ID   BPNT1_HUMAN             Reviewed;         308 AA.
AC   O95861; A8K7C8; B4DPS5; B4DUS9; D3DTA9; Q8WVL5; Q9UGJ3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
DE            EC=3.1.3.7 {ECO:0000269|PubMed:10675562};
DE   AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase {ECO:0000303|PubMed:10675562};
DE            Short=PAP phosphatase {ECO:0000303|PubMed:10675562};
DE   AltName: Full=Bisphosphate 3'-nucleotidase 1 {ECO:0000303|PubMed:10224133};
DE            Short=BPntase 1 {ECO:0000303|PubMed:10224133};
DE   AltName: Full=HsPIP {ECO:0000303|PubMed:10675562};
DE   AltName: Full=Inositol-polyphosphate 1-phosphatase {ECO:0000303|PubMed:10675562};
DE            EC=3.1.3.57 {ECO:0000269|PubMed:10675562};
GN   Name=BPNT1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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 bisphosphate
RT   3'-nucleotidase inhibited by inositol 1,4-bisphosphate.";
RL   J. Biol. Chem. 274:13619-13628(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   ACTIVITY REGULATION.
RC   TISSUE=B-cell;
RX   PubMed=10675562; DOI=10.1016/s0014-5793(00)01183-2;
RA   Yenush L., Belles J.M., Lopez-Coronado J.M., Gil-Mascarell R., Serrano R.,
RA   Rodriguez P.L.;
RT   "A novel target of lithium therapy.";
RL   FEBS Lett. 467:321-325(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
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., Buerckstuemmer T.,
RA   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   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [14] {ECO:0007744|PDB:2WEF}
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-308 IN COMPLEX WITH AMP; MG(2+)
RP   AND PHOSPHATE.
RG   Structural genomics consortium (SGC);
RT   "Human 3'(2'), 5'-bisphosphate nucleotidase 1 (BPNT1) in complex with AMP,
RT   PO4 and magnesium.";
RL   Submitted (APR-2009) to the PDB data bank.
CC   -!- FUNCTION: Phosphatase that converts 3'(2')-phosphoadenosine 5'-
CC       phosphate (PAP) to AMP and inositol 1,4-bisphosphate (Ins(1,4)P2) to
CC       inositol 4-phosphate (PubMed:10675562). Is also able to hydrolyze
CC       adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-
CC       phosphosulfate (APS) (By similarity). Probably prevents the toxic
CC       accumulation of PAP, a compound which inhibits a variety of proteins,
CC       including PAPS-utilizing enzymes such as sulfotransferases, and RNA
CC       processing enzymes. Could also play a role in inositol recycling and
CC       phosphoinositide metabolism. Is not active on 3'-AMP, inositol-1-
CC       phosphate and inositol-1,4,5-triphosphate (PubMed:10675562).
CC       {ECO:0000250|UniProtKB:Q9Z1N4, ECO:0000269|PubMed:10675562}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC         Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC         Evidence={ECO:0000269|PubMed:10675562};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041;
CC         Evidence={ECO:0000305|PubMed:10675562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 2',5'-bisphosphate + H2O = AMP + phosphate;
CC         Xref=Rhea:RHEA:77643, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:194156, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC         Evidence={ECO:0000269|PubMed:10675562};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77644;
CC         Evidence={ECO:0000305|PubMed:10675562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + H2O = adenosine 5'-phosphosulfate
CC         + phosphate; Xref=Rhea:RHEA:77639, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339; EC=3.1.3.7;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1N4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77640;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1N4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-
CC         phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57;
CC         Evidence={ECO:0000269|PubMed:10675562};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15554;
CC         Evidence={ECO:0000305|PubMed:10675562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol
CC         3,4-bisphosphate + phosphate; Xref=Rhea:RHEA:70319,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58414,
CC         ChEBI:CHEBI:83241; Evidence={ECO:0000250|UniProtKB:Q9Z1N4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70320;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1N4};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10675562};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|Ref.14};
CC   -!- ACTIVITY REGULATION: Is very sensitive to inhibition by Li(+)
CC       (IC(50)=0.3 mM for hydrolysis of PAP; IC(50)=0.6 mM for hydrolysis of
CC       inositol-1,4-bis-phosphate). Is not affected by high Na(+)
CC       concentrations. {ECO:0000269|PubMed:10675562}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.4 uM for 1D-myo-inositol 1,4-bisphosphate
CC         {ECO:0000269|PubMed:10675562};
CC         Vmax=1.1 umol/min/mg enzyme with adenosine 3',5'-bisphosphate as
CC         substrate {ECO:0000269|PubMed:10675562};
CC         Vmax=0.2 umol/min/mg enzyme with 1D-myo-inositol 1,4-bisphosphate as
CC         substrate {ECO:0000269|PubMed:10675562};
CC         Note=KM for adenosine 3',5'-bisphosphate is below 1 uM.
CC         {ECO:0000269|PubMed:10675562};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=O95861-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95861-2; Sequence=VSP_009937;
CC       Name=3;
CC         IsoId=O95861-3; Sequence=VSP_054807;
CC       Name=4;
CC         IsoId=O95861-4; Sequence=VSP_054808;
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver, pancreas and
CC       heart. Detected at lower levels in brain, placenta, lung and skeletal
CC       muscle. {ECO:0000269|PubMed:10224133}.
CC   -!- MISCELLANEOUS: Since this enzyme is sensitive to subtherapeutic
CC       concentrations of lithium, it is a potential target of lithium therapy,
CC       which could explain some of the side effects of this therapy.
CC       {ECO:0000305|PubMed:10675562}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF125042; AAD17329.1; -; mRNA.
DR   EMBL; AJ249339; CAB65115.1; -; mRNA.
DR   EMBL; AK291943; BAF84632.1; -; mRNA.
DR   EMBL; AK298476; BAG60687.1; -; mRNA.
DR   EMBL; AK300777; BAG62441.1; -; mRNA.
DR   EMBL; AC103590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471100; EAW93306.1; -; Genomic_DNA.
DR   EMBL; CH471100; EAW93308.1; -; Genomic_DNA.
DR   EMBL; BC017801; AAH17801.1; -; mRNA.
DR   CCDS; CCDS41469.1; -. [O95861-1]
DR   CCDS; CCDS65787.1; -. [O95861-3]
DR   CCDS; CCDS65788.1; -. [O95861-4]
DR   RefSeq; NP_001273078.1; NM_001286149.1. [O95861-3]
DR   RefSeq; NP_001273079.1; NM_001286150.1. [O95861-4]
DR   RefSeq; NP_001273080.1; NM_001286151.1. [O95861-3]
DR   RefSeq; NP_006076.4; NM_006085.5. [O95861-1]
DR   RefSeq; XP_005273057.1; XM_005273000.4. [O95861-1]
DR   RefSeq; XP_016855532.1; XM_017000043.1. [O95861-4]
DR   PDB; 2WEF; X-ray; 1.80 A; A=6-308.
DR   PDBsum; 2WEF; -.
DR   AlphaFoldDB; O95861; -.
DR   SMR; O95861; -.
DR   BioGRID; 115653; 92.
DR   IntAct; O95861; 54.
DR   STRING; 9606.ENSP00000446828; -.
DR   DEPOD; BPNT1; -.
DR   GlyGen; O95861; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O95861; -.
DR   MetOSite; O95861; -.
DR   PhosphoSitePlus; O95861; -.
DR   SwissPalm; O95861; -.
DR   BioMuta; BPNT1; -.
DR   REPRODUCTION-2DPAGE; IPI00410214; -.
DR   EPD; O95861; -.
DR   jPOST; O95861; -.
DR   MassIVE; O95861; -.
DR   MaxQB; O95861; -.
DR   PaxDb; 9606-ENSP00000446828; -.
DR   PeptideAtlas; O95861; -.
DR   ProteomicsDB; 4810; -.
DR   ProteomicsDB; 51094; -. [O95861-1]
DR   ProteomicsDB; 51095; -. [O95861-2]
DR   ProteomicsDB; 5212; -.
DR   Pumba; O95861; -.
DR   Antibodypedia; 34625; 243 antibodies from 29 providers.
DR   DNASU; 10380; -.
DR   Ensembl; ENST00000322067.12; ENSP00000318852.7; ENSG00000162813.18. [O95861-1]
DR   Ensembl; ENST00000414869.6; ENSP00000410348.2; ENSG00000162813.18. [O95861-4]
DR   Ensembl; ENST00000469520.6; ENSP00000446828.1; ENSG00000162813.18. [O95861-1]
DR   Ensembl; ENST00000544404.5; ENSP00000444398.1; ENSG00000162813.18. [O95861-3]
DR   GeneID; 10380; -.
DR   KEGG; hsa:10380; -.
DR   MANE-Select; ENST00000322067.12; ENSP00000318852.7; NM_006085.6; NP_006076.4.
DR   UCSC; uc010puh.3; human. [O95861-1]
DR   AGR; HGNC:1096; -.
DR   CTD; 10380; -.
DR   DisGeNET; 10380; -.
DR   GeneCards; BPNT1; -.
DR   HGNC; HGNC:1096; BPNT1.
DR   HPA; ENSG00000162813; Low tissue specificity.
DR   MIM; 604053; gene.
DR   neXtProt; NX_O95861; -.
DR   OpenTargets; ENSG00000162813; -.
DR   PharmGKB; PA25407; -.
DR   VEuPathDB; HostDB:ENSG00000162813; -.
DR   eggNOG; KOG3099; Eukaryota.
DR   GeneTree; ENSGT00940000157359; -.
DR   HOGENOM; CLU_034742_2_0_1; -.
DR   InParanoid; O95861; -.
DR   OMA; QTEADRC; -.
DR   OrthoDB; 3665671at2759; -.
DR   PhylomeDB; O95861; -.
DR   TreeFam; TF314300; -.
DR   BRENDA; 3.1.3.7; 2681.
DR   PathwayCommons; O95861; -.
DR   Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR   SignaLink; O95861; -.
DR   BioGRID-ORCS; 10380; 24 hits in 1169 CRISPR screens.
DR   ChiTaRS; BPNT1; human.
DR   EvolutionaryTrace; O95861; -.
DR   GenomeRNAi; 10380; -.
DR   Pharos; O95861; Tbio.
DR   PRO; PR:O95861; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O95861; Protein.
DR   Bgee; ENSG00000162813; Expressed in islet of Langerhans and 169 other cell types or tissues.
DR   ExpressionAtlas; O95861; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01640; IPPase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   PANTHER; PTHR43028; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR   PANTHER; PTHR43028:SF5; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
DR   Genevisible; O95861; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Hydrolase; Lithium;
KW   Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..308
FT                   /note="3'(2'),5'-bisphosphate nucleotidase 1"
FT                   /id="PRO_0000142527"
FT   ACT_SITE        51
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT   ACT_SITE        122
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         195
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         198
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         220
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         224
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:2WEF"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   MOD_RES         122
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         244
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z0S1"
FT   VAR_SEQ         1..55
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054807"
FT   VAR_SEQ         76..111
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054808"
FT   VAR_SEQ         277..308
FT                   /note="KHMNSAGVLATLRNYDYYASRVPESIKNALVP -> SHRTWPKPDFFRAQFF
FT                   LESHSCFSRNFKNVSTPIKNIYDVIIYAYETDL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009937"
FT   CONFLICT        221
FT                   /note="A -> V (in Ref. 6; AAH17801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="G -> S (in Ref. 2; CAB65115)"
FT                   /evidence="ECO:0000305"
FT   HELIX           7..32
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          38..42
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           49..65
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          112..120
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           122..126
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          134..141
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          144..152
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   TURN            153..158
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          167..172
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   TURN            173..175
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          176..180
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           201..208
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          213..217
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           221..229
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           245..257
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           291..295
FT                   /evidence="ECO:0007829|PDB:2WEF"
FT   HELIX           300..305
FT                   /evidence="ECO:0007829|PDB:2WEF"
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
//