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O95861

- BPNT1_HUMAN

UniProt

O95861 - BPNT1_HUMAN

Protein

3'(2'),5'-bisphosphate nucleotidase 1

Gene

BPNT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    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 Ins1P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6.1 Publication

    Catalytic activityi

    Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Uncompetitive inhibition by micromolar concentrations of lithium. Competitive inhibition by inositol 1,4-bisphosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi74 – 741Magnesium 1
    Binding sitei74 – 741SubstrateBy similarity
    Metal bindingi117 – 1171Magnesium 1
    Metal bindingi117 – 1171Magnesium 2
    Metal bindingi119 – 1191Magnesium 1; via carbonyl oxygen
    Metal bindingi120 – 1201Magnesium 2
    Metal bindingi247 – 2471Magnesium 2
    Binding sitei247 – 2471Substrate

    GO - Molecular functioni

    1. 3'(2'),5'-bisphosphate nucleotidase activity Source: ProtInc
    2. inositol-1,4-bisphosphate 1-phosphatase activity Source: Ensembl
    3. magnesium ion binding Source: Ensembl

    GO - Biological processi

    1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
    2. dephosphorylation Source: GOC
    3. nervous system development Source: ProtInc
    4. nucleobase-containing compound metabolic process Source: ProtInc
    5. phosphatidylinositol phosphorylation Source: InterPro
    6. small molecule metabolic process Source: Reactome
    7. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Lithium, Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.7. 2681.
    ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3'(2'),5'-bisphosphate nucleotidase 1 (EC:3.1.3.7)
    Alternative name(s):
    Bisphosphate 3'-nucleotidase 1
    PAP-inositol 1,4-phosphatase
    Short name:
    PIP
    Gene namesi
    Name:BPNT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1096. BPNT1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25407.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 3083073'(2'),5'-bisphosphate nucleotidase 1PRO_0000142527Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei244 – 2441N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO95861.
    PaxDbiO95861.
    PRIDEiO95861.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00410214.

    PTM databases

    PhosphoSiteiO95861.

    Expressioni

    Tissue specificityi

    Highly expressed in kidney, liver, pancreas and heart. Detected at lower levels in brain, placenta, lung and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiO95861.
    BgeeiO95861.
    CleanExiHS_BPNT1.
    GenevestigatoriO95861.

    Organism-specific databases

    HPAiHPA048461.

    Interactioni

    Protein-protein interaction databases

    BioGridi115653. 3 interactions.
    IntActiO95861. 1 interaction.
    MINTiMINT-5002343.
    STRINGi9606.ENSP00000318852.

    Structurei

    Secondary structure

    1
    308
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 3226
    Beta strandi38 – 425
    Beta strandi45 – 473
    Helixi49 – 6517
    Beta strandi70 – 756
    Helixi84 – 863
    Helixi93 – 964
    Helixi102 – 1043
    Helixi109 – 1113
    Beta strandi112 – 1209
    Helixi122 – 1265
    Helixi130 – 1323
    Beta strandi134 – 1418
    Beta strandi144 – 1529
    Turni153 – 1586
    Beta strandi167 – 1726
    Turni173 – 1753
    Beta strandi176 – 1805
    Beta strandi191 – 1944
    Beta strandi196 – 1983
    Helixi201 – 2088
    Beta strandi213 – 2175
    Helixi221 – 2299
    Beta strandi234 – 2385
    Helixi245 – 25713
    Beta strandi261 – 2633
    Beta strandi284 – 2896
    Helixi291 – 2955
    Helixi300 – 3056

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WEFX-ray1.80A6-308[»]
    ProteinModelPortaliO95861.
    SMRiO95861. Positions 6-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95861.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 1224Substrate binding
    Regioni195 – 1984Substrate binding

    Sequence similaritiesi

    Belongs to the inositol monophosphatase family.Curated

    Phylogenomic databases

    eggNOGiCOG0483.
    HOGENOMiHOG000293205.
    HOVERGENiHBG050719.
    KOiK01082.
    OMAiLQYNKEV.
    OrthoDBiEOG7WQ7SQ.
    PhylomeDBiO95861.
    TreeFamiTF314300.

    Family and domain databases

    InterProiIPR020583. Inositol_monoP_metal-BS.
    IPR000760. Inositol_monophosphatase.
    IPR020550. Inositol_monophosphatase_CS.
    [Graphical view]
    PANTHERiPTHR20854. PTHR20854. 1 hit.
    PfamiPF00459. Inositol_P. 1 hit.
    [Graphical view]
    PROSITEiPS00629. IMP_1. 1 hit.
    PS00630. IMP_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95861-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASSNTVLMR LVASAYSIAQ KAGMIVRRVI AEGDLGIVEK TCATDLQTKA    50
    DRLAQMSICS SLARKFPKLT IIGEEDLPSE EVDQELIEDS QWEEILKQPC 100
    PSQYSAIKEE DLVVWVDPLD GTKEYTEGLL DNVTVLIGIA YEGKAIAGVI 150
    NQPYYNYEAG PDAVLGRTIW GVLGLGAFGF QLKEVPAGKH IITTTRSHSN 200
    KLVTDCVAAM NPDAVLRVGG AGNKIIQLIE GKASAYVFAS PGCKKWDTCA 250
    PEVILHAVGG KLTDIHGNVL QYHKDVKHMN SAGVLATLRN YDYYASRVPE 300
    SIKNALVP 308
    Length:308
    Mass (Da):33,392
    Last modified:May 1, 1999 - v1
    Checksum:iA5952F5E31C8CFCB
    GO
    Isoform 2 (identifier: O95861-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         277-308: KHMNSAGVLATLRNYDYYASRVPESIKNALVP → SHRTWPKPDF...VIIYAYETDL

    Note: No experimental confirmation available.

    Show »
    Length:325
    Mass (Da):35,744
    Checksum:i87527CD609009E68
    GO
    Isoform 3 (identifier: O95861-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-55: Missing.

    Show »
    Length:253
    Mass (Da):27,543
    Checksum:i6253BEF5F96A25E1
    GO
    Isoform 4 (identifier: O95861-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         76-111: Missing.

    Show »
    Length:272
    Mass (Da):29,189
    Checksum:iFC6456F98BDED5AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti221 – 2211A → V in AAH17801. (PubMed:15489334)Curated
    Sequence conflicti260 – 2601G → S in CAB65115. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5555Missing in isoform 3. 1 PublicationVSP_054807Add
    BLAST
    Alternative sequencei76 – 11136Missing in isoform 4. 1 PublicationVSP_054808Add
    BLAST
    Alternative sequencei277 – 30832KHMNS…NALVP → SHRTWPKPDFFRAQFFLESH SCFSRNFKNVSTPIKNIYDV IIYAYETDL in isoform 2. 1 PublicationVSP_009937Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF125042 mRNA. Translation: AAD17329.1.
    AJ249339 mRNA. Translation: CAB65115.1.
    AK291943 mRNA. Translation: BAF84632.1.
    AK298476 mRNA. Translation: BAG60687.1.
    AK300777 mRNA. Translation: BAG62441.1.
    AC103590 Genomic DNA. No translation available.
    CH471100 Genomic DNA. Translation: EAW93306.1.
    CH471100 Genomic DNA. Translation: EAW93308.1.
    BC017801 mRNA. Translation: AAH17801.1.
    CCDSiCCDS41469.1. [O95861-1]
    CCDS65787.1. [O95861-3]
    CCDS65788.1. [O95861-4]
    RefSeqiNP_001273078.1. NM_001286149.1. [O95861-3]
    NP_001273079.1. NM_001286150.1. [O95861-4]
    NP_001273080.1. NM_001286151.1. [O95861-3]
    NP_006076.4. NM_006085.5. [O95861-1]
    XP_005273057.1. XM_005273000.2. [O95861-1]
    UniGeneiHs.406134.

    Genome annotation databases

    EnsembliENST00000322067; ENSP00000318852; ENSG00000162813. [O95861-1]
    ENST00000414869; ENSP00000410348; ENSG00000162813. [O95861-4]
    ENST00000469520; ENSP00000446828; ENSG00000162813. [O95861-1]
    ENST00000544404; ENSP00000444398; ENSG00000162813. [O95861-3]
    GeneIDi10380.
    KEGGihsa:10380.
    UCSCiuc001hma.3. human. [O95861-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF125042 mRNA. Translation: AAD17329.1 .
    AJ249339 mRNA. Translation: CAB65115.1 .
    AK291943 mRNA. Translation: BAF84632.1 .
    AK298476 mRNA. Translation: BAG60687.1 .
    AK300777 mRNA. Translation: BAG62441.1 .
    AC103590 Genomic DNA. No translation available.
    CH471100 Genomic DNA. Translation: EAW93306.1 .
    CH471100 Genomic DNA. Translation: EAW93308.1 .
    BC017801 mRNA. Translation: AAH17801.1 .
    CCDSi CCDS41469.1. [O95861-1 ]
    CCDS65787.1. [O95861-3 ]
    CCDS65788.1. [O95861-4 ]
    RefSeqi NP_001273078.1. NM_001286149.1. [O95861-3 ]
    NP_001273079.1. NM_001286150.1. [O95861-4 ]
    NP_001273080.1. NM_001286151.1. [O95861-3 ]
    NP_006076.4. NM_006085.5. [O95861-1 ]
    XP_005273057.1. XM_005273000.2. [O95861-1 ]
    UniGenei Hs.406134.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WEF X-ray 1.80 A 6-308 [» ]
    ProteinModelPortali O95861.
    SMRi O95861. Positions 6-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115653. 3 interactions.
    IntActi O95861. 1 interaction.
    MINTi MINT-5002343.
    STRINGi 9606.ENSP00000318852.

    PTM databases

    PhosphoSitei O95861.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00410214.

    Proteomic databases

    MaxQBi O95861.
    PaxDbi O95861.
    PRIDEi O95861.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322067 ; ENSP00000318852 ; ENSG00000162813 . [O95861-1 ]
    ENST00000414869 ; ENSP00000410348 ; ENSG00000162813 . [O95861-4 ]
    ENST00000469520 ; ENSP00000446828 ; ENSG00000162813 . [O95861-1 ]
    ENST00000544404 ; ENSP00000444398 ; ENSG00000162813 . [O95861-3 ]
    GeneIDi 10380.
    KEGGi hsa:10380.
    UCSCi uc001hma.3. human. [O95861-1 ]

    Organism-specific databases

    CTDi 10380.
    GeneCardsi GC01M220230.
    H-InvDB HIX0001601.
    HGNCi HGNC:1096. BPNT1.
    HPAi HPA048461.
    MIMi 604053. gene.
    neXtProti NX_O95861.
    PharmGKBi PA25407.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0483.
    HOGENOMi HOG000293205.
    HOVERGENi HBG050719.
    KOi K01082.
    OMAi LQYNKEV.
    OrthoDBi EOG7WQ7SQ.
    PhylomeDBi O95861.
    TreeFami TF314300.

    Enzyme and pathway databases

    BRENDAi 3.1.3.7. 2681.
    Reactomei REACT_6913. Cytosolic sulfonation of small molecules.

    Miscellaneous databases

    EvolutionaryTracei O95861.
    GenomeRNAii 10380.
    NextBioi 35473949.
    PROi O95861.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95861.
    Bgeei O95861.
    CleanExi HS_BPNT1.
    Genevestigatori O95861.

    Family and domain databases

    InterProi IPR020583. Inositol_monoP_metal-BS.
    IPR000760. Inositol_monophosphatase.
    IPR020550. Inositol_monophosphatase_CS.
    [Graphical view ]
    PANTHERi PTHR20854. PTHR20854. 1 hit.
    Pfami PF00459. Inositol_P. 1 hit.
    [Graphical view ]
    PROSITEi PS00629. IMP_1. 1 hit.
    PS00630. IMP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate."
      Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.
      J. Biol. Chem. 274:13619-13628(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
    2. "Hydrolysis of inositol-1,4-bisphosphate by human and yeast lithium sensitive 3'-phosphoadenosine 5'-phosphate nucleotidases."
      Yenush L., Gil-Mascarell M., Serrano R., Rodriguez P.L.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: B-cell.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    4. "The DNA sequence and biological annotation of human chromosome 1."
      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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Skeletal muscle.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Human 3'(2'), 5'-bisphosphate nucleotidase 1 (BPNT1) in complex with AMP, PO4 and magnesium."
      Structural genomics consortium (SGC)
      Submitted (APR-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-308 IN COMPLEX WITH MAGNESIUM IONS AND AMP.

    Entry informationi

    Entry nameiBPNT1_HUMAN
    AccessioniPrimary (citable) accession number: O95861
    Secondary accession number(s): A8K7C8
    , B4DPS5, B4DUS9, D3DTA9, Q8WVL5, Q9UGJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3