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Q9Z2L6

- MINP1_MOUSE

UniProt

Q9Z2L6 - MINP1_MOUSE

Protein

Multiple inositol polyphosphate phosphatase 1

Gene

Minpp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate By similarity. Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). May play a role in bone development (endochondral ossification).By similarity1 Publication

    Catalytic activityi

    Myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate.1 Publication
    2,3-bisphospho-D-glycerate + H2O = 2-phospho-D-glycerate + phosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei89 – 891Sequence Analysis

    GO - Molecular functioni

    1. acid phosphatase activity Source: InterPro
    2. bisphosphoglycerate 3-phosphatase activity Source: UniProtKB-EC
    3. inositol hexakisphosphate 2-phosphatase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BRENDAi3.1.3.62. 3474.
    ReactomeiREACT_196484. Synthesis of IPs in the ER lumen.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multiple inositol polyphosphate phosphatase 1 (EC:3.1.3.62)
    Alternative name(s):
    2,3-bisphosphoglycerate 3-phosphatase (EC:3.1.3.80)
    Short name:
    2,3-BPG phosphatase
    Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
    Short name:
    Ins(1,3,4,5)P(4) 3-phosphatase
    Gene namesi
    Name:Minpp1
    Synonyms:Mipp
    ORF Names:MNCb-1572
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1336159. Minpp1.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation. Cell membrane 1 Publication
    Note: Also attached to the plasma membrane in erythrocytes.Curated

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi89 – 891H → A: Loss of phosphatase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 481451Multiple inositol polyphosphate phosphatase 1PRO_0000019583Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9Z2L6.
    PaxDbiQ9Z2L6.
    PRIDEiQ9Z2L6.

    PTM databases

    PhosphoSiteiQ9Z2L6.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in kidney, intestine, thymus and liver.

    Developmental stagei

    Expressed in different stages of embryogenesis, from E7.5 through E14.5. The highest levels of expression is found in the visceral endoderm at E7.5 and E8.5 and in the fetal liver at E12.5 and E14.5.1 Publication

    Gene expression databases

    BgeeiQ9Z2L6.
    GenevestigatoriQ9Z2L6.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9Z2L6. 2 interactions.
    MINTiMINT-4119928.
    STRINGi10090.ENSMUSP00000025827.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z2L6.
    SMRiQ9Z2L6. Positions 79-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi478 – 4814Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG260296.
    GeneTreeiENSGT00390000018409.
    HOGENOMiHOG000113591.
    HOVERGENiHBG052872.
    InParanoidiQ3UA76.
    KOiK03103.
    OMAiADMEFGP.
    OrthoDBiEOG7992QC.
    TreeFamiTF324072.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    InterProiIPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    IPR016274. Histidine_acid_Pase_euk.
    [Graphical view]
    PfamiPF00328. His_Phos_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
    SUPFAMiSSF53254. SSF53254. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9Z2L6-1 [UniParc]FASTAAdd to Basket

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    MLRGARSHLP ASVAPAAVLA AALLSSFARC SLPGRGDPVA SVLSPYFGTK    50
    TRYEDANPWL LVDPVAPRRD PELLAGTCTP VQLVALIRHG TRYPTTKQIR 100
    KLKQLQGLLQ TRESRDGGSQ VAAALAEWPL WYGDWMDGQL VEKGRQDMRQ 150
    LALRLAALFP DLFSRENYDR LRLITSSKHR CVDSSAAFLQ GLWQHYHPGL 200
    PPPDVSDMEC GPPRINDKLM RFFDHCEKFL TDVERNETAL YHVEAFKTGP 250
    EMQKVLKKVA ATLQVPMNSL NADLIQVAFF TCSFDLAIKG VHSPWCDVFD 300
    VDDARVLEYL NDLKQYWKRS YGYTINSRSS CNLFQDIFLH LDKAVEQKQR 350
    SQPVSSPVIL QFGHAETLLP LLSLMGYFKD KEPLTAYNFE EQVNRKFRSG 400
    HIVPYASNLI FVLYHCDNAQ SPEEQFQIQL LLNEKVLPLA HSQRPVGLYE 450
    ELKTHYRDIL QSCQTSKECS PPKANITSDE L 481
    Length:481
    Mass (Da):54,537
    Last modified:July 27, 2011 - v3
    Checksum:i7CE78356B11F4606
    GO

    Sequence cautioni

    The sequence BAA95058.1 differs from that shown. Reason: Frameshift at positions 14 and 176.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti211 – 2111G → D in AAH21437. (PubMed:15489334)Curated
    Sequence conflicti257 – 2571K → Q in AAH21437. (PubMed:15489334)Curated
    Sequence conflicti267 – 2671M → V in AAH21437. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF046908 mRNA. Translation: AAD02434.1.
    AB041574 mRNA. Translation: BAA95058.1. Frameshift.
    AK151486 mRNA. Translation: BAE30439.1.
    BC021437 mRNA. Translation: AAH21437.1.
    CCDSiCCDS29751.1.
    RefSeqiNP_034929.1. NM_010799.2.
    UniGeneiMm.255116.

    Genome annotation databases

    EnsembliENSMUST00000025827; ENSMUSP00000025827; ENSMUSG00000024896.
    GeneIDi17330.
    KEGGimmu:17330.
    UCSCiuc008hfk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF046908 mRNA. Translation: AAD02434.1 .
    AB041574 mRNA. Translation: BAA95058.1 . Frameshift.
    AK151486 mRNA. Translation: BAE30439.1 .
    BC021437 mRNA. Translation: AAH21437.1 .
    CCDSi CCDS29751.1.
    RefSeqi NP_034929.1. NM_010799.2.
    UniGenei Mm.255116.

    3D structure databases

    ProteinModelPortali Q9Z2L6.
    SMRi Q9Z2L6. Positions 79-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Z2L6. 2 interactions.
    MINTi MINT-4119928.
    STRINGi 10090.ENSMUSP00000025827.

    PTM databases

    PhosphoSitei Q9Z2L6.

    Proteomic databases

    MaxQBi Q9Z2L6.
    PaxDbi Q9Z2L6.
    PRIDEi Q9Z2L6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025827 ; ENSMUSP00000025827 ; ENSMUSG00000024896 .
    GeneIDi 17330.
    KEGGi mmu:17330.
    UCSCi uc008hfk.2. mouse.

    Organism-specific databases

    CTDi 9562.
    MGIi MGI:1336159. Minpp1.

    Phylogenomic databases

    eggNOGi NOG260296.
    GeneTreei ENSGT00390000018409.
    HOGENOMi HOG000113591.
    HOVERGENi HBG052872.
    InParanoidi Q3UA76.
    KOi K03103.
    OMAi ADMEFGP.
    OrthoDBi EOG7992QC.
    TreeFami TF324072.

    Enzyme and pathway databases

    BRENDAi 3.1.3.62. 3474.
    Reactomei REACT_196484. Synthesis of IPs in the ER lumen.

    Miscellaneous databases

    NextBioi 291902.
    PROi Q9Z2L6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Z2L6.
    Genevestigatori Q9Z2L6.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    InterProi IPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    IPR016274. Histidine_acid_Pase_euk.
    [Graphical view ]
    Pfami PF00328. His_Phos_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000894. Acid_phosphatase. 1 hit.
    SUPFAMi SSF53254. SSF53254. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Multiple inositol polyphosphate phosphatase: evolution as a distinct group within the histidine phosphatase family and chromosomal localization of the human and mouse genes to chromosomes 10q23 and 19."
      Chi H., Tiller G.E., Dasouki M.J., Romano P.R., Wang J., O'keefe R.J., Puzas J.E., Rosier R.N., Reynolds P.R.
      Genomics 56:324-336(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-89.
      Strain: 129.
    2. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
      Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow.
    4. "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].
      Strain: Czech II.
      Tissue: Mammary gland.
    5. "Targeted deletion of Minpp1 provides new insight into the activity of multiple inositol polyphosphate phosphatase in vivo."
      Chi H., Yang X., Kingsley P.D., O'Keefe R.J., Puzas J.E., Rosier R.N., Shears S.B., Reynolds P.R.
      Mol. Cell. Biol. 20:6496-6507(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiMINP1_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2L6
    Secondary accession number(s): Q3UA76, Q8VDR0, Q9JJD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 100 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3