Full text data of BPNT1
BPNT1
[Confidence: low (only semi-automatic identification from reviews)]
3'(2'),5'-bisphosphate nucleotidase 1; 3.1.3.7 (Bisphosphate 3'-nucleotidase 1; PAP-inositol 1,4-phosphatase; PIP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
3'(2'),5'-bisphosphate nucleotidase 1; 3.1.3.7 (Bisphosphate 3'-nucleotidase 1; PAP-inositol 1,4-phosphatase; PIP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95861
ID BPNT1_HUMAN Reviewed; 308 AA.
AC O95861; A8K7C8; D3DTA9; Q8WVL5; Q9UGJ3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
DE EC=3.1.3.7;
DE AltName: Full=Bisphosphate 3'-nucleotidase 1;
DE AltName: Full=PAP-inositol 1,4-phosphatase;
DE Short=PIP;
GN Name=BPNT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=10224133; DOI=10.1074/jbc.274.19.13619;
RA Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.;
RT "Cloning and characterization of a mammalian lithium-sensitive
RT bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate.";
RL J. Biol. Chem. 274:13619-13628(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RA Yenush L., Gil-Mascarell M., Serrano R., Rodriguez P.L.;
RT "Hydrolysis of inositol-1,4-bisphosphate by human and yeast lithium
RT sensitive 3'-phosphoadenosine 5'-phosphate nucleotidases.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-308 IN COMPLEX WITH
RP MAGNESIUM IONS AND AMP.
RG Structural genomics consortium (SGC);
RT "Human 3'(2'), 5'-bisphosphate nucleotidase 1 (BPNT1) in complex with
RT AMP, PO4 and magnesium.";
RL Submitted (APR-2009) to the PDB data bank.
CC -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS)
CC to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
CC 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards
CC inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-
CC trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P,
CC Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6.
CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O =
CC adenosine 5'-phosphate + phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Uncompetitive inhibition by micromolar
CC concentrations of lithium. Competitive inhibition by inositol 1,4-
CC bisphosphate.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95861-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95861-2; Sequence=VSP_009937;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver, pancreas
CC and heart. Detected at lower levels in brain, placenta, lung and
CC skeletal muscle.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF125042; AAD17329.1; -; mRNA.
DR EMBL; AJ249339; CAB65115.1; -; mRNA.
DR EMBL; AK291943; BAF84632.1; -; mRNA.
DR EMBL; CH471100; EAW93306.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93308.1; -; Genomic_DNA.
DR EMBL; BC017801; AAH17801.1; -; mRNA.
DR RefSeq; NP_006076.4; NM_006085.5.
DR RefSeq; XP_005273057.1; XM_005273000.1.
DR UniGene; Hs.406134; -.
DR PDB; 2WEF; X-ray; 1.80 A; A=6-308.
DR PDBsum; 2WEF; -.
DR ProteinModelPortal; O95861; -.
DR SMR; O95861; 6-308.
DR IntAct; O95861; 1.
DR MINT; MINT-5002343; -.
DR STRING; 9606.ENSP00000318852; -.
DR PhosphoSite; O95861; -.
DR REPRODUCTION-2DPAGE; IPI00410214; -.
DR PaxDb; O95861; -.
DR PRIDE; O95861; -.
DR Ensembl; ENST00000322067; ENSP00000318852; ENSG00000162813.
DR Ensembl; ENST00000469520; ENSP00000446828; ENSG00000162813.
DR GeneID; 10380; -.
DR KEGG; hsa:10380; -.
DR UCSC; uc001hma.3; human.
DR CTD; 10380; -.
DR GeneCards; GC01M220230; -.
DR H-InvDB; HIX0001601; -.
DR HGNC; HGNC:1096; BPNT1.
DR HPA; HPA048461; -.
DR MIM; 604053; gene.
DR neXtProt; NX_O95861; -.
DR PharmGKB; PA25407; -.
DR eggNOG; COG0483; -.
DR HOGENOM; HOG000293205; -.
DR HOVERGEN; HBG050719; -.
DR KO; K01082; -.
DR OMA; INQPFYN; -.
DR OrthoDB; EOG7WQ7SQ; -.
DR BRENDA; 3.1.3.7; 2681.
DR Reactome; REACT_111217; Metabolism.
DR EvolutionaryTrace; O95861; -.
DR GenomeRNAi; 10380; -.
DR NextBio; 39323; -.
DR PRO; PR:O95861; -.
DR ArrayExpress; O95861; -.
DR Bgee; O95861; -.
DR CleanEx; HS_BPNT1; -.
DR Genevestigator; O95861; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; TAS:ProtInc.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; TAS:Reactome.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR PANTHER; PTHR20854; PTHR20854; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Hydrolase; Lithium; Magnesium; Metal-binding; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 308 3'(2'),5'-bisphosphate nucleotidase 1.
FT /FTId=PRO_0000142527.
FT REGION 119 122 Substrate binding.
FT REGION 195 198 Substrate binding.
FT METAL 74 74 Magnesium 1.
FT METAL 117 117 Magnesium 1.
FT METAL 117 117 Magnesium 2.
FT METAL 119 119 Magnesium 1; via carbonyl oxygen.
FT METAL 120 120 Magnesium 2.
FT METAL 247 247 Magnesium 2.
FT BINDING 74 74 Substrate (By similarity).
FT BINDING 247 247 Substrate.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 277 308 KHMNSAGVLATLRNYDYYASRVPESIKNALVP -> SHRTW
FT PKPDFFRAQFFLESHSCFSRNFKNVSTPIKNIYDVIIYAYE
FT TDL (in isoform 2).
FT /FTId=VSP_009937.
FT CONFLICT 221 221 A -> V (in Ref. 5; AAH17801).
FT CONFLICT 260 260 G -> S (in Ref. 2; CAB65115).
FT HELIX 7 32
FT STRAND 38 42
FT STRAND 45 47
FT HELIX 49 65
FT STRAND 70 75
FT HELIX 84 86
FT HELIX 93 96
FT HELIX 102 104
FT HELIX 109 111
FT STRAND 112 120
FT HELIX 122 126
FT HELIX 130 132
FT STRAND 134 141
FT STRAND 144 152
FT TURN 153 158
FT STRAND 167 172
FT TURN 173 175
FT STRAND 176 180
FT STRAND 191 194
FT STRAND 196 198
FT HELIX 201 208
FT STRAND 213 217
FT HELIX 221 229
FT STRAND 234 238
FT HELIX 245 257
FT STRAND 261 263
FT STRAND 284 289
FT HELIX 291 295
FT HELIX 300 305
SQ 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
//
ID BPNT1_HUMAN Reviewed; 308 AA.
AC O95861; A8K7C8; D3DTA9; Q8WVL5; Q9UGJ3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
DE EC=3.1.3.7;
DE AltName: Full=Bisphosphate 3'-nucleotidase 1;
DE AltName: Full=PAP-inositol 1,4-phosphatase;
DE Short=PIP;
GN Name=BPNT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=10224133; DOI=10.1074/jbc.274.19.13619;
RA Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.;
RT "Cloning and characterization of a mammalian lithium-sensitive
RT bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate.";
RL J. Biol. Chem. 274:13619-13628(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RA Yenush L., Gil-Mascarell M., Serrano R., Rodriguez P.L.;
RT "Hydrolysis of inositol-1,4-bisphosphate by human and yeast lithium
RT sensitive 3'-phosphoadenosine 5'-phosphate nucleotidases.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-308 IN COMPLEX WITH
RP MAGNESIUM IONS AND AMP.
RG Structural genomics consortium (SGC);
RT "Human 3'(2'), 5'-bisphosphate nucleotidase 1 (BPNT1) in complex with
RT AMP, PO4 and magnesium.";
RL Submitted (APR-2009) to the PDB data bank.
CC -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS)
CC to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
CC 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards
CC inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-
CC trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P,
CC Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6.
CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O =
CC adenosine 5'-phosphate + phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Uncompetitive inhibition by micromolar
CC concentrations of lithium. Competitive inhibition by inositol 1,4-
CC bisphosphate.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95861-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95861-2; Sequence=VSP_009937;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver, pancreas
CC and heart. Detected at lower levels in brain, placenta, lung and
CC skeletal muscle.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF125042; AAD17329.1; -; mRNA.
DR EMBL; AJ249339; CAB65115.1; -; mRNA.
DR EMBL; AK291943; BAF84632.1; -; mRNA.
DR EMBL; CH471100; EAW93306.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93308.1; -; Genomic_DNA.
DR EMBL; BC017801; AAH17801.1; -; mRNA.
DR RefSeq; NP_006076.4; NM_006085.5.
DR RefSeq; XP_005273057.1; XM_005273000.1.
DR UniGene; Hs.406134; -.
DR PDB; 2WEF; X-ray; 1.80 A; A=6-308.
DR PDBsum; 2WEF; -.
DR ProteinModelPortal; O95861; -.
DR SMR; O95861; 6-308.
DR IntAct; O95861; 1.
DR MINT; MINT-5002343; -.
DR STRING; 9606.ENSP00000318852; -.
DR PhosphoSite; O95861; -.
DR REPRODUCTION-2DPAGE; IPI00410214; -.
DR PaxDb; O95861; -.
DR PRIDE; O95861; -.
DR Ensembl; ENST00000322067; ENSP00000318852; ENSG00000162813.
DR Ensembl; ENST00000469520; ENSP00000446828; ENSG00000162813.
DR GeneID; 10380; -.
DR KEGG; hsa:10380; -.
DR UCSC; uc001hma.3; human.
DR CTD; 10380; -.
DR GeneCards; GC01M220230; -.
DR H-InvDB; HIX0001601; -.
DR HGNC; HGNC:1096; BPNT1.
DR HPA; HPA048461; -.
DR MIM; 604053; gene.
DR neXtProt; NX_O95861; -.
DR PharmGKB; PA25407; -.
DR eggNOG; COG0483; -.
DR HOGENOM; HOG000293205; -.
DR HOVERGEN; HBG050719; -.
DR KO; K01082; -.
DR OMA; INQPFYN; -.
DR OrthoDB; EOG7WQ7SQ; -.
DR BRENDA; 3.1.3.7; 2681.
DR Reactome; REACT_111217; Metabolism.
DR EvolutionaryTrace; O95861; -.
DR GenomeRNAi; 10380; -.
DR NextBio; 39323; -.
DR PRO; PR:O95861; -.
DR ArrayExpress; O95861; -.
DR Bgee; O95861; -.
DR CleanEx; HS_BPNT1; -.
DR Genevestigator; O95861; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; TAS:ProtInc.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; TAS:Reactome.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR PANTHER; PTHR20854; PTHR20854; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Hydrolase; Lithium; Magnesium; Metal-binding; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 308 3'(2'),5'-bisphosphate nucleotidase 1.
FT /FTId=PRO_0000142527.
FT REGION 119 122 Substrate binding.
FT REGION 195 198 Substrate binding.
FT METAL 74 74 Magnesium 1.
FT METAL 117 117 Magnesium 1.
FT METAL 117 117 Magnesium 2.
FT METAL 119 119 Magnesium 1; via carbonyl oxygen.
FT METAL 120 120 Magnesium 2.
FT METAL 247 247 Magnesium 2.
FT BINDING 74 74 Substrate (By similarity).
FT BINDING 247 247 Substrate.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 277 308 KHMNSAGVLATLRNYDYYASRVPESIKNALVP -> SHRTW
FT PKPDFFRAQFFLESHSCFSRNFKNVSTPIKNIYDVIIYAYE
FT TDL (in isoform 2).
FT /FTId=VSP_009937.
FT CONFLICT 221 221 A -> V (in Ref. 5; AAH17801).
FT CONFLICT 260 260 G -> S (in Ref. 2; CAB65115).
FT HELIX 7 32
FT STRAND 38 42
FT STRAND 45 47
FT HELIX 49 65
FT STRAND 70 75
FT HELIX 84 86
FT HELIX 93 96
FT HELIX 102 104
FT HELIX 109 111
FT STRAND 112 120
FT HELIX 122 126
FT HELIX 130 132
FT STRAND 134 141
FT STRAND 144 152
FT TURN 153 158
FT STRAND 167 172
FT TURN 173 175
FT STRAND 176 180
FT STRAND 191 194
FT STRAND 196 198
FT HELIX 201 208
FT STRAND 213 217
FT HELIX 221 229
FT STRAND 234 238
FT HELIX 245 257
FT STRAND 261 263
FT STRAND 284 289
FT HELIX 291 295
FT HELIX 300 305
SQ 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
//
MIM
604053
*RECORD*
*FIELD* NO
604053
*FIELD* TI
*604053 3-PRIME(2-PRIME),5-PRIME-@BISPHOSPHATE NUCLEOTIDASE 1; BPNT1
;;BISPHOSPHATE 3-PRIME-NUCLEOTIDASE
read more*FIELD* TX
At subtherapeutic concentrations, lithium, a major drug used to treat
manic depression, inhibits members of a magnesium-dependent
phosphomonoesterase family. Fructose 1,6-bisphosphatase (611570),
inositol monophosphatase (602064), and inositol polyphosphate
1-phosphatase (1ptase; 147263), members of this family, contain a
conserved motif involved in metal/lithium binding and catalysis. By
searching EST databases for sequences related to the conserved motif in
1ptase, Spiegelberg et al. (1999) identified mouse and human cDNAs
encoding a novel magnesium-dependent phosphomonoesterase that they
called bisphosphate 3-prime-nucleotidase, or BPntase (EC 3.1.3.7). The
predicted 309-amino acid human protein is 92% identical to mouse
BPntase. Both native and recombinant BPntase exhibited intrinsic
magnesium-dependent bisphosphate nucleotidase activity. Lithium acted as
an uncompetitive inhibitor of the enzyme. Inositol 1,4-bisphosphate was
a competitive inhibitor, suggesting that BPntase's physiologic role in
nucleotide metabolism may be regulated by inositol signaling pathways.
Expression of mammalian BPntase complemented mutations in the S.
cerevisiae HAL2 gene, which encodes a protein involved in methionine
biosynthesis and sodium tolerance. Northern blot analysis revealed that
the 2.5-kb human BPntase mRNA was expressed in all tissues tested, with
the highest level observed in kidney. Spiegelberg et al. (1999) noted
that the high expression of BPntase in kidney is consistent with the
hypothesis that increases in nucleotidase activity are associated with
resistance to salt. They proposed that inhibition of human BPntase may
account for lithium-induced nephrotoxicity.
*FIELD* RF
1. 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-prime-nucleotidase inhibited by inositol 1,4-bisphosphate. J.
Biol. Chem. 274: 13619-13628, 1999.
*FIELD* CD
Rebekah S. Rasooly: 7/22/1999
*FIELD* ED
carol: 11/02/2007
jlewis: 7/23/1999
jlewis: 7/22/1999
*RECORD*
*FIELD* NO
604053
*FIELD* TI
*604053 3-PRIME(2-PRIME),5-PRIME-@BISPHOSPHATE NUCLEOTIDASE 1; BPNT1
;;BISPHOSPHATE 3-PRIME-NUCLEOTIDASE
read more*FIELD* TX
At subtherapeutic concentrations, lithium, a major drug used to treat
manic depression, inhibits members of a magnesium-dependent
phosphomonoesterase family. Fructose 1,6-bisphosphatase (611570),
inositol monophosphatase (602064), and inositol polyphosphate
1-phosphatase (1ptase; 147263), members of this family, contain a
conserved motif involved in metal/lithium binding and catalysis. By
searching EST databases for sequences related to the conserved motif in
1ptase, Spiegelberg et al. (1999) identified mouse and human cDNAs
encoding a novel magnesium-dependent phosphomonoesterase that they
called bisphosphate 3-prime-nucleotidase, or BPntase (EC 3.1.3.7). The
predicted 309-amino acid human protein is 92% identical to mouse
BPntase. Both native and recombinant BPntase exhibited intrinsic
magnesium-dependent bisphosphate nucleotidase activity. Lithium acted as
an uncompetitive inhibitor of the enzyme. Inositol 1,4-bisphosphate was
a competitive inhibitor, suggesting that BPntase's physiologic role in
nucleotide metabolism may be regulated by inositol signaling pathways.
Expression of mammalian BPntase complemented mutations in the S.
cerevisiae HAL2 gene, which encodes a protein involved in methionine
biosynthesis and sodium tolerance. Northern blot analysis revealed that
the 2.5-kb human BPntase mRNA was expressed in all tissues tested, with
the highest level observed in kidney. Spiegelberg et al. (1999) noted
that the high expression of BPntase in kidney is consistent with the
hypothesis that increases in nucleotidase activity are associated with
resistance to salt. They proposed that inhibition of human BPntase may
account for lithium-induced nephrotoxicity.
*FIELD* RF
1. 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-prime-nucleotidase inhibited by inositol 1,4-bisphosphate. J.
Biol. Chem. 274: 13619-13628, 1999.
*FIELD* CD
Rebekah S. Rasooly: 7/22/1999
*FIELD* ED
carol: 11/02/2007
jlewis: 7/23/1999
jlewis: 7/22/1999