Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 96 (13 Nov 2019)
Sequence version 1 (21 Dec 2004)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

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

Gene

PIK3C2A

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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 (By similarity). Involved in the regulation of ciliogenesis and trafficking of ciliary components (By similarity).By similarity

<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+By similarity, Mg2+By similarityNote: Ca2+ or Mg2+. Mn2+ cannot be used.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

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

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

GO - Biological processi

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

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

<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>OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
<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 identifieri9601 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
<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
  • UP000001595 <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: Unplaced

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

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

Keywords - Cellular componenti

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

<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 methionineiRemovedBy similarity
<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_00000887972 – 1685Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alphaAdd BLAST1684

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-acetylalanineBy similarity1
Modified residuei60PhosphoserineBy similarity1
Modified residuei108PhosphoserineBy similarity1
Modified residuei259PhosphoserineBy similarity1
Modified residuei327PhosphoserineBy similarity1
Modified residuei338PhosphoserineBy similarity1
Modified residuei628PhosphoserineBy similarity1
Modified residuei1551PhosphoserineBy similarity1

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

Phosphorylated on Ser-259 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation. Phosphorylated upon insulin stimulation; which may lead to enzyme activation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q5RAY1

<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 (By similarity).

Interacts with clathrin trimers (By similarity).

Interacts with SBF2/MTMR13 (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9601.ENSPPYP00000003968

<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>Domaini419 – 507PI3K-RBDPROSITE-ProRule annotationAdd BLAST89
Domaini680 – 839C2 PI3K-typePROSITE-ProRule annotationAdd BLAST160
Domaini859 – 1035PIK helicalPROSITE-ProRule annotationAdd BLAST177
Domaini1131 – 1395PI3K/PI4KPROSITE-ProRule annotationAdd BLAST265
Domaini1420 – 1536PXPROSITE-ProRule annotationAdd BLAST117
Domaini1558 – 1661C2PROSITE-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 assemblyBy similarityAdd BLAST141
Regioni1486 – 1491Interaction with PtdIns(4,5)P2-containing membranesBy similarity6

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>Motifi1607 – 1618Nuclear localization signalBy similarityAdd 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

More...
eggNOGi
KOG0905 Eukaryota
COG5032 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5RAY1

KEGG Orthology (KO)

More...
KOi
K00923

Database of Orthologous Groups

More...
OrthoDBi
204282at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05176 PI3Kc_C2_alpha, 1 hit
cd07289 PX_PI3K_C2_alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1070.11, 1 hit
1.25.40.70, 1 hit
2.60.40.150, 2 hits
3.30.1520.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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
IPR001263 PI3K_accessory_dom
IPR042236 PI3K_accessory_sf
IPR002420 PI3K_C2_dom
IPR000341 PI3K_Ras-bd_dom
IPR015433 PI_Kinase
IPR036871 PX_dom_sf
IPR042133 PX_PI3K_C2_alpha
IPR029071 Ubiquitin-like_domsf

The PANTHER Classification System

More...
PANTHERi
PTHR10048 PTHR10048, 1 hit

Pfam protein domain database

More...
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

More...
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

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

PROSITE; a protein domain and family database

More...
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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

Q5RAY1-1 [UniParc]FASTAAdd to basket
« 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
EKLLLDDSLE TRKTPVLPVT PILSPSFSAQ LYFRPTIQRG QWPPGLSGPS
160 170 180 190 200
TYALPSIYPS TYSKQAAFQN GFNPRMPTFP STEPIYLSLP GQSPYFSYPL
210 220 230 240 250
TPATPFHPQG SLPIYRPVVS PDMAKLFDKI ASTSEFLKNG KARADLEITD
260 270 280 290 300
SKVSNLQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA
310 320 330 340 350
KDPWDAVLLE ERSTANCHLE RKMNGKSLSV ATVTRSQSLN IRTTQLAKAH
360 370 380 390 400
ISQKDPNGTS SLPTGSSLLQ EVEVQNEEMA AFSRSITKLK TKFPYTNHHT
410 420 430 440 450
NPGYLLSPVT AQRNICGENA SVKVSIDIEG FQLPVTFTCD VSSTVEIIIM
460 470 480 490 500
QALCWVHDDL NQVDVGSYVL KVCGQEEVLQ NNHCLGSHEH IQNCRKWDTE
510 520 530 540 550
IRLQLLTFSA MCQNLARTAE DDETPVDLNK HLYQIEKPYK EAMTRHPVEE
560 570 580 590 600
LLDSYHNQVE LALQIENQHR AVDQVIKAVR KICSALDGVE TLAITESVKK
610 620 630 640 650
LKRAVNLPRS KTADVASLFG GEDTSKSSTR GSLNPENPVQ VSINQLTAAI
660 670 680 690 700
YDLLRLHANS GRSPTDCAQS SKSVKEAWTT TEQLQFTIFA AHGISSNWVS
710 720 730 740 750
NYEKYYLICS LSHNGKDLFK PIQSKKVGTY KNFFYLIKWD ELIIFPIQIS
760 770 780 790 800
QLPLESLLHL TLFGILNQSS GSSPDSNKQR KGPEALGKVS LPLFDFKRFL
810 820 830 840 850
TCGTKLLYLW TSSHTNSVPG AVTKKGYVME RIVLQVDFPS PAFDIIYTTP
860 870 880 890 900
QVDRSIIQQH NLETLENDVK GKLLDILHKD SSLGLSKEDK AFLWEKRYYC
910 920 930 940 950
FKHPNCLPKI LASAPNWKWV NLAKTYSLLH QWPALYPLIA LELLDSKFAD
960 970 980 990 1000
QEVRSLAVTW IEAISDDELT DLLPQFVQAL KYEIYLNSSL VQFLLSRALG
1010 1020 1030 1040 1050
NIQIAHNLYW LLKDALHDVQ FSTRYEHVLG ALLSVGGKRL REELRKQTKL
1060 1070 1080 1090 1100
VQLLGGVAEK VRQASGSARQ VVLQRSMERV QSFFQKNKCR LPLKPSLVAK
1110 1120 1130 1140 1150
ELSIKSCSFF SSNAVPLKVT MVNADPMGEE INVMFKVGED LRQDMLALQM
1160 1170 1180 1190 1200
IKIMDKIWLK EGLDLRMVIF KCLSTGRDRG MVELVPASDT LRKIQVEYGV
1210 1220 1230 1240 1250
TGSFKDKPLA EWLRKYNPSE EEYEKASENF IYSCAGCCVA TYVLGICDRH
1260 1270 1280 1290 1300
NDNIMLRSTG HMFHIDFGKF LGHAQMFGTF KRDRAPFVLT SDMAYVINGG
1310 1320 1330 1340 1350
EKPTIRFQLF VDLCCQAYNL IRKQTNLFLN LLSLMIPSGL PELTSIQDLK
1360 1370 1380 1390 1400
YVRDALQPQT TDAEATIFFT RLIESSLGSI ATKFNFLIHN LAQLRFSGLP
1410 1420 1430 1440 1450
SNDEPILSFS PKTYSFKQDG RIKEVSVFTY HKKYNPDKHY IYVVRILREG
1460 1470 1480 1490 1500
QIEPSFVFRT FDEFQELHNK LSIIFPLWKL PGFPNRMVLG RTHIKDVAAK
1510 1520 1530 1540 1550
RKIELNSYLQ SLMNASTDVA ECDLVCTFFH PLLRDEKAEG IARSADAGSF
1560 1570 1580 1590 1600
SPPTPGQIGG AVKLSISYRN GTLFIMVMHT KDLVTEDGAD PNPYVKTYLL
1610 1620 1630 1640 1650
PDNHKTSKRK TKISRKTRNP TFNEMLVYSG YSKETLRQRE LQLSVLSAES
1660 1670 1680
LRENFFLGGV TLPLKDFNLS KETVKWYQLT AATYL
Length:1,685
Mass (Da):190,466
Last modified:December 21, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2C48ED378DE0C2BD
GO

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
CR858880 mRNA Translation: CAH91079.1

NCBI Reference Sequences

More...
RefSeqi
NP_001125626.1, NM_001132154.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100457125

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pon:100457125

<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
CR858880 mRNA Translation: CAH91079.1
RefSeqiNP_001125626.1, NM_001132154.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000003968

Proteomic databases

PRIDEiQ5RAY1

Genome annotation databases

GeneIDi100457125
KEGGipon:100457125

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5286

Phylogenomic databases

eggNOGiKOG0905 Eukaryota
COG5032 LUCA
InParanoidiQ5RAY1
KOiK00923
OrthoDBi204282at2759

Family and domain databases

CDDicd05176 PI3Kc_C2_alpha, 1 hit
cd07289 PX_PI3K_C2_alpha, 1 hit
Gene3Di1.10.1070.11, 1 hit
1.25.40.70, 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
IPR001263 PI3K_accessory_dom
IPR042236 PI3K_accessory_sf
IPR002420 PI3K_C2_dom
IPR000341 PI3K_Ras-bd_dom
IPR015433 PI_Kinase
IPR036871 PX_dom_sf
IPR042133 PX_PI3K_C2_alpha
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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_PONAB
<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: Q5RAY1
<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: December 21, 2004
Last modified: November 13, 2019
This is version 96 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again