Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9ES52 (SHIP1_MOUSE)

Entry version 153 (08 May 2019)
Sequence version 2 (11 Sep 2007)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1

Gene

Inpp5d

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. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6.19 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.

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionHydrolase
Biological processApoptosis, Immunity

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1660499 Synthesis of PIPs at the plasma membrane
R-MMU-1855204 Synthesis of IP3 and IP4 in the cytosol
R-MMU-202424 Downstream TCR signaling
R-MMU-210990 PECAM1 interactions
R-MMU-912526 Interleukin receptor SHC signaling

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000873

<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 1 (EC:3.1.3.86)
Alternative name(s):
Inositol polyphosphate-5-phosphatase of 145 kDa
Short name:
SIP-145
SH2 domain-containing inositol 5'-phosphatase 1
Short name:
SH2 domain-containing inositol phosphatase 1
Short name:
SHIP-1
p150Ship
<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:Inpp5d
Synonyms:7a33, Ship, Ship1
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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 1

Organism-specific databases

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

More...MGIi		MGI:107357 Inpp5d

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, 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 and fertile. They however fail to thrive and only 40% survive by 14 weeks of age. Mortality is associated with extensive consolidation of the lungs resulting from infiltration by myeloid cells. Increased numbers of granulocyte-macrophage progenitors are observed in both the bone marrow and spleen. Absence of Inpp5d leads to steel factor-induced degranulation of mast cells. They also display increased numbers of osteoclast precursors leading to a severe osteoporosis.3 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>Mutagenesisi676D → G: Loss of function. 1 Publication1
Mutagenesisi918Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-1021. 3 Publications1
Mutagenesisi1021Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-918. 3 Publications1

<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_00003028671 – 1191Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1Add BLAST1191

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 residuei246PhosphoserineCombined sources1
Modified residuei918Phosphotyrosine1 Publication1
Modified residuei935PhosphoserineCombined sources1
Modified residuei945PhosphotyrosineCombined sources1
Modified residuei964PhosphothreonineCombined sources1
Modified residuei967PhosphoserineCombined sources1
Modified residuei972PhosphoserineCombined sources1
Modified residuei1021Phosphotyrosine1 Publication1

<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 cytokines, growth factors, antibodies, chemokines, integrin ligands and hypertonic and oxidative stress. Phosphorylated upon IgG receptor FCGR2B-binding.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9ES52

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

More...PaxDbi		Q9ES52

PeptideAtlas

More...PeptideAtlasi		Q9ES52

PRoteomics IDEntifications database

More...PRIDEi		Q9ES52

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9ES52

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

More...PhosphoSitePlusi		Q9ES52

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q9ES52

<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

Specifically expressed in immune and hematopoietic cells. Levels vary considerably within this compartment. Lost during erythropoiesis when erythroid cells become Ter119+. Increases substantially with T-cell maturation and when resting B-cells are activated. Also present in mature granulocytes, monocyte/macrophages, mast cells and platelets. Isoform 5 is the only form expressed in embryonic stem (ES) cells and is coexpressed with other isoforms in hematopoietic stem cells, and disappears with differentiation.4 Publications

<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

Expressed in late primitive-streak stage embryos (7.5 dpc), when hematopoiesis is thought to begin, and the expression is restricted to the hematopoietic lineage in embryo. In adults expression continues to be in the majority of cells from hematopoietic origin, including granulocytes, monocytes and lymphocytes, and is also found in the spermatids of the testis.2 Publications

<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

By activin/TGF-beta (at protein level). Regulated by the Smad pathway. Isoform 3 is expressed during myeloid development.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000026288 Expressed in 216 organ(s), highest expression level in stroma of bone marrow

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9ES52 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9ES52 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 (PubMed:8654924, PubMed:8643691, PubMed:10068665, PubMed:9083021, PubMed:9099679, PubMed:10395202). Interacts with tyrosine phosphorylated form of DOK1 (PubMed:11031258). Interacts with tyrosine phosphorylated form of DOK3 (PubMed:14993273). Interacts with tyrosine phosphorylated form of SLAMF1/CD150 (By similarity). Interacts with PTPN11/SHP-2 in response to IL-3 (PubMed:9110989, PubMed:9393882). Interacts with receptor EPOR (PubMed:10660611). Interacts with receptors MS4A2/FCER1B and FCER1G (By similarity). Interacts with receptors FCGR2B and FCGR3 (PubMed:10395202, PubMed:11016922, PubMed:10779347, PubMed:15456754, PubMed:12393695). Interacts with receptor FCGR2A, leading to regulate gene expression during the phagocytic process (PubMed:12370370). Interacts with GRB2 (PubMed:8643691, PubMed:10068665). Interacts with PLCG1 (PubMed:16000869). Interacts with tyrosine kinases SRC and TEC (PubMed:10794720, PubMed:15492005). Interacts with CRKL (PubMed:11031258). Interacts with c-Met/MET (PubMed:11896575). Interacts with MILR1 (tyrosine-phosphorylated) (PubMed:20526344). Isoform 5 interacts with IL6ST/gp130 (PubMed:17105399). Can weakly interact (via NPXY motif 2) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif (PubMed:11247302).By similarity23 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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		200769, 25 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9ES52

Protein interaction database and analysis system

More...IntActi		Q9ES52, 16 interactors

Molecular INTeraction database

More...MINTi		Q9ES52

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000127941

<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

3D structure databases

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

More...SMRi		Q9ES52

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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>Domaini8 – 104SH2PROSITE-ProRule annotationAdd BLAST97

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1015 – 1029Interaction with DAB21 PublicationAdd BLAST15

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>Motifi127 – 132SH3-binding 16
Motifi915 – 918NPXY motif 14
Motifi970 – 975SH3-binding 26
Motifi1018 – 1021NPXY motif 24
Motifi1039 – 1050SH3-binding 3Add BLAST12

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 biasi962 – 1153Pro-richAdd BLAST192

<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 PTPN11/SHP-2. It competes with that of GRB2 for binding to phosphorylated SHC1 to inhibit the Ras pathway. It is also required for tyrosine phosphorylation.1 Publication
The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain.1 Publication

<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

Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.Curated

Keywords - Domaini

Repeat, SH2 domain, SH3-binding

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0565 Eukaryota
COG5411 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156202

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9ES52

KEGG Orthology (KO)

More...KOi		K03084

Identification of Orthologs from Complete Genome Data

More...OMAi		HFQGEIK

Database of Orthologous Groups

More...OrthoDBi		311217at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9ES52

TreeFam database of animal gene trees

More...TreeFami		TF323475

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.505.10, 1 hit
3.60.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036691 Endo/exonu/phosph_ase_sf
IPR005135 Endo/exonuclease/phosphatase
IPR000300 IPPc
IPR000980 SH2
IPR036860 SH2_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03372 Exo_endo_phos, 1 hit
PF00017 SH2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00401 SH2DOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00128 IPPc, 1 hit
SM00252 SH2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55550 SSF55550, 1 hit
SSF56219 SSF56219, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
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>Sequences (6+)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 describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9ES52-1) [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
        10         20         30         40         50
MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR 
        60         70         80         90        100
NCVYTYRILP NEDDKFTVQA SEGVPMRFFT KLDQLIDFYK KENMGLVTHL 
       110        120        130        140        150
QYPVPLEEED AIDEAEEDTV ESVMSPPELP PRNIPMSAGP SEAKDLPLAT 
       160        170        180        190        200
ENPRAPEVTR LSLSETLFQR LQSMDTSGLP EEHLKAIQDY LSTQLLLDSD 
       210        220        230        240        250
FLKTGSSNLP HLKKLMSLLC KELHGEVIRT LPSLESLQRL FDQQLSPGLR 
       260        270        280        290        300
PRPQVPGEAS PITMVAKLSQ LTSLLSSIED KVKSLLHEGS ESTNRRSLIP 
       310        320        330        340        350
PVTFEVKSES LGIPQKMHLK VDVESGKLIV KKSKDGSEDK FYSHKKILQL 
       360        370        380        390        400
IKSQKFLNKL VILVETEKEK ILRKEYVFAD SKKREGFCQL LQQMKNKHSE 
       410        420        430        440        450
QPEPDMITIF IGTWNMGNAP PPKKITSWFL SKGQGKTRDD SADYIPHDIY 
       460        470        480        490        500
VIGTQEDPLG EKEWLELLRH SLQEVTSMTF KTVAIHTLWN IRIVVLAKPE 
       510        520        530        540        550
HENRISHICT DNVKTGIANT LGNKGAVGVS FMFNGTSLGF VNSHLTSGSE 
       560        570        580        590        600
KKLRRNQNYM NILRFLALGD KKLSPFNITH RFTHLFWLGD LNYRVELPTW 
       610        620        630        640        650
EAEAIIQKIK QQQYSDLLAH DQLLLERKDQ KVFLHFEEEE ITFAPTYRFE 
       660        670        680        690        700
RLTRDKYAYT KQKATGMKYN LPSWCDRVLW KSYPLVHVVC QSYGSTSDIM 
       710        720        730        740        750
TSDHSPVFAT FEAGVTSQFV SKNGPGTVDS QGQIEFLACY ATLKTKSQTK 
       760        770        780        790        800
FYLEFHSSCL ESFVKSQEGE NEEGSEGELV VRFGETLPKL KPIISDPEYL 
       810        820        830        840        850
LDQHILISIK SSDSDESYGE GCIALRLETT EAQHPIYTPL THHGEMTGHF 
       860        870        880        890        900
RGEIKLQTSQ GKMREKLYDF VKTERDESSG MKCLKNLTSH DPMRQWEPSG 
       910        920        930        940        950
RVPACGVSSL NEMINPNYIG MGPFGQPLHG KSTLSPDQQL TAWSYDQLPK 
       960        970        980        990       1000
DSSLGPGRGE GPPTPPSQPP LSPKKFSSST ANRGPCPRVQ EARPGDLGKV 
      1010       1020       1030       1040       1050
EALLQEDLLL TKPEMFENPL YGSVSSFPKL VPRKEQESPK MLRKEPPPCP 
      1060       1070       1080       1090       1100
DPGISSPSIV LPKAQEVESV KGTSKQAPVP VLGPTPRIRS FTCSSSAEGR 
      1110       1120       1130       1140       1150
MTSGDKSQGK PKASASSQAP VPVKRPVKPS RSEMSQQTTP IPAPRPPLPV 
      1160       1170       1180       1190 
KSPAVLQLQH SKGRDYRDNT ELPHHGKHRQ EEGLLGRTAM Q
Length:1,191
Mass (Da):133,542
Last modified:September 11, 2007 - v2
<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:iAF9F21326A59EC7A
GO
Isoform 2 (identifier: Q9ES52-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     120-120: Missing.

Show »
Length:1,190
Mass (Da):133,443
Checksum:iDF81F3046F33A07F
GO
Isoform 3 (identifier: Q9ES52-3) [UniParc]FASTAAdd to basket
Also known as: 135 kDa SHIP

The sequence of this isoform differs from the canonical sequence as follows:
     920-980: Missing.

Show »
Length:1,130
Mass (Da):127,199
Checksum:iC3E2F1EB206034BF
GO
Isoform 4 (identifier: Q9ES52-4) [UniParc]FASTAAdd to basket
Also known as: SHIPdelta

The sequence of this isoform differs from the canonical sequence as follows:
     120-120: Missing.
     920-960: GMGPFGQPLH...DSSLGPGRGE → VFIFHSQPRS...GPAADEARDV
     961-1191: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:959
Mass (Da):108,345
Checksum:iB95D49476957345E
GO
Isoform 5 (identifier: Q9ES52-5) [UniParc]FASTAAdd to basket
Also known as: s-SHIP

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: Missing.

Show »
Length:928
Mass (Da):104,101
Checksum:i7390D08E57505B82
GO
Isoform 6 (identifier: Q9ES52-6) [UniParc]FASTAAdd to basket
Also known as: s-SHIPD183

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: Missing.
     920-980: Missing.

Show »
Length:867
Mass (Da):97,758
Checksum:iF848515DE853AD65
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F7BZA7F7BZA7_MOUSE
Phosphatidylinositol 3,4,5-trisphos...
Inpp5d
124Annotation 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>
E9Q752E9Q752_MOUSE
Phosphatidylinositol 3,4,5-trisphos...
Inpp5d
35Annotation 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>

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 conflicti43Y → C in AAB18937 (PubMed:8643691).Curated1
Sequence conflicti527V → A in AAC53023 (PubMed:9027494).Curated1
Sequence conflicti534N → I in AAC53023 (PubMed:9027494).Curated1
Sequence conflicti905C → E AA sequence (PubMed:8643691).Curated1
Sequence conflicti981A → T in AAB18937 (PubMed:8643691).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0279801 – 263Missing in isoform 5 and isoform 6. 1 PublicationAdd BLAST263
Alternative sequenceiVSP_027981120Missing in isoform 2 and isoform 4. 4 Publications1
Alternative sequenceiVSP_027982920 – 980Missing in isoform 3 and isoform 6. 1 PublicationAdd BLAST61
Alternative sequenceiVSP_027983920 – 960GMGPF…PGRGE → VFIFHSQPRSLPQGARGKTW GSGKGGSSAPGGPAADEARD V in isoform 4. 1 PublicationAdd BLAST41
Alternative sequenceiVSP_027984961 – 1191Missing in isoform 4. 1 PublicationAdd BLAST231

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U51742 mRNA Translation: AAC52606.1
U39203 mRNA Translation: AAB18937.1
U52044 mRNA Translation: AAC53023.1
AF125996 mRNA Translation: AAD37118.1
AF235502
, AF235496, AF235498, AF235499, AF235500, AF235501 Genomic DNA Translation: AAG23922.1
AF228679 mRNA Translation: AAF69143.1
AF184912 mRNA Translation: AAF25823.1
AF184913 mRNA Translation: AAF25824.1
AK143560 mRNA Translation: BAE25436.1
BC108328 mRNA Translation: AAI08329.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS35655.1 [Q9ES52-1]
CCDS48310.1 [Q9ES52-3]
CCDS48311.1 [Q9ES52-2]

Protein sequence database of the Protein Information Resource

More...PIRi		JC6118

NCBI Reference Sequences

More...RefSeqi		NP_001103662.1, NM_001110192.2 [Q9ES52-2]
NP_001103663.1, NM_001110193.2 [Q9ES52-3]
NP_034696.2, NM_010566.3 [Q9ES52-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000042275; ENSMUSP00000044647; ENSMUSG00000026288 [Q9ES52-2]
ENSMUST00000072999; ENSMUSP00000072763; ENSMUSG00000026288 [Q9ES52-4]
ENSMUST00000167032; ENSMUSP00000126569; ENSMUSG00000026288 [Q9ES52-5]
ENSMUST00000168783; ENSMUSP00000131244; ENSMUSG00000026288 [Q9ES52-3]
ENSMUST00000169754; ENSMUSP00000127941; ENSMUSG00000026288 [Q9ES52-1]
ENSMUST00000170300; ENSMUSP00000132384; ENSMUSG00000026288 [Q9ES52-6]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		16331

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:16331

UCSC genome browser

More...UCSCi		uc007bxc.3 mouse [Q9ES52-1]
uc007bxd.3 mouse [Q9ES52-3]
uc007bxf.3 mouse [Q9ES52-2]
uc007bxg.3 mouse [Q9ES52-6]

Keywords - Coding sequence diversityi

Alternative splicing

<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
U51742 mRNA Translation: AAC52606.1
U39203 mRNA Translation: AAB18937.1
U52044 mRNA Translation: AAC53023.1
AF125996 mRNA Translation: AAD37118.1
AF235502
, AF235496, AF235498, AF235499, AF235500, AF235501 Genomic DNA Translation: AAG23922.1
AF228679 mRNA Translation: AAF69143.1
AF184912 mRNA Translation: AAF25823.1
AF184913 mRNA Translation: AAF25824.1
AK143560 mRNA Translation: BAE25436.1
BC108328 mRNA Translation: AAI08329.1
CCDSiCCDS35655.1 [Q9ES52-1]
CCDS48310.1 [Q9ES52-3]
CCDS48311.1 [Q9ES52-2]
PIRiJC6118
RefSeqiNP_001103662.1, NM_001110192.2 [Q9ES52-2]
NP_001103663.1, NM_001110193.2 [Q9ES52-3]
NP_034696.2, NM_010566.3 [Q9ES52-1]

3D structure databases

SMRiQ9ES52
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200769, 25 interactors
CORUMiQ9ES52
IntActiQ9ES52, 16 interactors
MINTiQ9ES52
STRINGi10090.ENSMUSP00000127941

Chemistry databases

SwissLipidsiSLP:000000873

PTM databases

iPTMnetiQ9ES52
PhosphoSitePlusiQ9ES52
SwissPalmiQ9ES52

Proteomic databases

jPOSTiQ9ES52
PaxDbiQ9ES52
PeptideAtlasiQ9ES52
PRIDEiQ9ES52

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042275; ENSMUSP00000044647; ENSMUSG00000026288 [Q9ES52-2]
ENSMUST00000072999; ENSMUSP00000072763; ENSMUSG00000026288 [Q9ES52-4]
ENSMUST00000167032; ENSMUSP00000126569; ENSMUSG00000026288 [Q9ES52-5]
ENSMUST00000168783; ENSMUSP00000131244; ENSMUSG00000026288 [Q9ES52-3]
ENSMUST00000169754; ENSMUSP00000127941; ENSMUSG00000026288 [Q9ES52-1]
ENSMUST00000170300; ENSMUSP00000132384; ENSMUSG00000026288 [Q9ES52-6]
GeneIDi16331
KEGGimmu:16331
UCSCiuc007bxc.3 mouse [Q9ES52-1]
uc007bxd.3 mouse [Q9ES52-3]
uc007bxf.3 mouse [Q9ES52-2]
uc007bxg.3 mouse [Q9ES52-6]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3635
MGIiMGI:107357 Inpp5d

Phylogenomic databases

eggNOGiKOG0565 Eukaryota
COG5411 LUCA
GeneTreeiENSGT00940000156202
InParanoidiQ9ES52
KOiK03084
OMAiHFQGEIK
OrthoDBi311217at2759
PhylomeDBiQ9ES52
TreeFamiTF323475

Enzyme and pathway databases

ReactomeiR-MMU-1660499 Synthesis of PIPs at the plasma membrane
R-MMU-1855204 Synthesis of IP3 and IP4 in the cytosol
R-MMU-202424 Downstream TCR signaling
R-MMU-210990 PECAM1 interactions
R-MMU-912526 Interleukin receptor SHC signaling

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q9ES52

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000026288 Expressed in 216 organ(s), highest expression level in stroma of bone marrow
ExpressionAtlasiQ9ES52 baseline and differential
GenevisibleiQ9ES52 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
IPR000980 SH2
IPR036860 SH2_dom_sf
PfamiView protein in Pfam
PF03372 Exo_endo_phos, 1 hit
PF00017 SH2, 1 hit
PRINTSiPR00401 SH2DOMAIN
SMARTiView protein in SMART
SM00128 IPPc, 1 hit
SM00252 SH2, 1 hit
SUPFAMiSSF55550 SSF55550, 1 hit
SSF56219 SSF56219, 1 hit
PROSITEiView protein in PROSITE
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 nameiSHIP1_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: Q9ES52
Secondary accession number(s): Q3UPF9
, Q4U212, Q61034, Q61173, Q61181, Q9JKR7, Q9JLF9, Q9JLG0, Q9QVN8, Q9WUC2
<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: September 11, 2007
Last modified: May 8, 2019
This is version 153 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again