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Protein

Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform

Gene

Pik3ca

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Also has serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS. Plays a role in the positive regulation of phagocytosis and pinocytosis (PubMed:19604150).7 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.By similarity
ATP + a protein = ADP + a phosphoprotein.By similarity

GO - Molecular functioni

GO - Biological processi

  • adipose tissue development Source: MGI
  • angiogenesis Source: UniProtKB-KW
  • cellular response to glucose stimulus Source: MGI
  • energy homeostasis Source: MGI
  • glucose metabolic process Source: MGI
  • hypomethylation of CpG island Source: BHF-UCL
  • liver development Source: MGI
  • mitophagy in response to mitochondrial depolarization Source: Ensembl
  • negative regulation of anoikis Source: MGI
  • negative regulation of fibroblast apoptotic process Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • phagocytosis Source: UniProtKB-KW
  • phosphatidylinositol-mediated signaling Source: InterPro
  • phosphorylation Source: MGI
  • positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • protein kinase B signaling Source: MGI
  • protein phosphorylation Source: MGI
  • regulation of cellular respiration Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of genetic imprinting Source: BHF-UCL
  • regulation of multicellular organism growth Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Angiogenesis, Phagocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.137. 3474.
2.7.1.153. 3474.
ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1250342. PI3K events in ERBB4 signaling.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1660499. Synthesis of PIPs at the plasma membrane.
R-MMU-180292. GAB1 signalosome.
R-MMU-186763. Downstream signal transduction.
R-MMU-1963642. PI3K events in ERBB2 signaling.
R-MMU-198203. PI3K/AKT activation.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2029485. Role of phospholipids in phagocytosis.
R-MMU-210993. Tie2 Signaling.
R-MMU-2424491. DAP12 signaling.
R-MMU-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-MMU-388841. Costimulation by the CD28 family.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-392451. G beta:gamma signalling through PI3Kgamma.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654695. PI-3K cascade:FGFR2.
R-MMU-5654710. PI-3K cascade:FGFR3.
R-MMU-5654720. PI-3K cascade:FGFR4.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-8851907. MET activates PI3K/AKT signaling.
R-MMU-8853659. RET signaling.
R-MMU-912526. Interleukin receptor SHC signaling.
R-MMU-912631. Regulation of signaling by CBL.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (EC:2.7.1.153By similarity)
Short name:
PI3-kinase subunit alpha
Short name:
PI3K-alpha
Short name:
PI3Kalpha
Short name:
PtdIns-3-kinase subunit alpha
Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha
Short name:
PtdIns-3-kinase subunit p110-alpha
Short name:
p110alpha
Phosphoinositide-3-kinase catalytic alpha polypeptide
Serine/threonine protein kinase PIK3CA (EC:2.7.11.1By similarity)
Gene namesi
Name:Pik3ca
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1206581. Pik3ca.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
  • lamellipodium Source: MGI
  • phosphatidylinositol 3-kinase complex Source: MGI
  • phosphatidylinositol 3-kinase complex, class IA Source: MGI
  • plasma membrane Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Lethal. Embryonic fibroblasts cells are resistant to oncogenic transformation induced by oncogenic receptor tyrosine kinases (RTKs), are unable to differentiate into adipocytes and deficient in cellular signaling in response to various growth factors. Defective responsiveness to insulin led to reduced somatic growth, hyperinsulinemia, glucose intolerance, hyperphagia and increased adiposity.4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi208T → D: Abolishes binding to HRAS and KRAS; does not affect kinase activity; displays defective development of the lymphatic vasculature, resulting in perinatal appearance of chylous ascites and is highly resistant to endogenous Ras oncogene-induced tumorigenesis; when associated with A-227. 1 Publication1
Mutagenesisi227K → A: Abolishes binding to HRAS and KRAS; does not affect kinase activity; displays defective development of the lymphatic vasculature, resulting in perinatal appearance of chylous ascites and is highly resistant to endogenous Ras oncogene-induced tumorigenesis; when associated with D-208. 1 Publication1
Mutagenesisi933D → A: Loss of kinase activity; displays early embryonic lethality at E10-11 and severe defects in angiogenic sprouting and vascular remodeling. Heterozygous mice yield adult mice with markedly impaired insulin signaling and reduced activation of effector pathways such as Akt/PKB. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBLiCHEMBL2499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000887861 – 1068Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoformAdd BLAST1068

Proteomic databases

EPDiP42337.
MaxQBiP42337.
PaxDbiP42337.
PRIDEiP42337.

PTM databases

iPTMnetiP42337.
PhosphoSitePlusiP42337.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027665.
ExpressionAtlasiP42337. baseline and differential.
GenevisibleiP42337. MM.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CA and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3) (PubMed:8139567). Interacts with IRS1 in nuclear extracts (PubMed:15197263). Interacts with RUFY3. Interacts with RASD2. Interacts with APPL1 (By similarity). Interacts with HRAS and KRAS (PubMed:17540175). Interaction with HRAS/KRAS is required for PI3K pathway signaling and cell proliferation stimulated by EGF and FGF2 (PubMed:17540175). Interacts with FAM83B; activates the PI3K/AKT signaling cascade (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HRASP011122EBI-641748,EBI-350145From a different organism.
Pik3r1P264506EBI-641748,EBI-641764

GO - Molecular functioni

  • insulin receptor substrate binding Source: MGI

Protein-protein interaction databases

BioGridi202160. 5 interactors.
DIPiDIP-32095N.
IntActiP42337. 10 interactors.
MINTiMINT-219865.
STRINGi10090.ENSMUSP00000029201.

Chemistry databases

BindingDBiP42337.

Structurei

Secondary structure

11068
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Beta strandi18 – 25Combined sources8
Beta strandi31 – 37Combined sources7
Helixi42 – 52Combined sources11
Helixi53 – 55Combined sources3
Turni57 – 60Combined sources4
Helixi65 – 67Combined sources3
Beta strandi69 – 74Combined sources6
Beta strandi77 – 81Combined sources5
Helixi90 – 92Combined sources3
Beta strandi94 – 102Combined sources9
Helixi109 – 112Combined sources4
Helixi117 – 121Combined sources5
Helixi125 – 129Combined sources5
Helixi134 – 142Combined sources9
Helixi144 – 153Combined sources10
Turni154 – 157Combined sources4
Helixi158 – 165Combined sources8
Helixi179 – 182Combined sources4
Beta strandi189 – 196Combined sources8
Turni199 – 202Combined sources4
Beta strandi205 – 212Combined sources8
Helixi217 – 230Combined sources14
Helixi236 – 246Combined sources11
Helixi247 – 249Combined sources3
Beta strandi250 – 254Combined sources5
Helixi267 – 269Combined sources3
Helixi271 – 279Combined sources9
Beta strandi284 – 289Combined sources6
Helixi290 – 295Combined sources6
Beta strandi324 – 327Combined sources4
Beta strandi332 – 340Combined sources9
Beta strandi348 – 350Combined sources3
Beta strandi354 – 364Combined sources11
Beta strandi378 – 380Combined sources3
Beta strandi382 – 392Combined sources11
Turni393 – 395Combined sources3
Beta strandi401 – 408Combined sources8
Beta strandi423 – 430Combined sources8
Beta strandi434 – 436Combined sources3
Beta strandi439 – 444Combined sources6
Beta strandi454 – 456Combined sources3
Beta strandi458 – 460Combined sources3
Beta strandi468 – 470Combined sources3
Beta strandi472 – 477Combined sources6
Beta strandi481 – 485Combined sources5
Helixi489 – 499Combined sources11
Turni529 – 535Combined sources7
Helixi545 – 553Combined sources9
Helixi555 – 558Combined sources4
Helixi562 – 564Combined sources3
Helixi565 – 569Combined sources5
Helixi578 – 588Combined sources11
Helixi595 – 598Combined sources4
Turni599 – 602Combined sources4
Helixi609 – 621Combined sources13
Helixi625 – 630Combined sources6
Helixi632 – 636Combined sources5
Helixi639 – 641Combined sources3
Beta strandi643 – 646Combined sources4
Helixi648 – 659Combined sources12
Helixi661 – 673Combined sources13
Helixi678 – 694Combined sources17
Turni695 – 697Combined sources3
Helixi698 – 720Combined sources23
Helixi728 – 738Combined sources11
Helixi742 – 747Combined sources6
Beta strandi749 – 752Combined sources4
Beta strandi759 – 761Combined sources3
Beta strandi779 – 784Combined sources6
Helixi790 – 792Combined sources3
Beta strandi795 – 805Combined sources11
Helixi808 – 827Combined sources20
Beta strandi838 – 842Combined sources5
Beta strandi845 – 849Combined sources5
Beta strandi854 – 856Combined sources3
Helixi857 – 860Combined sources4
Helixi876 – 884Combined sources9
Helixi887 – 889Combined sources3
Helixi890 – 911Combined sources22
Turni918 – 920Combined sources3
Beta strandi921 – 924Combined sources4
Beta strandi929 – 931Combined sources3
Helixi941 – 945Combined sources5
Helixi957 – 964Combined sources8
Beta strandi965 – 967Combined sources3
Helixi975 – 993Combined sources19
Helixi995 – 1004Combined sources10
Beta strandi1013 – 1015Combined sources3
Helixi1016 – 1025Combined sources10
Helixi1032 – 1043Combined sources12
Turni1046 – 1049Combined sources4
Turni1057 – 1059Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A55X-ray3.50A1-1068[»]
ProteinModelPortaliP42337.
SMRiP42337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 105PI3K-ABDPROSITE-ProRule annotationAdd BLAST90
Domaini187 – 289PI3K-RBDPROSITE-ProRule annotationAdd BLAST103
Domaini330 – 487C2 PI3K-typePROSITE-ProRule annotationAdd BLAST158
Domaini517 – 694PIK helicalPROSITE-ProRule annotationAdd BLAST178
Domaini797 – 1068PI3K/PI4KPROSITE-ProRule annotationAdd BLAST272

Domaini

The PI3K-ABD domain and the PI3K-RBD domain interact with the PI3K/PI4K kinase domain. The C2 PI3K-type domain may facilitate the recruitment to the plasma membrane. The inhibitory interactions with PIK3R1 are mediated by the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1, and the C2 PI3K-type domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with the nSH2 (N-terminal SH2) region of PIK3R1.By similarity

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
Contains 1 C2 PI3K-type domain.PROSITE-ProRule annotation
Contains 1 PI3K-ABD domain.PROSITE-ProRule annotation
Contains 1 PI3K-RBD domain.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 1 PIK helical domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0904. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000252911.
HOVERGENiHBG052721.
InParanoidiP42337.
KOiK00922.
OMAiPMVRAFA.
OrthoDBiEOG091G027R.
TreeFamiTF102031.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003113. PI3K_adapt-bd_dom.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10048. PTHR10048. 1 hit.
PfamiPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF02192. PI3K_p85B. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
SMARTiSM00142. PI3K_C2. 1 hit.
SM00143. PI3K_p85B. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51544. PI3K_ABD. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLVTIKHELF
60 70 80 90 100
REARKYPLHQ LLQDETSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK
110 120 130 140 150
VIEPVGNREE KILNREIGFV IGMPVCEFDM VKDPEVQDFR RNILNVCKEA
160 170 180 190 200
VDLRDLNSPH SRAMYVYPPN VESSPELPKH IYNKLDKGQI IVVIWVIVSP
210 220 230 240 250
NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK LCVLEYQGKY
260 270 280 290 300
ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPID
310 320 330 340 350
SFTMPSYSRR ISTATPYMNG ETSTKSLWVI NSALRIKILC ATYVNVNIRD
360 370 380 390 400
IDKIYVRTGI YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA
410 420 430 440 450
RLCLSICSVK GRKGAKEEHC PLAWGNINLF DYTDTLVSGK MALNLWPVPH
460 470 480 490 500
GLEDLLNPIG VTGSNPNKET PCLELEFDWF SSVVKFPDMS VIEEHANWSV
510 520 530 540 550
SREAGFSYSH TGLSNRLARD NELRENDKEQ LRALCTRDPL SEITEQEKDF
560 570 580 590 600
LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME
610 620 630 640 650
LLDCNYPDPM VRSFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV
660 670 680 690 700
RFLLKKALTN QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK
710 720 730 740 750
HLNRQVEAME KLINLTDILK QEKKDETQKV QMKFLVEQMR QPDFMDALQG
760 770 780 790 800
FLSPLNPAHQ LGNLRLEECR IMSSAKRPLW LNWENPDIMS ELLFQNNEII
810 820 830 840 850
FKNGDDLRQD MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS IGDCVGLIEV
860 870 880 890 900
VRNSHTIMQI QCKGGLKGAL QFNSHTLHQW LKDKNKGEIY DAAIDLFTRS
910 920 930 940 950
CAGYCVATFI LGIGDRHNSN IMVKDDGQLF HIDFGHFLDH KKKKFGYKRE
960 970 980 990 1000
RVPFVLTQDF LIVISKGAQE YTKTREFERF QEMCYKAYLA IRQHANLFIN
1010 1020 1030 1040 1050
LFSMMLGSGM PELQSFDDIA YIRKTLALDK TEQEALEYFT KQMNDAHHGG
1060
WTTKMDWIFH TIKQHALN
Length:1,068
Mass (Da):124,412
Last modified:July 27, 2011 - v2
Checksum:iD593283B416ABFD0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti399A → L in AAA18334 (PubMed:8139567).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03279 mRNA. Translation: AAA18334.1.
CH466530 Genomic DNA. Translation: EDL34990.1.
BC089038 mRNA. Translation: AAH89038.1.
BC130228 mRNA. Translation: AAI30229.1.
CCDSiCCDS38409.1.
RefSeqiNP_032865.2. NM_008839.2.
XP_006535472.1. XM_006535409.3.
XP_006535473.1. XM_006535410.3.
UniGeneiMm.260521.

Genome annotation databases

EnsembliENSMUST00000029201; ENSMUSP00000029201; ENSMUSG00000027665.
ENSMUST00000108243; ENSMUSP00000103878; ENSMUSG00000027665.
GeneIDi18706.
KEGGimmu:18706.
UCSCiuc008owd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03279 mRNA. Translation: AAA18334.1.
CH466530 Genomic DNA. Translation: EDL34990.1.
BC089038 mRNA. Translation: AAH89038.1.
BC130228 mRNA. Translation: AAI30229.1.
CCDSiCCDS38409.1.
RefSeqiNP_032865.2. NM_008839.2.
XP_006535472.1. XM_006535409.3.
XP_006535473.1. XM_006535410.3.
UniGeneiMm.260521.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A55X-ray3.50A1-1068[»]
ProteinModelPortaliP42337.
SMRiP42337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202160. 5 interactors.
DIPiDIP-32095N.
IntActiP42337. 10 interactors.
MINTiMINT-219865.
STRINGi10090.ENSMUSP00000029201.

Chemistry databases

BindingDBiP42337.
ChEMBLiCHEMBL2499.

PTM databases

iPTMnetiP42337.
PhosphoSitePlusiP42337.

Proteomic databases

EPDiP42337.
MaxQBiP42337.
PaxDbiP42337.
PRIDEiP42337.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029201; ENSMUSP00000029201; ENSMUSG00000027665.
ENSMUST00000108243; ENSMUSP00000103878; ENSMUSG00000027665.
GeneIDi18706.
KEGGimmu:18706.
UCSCiuc008owd.2. mouse.

Organism-specific databases

CTDi5290.
MGIiMGI:1206581. Pik3ca.

Phylogenomic databases

eggNOGiKOG0904. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000252911.
HOVERGENiHBG052721.
InParanoidiP42337.
KOiK00922.
OMAiPMVRAFA.
OrthoDBiEOG091G027R.
TreeFamiTF102031.

Enzyme and pathway databases

BRENDAi2.7.1.137. 3474.
2.7.1.153. 3474.
ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1250342. PI3K events in ERBB4 signaling.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1660499. Synthesis of PIPs at the plasma membrane.
R-MMU-180292. GAB1 signalosome.
R-MMU-186763. Downstream signal transduction.
R-MMU-1963642. PI3K events in ERBB2 signaling.
R-MMU-198203. PI3K/AKT activation.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2029485. Role of phospholipids in phagocytosis.
R-MMU-210993. Tie2 Signaling.
R-MMU-2424491. DAP12 signaling.
R-MMU-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-MMU-388841. Costimulation by the CD28 family.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-392451. G beta:gamma signalling through PI3Kgamma.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654695. PI-3K cascade:FGFR2.
R-MMU-5654710. PI-3K cascade:FGFR3.
R-MMU-5654720. PI-3K cascade:FGFR4.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-8851907. MET activates PI3K/AKT signaling.
R-MMU-8853659. RET signaling.
R-MMU-912526. Interleukin receptor SHC signaling.
R-MMU-912631. Regulation of signaling by CBL.

Miscellaneous databases

ChiTaRSiPik3ca. mouse.
PROiP42337.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027665.
ExpressionAtlasiP42337. baseline and differential.
GenevisibleiP42337. MM.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003113. PI3K_adapt-bd_dom.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10048. PTHR10048. 1 hit.
PfamiPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF02192. PI3K_p85B. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
SMARTiSM00142. PI3K_C2. 1 hit.
SM00143. PI3K_p85B. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51544. PI3K_ABD. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPK3CA_MOUSE
AccessioniPrimary (citable) accession number: P42337
Secondary accession number(s): Q0VGQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.