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3'(2'),5'-bisphosphate nucleotidase 1 (EC 3.1.3.7) (Bisphosphate 3'-nucleotidase 1) (PAP-inositol 1,4-phosphatase) (PIP)

 BPNT1_HUMAN             Reviewed;         308 AA.
O95861; A8K7C8; B4DPS5; B4DUS9; D3DTA9; Q8WVL5; Q9UGJ3;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
18-JUL-2018, entry version 153.
RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
EC=3.1.3.7;
AltName: Full=Bisphosphate 3'-nucleotidase 1;
AltName: Full=PAP-inositol 1,4-phosphatase;
Short=PIP;
Name=BPNT1;
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, ENZYME REGULATION,
AND TISSUE SPECIFICITY.
PubMed=10224133; DOI=10.1074/jbc.274.19.13619;
Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.;
"Cloning and characterization of a mammalian lithium-sensitive
bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate.";
J. Biol. Chem. 274:13619-13628(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=B-cell;
Yenush L., Gil-Mascarell M., Serrano R., Rodriguez P.L.;
"Hydrolysis of inositol-1,4-bisphosphate by human and yeast lithium
sensitive 3'-phosphoadenosine 5'-phosphate nucleotidases.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
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=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[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 2).
TISSUE=Skeletal muscle;
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]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
[8]
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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND 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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-308 IN COMPLEX WITH
MAGNESIUM IONS AND AMP.
Structural genomics consortium (SGC);
"Human 3'(2'), 5'-bisphosphate nucleotidase 1 (BPNT1) in complex with
AMP, PO4 and magnesium.";
Submitted (APR-2009) to the PDB data bank.
-!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS)
to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards
inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-
trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P,
Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6.
{ECO:0000269|PubMed:10224133}.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O =
adenosine 5'-phosphate + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Uncompetitive inhibition by micromolar
concentrations of lithium. Competitive inhibition by inositol 1,4-
bisphosphate. {ECO:0000269|PubMed:10224133}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O95861-1; Sequence=Displayed;
Name=2;
IsoId=O95861-2; Sequence=VSP_009937;
Note=No experimental confirmation available.;
Name=3;
IsoId=O95861-3; Sequence=VSP_054807;
Name=4;
IsoId=O95861-4; Sequence=VSP_054808;
-!- TISSUE SPECIFICITY: Highly expressed in kidney, liver, pancreas
and heart. Detected at lower levels in brain, placenta, lung and
skeletal muscle. {ECO:0000269|PubMed:10224133}.
-!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
{ECO:0000305}.
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EMBL; AF125042; AAD17329.1; -; mRNA.
EMBL; AJ249339; CAB65115.1; -; mRNA.
EMBL; AK291943; BAF84632.1; -; mRNA.
EMBL; AK298476; BAG60687.1; -; mRNA.
EMBL; AK300777; BAG62441.1; -; mRNA.
EMBL; AC103590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471100; EAW93306.1; -; Genomic_DNA.
EMBL; CH471100; EAW93308.1; -; Genomic_DNA.
EMBL; BC017801; AAH17801.1; -; mRNA.
CCDS; CCDS41469.1; -. [O95861-1]
CCDS; CCDS65787.1; -. [O95861-3]
CCDS; CCDS65788.1; -. [O95861-4]
RefSeq; NP_001273078.1; NM_001286149.1. [O95861-3]
RefSeq; NP_001273079.1; NM_001286150.1. [O95861-4]
RefSeq; NP_001273080.1; NM_001286151.1. [O95861-3]
RefSeq; NP_006076.4; NM_006085.5. [O95861-1]
RefSeq; XP_005273057.1; XM_005273000.4. [O95861-1]
RefSeq; XP_016855532.1; XM_017000043.1. [O95861-4]
UniGene; Hs.406134; -.
PDB; 2WEF; X-ray; 1.80 A; A=6-308.
PDBsum; 2WEF; -.
ProteinModelPortal; O95861; -.
SMR; O95861; -.
BioGrid; 115653; 63.
IntAct; O95861; 5.
STRING; 9606.ENSP00000318852; -.
DEPOD; O95861; -.
iPTMnet; O95861; -.
PhosphoSitePlus; O95861; -.
REPRODUCTION-2DPAGE; IPI00410214; -.
EPD; O95861; -.
PaxDb; O95861; -.
PeptideAtlas; O95861; -.
PRIDE; O95861; -.
ProteomicsDB; 51094; -.
ProteomicsDB; 51095; -. [O95861-2]
Ensembl; ENST00000322067; ENSP00000318852; ENSG00000162813. [O95861-1]
Ensembl; ENST00000414869; ENSP00000410348; ENSG00000162813. [O95861-4]
Ensembl; ENST00000469520; ENSP00000446828; ENSG00000162813. [O95861-1]
Ensembl; ENST00000544404; ENSP00000444398; ENSG00000162813. [O95861-3]
GeneID; 10380; -.
KEGG; hsa:10380; -.
UCSC; uc010puh.3; human. [O95861-1]
CTD; 10380; -.
DisGeNET; 10380; -.
EuPathDB; HostDB:ENSG00000162813.17; -.
GeneCards; BPNT1; -.
H-InvDB; HIX0001601; -.
HGNC; HGNC:1096; BPNT1.
HPA; HPA048461; -.
MIM; 604053; gene.
neXtProt; NX_O95861; -.
OpenTargets; ENSG00000162813; -.
PharmGKB; PA25407; -.
eggNOG; KOG3099; Eukaryota.
eggNOG; ENOG410XNMV; LUCA.
GeneTree; ENSGT00530000063462; -.
HOGENOM; HOG000293205; -.
HOVERGEN; HBG050719; -.
KO; K01082; -.
OMA; GTSEYTQ; -.
OrthoDB; EOG091G0CFP; -.
PhylomeDB; O95861; -.
TreeFam; TF314300; -.
BRENDA; 3.1.3.7; 2681.
Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
EvolutionaryTrace; O95861; -.
GenomeRNAi; 10380; -.
PRO; PR:O95861; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162813; -.
CleanEx; HS_BPNT1; -.
ExpressionAtlas; O95861; baseline and differential.
Genevisible; O95861; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; TAS:Reactome.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
InterPro; IPR020583; Inositol_monoP_metal-BS.
InterPro; IPR000760; Inositol_monophosphatase-like.
InterPro; IPR020550; Inositol_monophosphatase_CS.
Pfam; PF00459; Inositol_P; 1.
PROSITE; PS00629; IMP_1; 1.
PROSITE; PS00630; IMP_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Hydrolase; Lithium; Magnesium; Metal-binding; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 308 3'(2'),5'-bisphosphate nucleotidase 1.
/FTId=PRO_0000142527.
REGION 119 122 Substrate binding.
REGION 195 198 Substrate binding.
METAL 74 74 Magnesium 1.
METAL 117 117 Magnesium 1.
METAL 117 117 Magnesium 2.
METAL 119 119 Magnesium 1; via carbonyl oxygen.
METAL 120 120 Magnesium 2.
METAL 247 247 Magnesium 2.
BINDING 74 74 Substrate. {ECO:0000250}.
BINDING 247 247 Substrate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 122 122 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 244 244 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9Z0S1}.
VAR_SEQ 1 55 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054807.
VAR_SEQ 76 111 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054808.
VAR_SEQ 277 308 KHMNSAGVLATLRNYDYYASRVPESIKNALVP -> SHRTW
PKPDFFRAQFFLESHSCFSRNFKNVSTPIKNIYDVIIYAYE
TDL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009937.
CONFLICT 221 221 A -> V (in Ref. 6; AAH17801).
{ECO:0000305}.
CONFLICT 260 260 G -> S (in Ref. 2; CAB65115).
{ECO:0000305}.
HELIX 7 32 {ECO:0000244|PDB:2WEF}.
STRAND 38 42 {ECO:0000244|PDB:2WEF}.
STRAND 45 47 {ECO:0000244|PDB:2WEF}.
HELIX 49 65 {ECO:0000244|PDB:2WEF}.
STRAND 70 75 {ECO:0000244|PDB:2WEF}.
HELIX 84 86 {ECO:0000244|PDB:2WEF}.
HELIX 93 96 {ECO:0000244|PDB:2WEF}.
HELIX 102 104 {ECO:0000244|PDB:2WEF}.
HELIX 109 111 {ECO:0000244|PDB:2WEF}.
STRAND 112 120 {ECO:0000244|PDB:2WEF}.
HELIX 122 126 {ECO:0000244|PDB:2WEF}.
HELIX 130 132 {ECO:0000244|PDB:2WEF}.
STRAND 134 141 {ECO:0000244|PDB:2WEF}.
STRAND 144 152 {ECO:0000244|PDB:2WEF}.
TURN 153 158 {ECO:0000244|PDB:2WEF}.
STRAND 167 172 {ECO:0000244|PDB:2WEF}.
TURN 173 175 {ECO:0000244|PDB:2WEF}.
STRAND 176 180 {ECO:0000244|PDB:2WEF}.
STRAND 191 194 {ECO:0000244|PDB:2WEF}.
STRAND 196 198 {ECO:0000244|PDB:2WEF}.
HELIX 201 208 {ECO:0000244|PDB:2WEF}.
STRAND 213 217 {ECO:0000244|PDB:2WEF}.
HELIX 221 229 {ECO:0000244|PDB:2WEF}.
STRAND 234 238 {ECO:0000244|PDB:2WEF}.
HELIX 245 257 {ECO:0000244|PDB:2WEF}.
STRAND 261 263 {ECO:0000244|PDB:2WEF}.
STRAND 284 289 {ECO:0000244|PDB:2WEF}.
HELIX 291 295 {ECO:0000244|PDB:2WEF}.
HELIX 300 305 {ECO:0000244|PDB:2WEF}.
SEQUENCE 308 AA; 33392 MW; A5952F5E31C8CFCB CRC64;
MASSNTVLMR LVASAYSIAQ KAGMIVRRVI AEGDLGIVEK TCATDLQTKA DRLAQMSICS
SLARKFPKLT IIGEEDLPSE EVDQELIEDS QWEEILKQPC PSQYSAIKEE DLVVWVDPLD
GTKEYTEGLL DNVTVLIGIA YEGKAIAGVI NQPYYNYEAG PDAVLGRTIW GVLGLGAFGF
QLKEVPAGKH IITTTRSHSN KLVTDCVAAM NPDAVLRVGG AGNKIIQLIE GKASAYVFAS
PGCKKWDTCA PEVILHAVGG KLTDIHGNVL QYHKDVKHMN SAGVLATLRN YDYYASRVPE
SIKNALVP


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BPTF BPNT1 Gene 3'(2'), 5'-bisphosphate nucleotidase 1
enz-061 Recombinant Human 3(2) 5-Bisphosphate Nucleotidase 1 ENZYMES 10
enz-061 Recombinant Human 3(2) 5-Bisphosphate Nucleotidase 1 ENZYMES 2
GWB-9A41AD Bisphosphate 3\\"-nucleotidase Immunizing Peptide
201-12-3048 Human 3',5'-Bisphosphate Nucleotidase 1(BPNT1)ELISA Kit 96T
QY-E05219 Human 3',5'-Bisphosphate Nucleotidase 1(BPNT1)ELISA Kit 96T
UT-E05219 Human 3',5'-Bisphosphate Nucleotidase 1 (BPNT1) ELISA Kit 96T


 

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