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Protein

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

Gene

INPPL1

Organism
Homo sapiens (Human)
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 (PubMed:21624956). 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.10 Publications

Miscellaneous

Its ability to confer resistance to dietary obesity suggests that it may serve as a possible therapeutic target in cases of type 2 diabetes and obesity.

<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.1 Publication

<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

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS09233-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.1.3.86 2681

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O15357

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
O15357

SIGNOR Signaling Network Open Resource

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SIGNORi
O15357

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000000953

<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):
Inositol polyphosphate phosphatase-like protein 1
Short name:
INPPL-1
Protein 51C
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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000165458.13

Human Gene Nomenclature Database

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HGNCi
HGNC:6080 INPPL1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600829 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O15357

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Diabetes mellitus, non-insulin-dependent (NIDDM)2 Publications
Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Disease descriptionA multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
See also OMIM:125853
Genetic variations in INPPL1 may be a cause of susceptibility to metabolic syndrome. Metabolic syndrome is characterized by diabetes, insulin resistance, hypertension, and hypertriglyceridemia is absent.2 Publications
Opsismodysplasia (OPSMD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare skeletal dysplasia involving delayed bone maturation. Clinical signs observed at birth include short limbs, small hands and feet, relative macrocephaly with a large anterior fontanel, and characteristic craniofacial abnormalities including a prominent brow, depressed nasal bridge, a small anteverted nose, and a relatively long philtrum. Death secondary to respiratory failure during the first few years of life has been reported, but there can be long-term survival. Typical radiographic findings include shortened long bones with very delayed epiphyseal ossification, severe platyspondyly, metaphyseal cupping, and characteristic abnormalities of the metacarpals and phalanges.
See also OMIM:258480
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_069586401R → W in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514511EnsemblClinVar.1
Natural variantiVAR_069587659P → S in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514510EnsemblClinVar.1
Natural variantiVAR_069588688W → C in OPSMD. 1 Publication1
Natural variantiVAR_069589722F → I in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514512EnsemblClinVar.1

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 → G: Abolishes interaction with p130Cas/BCAR1 and its ability to induce increased adhesion. Abolishes phosphorylation upon FCGR2A clustering. 2 Publications1
Mutagenesisi140 – 141PL → AA: Abolishes interaction with SH3YL1. 1 Publication2
Mutagenesisi607D → A: Abolishes enzyme activity but not phosphorylation upon FCGR2A clustering. 1 Publication1
Mutagenesisi958T → A: Reduces PDGF-stimulated tyrosine phosphorylation and association with SHC1. 1 Publication1
Mutagenesisi986 – 987YY → FF: Inducer a strong reduction of phosphorylation upon re-plating on collagen I. 1 Publication2

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
3636

MalaCards human disease database

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MalaCardsi
INPPL1
MIMi125853 phenotype
258480 phenotype

Open Targets

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OpenTargetsi
ENSG00000165458

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
2746 Opsismodysplasia
3144 Schneckenbecken dysplasia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29888

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2331064

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1459

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
INPPL1

<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_00003028701 – 1258Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2Add BLAST1258

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 residuei165PhosphothreonineCombined sources1
Modified residuei241PhosphoserineCombined sources1
Modified residuei352PhosphoserineCombined sources1
Modified residuei886PhosphotyrosineCombined sources1
Modified residuei890PhosphoserineCombined sources1
Modified residuei958PhosphothreonineCombined sources1 Publication1
Modified residuei986Phosphotyrosine; by SRC2 Publications1
Modified residuei1131PhosphoserineCombined sources1
Modified residuei1135PhosphotyrosineCombined sources1
Modified residuei1162PhosphotyrosineCombined sources1 Publication1
Modified residuei1257PhosphoserineCombined sources1

<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-986 following cell attachment and spreading. Phosphorylated at Tyr-1162 following EGF signaling pathway stimulation. Phosphorylated at Thr-958 in response to PDGF.8 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O15357

MaxQB - The MaxQuant DataBase

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MaxQBi
O15357

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

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PaxDbi
O15357

PeptideAtlas

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PeptideAtlasi
O15357

PRoteomics IDEntifications database

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PRIDEi
O15357

ProteomicsDB human proteome resource

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ProteomicsDBi
48609
48610 [O15357-2]

PTM databases

DEPOD human dephosphorylation database

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DEPODi
O15357

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O15357

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

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PhosphoSitePlusi
O15357

<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, most prominently in skeletal muscle, heart and brain. Present in platelets. Expressed in transformed myeloid cells and in primary macrophages, but not in peripheral blood monocytes.5 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 bacterial lipopolysaccharides (LPS).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000165458 Expressed in 191 organ(s), highest expression level in left lobe of thyroid gland

CleanEx database of gene expression profiles

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CleanExi
HS_INPPL1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O15357 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O15357 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA037601

<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:9660833, PubMed:10194451, PubMed:11349134). Interacts with EGFR (PubMed:11349134). Upon stimulation by the EGF signaling pathway, it forms a complex with SHC1 and EGFR (PubMed:11349134). Interacts with cytoskeletal protein SORBS3/vinexin, promoting its localization to the periphery of cells (PubMed:16302969). Forms a complex with filamin (FLNA or FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and submembraneous actin (PubMed:11739414, PubMed:12676785). Interacts with c-Met/MET, when c-Met/MET is phosphorylated on 'Tyr-1356' (PubMed:15735664). Interacts with p130Cas/BCAR1 (PubMed:11158326). Interacts with CENTD3/ARAP3 via its SAM domain (PubMed:17314030). Interacts with c-Cbl/CBL and CAP/SORBS1 (PubMed:12504111). Interacts with activated EPHA2 receptor (PubMed:17135240). Interacts with receptor FCGR2A (PubMed:12690104). Interacts with receptor FCGR2B (PubMed:11016922). Interacts with tyrosine kinase ABL1 (PubMed:10194451). Interacts with tyrosine kinase TEC (By similarity). Interacts with CSF1R (By similarity). Interacts (via N-terminus) with SH3YL1 (via SH3 domain) (PubMed:21624956). Interacts with FCRL6 (tyrosine phosphorylated form) (PubMed:20933011).By similarity14 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109848, 118 interactors

Database of interacting proteins

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DIPi
DIP-39733N

Protein interaction database and analysis system

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IntActi
O15357, 30 interactors

Molecular INTeraction database

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MINTi
O15357

STRING: functional protein association networks

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STRINGi
9606.ENSP00000298229

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O15357

<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

11258
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
O15357

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

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SMRi
O15357

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O15357

<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
Domaini1196 – 1258SAMPROSITE-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>Motifi944 – 949SH3-binding6
Motifi983 – 986NPXY 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 biasi935 – 1105Pro-richAdd BLAST171

<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.
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
O15357

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
O15357

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>Sequences (2+)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 2 <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 2 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O15357-1) [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
MASACGAPGP GGALGSQAPS WYHRDLSRAA AEELLARAGR DGSFLVRDSE
60 70 80 90 100
SVAGAFALCV LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG
110 120 130 140 150
LYAQPNQGLV CALLLPVEGE REPDPPDDRD ASDGEDEKPP LPPRSGSTSI
160 170 180 190 200
SAPTGPSSPL PAPETPTAPA AESAPNGLST VSHDYLKGSY GLDLEAVRGG
210 220 230 240 250
ASHLPHLTRT LATSCRRLHS EVDKVLSGLE ILSKVFDQQS SPMVTRLLQQ
260 270 280 290 300
QNLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPQPS
310 320 330 340 350
TRKAKTIPVQ AFEVKLDVTL GDLTKIGKSQ KFTLSVDVEG GRLVLLRRQR
360 370 380 390 400
DSQEDWTTFT HDRIRQLIKS QRVQNKLGVV FEKEKDRTQR KDFIFVSARK
410 420 430 440 450
REAFCQLLQL MKNKHSKQDE PDMISVFIGT WNMGSVPPPK NVTSWFTSKG
460 470 480 490 500
LGKTLDEVTV TIPHDIYVFG TQENSVGDRE WLDLLRGGLK ELTDLDYRPI
510 520 530 540 550
AMQSLWNIKV AVLVKPEHEN RISHVSTSSV KTGIANTLGN KGAVGVSFMF
560 570 580 590 600
NGTSFGFVNC HLTSGNEKTA RRNQNYLDIL RLLSLGDRQL NAFDISLRFT
610 620 630 640 650
HLFWFGDLNY RLDMDIQEIL NYISRKEFEP LLRVDQLNLE REKHKVFLRF
660 670 680 690 700
SEEEISFPPT YRYERGSRDT YAWHKQKPTG VRTNVPSWCD RILWKSYPET
710 720 730 740 750
HIICNSYGCT DDIVTSDHSP VFGTFEVGVT SQFISKKGLS KTSDQAYIEF
760 770 780 790 800
ESIEAIVKTA SRTKFFIEFY STCLEEYKKS FENDAQSSDN INFLKVQWSS
810 820 830 840 850
RQLPTLKPIL ADIEYLQDQH LLLTVKSMDG YESYGECVVA LKSMIGSTAQ
860 870 880 890 900
QFLTFLSHRG EETGNIRGSM KVRVPTERLG TRERLYEWIS IDKDEAGAKS
910 920 930 940 950
KAPSVSRGSQ EPRSGSRKPA FTEASCPLSR LFEEPEKPPP TGRPPAPPRA
960 970 980 990 1000
APREEPLTPR LKPEGAPEPE GVAAPPPKNS FNNPAYYVLE GVPHQLLPPE
1010 1020 1030 1040 1050
PPSPARAPVP SATKNKVAIT VPAPQLGHHR HPRVGEGSSS DEESGGTLPP
1060 1070 1080 1090 1100
PDFPPPPLPD SAIFLPPSLD PLPGPVVRGR GGAEARGPPP PKAHPRPPLP
1110 1120 1130 1140 1150
PGPSPASTFL GEVASGDDRS CSVLQMAKTL SEVDYAPAGP ARSALLPGPL
1160 1170 1180 1190 1200
ELQPPRGLPS DYGRPLSFPP PRIRESIQED LAEEAPCLQG GRASGLGEAG
1210 1220 1230 1240 1250
MSAWLRAIGL ERYEEGLVHN GWDDLEFLSD ITEEDLEEAG VQDPAHKRLL

LDTLQLSK
Length:1,258
Mass (Da):138,599
Last modified:November 24, 2009 - 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:iD76B5AA8ACDE8CBA
GO
Isoform 2 (identifier: O15357-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-242: Missing.

Show »
Length:1,016
Mass (Da):113,176
Checksum:iF99D2FBEDA102C1F
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 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A0MTP6A0A0A0MTP6_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
1,146Annotation 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>
H7BXR2H7BXR2_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
149Annotation 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>
F5GY16F5GY16_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
127Annotation 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>
H0YFZ4H0YFZ4_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
197Annotation 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>
F5H588F5H588_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
33Annotation 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>
F5GYK9F5GYK9_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
22Annotation 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>
H0YFB4H0YFB4_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
41Annotation 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>
F5GWY9F5GWY9_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
17Annotation 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 AAA50503 differs from that shown. Reason: Frameshift at position 1153.Curated
The sequence AAA96658 differs from that shown. Reason: Frameshift at several positions.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 conflicti307I → M in AAA96658 (PubMed:8530088).Curated1
Sequence conflicti1142R → A in AAA50503 (PubMed:8530088).Curated1
Sequence conflicti1142R → A in AAA96658 (PubMed:8530088).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069586401R → W in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514511EnsemblClinVar.1
Natural variantiVAR_034980632L → I Associated with susceptibility to NIDDM. 1 PublicationCorresponds to variant dbSNP:rs61749195Ensembl.1
Natural variantiVAR_069587659P → S in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514510EnsemblClinVar.1
Natural variantiVAR_069588688W → C in OPSMD. 1 Publication1
Natural variantiVAR_034981721V → M1 PublicationCorresponds to variant dbSNP:rs116848359Ensembl.1
Natural variantiVAR_069589722F → I in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514512EnsemblClinVar.1
Natural variantiVAR_034982982N → S Associated with susceptibility to NIDDM. 1 PublicationCorresponds to variant dbSNP:rs70940821Ensembl.1
Natural variantiVAR_0349831083A → G1 PublicationCorresponds to variant dbSNP:rs11548491Ensembl.1
Natural variantiVAR_0349841114A → G3 PublicationsCorresponds to variant dbSNP:rs1049472Ensembl.1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0279851 – 242Missing in isoform 2. 1 PublicationAdd BLAST242

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
L24444 mRNA Translation: AAA50503.1 Frameshift.
L36818 mRNA Translation: AAA96658.1 Frameshift.
Y14385 mRNA Translation: CAA74743.1
AP000593 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74855.1
BC140853 mRNA Translation: AAI40854.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS8213.1 [O15357-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC5765

NCBI Reference Sequences

More...
RefSeqi
NP_001558.3, NM_001567.3 [O15357-1]
XP_011543301.1, XM_011544999.2 [O15357-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.523875

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000298229; ENSP00000298229; ENSG00000165458 [O15357-1]
ENST00000538751; ENSP00000444619; ENSG00000165458 [O15357-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3636

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3636

UCSC genome browser

More...
UCSCi
uc001osf.4 human [O15357-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24444 mRNA Translation: AAA50503.1 Frameshift.
L36818 mRNA Translation: AAA96658.1 Frameshift.
Y14385 mRNA Translation: CAA74743.1
AP000593 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74855.1
BC140853 mRNA Translation: AAI40854.1
CCDSiCCDS8213.1 [O15357-1]
PIRiJC5765
RefSeqiNP_001558.3, NM_001567.3 [O15357-1]
XP_011543301.1, XM_011544999.2 [O15357-1]
UniGeneiHs.523875

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K4PNMR-A1194-1258[»]
2KSONMR-B1200-1258[»]
2MK2NMR-A20-117[»]
3NR8X-ray2.80A/B419-732[»]
4A9CX-ray2.10A/B419-732[»]
5OKMX-ray1.96A/B/C/D/E/F/G/H420-878[»]
5OKNX-ray2.65A/B/C/D/E/F/G/H420-878[»]
5OKOX-ray1.94A/B420-878[»]
5OKPX-ray1.85A420-878[»]
ProteinModelPortaliO15357
SMRiO15357
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109848, 118 interactors
DIPiDIP-39733N
IntActiO15357, 30 interactors
MINTiO15357
STRINGi9606.ENSP00000298229

Chemistry databases

BindingDBiO15357
ChEMBLiCHEMBL2331064
GuidetoPHARMACOLOGYi1459
SwissLipidsiSLP:000000953

PTM databases

DEPODiO15357
iPTMnetiO15357
PhosphoSitePlusiO15357

Polymorphism and mutation databases

BioMutaiINPPL1

Proteomic databases

EPDiO15357
MaxQBiO15357
PaxDbiO15357
PeptideAtlasiO15357
PRIDEiO15357
ProteomicsDBi48609
48610 [O15357-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298229; ENSP00000298229; ENSG00000165458 [O15357-1]
ENST00000538751; ENSP00000444619; ENSG00000165458 [O15357-2]
GeneIDi3636
KEGGihsa:3636
UCSCiuc001osf.4 human [O15357-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3636
DisGeNETi3636
EuPathDBiHostDB:ENSG00000165458.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
INPPL1

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0201720
HGNCiHGNC:6080 INPPL1
HPAiHPA037601
MalaCardsiINPPL1
MIMi125853 phenotype
258480 phenotype
600829 gene
neXtProtiNX_O15357
OpenTargetsiENSG00000165458
Orphaneti2746 Opsismodysplasia
3144 Schneckenbecken dysplasia
PharmGKBiPA29888

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0565 Eukaryota
KOG4384 Eukaryota
COG5411 LUCA
GeneTreeiENSGT00940000156576
HOGENOMiHOG000004836
HOVERGENiHBG106726
InParanoidiO15357
KOiK15909
OMAiRVGWSNK
OrthoDBiEOG091G00P6
PhylomeDBiO15357
TreeFamiTF323475

Enzyme and pathway databases

BioCyciMetaCyc:HS09233-MONOMER
BRENDAi3.1.3.86 2681
ReactomeiR-HSA-1660499 Synthesis of PIPs at the plasma membrane
R-HSA-1855204 Synthesis of IP3 and IP4 in the cytosol
R-HSA-912526 Interleukin receptor SHC signaling
SABIO-RKiO15357
SignaLinkiO15357
SIGNORiO15357

Miscellaneous databases

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

More...
ChiTaRSi
INPPL1 human
EvolutionaryTraceiO15357

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
INPPL1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
3636

Protein Ontology

More...
PROi
PR:O15357

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000165458 Expressed in 191 organ(s), highest expression level in left lobe of thyroid gland
CleanExiHS_INPPL1
ExpressionAtlasiO15357 baseline and differential
GenevisibleiO15357 HS

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_HUMAN
<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: O15357
Secondary accession number(s): B2RTX5, Q13577, Q13578
<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: November 24, 2009
Last modified: December 5, 2018
This is version 149 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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