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Protein

Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2

Gene

Inppl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity).By similarity6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane. Enzymatic activity is enhanced in the presence of phosphatidylserine (By similarity).By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActin-binding, Hydrolase
Biological processCell adhesion, Immunity

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.3.36 3474

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-MMU-1660499 Synthesis of PIPs at the plasma membrane
R-MMU-1855204 Synthesis of IP3 and IP4 in the cytosol
R-MMU-912526 Interleukin receptor SHC signaling

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC:3.1.3.86)
Alternative name(s):
AblSH3-binding protein
Inositol polyphosphate phosphatase-like protein 1
Short name:
INPPL-1
SH2 domain-containing inositol 5'-phosphatase 2
Short name:
SH2 domain-containing inositol phosphatase 2
Short name:
SHIP-2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Inppl1
Synonyms:Ship2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1333787 Inppl1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice are viable, have normal glucose and insulin levels, and normal insulin and glucose tolerance. They are however highly resistant to weight gain when placed on a high-fat diet, suggesting that inhibition of Inppl1 would be useful in the effort to ameliorate diet-induced obesity. According to preliminary results from PubMed:11343120, mice display increased sensitivity to insulin, characterized by severe neonatal hypoglycemia, deregulated expression of the genes involved in gluconeogenesis, and perinatal death. They display increased glucose tolerance and insulin sensitivity associated with an increased recruitment of the Slc2a4/Glut4 glucose transporter and increased glycogen synthesis in skeletal muscles. However, these knockout mice also contain a deletion of the last exon of Phox2a gene. It is therefore unknown whether the insulin sensitivity observed in these mice result from inactivation of either Inppl1 or Phox2a.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi47R → A: Does not affect the ability to inhibit PKB activity. 1 Publication1
Mutagenesisi608D → A: Abolishes both enzyme activity and ability to inhibit PKB activity. 1 Publication1
Mutagenesisi690C → A: Induces little effect. 1 Publication1
Mutagenesisi692R → A: Still partially active. 1 Publication1
Mutagenesisi987Y → F: Does not affect the ability to inhibit PKB activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2331063

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003028711 – 1257Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2Add BLAST1257

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei132PhosphoserineCombined sources1
Modified residuei165PhosphothreonineBy similarity1
Modified residuei241PhosphoserineBy similarity1
Modified residuei353PhosphoserineBy similarity1
Modified residuei887PhosphotyrosineBy similarity1
Modified residuei891PhosphoserineBy similarity1
Modified residuei987PhosphotyrosineBy similarity1
Modified residuei1132PhosphoserineBy similarity1
Modified residuei1136PhosphotyrosineBy similarity1
Modified residuei1161PhosphotyrosineBy similarity1
Modified residuei1256PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as insulin, growth factors such as EGF or PDGF, chemokines, integrin ligands and hypertonic and oxidative stress. May be phosphorylated upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-987 following cell attachment and spreading. Phosphorylated at Tyr-1161 following EGF signaling pathway stimulation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q6P549

MaxQB - The MaxQuant DataBase

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MaxQBi
Q6P549

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q6P549

PeptideAtlas

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PeptideAtlasi
Q6P549

PRoteomics IDEntifications database

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PRIDEi
Q6P549

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q6P549

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q6P549

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In E15.5 embryos, it is strongly expressed in the liver, specific regions of the central nervous system, the thymus, the lung, and the cartilage perichondrium. In adult it is markedly present in the brain and the thymus and at different stages of spermatozoa maturation in the seminiferous tubules.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Overexpressed in diabetic db/db mice.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000032737 Expressed in 299 organ(s), highest expression level in heart

CleanEx database of gene expression profiles

More...
CleanExi
MM_INPPL1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q6P549 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q6P549 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with tyrosine phosphorylated form of SHC1 (By similarity). Interacts with EGFR (By similarity). Upon stimulation by the EGF signaling pathway, it forms a complex with SHC1 and EGFR (By similarity). Interacts with cytoskeletal protein SORBS3/vinexin, promoting its localization to the periphery of cells (By similarity). Forms a complex with filamin (FLNA or FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and submembraneous actin (By similarity). Interacts with c-Met/MET, when c-Met/MET is phosphorylated on 'Tyr-1356' (By similarity). Interacts with p130Cas/BCAR1 (By similarity). Interacts with CENTD3/ARAP3 via its SAM domain (By similarity). Interacts with c-Cbl/CBL and CAP/SORBS1 (By similarity). Interacts with activated EPHA2 receptor (By similarity). Interacts with receptors FCGR2A (By similarity). Interacts with FCGR2B (PubMed:10789675, PubMed:15456754). Interacts with tyrosine kinase ABL1 (By similarity). Interacts with tyrosine kinase TEC (PubMed:15492005). Interacts with CSF1R (PubMed:15557176). Interacts (via N-terminus) with SH3YL1 (via SH3 domain) (PubMed:21624956).By similarity5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Itsn1Q9Z0R4-22EBI-2642932,EBI-8052786

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
200770, 5 interactors

Protein interaction database and analysis system

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IntActi
Q6P549, 6 interactors

Molecular INTeraction database

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MINTi
Q6P549

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000048057

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q6P549

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q6P549

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini21 – 117SH2PROSITE-ProRule annotationAdd BLAST97
Domaini1195 – 1257SAMPROSITE-ProRule annotationAdd BLAST63

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi945 – 950SH3-binding6
Motifi984 – 987NPXY motif4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi936 – 1170Pro-richAdd BLAST235

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The SH2 domain interacts with tyrosine phosphorylated forms of proteins such as SHC1 or FCGR2A. It also mediates the interaction with p130Cas/BCAR1 (By similarity).By similarity
The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

SH2 domain, SH3-binding

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0565 Eukaryota
KOG4384 Eukaryota
COG5411 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156576

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000004836

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG106726

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q6P549

KEGG Orthology (KO)

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KOi
K15909

Identification of Orthologs from Complete Genome Data

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OMAi
RVGWSNK

Database of Orthologous Groups

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OrthoDBi
EOG091G00P6

Database for complete collections of gene phylogenies

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PhylomeDBi
Q6P549

TreeFam database of animal gene trees

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TreeFami
TF323475

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.505.10, 1 hit
3.60.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036691 Endo/exonu/phosph_ase_sf
IPR005135 Endo/exonuclease/phosphatase
IPR000300 IPPc
IPR001660 SAM
IPR013761 SAM/pointed_sf
IPR000980 SH2
IPR036860 SH2_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF03372 Exo_endo_phos, 1 hit
PF00536 SAM_1, 1 hit
PF00017 SH2, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00401 SH2DOMAIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00128 IPPc, 1 hit
SM00454 SAM, 1 hit
SM00252 SH2, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47769 SSF47769, 1 hit
SSF55550 SSF55550, 1 hit
SSF56219 SSF56219, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50105 SAM_DOMAIN, 1 hit
PS50001 SH2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q6P549-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASVCGTPSP GGALGSPAPA WYHRDLSRAA AEELLARAGR DGSFLVRDSE
60 70 80 90 100
SVAGAFALCV LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG
110 120 130 140 150
LYAQPNQGLV CALLLPVEGE REPDPPDDRD ASDVEDEKPP LPPRSGSTSI
160 170 180 190 200
SAPVGPSSPL PTPETPTTPA AESTPNGLST VSHEYLKGSY GLDLEAVRGG
210 220 230 240 250
ASNLPHLTRT LVTSCRRLHS EVDKVLSGLE ILSKVFDQQS SPMVTRLLQQ
260 270 280 290 300
QSLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPLQP
310 320 330 340 350
SIRKAKTIPV QAFEVKLDVT LGDLTKIGKS QKFTLSVDVE GGRLVLLRRQ
360 370 380 390 400
RDSQEDWTTF THDRIRQLIK SQRVQNKLGV VFEKEKDRTQ RKDFIFVSAR
410 420 430 440 450
KREAFCQLLQ LMKNRHSKQD EPDMISVFIG TWNMGSVPPP KNVTSWFTSK
460 470 480 490 500
GLGKALDEVT VTIPHDIYVF GTQENSVGDR EWLDLLRGGL KELTDLDYRP
510 520 530 540 550
IAMQSLWNIK VAVLVKPEHE NRISHVSTSS VKTGIANTLG NKGAVGVSFM
560 570 580 590 600
FNGTSFGFVN CHLTSGNEKT TRRNQNYLDI LRLLSLGDRQ LSAFDISLRF
610 620 630 640 650
THLFWFGDLN YRLDMDIQEI LNYISRREFE PLLRVDQLNL EREKHKVFLR
660 670 680 690 700
FSEEEISFPP TYRYERGSRD TYAWHKQKPT GVRTNVPSWC DRILWKSYPE
710 720 730 740 750
THIICNSYGC TDDIVTSDHS PVFGTFEVGV TSQFISKKGL SKTSDQAYIE
760 770 780 790 800
FESIEAIVKT ASRTKFFIEF YSTCLEEYKK SFENDAQSSD NINFLKVQWS
810 820 830 840 850
SRQLPTLKPI LADIEYLQDQ HLLLTVKSMD GYESYGECVV ALKSMIGSTA
860 870 880 890 900
QQFLTFLSHR GEETGNIRGS MKVRVPTERL GTRERLYEWI SIDKDDTGAK
910 920 930 940 950
SKVPSVSRGS QEHRSGSRKP ASTETSCPLS KLFEEPEKPP PTGRPPAPPR
960 970 980 990 1000
AVPREEPLNP RLKSEGTSEQ EGVAAPPPKN SFNNPAYYVL EGVPHQLLPL
1010 1020 1030 1040 1050
EPPSLARAPL PPATKNKVAI TVPAPQLGRH RTPRVGEGSS SDEDSGGTLP
1060 1070 1080 1090 1100
PPDFPPPPLP DSAIFLPPNL DPLSMPVVRG RSGGEARGPP PPKAHPRPPL
1110 1120 1130 1140 1150
PPGTSPASTF LGEVASGDDR SCSVLQMAKT LSEVDYAPGP GRSALLPNPL
1160 1170 1180 1190 1200
ELQPPRGPSD YGRPLSFPPP RIRESIQEDL AEEAPCPQGG RASGLGEAGM
1210 1220 1230 1240 1250
GAWLRAIGLE RYEEGLVHNG WDDLEFLSDI TEEDLEEAGV QDPAHKRLLL

DTLQLSK
Length:1,257
Mass (Da):138,973
Last modified:July 5, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB66DF96BEF22F01E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WPT7A0A087WPT7_MOUSE
Phosphatidylinositol 3,4,5-trisphos...
Inppl1
1,166Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GST7A0A1B0GST7_MOUSE
Phosphatidylinositol 3,4,5-trisphos...
Inppl1
276Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GR64A0A1B0GR64_MOUSE
Phosphatidylinositol 3,4,5-trisphos...
Inppl1
603Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAI19454 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti412M → I in AAF28187 (PubMed:10610720).Curated1
Sequence conflicti506L → I in AAF28187 (PubMed:10610720).Curated1
Sequence conflicti705C → S in AAB82337 (PubMed:9126384).Curated1
Sequence conflicti972G → V in AAF28187 (PubMed:10610720).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF162781 mRNA Translation: AAF28187.1
BC049961 mRNA Translation: AAH49961.1
BC063080 mRNA Translation: AAH63080.1
BC119453 mRNA Translation: AAI19454.1 Different initiation.
U92477 mRNA Translation: AAB82337.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS21515.1

NCBI Reference Sequences

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RefSeqi
NP_001116211.1, NM_001122739.1
NP_034697.2, NM_010567.2
XP_006507454.1, XM_006507391.3
XP_011239984.1, XM_011241682.2
XP_017177480.1, XM_017321991.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.476000

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000035836; ENSMUSP00000048057; ENSMUSG00000032737
ENSMUST00000165052; ENSMUSP00000132883; ENSMUSG00000032737

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
16332

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:16332

UCSC genome browser

More...
UCSCi
uc009ipg.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF162781 mRNA Translation: AAF28187.1
BC049961 mRNA Translation: AAH49961.1
BC063080 mRNA Translation: AAH63080.1
BC119453 mRNA Translation: AAI19454.1 Different initiation.
U92477 mRNA Translation: AAB82337.1
CCDSiCCDS21515.1
RefSeqiNP_001116211.1, NM_001122739.1
NP_034697.2, NM_010567.2
XP_006507454.1, XM_006507391.3
XP_011239984.1, XM_011241682.2
XP_017177480.1, XM_017321991.1
UniGeneiMm.476000

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5ZRXX-ray1.50A/B1200-1257[»]
ProteinModelPortaliQ6P549
SMRiQ6P549
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200770, 5 interactors
IntActiQ6P549, 6 interactors
MINTiQ6P549
STRINGi10090.ENSMUSP00000048057

Chemistry databases

ChEMBLiCHEMBL2331063

PTM databases

iPTMnetiQ6P549
PhosphoSitePlusiQ6P549

Proteomic databases

EPDiQ6P549
MaxQBiQ6P549
PaxDbiQ6P549
PeptideAtlasiQ6P549
PRIDEiQ6P549

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035836; ENSMUSP00000048057; ENSMUSG00000032737
ENSMUST00000165052; ENSMUSP00000132883; ENSMUSG00000032737
GeneIDi16332
KEGGimmu:16332
UCSCiuc009ipg.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3636
MGIiMGI:1333787 Inppl1

Phylogenomic databases

eggNOGiKOG0565 Eukaryota
KOG4384 Eukaryota
COG5411 LUCA
GeneTreeiENSGT00940000156576
HOGENOMiHOG000004836
HOVERGENiHBG106726
InParanoidiQ6P549
KOiK15909
OMAiRVGWSNK
OrthoDBiEOG091G00P6
PhylomeDBiQ6P549
TreeFamiTF323475

Enzyme and pathway databases

BRENDAi3.1.3.36 3474
ReactomeiR-MMU-1660499 Synthesis of PIPs at the plasma membrane
R-MMU-1855204 Synthesis of IP3 and IP4 in the cytosol
R-MMU-912526 Interleukin receptor SHC signaling

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Inppl1 mouse

Protein Ontology

More...
PROi
PR:Q6P549

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000032737 Expressed in 299 organ(s), highest expression level in heart
CleanExiMM_INPPL1
ExpressionAtlasiQ6P549 baseline and differential
GenevisibleiQ6P549 MM

Family and domain databases

Gene3Di3.30.505.10, 1 hit
3.60.10.10, 1 hit
InterProiView protein in InterPro
IPR036691 Endo/exonu/phosph_ase_sf
IPR005135 Endo/exonuclease/phosphatase
IPR000300 IPPc
IPR001660 SAM
IPR013761 SAM/pointed_sf
IPR000980 SH2
IPR036860 SH2_dom_sf
PfamiView protein in Pfam
PF03372 Exo_endo_phos, 1 hit
PF00536 SAM_1, 1 hit
PF00017 SH2, 1 hit
PRINTSiPR00401 SH2DOMAIN
SMARTiView protein in SMART
SM00128 IPPc, 1 hit
SM00454 SAM, 1 hit
SM00252 SH2, 1 hit
SUPFAMiSSF47769 SSF47769, 1 hit
SSF55550 SSF55550, 1 hit
SSF56219 SSF56219, 1 hit
PROSITEiView protein in PROSITE
PS50105 SAM_DOMAIN, 1 hit
PS50001 SH2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSHIP2_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6P549
Secondary accession number(s): O08611
, Q0VDX5, Q80YB9, Q9JLL7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 5, 2004
Last modified: December 5, 2018
This is version 124 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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