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Protein

Inositol polyphosphate 1-phosphatase

Gene

Inpp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate.

Cofactori

Enzyme regulationi

Inhibited by Li+.By similarity

Pathwayi: phosphatidylinositol signaling pathway

This protein is involved in the pathway phosphatidylinositol signaling pathway, which is part of Signal transduction.
View all proteins of this organism that are known to be involved in the pathway phosphatidylinositol signaling pathway and in Signal transduction.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Magnesium 1By similarity
Binding sitei119 – 1191SubstrateBy similarity
Metal bindingi153 – 1531Magnesium 1By similarity
Metal bindingi153 – 1531Magnesium 2By similarity
Metal bindingi155 – 1551Magnesium 1; via carbonyl oxygenBy similarity
Metal bindingi156 – 1561Magnesium 2By similarity
Metal bindingi313 – 3131Magnesium 2By similarity
Binding sitei313 – 3131SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Lithium, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.57. 3474.
ReactomeiR-MMU-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
UniPathwayiUPA00944.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol polyphosphate 1-phosphatase (EC:3.1.3.57)
Short name:
IPP
Short name:
IPPase
Gene namesi
Name:Inpp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:104848. Inpp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Inositol polyphosphate 1-phosphatasePRO_0000142511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei314 – 3141PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP49442.
MaxQBiP49442.
PaxDbiP49442.
PeptideAtlasiP49442.
PRIDEiP49442.

2D gel databases

UCD-2DPAGEP49442.

PTM databases

iPTMnetiP49442.
PhosphoSiteiP49442.

Expressioni

Gene expression databases

BgeeiP49442.
CleanExiMM_INPP1.
ExpressionAtlasiP49442. baseline and differential.
GenevisibleiP49442. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi200767. 1 interaction.
IntActiP49442. 1 interaction.
STRINGi10090.ENSMUSP00000027271.

Structurei

3D structure databases

ProteinModelPortaliP49442.
SMRiP49442. Positions 1-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni155 – 1584Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiKOG3099. Eukaryota.
ENOG410XNMV. LUCA.
GeneTreeiENSGT00530000063462.
HOGENOMiHOG000007839.
HOVERGENiHBG006163.
InParanoidiP49442.
KOiK01107.
OMAiAGYKSLC.
OrthoDBiEOG7G4QG6.
PhylomeDBiP49442.
TreeFamiTF314300.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 2 hits.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDILLELLC VSEKAANIAR ACRQQETLFQ LLIEEKKGAE KNKKFAADFK
60 70 80 90 100
TLADVLVQEV IKQNMENKFP GLGKKVFGEE SNEFTNDLGE KITVELQSTE
110 120 130 140 150
EETAELLSKV LNGNMPASEA LAQVVHEDVD LTDPTLESLD ISIPHESLGI
160 170 180 190 200
WVDPIDSTYQ YIKGSANVKS NQGIFPSGLQ CVTILIGVYD LQTGLPLMGV
210 220 230 240 250
INQPFASQNL TTLRWKGQCY WGLSYMGTNI HSLQLAISKS DSETQTENSD
260 270 280 290 300
REFSSPFSAV ISTSEKDTIK AALSRVCGGS VFPAAGAGYK SLCVIQGLAD
310 320 330 340 350
IYIFSEDTTY KWDSCAAHAI LRAMGGGIVD MKECLERSPD TGLDLPQLLY
360 370 380 390
HVENKGASGV ELWANKGGLI AYRSRNRLDT FLSRLIQNLG PVKTQA
Length:396
Mass (Da):43,346
Last modified:August 31, 2004 - v2
Checksum:i799D555B153FC975
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101C → R in AAA97574 (PubMed:8586440).Curated
Sequence conflicti276 – 2761V → A in AAA97574 (PubMed:8586440).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27295 mRNA. Translation: AAA97574.1.
AK078382 mRNA. Translation: BAC37245.1.
BC025072 mRNA. Translation: AAH25072.1.
CCDSiCCDS14947.1.
RefSeqiNP_032410.2. NM_008384.2.
XP_011236743.1. XM_011238441.1.
XP_011236744.1. XM_011238442.1.
UniGeneiMm.917.

Genome annotation databases

EnsembliENSMUST00000027271; ENSMUSP00000027271; ENSMUSG00000026102.
GeneIDi16329.
KEGGimmu:16329.
UCSCiuc007ayo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27295 mRNA. Translation: AAA97574.1.
AK078382 mRNA. Translation: BAC37245.1.
BC025072 mRNA. Translation: AAH25072.1.
CCDSiCCDS14947.1.
RefSeqiNP_032410.2. NM_008384.2.
XP_011236743.1. XM_011238441.1.
XP_011236744.1. XM_011238442.1.
UniGeneiMm.917.

3D structure databases

ProteinModelPortaliP49442.
SMRiP49442. Positions 1-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200767. 1 interaction.
IntActiP49442. 1 interaction.
STRINGi10090.ENSMUSP00000027271.

PTM databases

iPTMnetiP49442.
PhosphoSiteiP49442.

2D gel databases

UCD-2DPAGEP49442.

Proteomic databases

EPDiP49442.
MaxQBiP49442.
PaxDbiP49442.
PeptideAtlasiP49442.
PRIDEiP49442.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027271; ENSMUSP00000027271; ENSMUSG00000026102.
GeneIDi16329.
KEGGimmu:16329.
UCSCiuc007ayo.2. mouse.

Organism-specific databases

CTDi3628.
MGIiMGI:104848. Inpp1.

Phylogenomic databases

eggNOGiKOG3099. Eukaryota.
ENOG410XNMV. LUCA.
GeneTreeiENSGT00530000063462.
HOGENOMiHOG000007839.
HOVERGENiHBG006163.
InParanoidiP49442.
KOiK01107.
OMAiAGYKSLC.
OrthoDBiEOG7G4QG6.
PhylomeDBiP49442.
TreeFamiTF314300.

Enzyme and pathway databases

UniPathwayiUPA00944.
BRENDAi3.1.3.57. 3474.
ReactomeiR-MMU-1855183. Synthesis of IP2, IP, and Ins in the cytosol.

Miscellaneous databases

ChiTaRSiInpp1. mouse.
PROiP49442.
SOURCEiSearch...

Gene expression databases

BgeeiP49442.
CleanExiMM_INPP1.
ExpressionAtlasiP49442. baseline and differential.
GenevisibleiP49442. MM.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 2 hits.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and chromosomal mapping of the mouse inositol polyphosphate 1-phosphatase gene."
    Okabe I., Nussbaum R.L.
    Genomics 30:358-360(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Cerebellum.
  3. "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: FVB/N.
    Tissue: Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiINPP_MOUSE
AccessioniPrimary (citable) accession number: P49442
Secondary accession number(s): Q8R3L1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 31, 2004
Last modified: July 6, 2016
This is version 133 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.