00000086475. [P49903-1]
Ensembl; ENST00000378614; ENSP00000367877; ENSG00000086475. [P49903-2]
Ensembl; ENST00000545675; ENSP00000441119; ENSG00000086475. [P49903-3]
GeneID; 22929; -.
KEGG; hsa:22929; -.
UCSC; uc001imk.4; human. [P49903-1]
CTD; 22929; -.
DisGeNET; 22929; -.
EuPathDB; HostDB:ENSG00000086475.14; -.
GeneCards; SEPHS1; -.
HGNC; HGNC:19685; SEPHS1.
HPA; HPA037645; -.
MIM; 600902; gene.
neXtProt; NX_P49903; -.
OpenTargets; ENSG00000086475; -.
PharmGKB; PA134905215; -.
eggNOG; KOG3939; Eukaryota.
eggNOG; COG0709; LUCA.
GeneTree; ENSGT00390000000950; -.
HOGENOM; HOG000219301; -.
HOVERGEN; HBG001207; -.
InParanoid; P49903; -.
KO; K01008; -.
OMA; GCIPGGT; -.
OrthoDB; EOG091G0B7N; -.
PhylomeDB; P49903; -.
TreeFam; TF313811; -.
BRENDA; 2.7.9.3; 2681.
EvolutionaryTrace; P49903; -.
GeneWiki; Selenophosphate_synthetase_1; -.
GenomeRNAi; 22929; -.
PRO; PR:P49903; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000086475; -.
CleanEx; HS_SEPHS1; -.
ExpressionAtlas; P49903; baseline and differential.
Genevisible; P49903; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0005525; F:GTP binding; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004756; F:selenide, water dikinase activity; IEA:UniProtKB-EC.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:InterPro.
CDD; cd02195; SelD; 1.
Gene3D; 3.30.1330.10; -; 1.
Gene3D; 3.90.650.10; -; 2.
InterPro; IPR010918; PurM-like_C_dom.
InterPro; IPR036676; PurM-like_C_sf.
InterPro; IPR016188; PurM-like_N.
InterPro; IPR036921; PurM-like_N_sf.
InterPro; IPR023061; SelD_I.
InterPro; IPR004536; SPS/SelD.
PANTHER; PTHR10256; PTHR10256; 1.
Pfam; PF00586; AIRS; 1.
Pfam; PF02769; AIRS_C; 1.
PIRSF; PIRSF036407; Selenphspht_syn; 1.
SUPFAM; SSF55326; SSF55326; 1.
SUPFAM; SSF56042; SSF56042; 1.
TIGRFAMs; TIGR00476; selD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Kinase; Membrane; Nucleotide-binding;
Nucleus; Reference proteome; Selenium; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 392 Selenide, water dikinase 1.
/FTId=PRO_0000127648.
NP_BIND 67 69 ATP.
NP_BIND 162 164 ATP; shared with dimeric partner.
NP_BIND 267 273 ATP.
ACT_SITE 31 31 {ECO:0000255}.
BINDING 32 32 ATP.
BINDING 87 87 ATP.
BINDING 110 110 ATP.
SITE 32 32 Important for catalytic activity.
{ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
VAR_SEQ 1 67 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:20471958}.
/FTId=VSP_046701.
VAR_SEQ 251 321 Missing (in isoform 2).
{ECO:0000303|PubMed:20471958}.
/FTId=VSP_046702.
VAR_SEQ 322 392 GGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNR
TARIIDKPRIIEVAPQVATQNVNPTPGATS -> DVQ (in
isoform 4).
{ECO:0000303|PubMed:20471958}.
/FTId=VSP_047451.
MUTAGEN 85 85 T->A: Strongly reduced ADP hydrolysis.
{ECO:0000269|PubMed:19477186}.
MUTAGEN 268 268 G->C: No change in ATP-binding.
{ECO:0000269|PubMed:7665581}.
MUTAGEN 270 270 G->R: No change in ATP-binding.
{ECO:0000269|PubMed:7665581}.
MUTAGEN 273 273 G->A,D,V: Loss of ATP-binding.
{ECO:0000269|PubMed:7665581}.
MUTAGEN 274 274 H->N: Reduced ATP-binding.
{ECO:0000269|PubMed:7665581}.
MUTAGEN 274 274 H->Y: Increased ATP-binding.
{ECO:0000269|PubMed:7665581}.
CONFLICT 260 260 A -> T (in Ref. 1; AAA87567).
{ECO:0000305}.
HELIX 10 12 {ECO:0000244|PDB:3FD5}.
HELIX 20 23 {ECO:0000244|PDB:3FD5}.
HELIX 35 42 {ECO:0000244|PDB:3FD5}.
STRAND 68 74 {ECO:0000244|PDB:3FD5}.
STRAND 81 89 {ECO:0000244|PDB:3FD5}.
HELIX 96 113 {ECO:0000244|PDB:3FD5}.
STRAND 120 129 {ECO:0000244|PDB:3FD5}.
HELIX 134 154 {ECO:0000244|PDB:3FD5}.
STRAND 159 169 {ECO:0000244|PDB:3FD5}.
STRAND 171 180 {ECO:0000244|PDB:3FD5}.
HELIX 182 184 {ECO:0000244|PDB:3FD5}.
STRAND 196 201 {ECO:0000244|PDB:3FD5}.
HELIX 205 213 {ECO:0000244|PDB:3FD5}.
HELIX 218 224 {ECO:0000244|PDB:3FD5}.
HELIX 230 245 {ECO:0000244|PDB:3FD5}.
HELIX 249 257 {ECO:0000244|PDB:3FD5}.
STRAND 262 265 {ECO:0000244|PDB:3FD5}.
HELIX 270 279 {ECO:0000244|PDB:3FD5}.
STRAND 283 296 {ECO:0000244|PDB:3FD5}.
HELIX 299 305 {ECO:0000244|PDB:3FD5}.
TURN 306 308 {ECO:0000244|PDB:3FD5}.
HELIX 312 314 {ECO:0000244|PDB:3FD5}.
STRAND 324 328 {ECO:0000244|PDB:3FD5}.
HELIX 330 341 {ECO:0000244|PDB:3FD5}.
STRAND 352 362 {ECO:0000244|PDB:3FD5}.
STRAND 364 375 {ECO:0000244|PDB:3FD5}.
SEQUENCE 392 AA; 42911 MW; E9636E38146D926D CRC64;
MSTRESFNPE SYELDKSFRL TRFTELKGTG CKVPQDVLQK LLESLQENHF QEDEQFLGAV
MPRLGIGMDT CVIPLRHGGL SLVQTTDYIY PIVDDPYMMG RIACANVLSD LYAMGVTECD
NMLMLLGVSN KMTDRERDKV MPLIIQGFKD AAEEAGTSVT GGQTVLNPWI VLGGVATTVC
QPNEFIMPDN AVPGDVLVLT KPLGTQVAVA VHQWLDIPEK WNKIKLVVTQ EDVELAYQEA
MMNMARLNRT AAGLMHTFNA HAATDITGFG ILGHAQNLAK QQRNEVSFVI HNLPVLAKMA
AVSKACGNMF GLMHGTCPET SGGLLICLPR EQAARFCAEI KSPKYGEGHQ AWIIGIVEKG
NRTARIIDKP RIIEVAPQVA TQNVNPTPGA TS


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30-442 SEPHS1 is an enzyme that synthesizes selenophosphate from selenide and ATP. Selenophosphate is the selenium donor used to synthesize selenocysteine, which is co-translationally incorporated into selen 0.1 mg
G9412 Selenide, water dikinase 2 (SEPHS2), Pig, ELISA Kit 96T
E12020m Mouse ELISA Kit FOR Selenide, water dikinase 1 96T
YHB0196Bo Bovine Selenide, water dikinase 1,SEPHS1 ELISA kit 96T
YHB0196Bo Bovine Selenide, water dikinase 1,SEPHS1 ELISA kit 48T
E3248Hu Human Selenide, water dikinase 1,SEPHS1 ELISA kit 96T
YHB0338Po Porcine Selenide, water dikinase 2,SEPHS2 ELISA kit 48T
YHB1196Mo Mouse Selenide, water dikinase 2,SEPHS2 ELISA kit 48T
E3248Hu Human Selenide, water dikinase 1,SEPHS1 ELISA kit 48T
YHB1195Mo Mouse Selenide, water dikinase 1,SEPHS1 ELISA kit 48T
E1369Mo Mouse Selenide, water dikinase 2,SEPHS2 ELISA kit 48T
YHB2647Hu Human Selenide, water dikinase 1,SEPHS1 ELISA kit 96T
G9407 Selenide, water dikinase 1 (SEPHS1), Bovine, ELISA Kit 96T
YHB1196Mo Mouse Selenide, water dikinase 2,SEPHS2 ELISA kit 96T
YHB1195Mo Mouse Selenide, water dikinase 1,SEPHS1 ELISA kit 96T
CSB-EL021015MO Mouse Selenide, water dikinase 1(SEPHS1) ELISA kit 96T
E3248Hu Human Selenide, water dikinase 2,SEPHS2 ELISA kit 48T
E3247Hu Human Selenide, water dikinase 1,SEPHS1 ELISA kit 48T
CSB-EL021016MO Mouse Selenide, water dikinase 2(SEPHS2) ELISA kit 96T


 

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