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Protein

Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha

Gene

PIK3C2A

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

Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function.7 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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+2 Publications, Mg2+2 PublicationsNote: Ca2+ or Mg2+. Mn2+ cannot be used.2 Publications

<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 by insulin (By similarity). Only slightly inhibited by wortmannin and LY294002. Activated by clathrin.By similarity3 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

In the absence of the carrier phosphatidylserine, enzymatic kinetics toward PtdIns4P are non-linear.
  1. KM=122 µM for PtdIns (in the absence of phosphatidylserine)1 Publication
  2. KM=64 µM for PtdIns (in the presence of phosphatidylserine)1 Publication
  3. KM=25 µM for PtdIns4P (in the presence of phosphatidylserine)1 Publication
  4. KM=15 µM for ATP (with PtdIns as substrate) (in the absence of phosphatidylserine)1 Publication
  5. KM=32 µM for ATP (with PtdIns as substrate) (in the presence of phosphatidylserine)1 Publication
  6. KM=54 µM for ATP (with PtdIns4P as substrate) (in the presence of phosphatidylserine)1 Publication
  1. Vmax=990 pmol/min/mg enzyme with PtdIns as substrate (in the absence of phosphatidylserine)1 Publication
  2. Vmax=200 pmol/min/mg enzyme with PtdIns as substrate (in the presence of phosphatidylserine)1 Publication
  3. Vmax=240 pmol/min/mg enzyme with PtdIns4P as substrate (in the presence of phosphatidylserine)1 Publication
  4. Vmax=6800 pmol/min/mg enzyme toward ATP with PtdIns as substrate (in the absence of phosphatidylserine)1 Publication
  5. Vmax=805 pmol/min/mg enzyme toward ATP with PtdIns as substrate (in the presence of phosphatidylserine)1 Publication
  6. Vmax=880 pmol/min/mg enzyme toward ATP with PtdIns4P as substrate (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

  • 1-phosphatidylinositol-3-kinase activity Source: GO_Central
  • 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • phosphatidylinositol 3-kinase activity Source: UniProtKB
  • phosphatidylinositol binding Source: InterPro

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 functionKinase, Transferase
Biological processEndocytosis, Exocytosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS00315-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.1.154 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-1660514 Synthesis of PIPs at the Golgi membrane
R-HSA-1660516 Synthesis of PIPs at the early endosome membrane
R-HSA-1660517 Synthesis of PIPs at the late endosome membrane
R-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-8856828 Clathrin-mediated endocytosis

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
O00443

SIGNOR Signaling Network Open Resource

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SIGNORi
O00443

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000000892

<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 4-phosphate 3-kinase C2 domain-containing subunit alpha (EC:2.7.1.154)
Short name:
PI3K-C2-alpha
Short name:
PtdIns-3-kinase C2 subunit alpha
Alternative name(s):
Phosphoinositide 3-kinase-C2-alpha
<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:PIK3C2A
<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:ENSG00000011405.13

Human Gene Nomenclature Database

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HGNCi
HGNC:8971 PIK3C2A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603601 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O00443

<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 membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Nucleus

<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

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>Mutagenesisi103 – 107LLLDD → AAAAA: Reduces clathrin binding. 1 Publication5
Mutagenesisi254S → A: No effect on phosphorylation in vitro. 1 Publication1
Mutagenesisi259S → A, D or E: Abolishes phosphorylation, no change in activity. 1 Publication1
Mutagenesisi259S → A: Protects from proteolysis. 1 Publication1
Mutagenesisi262S → A: No effect on phosphorylation in vitro. 1 Publication1
Mutagenesisi266S → A: No effect on phosphorylation in vitro. 1 Publication1
Mutagenesisi1250D → A: Abolishes lipid kinase activity. Affects clathrin distribution when combined with a truncation encompassing the region of clathrin interaction. 1 Publication1
Mutagenesisi1488R → A: Reduces affinity for PtdIns(4,5)P2-containing membranes 7-fold. 1 Publication1
Mutagenesisi1490V → A: Reduces affinity for PtdIns(4,5)P2-containing membranes 7-fold. 1 Publication1
Mutagenesisi1491L → A: Reduces affinity for PtdIns(4,5)P2-containing membranes 5-fold. 1 Publication1
Mutagenesisi1493R → A: Reduces affinity for PtdIns(4,5)P2-containing membranes 23-fold. 1 Publication1
Mutagenesisi1503R → A: Abolishes interaction with PtdIns(4,5)P2-containing membranes. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5286

Open Targets

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OpenTargetsi
ENSG00000011405

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33304

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1075102

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2150

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PIK3C2A

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000887952 – 1686Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alphaAdd BLAST1685

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 residuei2N-acetylalanineCombined sources1
Modified residuei60PhosphoserineCombined sources1
Modified residuei108PhosphoserineCombined sources1
Modified residuei259PhosphoserineCombined sources1 Publication1
Modified residuei327PhosphoserineCombined sources1
Modified residuei338PhosphoserineCombined sources1
Modified residuei630PhosphoserineCombined sources1
Modified residuei1281PhosphoserineCombined sources1
Modified residuei1553PhosphoserineCombined 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

Phosphorylated upon insulin stimulation; which may lead to enzyme activation (By similarity). Phosphorylated on Ser-259 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation. Ser-259 phosphorylation may be mediated by CDK1 or JNK, depending on the physiological state of the cell.By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei244Not phosphorylated1 Publication1
Sitei249Not phosphorylated1 Publication1
Sitei251Not phosphorylated1 Publication1
Sitei254Not phosphorylated1 Publication1
Sitei262Not phosphorylated1 Publication1
Sitei266Not phosphorylated1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O00443

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O00443

MaxQB - The MaxQuant DataBase

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MaxQBi
O00443

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

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PaxDbi
O00443

PeptideAtlas

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PeptideAtlasi
O00443

PRoteomics IDEntifications database

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PRIDEi
O00443

ProteomicsDB human proteome resource

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ProteomicsDBi
47892

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O00443

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

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PhosphoSitePlusi
O00443

<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

Expressed in columnar and transitional epithelia, mononuclear cells, smooth muscle cells, and endothelial cells lining capillaries and small venules (at protein level). Ubiquitously expressed, with highest levels in heart, placenta and ovary, and lowest levels in the kidney. Detected at low levels in islets of Langerhans from type 2 diabetes mellitus individuals.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000011405 Expressed in 242 organ(s), highest expression level in upper lobe of lung

CleanEx database of gene expression profiles

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CleanExi
HS_PIK3C2A

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O00443 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O00443 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA037641
HPA037642

<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

Part of a complex with ERBB2 and EGFR (PubMed:10805725). Interacts with clathrin trimers (PubMed:11239472, PubMed:16215232). Interacts with SBF2/MTMR13 (By similarity).By similarity3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111304, 73 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O00443

Database of interacting proteins

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DIPi
DIP-33727N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O00443

Protein interaction database and analysis system

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IntActi
O00443, 47 interactors

Molecular INTeraction database

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MINTi
O00443

STRING: functional protein association networks

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STRINGi
9606.ENSP00000265970

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O00443

<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

11686
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AR5X-ray1.80A1421-1532[»]
2IWLX-ray2.60X1405-1544[»]
2REAX-ray2.50A1421-1532[»]
2REDX-ray2.10A1421-1532[»]
6BTYX-ray1.68A/B1559-1686[»]
6BTZX-ray1.85A/B/C/D1559-1686[»]
6BU0X-ray2.43A/B/C1559-1686[»]
6BUBX-ray2.60A1405-1544[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O00443

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

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SMRi
O00443

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
O00443

<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>Domaini421 – 509PI3K-RBDPROSITE-ProRule annotationAdd BLAST89
Domaini682 – 841C2 PI3K-typePROSITE-ProRule annotationAdd BLAST160
Domaini861 – 1037PIK helicalPROSITE-ProRule annotationAdd BLAST177
Domaini1133 – 1397PI3K/PI4KPROSITE-ProRule annotationAdd BLAST265
Domaini1422 – 1538PXPROSITE-ProRule annotationAdd BLAST117
Domaini1559 – 1662C2PROSITE-ProRule annotationAdd BLAST104

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>Regioni2 – 142Interaction with clathrin; sufficient to induce clathrin assemblyAdd BLAST141
Regioni1488 – 1493Interaction with PtdIns(4,5)P2-containing membranes6

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>Motifi1608 – 1619Nuclear localization signal1 PublicationAdd BLAST12

<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 PI3/PI4-kinase family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0905 Eukaryota
COG5032 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157813

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000006920

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG082099

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O00443

KEGG Orthology (KO)

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KOi
K00923

Identification of Orthologs from Complete Genome Data

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OMAi
TIQRGQW

Database of Orthologous Groups

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OrthoDBi
892946at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O00443

TreeFam database of animal gene trees

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TreeFami
TF102031

Family and domain databases

Conserved Domains Database

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CDDi
cd05176 PI3Kc_C2_alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1070.11, 1 hit
2.60.40.150, 2 hits
3.30.1520.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR016024 ARM-type_fold
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR011009 Kinase-like_dom_sf
IPR001683 Phox
IPR000403 PI3/4_kinase_cat_dom
IPR036940 PI3/4_kinase_cat_sf
IPR018936 PI3/4_kinase_CS
IPR037705 PI3K-C2-alpha_dom
IPR002420 PI3K_C2_dom
IPR000341 PI3K_Ras-bd_dom
IPR015433 PI_Kinase
IPR001263 PInositide-3_kin_accessory_dom
IPR036871 PX_dom_sf
IPR029071 Ubiquitin-like_domsf

The PANTHER Classification System

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PANTHERi
PTHR10048 PTHR10048, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00168 C2, 1 hit
PF00454 PI3_PI4_kinase, 1 hit
PF00792 PI3K_C2, 1 hit
PF00794 PI3K_rbd, 1 hit
PF00613 PI3Ka, 1 hit
PF00787 PX, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00239 C2, 2 hits
SM00142 PI3K_C2, 1 hit
SM00144 PI3K_rbd, 1 hit
SM00145 PI3Ka, 1 hit
SM00146 PI3Kc, 1 hit
SM00312 PX, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48371 SSF48371, 1 hit
SSF54236 SSF54236, 1 hit
SSF56112 SSF56112, 1 hit
SSF64268 SSF64268, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50004 C2, 1 hit
PS00915 PI3_4_KINASE_1, 1 hit
PS00916 PI3_4_KINASE_2, 1 hit
PS50290 PI3_4_KINASE_3, 1 hit
PS51547 PI3K_C2, 1 hit
PS51546 PI3K_RBD, 1 hit
PS51545 PIK_HELICAL, 1 hit
PS50195 PX, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O00443-1) [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
MAQISSNSGF KECPSSHPEP TRAKDVDKEE ALQMEAEALA KLQKDRQVTD
60 70 80 90 100
NQRGFELSSS TRKKAQVYNK QDYDLMVFPE SDSQKRALDI DVEKLTQAEL
110 120 130 140 150
EKLLLDDSFE TKKTPVLPVT PILSPSFSAQ LYFRPTIQRG QWPPGLPGPS
160 170 180 190 200
TYALPSIYPS TYSKQAAFQN GFNPRMPTFP STEPIYLSLP GQSPYFSYPL
210 220 230 240 250
TPATPFHPQG SLPIYRPVVS TDMAKLFDKI ASTSEFLKNG KARTDLEITD
260 270 280 290 300
SKVSNLQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA
310 320 330 340 350
KDPWDAVLLE ERSTANCHLE RKVNGKSLSV ATVTRSQSLN IRTTQLAKAQ
360 370 380 390 400
GHISQKDPNG TSSLPTGSSL LQEVEVQNEE MAAFCRSITK LKTKFPYTNH
410 420 430 440 450
RTNPGYLLSP VTAQRNICGE NASVKVSIDI EGFQLPVTFT CDVSSTVEII
460 470 480 490 500
IMQALCWVHD DLNQVDVGSY VLKVCGQEEV LQNNHCLGSH EHIQNCRKWD
510 520 530 540 550
TEIRLQLLTF SAMCQNLART AEDDETPVDL NKHLYQIEKP CKEAMTRHPV
560 570 580 590 600
EELLDSYHNQ VELALQIENQ HRAVDQVIKA VRKICSALDG VETLAITESV
610 620 630 640 650
KKLKRAVNLP RSKTADVTSL FGGEDTSRSS TRGSLNPENP VQVSINQLTA
660 670 680 690 700
AIYDLLRLHA NSGRSPTDCA QSSKSVKEAW TTTEQLQFTI FAAHGISSNW
710 720 730 740 750
VSNYEKYYLI CSLSHNGKDL FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ
760 770 780 790 800
ISQLPLESVL HLTLFGILNQ SSGSSPDSNK QRKGPEALGK VSLPLFDFKR
810 820 830 840 850
FLTCGTKLLY LWTSSHTNSV PGTVTKKGYV MERIVLQVDF PSPAFDIIYT
860 870 880 890 900
TPQVDRSIIQ QHNLETLEND IKGKLLDILH KDSSLGLSKE DKAFLWEKRY
910 920 930 940 950
YCFKHPNCLP KILASAPNWK WVNLAKTYSL LHQWPALYPL IALELLDSKF
960 970 980 990 1000
ADQEVRSLAV TWIEAISDDE LTDLLPQFVQ ALKYEIYLNS SLVQFLLSRA
1010 1020 1030 1040 1050
LGNIQIAHNL YWLLKDALHD VQFSTRYEHV LGALLSVGGK RLREELLKQT
1060 1070 1080 1090 1100
KLVQLLGGVA EKVRQASGSA RQVVLQRSME RVQSFFQKNK CRLPLKPSLV
1110 1120 1130 1140 1150
AKELNIKSCS FFSSNAVPLK VTMVNADPMG EEINVMFKVG EDLRQDMLAL
1160 1170 1180 1190 1200
QMIKIMDKIW LKEGLDLRMV IFKCLSTGRD RGMVELVPAS DTLRKIQVEY
1210 1220 1230 1240 1250
GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD
1260 1270 1280 1290 1300
RHNDNIMLRS TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN
1310 1320 1330 1340 1350
GGEKPTIRFQ LFVDLCCQAY NLIRKQTNLF LNLLSLMIPS GLPELTSIQD
1360 1370 1380 1390 1400
LKYVRDALQP QTTDAEATIF FTRLIESSLG SIATKFNFFI HNLAQLRFSG
1410 1420 1430 1440 1450
LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK HYIYVVRILR
1460 1470 1480 1490 1500
EGQIEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA
1510 1520 1530 1540 1550
AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSADAG
1560 1570 1580 1590 1600
SFSPTPGQIG GAVKLSISYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL
1610 1620 1630 1640 1650
LPDNHKTSKR KTKISRKTRN PTFNEMLVYS GYSKETLRQR ELQLSVLSAE
1660 1670 1680
SLRENFFLGG VTLPLKDFNL SKETVKWYQL TAATYL
Length:1,686
Mass (Da):190,680
Last modified:July 10, 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:i904AA5470F80DAC6
GO
Isoform 2 (identifier: O00443-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     484-1686: Missing.

Note: No experimental confirmation available.
Show »
Length:483
Mass (Da):53,742
Checksum:iB63EDBEA18725E91
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
A0A0C4DGF9A0A0C4DGF9_HUMAN
Phosphatidylinositol 4-phosphate 3-...
PIK3C2A
483Annotation 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>
E9PPP3E9PPP3_HUMAN
Phosphatidylinositol 4-phosphate 3-...
PIK3C2A
130Annotation 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 conflicti5S → F in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti15S → F in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti483N → K in BAG65126 (PubMed:14702039).Curated1
Sequence conflicti796F → C in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti799K → R in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti922V → G in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti1129M → L in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti1450R → W in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti1464D → V in CAA73797 (PubMed:9337861).Curated1

Natural variant

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_0233331415T → A. Corresponds to variant dbSNP:rs11604561Ensembl.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_056158484 – 1686Missing in isoform 2. 1 PublicationAdd BLAST1203

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
Y13367 mRNA Translation: CAA73797.1
AK304262 mRNA Translation: BAG65126.1
EU332862 Genomic DNA Translation: ABY87551.1
AC107956 Genomic DNA No translation available.
AC116533 Genomic DNA No translation available.
AC126389 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW68447.1
BC113658 mRNA Translation: AAI13659.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS7824.1 [O00443-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
PC4345

NCBI Reference Sequences

More...
RefSeqi
NP_001308307.1, NM_001321378.1 [O00443-1]
NP_002636.2, NM_002645.3 [O00443-1]
XP_016873413.1, XM_017017924.1 [O00443-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.175343
Hs.736397

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000265970; ENSP00000265970; ENSG00000011405 [O00443-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5286

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5286

UCSC genome browser

More...
UCSCi
uc001mmq.6 human [O00443-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13367 mRNA Translation: CAA73797.1
AK304262 mRNA Translation: BAG65126.1
EU332862 Genomic DNA Translation: ABY87551.1
AC107956 Genomic DNA No translation available.
AC116533 Genomic DNA No translation available.
AC126389 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW68447.1
BC113658 mRNA Translation: AAI13659.1
CCDSiCCDS7824.1 [O00443-1]
PIRiPC4345
RefSeqiNP_001308307.1, NM_001321378.1 [O00443-1]
NP_002636.2, NM_002645.3 [O00443-1]
XP_016873413.1, XM_017017924.1 [O00443-1]
UniGeneiHs.175343
Hs.736397

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AR5X-ray1.80A1421-1532[»]
2IWLX-ray2.60X1405-1544[»]
2REAX-ray2.50A1421-1532[»]
2REDX-ray2.10A1421-1532[»]
6BTYX-ray1.68A/B1559-1686[»]
6BTZX-ray1.85A/B/C/D1559-1686[»]
6BU0X-ray2.43A/B/C1559-1686[»]
6BUBX-ray2.60A1405-1544[»]
ProteinModelPortaliO00443
SMRiO00443
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111304, 73 interactors
CORUMiO00443
DIPiDIP-33727N
ELMiO00443
IntActiO00443, 47 interactors
MINTiO00443
STRINGi9606.ENSP00000265970

Chemistry databases

BindingDBiO00443
ChEMBLiCHEMBL1075102
GuidetoPHARMACOLOGYi2150
SwissLipidsiSLP:000000892

PTM databases

iPTMnetiO00443
PhosphoSitePlusiO00443

Polymorphism and mutation databases

BioMutaiPIK3C2A

Proteomic databases

EPDiO00443
jPOSTiO00443
MaxQBiO00443
PaxDbiO00443
PeptideAtlasiO00443
PRIDEiO00443
ProteomicsDBi47892

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5286
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265970; ENSP00000265970; ENSG00000011405 [O00443-1]
GeneIDi5286
KEGGihsa:5286
UCSCiuc001mmq.6 human [O00443-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5286
DisGeNETi5286
EuPathDBiHostDB:ENSG00000011405.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PIK3C2A
HGNCiHGNC:8971 PIK3C2A
HPAiHPA037641
HPA037642
MIMi603601 gene
neXtProtiNX_O00443
OpenTargetsiENSG00000011405
PharmGKBiPA33304

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0905 Eukaryota
COG5032 LUCA
GeneTreeiENSGT00940000157813
HOGENOMiHOG000006920
HOVERGENiHBG082099
InParanoidiO00443
KOiK00923
OMAiTIQRGQW
OrthoDBi892946at2759
PhylomeDBiO00443
TreeFamiTF102031

Enzyme and pathway databases

BioCyciMetaCyc:HS00315-MONOMER
BRENDAi2.7.1.154 2681
ReactomeiR-HSA-1660499 Synthesis of PIPs at the plasma membrane
R-HSA-1660514 Synthesis of PIPs at the Golgi membrane
R-HSA-1660516 Synthesis of PIPs at the early endosome membrane
R-HSA-1660517 Synthesis of PIPs at the late endosome membrane
R-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-8856828 Clathrin-mediated endocytosis
SABIO-RKiO00443
SIGNORiO00443

Miscellaneous databases

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

More...
ChiTaRSi
PIK3C2A human
EvolutionaryTraceiO00443

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PIK3C2A

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

More...
GenomeRNAii
5286

Protein Ontology

More...
PROi
PR:O00443

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000011405 Expressed in 242 organ(s), highest expression level in upper lobe of lung
CleanExiHS_PIK3C2A
ExpressionAtlasiO00443 baseline and differential
GenevisibleiO00443 HS

Family and domain databases

CDDicd05176 PI3Kc_C2_alpha, 1 hit
Gene3Di1.10.1070.11, 1 hit
2.60.40.150, 2 hits
3.30.1520.10, 1 hit
InterProiView protein in InterPro
IPR016024 ARM-type_fold
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR011009 Kinase-like_dom_sf
IPR001683 Phox
IPR000403 PI3/4_kinase_cat_dom
IPR036940 PI3/4_kinase_cat_sf
IPR018936 PI3/4_kinase_CS
IPR037705 PI3K-C2-alpha_dom
IPR002420 PI3K_C2_dom
IPR000341 PI3K_Ras-bd_dom
IPR015433 PI_Kinase
IPR001263 PInositide-3_kin_accessory_dom
IPR036871 PX_dom_sf
IPR029071 Ubiquitin-like_domsf
PANTHERiPTHR10048 PTHR10048, 1 hit
PfamiView protein in Pfam
PF00168 C2, 1 hit
PF00454 PI3_PI4_kinase, 1 hit
PF00792 PI3K_C2, 1 hit
PF00794 PI3K_rbd, 1 hit
PF00613 PI3Ka, 1 hit
PF00787 PX, 1 hit
SMARTiView protein in SMART
SM00239 C2, 2 hits
SM00142 PI3K_C2, 1 hit
SM00144 PI3K_rbd, 1 hit
SM00145 PI3Ka, 1 hit
SM00146 PI3Kc, 1 hit
SM00312 PX, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
SSF54236 SSF54236, 1 hit
SSF56112 SSF56112, 1 hit
SSF64268 SSF64268, 1 hit
PROSITEiView protein in PROSITE
PS50004 C2, 1 hit
PS00915 PI3_4_KINASE_1, 1 hit
PS00916 PI3_4_KINASE_2, 1 hit
PS50290 PI3_4_KINASE_3, 1 hit
PS51547 PI3K_C2, 1 hit
PS51546 PI3K_RBD, 1 hit
PS51545 PIK_HELICAL, 1 hit
PS50195 PX, 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 nameiP3C2A_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: O00443
Secondary accession number(s): B0LPH2, B4E2G4, Q14CQ9
<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: August 30, 2005
Last sequence update: July 10, 2007
Last modified: January 16, 2019
This is version 175 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
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