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P42337

- PK3CA_MOUSE

UniProt

P42337 - PK3CA_MOUSE

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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: 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 in breast cancer cells 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. Has also serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS.6 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. 1-phosphatidylinositol-3-kinase activity Source: MGI
  2. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: RefGenome
  3. ATP binding Source: UniProtKB-KW
  4. insulin receptor substrate binding Source: MGI
  5. phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: RefGenome
  6. protein kinase activator activity Source: BHF-UCL
  7. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. glucose metabolic process Source: MGI
  3. hypomethylation of CpG island Source: BHF-UCL
  4. negative regulation of anoikis Source: Ensembl
  5. negative regulation of fibroblast apoptotic process Source: MGI
  6. negative regulation of neuron apoptotic process Source: MGI
  7. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  8. phosphatidylinositol-mediated signaling Source: InterPro
  9. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  10. positive regulation of protein kinase activity Source: GOC
  11. protein kinase B signaling Source: MGI
  12. protein phosphorylation Source: MGI
  13. regulation of genetic imprinting Source: BHF-UCL
  14. regulation of multicellular organism growth Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.137. 3474.
ReactomeiREACT_188185. DAP12 signaling.
REACT_188578. Signaling by SCF-KIT.
REACT_196455. Signaling by FGFR mutants.
REACT_196460. Signaling by FGFR1 fusion mutants.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198634. Regulation of signaling by CBL.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_199123. Signaling by constitutively active EGFR.
REACT_203296. PI3K events in ERBB4 signaling.
REACT_204733. G alpha (12/13) signalling events.
REACT_205300. PI3K/AKT activation.
REACT_206286. GAB1 signalosome.
REACT_207651. G alpha (q) signalling events.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_210793. Interleukin receptor SHC signaling.
REACT_211860. Tie2 Signaling.
REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_215348. PI3K events in ERBB2 signaling.
REACT_220092. GPVI-mediated activation cascade.
REACT_223974. G beta:gamma signalling through PI3Kgamma.
REACT_223993. PI-3K cascade.
REACT_225145. Downstream TCR signaling.
REACT_225477. Costimulation by the CD28 family.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_226151. CD28 dependent PI3K/Akt signaling.
REACT_226341. PIP3 activates AKT signaling.
REACT_230639. Downstream signal transduction.
REACT_240139. PI3K Cascade.
REACT_257032. Nephrin interactions.
REACT_257088. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (EC:2.7.1.153)
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:2.7.11.1)
Gene namesi
Name:Pik3ca
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1206581. Pik3ca.

Subcellular locationi

GO - Cellular componenti

  1. lamellipodium Source: MGI
  2. phosphatidylinositol 3-kinase complex Source: MGI
  3. phosphatidylinositol 3-kinase complex, class IA Source: Ensembl
  4. plasma membrane Source: RefGenome
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi208 – 2081T → 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 Publication
Mutagenesisi227 – 2271K → 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 Publication
Mutagenesisi933 – 9331D → 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 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10681068Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoformPRO_0000088786Add
BLAST

Proteomic databases

MaxQBiP42337.
PaxDbiP42337.
PRIDEiP42337.

PTM databases

PhosphoSiteiP42337.

Expressioni

Gene expression databases

BgeeiP42337.
ExpressionAtlasiP42337. baseline and differential.
GenevestigatoriP42337.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CA and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interacts with IRS1 in nuclear extracts. Interacts with RUFY3. Interacts with RASD2. Interacts with APPL1. Interacts with HRAS and KRAS. Interaction with HRAS/KRAS is required for PI3K pathway signaling and cell proliferation stimulated by EGF and FGF2.By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi202160. 5 interactions.
DIPiDIP-32095N.
IntActiP42337. 10 interactions.
MINTiMINT-219865.
STRINGi10090.ENSMUSP00000103878.

Structurei

Secondary structure

1
1068
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Beta strandi18 – 258Combined sources
Beta strandi31 – 377Combined sources
Helixi42 – 5211Combined sources
Helixi53 – 553Combined sources
Turni57 – 604Combined sources
Helixi65 – 673Combined sources
Beta strandi69 – 746Combined sources
Beta strandi77 – 815Combined sources
Helixi90 – 923Combined sources
Beta strandi94 – 1029Combined sources
Helixi109 – 1124Combined sources
Helixi117 – 1215Combined sources
Helixi125 – 1295Combined sources
Helixi134 – 1429Combined sources
Helixi144 – 15310Combined sources
Turni154 – 1574Combined sources
Helixi158 – 1658Combined sources
Helixi179 – 1824Combined sources
Beta strandi189 – 1968Combined sources
Turni199 – 2024Combined sources
Beta strandi205 – 2128Combined sources
Helixi217 – 23014Combined sources
Helixi236 – 24611Combined sources
Helixi247 – 2493Combined sources
Beta strandi250 – 2545Combined sources
Helixi267 – 2693Combined sources
Helixi271 – 2799Combined sources
Beta strandi284 – 2896Combined sources
Helixi290 – 2956Combined sources
Beta strandi324 – 3274Combined sources
Beta strandi332 – 3409Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi354 – 36411Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi382 – 39211Combined sources
Turni393 – 3953Combined sources
Beta strandi401 – 4088Combined sources
Beta strandi423 – 4308Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi439 – 4446Combined sources
Beta strandi454 – 4563Combined sources
Beta strandi458 – 4603Combined sources
Beta strandi468 – 4703Combined sources
Beta strandi472 – 4776Combined sources
Beta strandi481 – 4855Combined sources
Helixi489 – 49911Combined sources
Turni529 – 5357Combined sources
Helixi545 – 5539Combined sources
Helixi555 – 5584Combined sources
Helixi562 – 5643Combined sources
Helixi565 – 5695Combined sources
Helixi578 – 58811Combined sources
Helixi595 – 5984Combined sources
Turni599 – 6024Combined sources
Helixi609 – 62113Combined sources
Helixi625 – 6306Combined sources
Helixi632 – 6365Combined sources
Helixi639 – 6413Combined sources
Beta strandi643 – 6464Combined sources
Helixi648 – 65912Combined sources
Helixi661 – 67313Combined sources
Helixi678 – 69417Combined sources
Turni695 – 6973Combined sources
Helixi698 – 72023Combined sources
Helixi728 – 73811Combined sources
Helixi742 – 7476Combined sources
Beta strandi749 – 7524Combined sources
Beta strandi759 – 7613Combined sources
Beta strandi779 – 7846Combined sources
Helixi790 – 7923Combined sources
Beta strandi795 – 80511Combined sources
Helixi808 – 82720Combined sources
Beta strandi838 – 8425Combined sources
Beta strandi845 – 8495Combined sources
Beta strandi854 – 8563Combined sources
Helixi857 – 8604Combined sources
Helixi876 – 8849Combined sources
Helixi887 – 8893Combined sources
Helixi890 – 91122Combined sources
Turni918 – 9203Combined sources
Beta strandi921 – 9244Combined sources
Beta strandi929 – 9313Combined sources
Helixi941 – 9455Combined sources
Helixi957 – 9648Combined sources
Beta strandi965 – 9673Combined sources
Helixi975 – 99319Combined sources
Helixi995 – 100410Combined sources
Beta strandi1013 – 10153Combined sources
Helixi1016 – 102510Combined sources
Helixi1032 – 104312Combined sources
Turni1046 – 10494Combined sources
Turni1057 – 10593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A55X-ray3.50A1-1068[»]
ProteinModelPortaliP42337.
SMRiP42337. Positions 16-105, 107-1046.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 10590PI3K-ABDPROSITE-ProRule annotationAdd
BLAST
Domaini187 – 289103PI3K-RBDPROSITE-ProRule annotationAdd
BLAST
Domaini330 – 487158C2 PI3K-typePROSITE-ProRule annotationAdd
BLAST
Domaini517 – 694178PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini797 – 1068272PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG5032.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000252911.
HOVERGENiHBG052721.
InParanoidiP42337.
KOiK00922.
OMAiAFAVRCL.
OrthoDBiEOG70CR65.
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]
SMARTiSM00239. C2. 1 hit.
SM00142. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti399 – 3991A → L in AAA18334. (PubMed:8139567)Curated

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_006535409.1.
XP_006535473.1. XM_006535410.1.
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 .
CCDSi CCDS38409.1.
RefSeqi NP_032865.2. NM_008839.2.
XP_006535472.1. XM_006535409.1.
XP_006535473.1. XM_006535410.1.
UniGenei Mm.260521.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4A55 X-ray 3.50 A 1-1068 [» ]
ProteinModelPortali P42337.
SMRi P42337. Positions 16-105, 107-1046.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202160. 5 interactions.
DIPi DIP-32095N.
IntActi P42337. 10 interactions.
MINTi MINT-219865.
STRINGi 10090.ENSMUSP00000103878.

Chemistry

BindingDBi P42337.
ChEMBLi CHEMBL2499.

PTM databases

PhosphoSitei P42337.

Proteomic databases

MaxQBi P42337.
PaxDbi P42337.
PRIDEi P42337.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029201 ; ENSMUSP00000029201 ; ENSMUSG00000027665 .
ENSMUST00000108243 ; ENSMUSP00000103878 ; ENSMUSG00000027665 .
GeneIDi 18706.
KEGGi mmu:18706.
UCSCi uc008owd.2. mouse.

Organism-specific databases

CTDi 5290.
MGIi MGI:1206581. Pik3ca.

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00760000119110.
HOGENOMi HOG000252911.
HOVERGENi HBG052721.
InParanoidi P42337.
KOi K00922.
OMAi AFAVRCL.
OrthoDBi EOG70CR65.
TreeFami TF102031.

Enzyme and pathway databases

BRENDAi 2.7.1.137. 3474.
Reactomei REACT_188185. DAP12 signaling.
REACT_188578. Signaling by SCF-KIT.
REACT_196455. Signaling by FGFR mutants.
REACT_196460. Signaling by FGFR1 fusion mutants.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198634. Regulation of signaling by CBL.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_199123. Signaling by constitutively active EGFR.
REACT_203296. PI3K events in ERBB4 signaling.
REACT_204733. G alpha (12/13) signalling events.
REACT_205300. PI3K/AKT activation.
REACT_206286. GAB1 signalosome.
REACT_207651. G alpha (q) signalling events.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_210793. Interleukin receptor SHC signaling.
REACT_211860. Tie2 Signaling.
REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_215348. PI3K events in ERBB2 signaling.
REACT_220092. GPVI-mediated activation cascade.
REACT_223974. G beta:gamma signalling through PI3Kgamma.
REACT_223993. PI-3K cascade.
REACT_225145. Downstream TCR signaling.
REACT_225477. Costimulation by the CD28 family.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_226151. CD28 dependent PI3K/Akt signaling.
REACT_226341. PIP3 activates AKT signaling.
REACT_230639. Downstream signal transduction.
REACT_240139. PI3K Cascade.
REACT_257032. Nephrin interactions.
REACT_257088. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

ChiTaRSi Pik3ca. mouse.
NextBioi 294769.
PROi P42337.
SOURCEi Search...

Gene expression databases

Bgeei P42337.
ExpressionAtlasi P42337. baseline and differential.
Genevestigatori P42337.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProi IPR016024. 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 ]
PANTHERi PTHR10048. PTHR10048. 1 hit.
Pfami PF00454. 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 ]
SMARTi SM00239. C2. 1 hit.
SM00142. PI3K_C2. 1 hit.
SM00143. PI3K_p85B. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00915. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity."
    Klippel A., Escobedo J.A., Hirano M., Williams L.T.
    Mol. Cell. Biol. 14:2675-2685(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Eye.
  4. "Control of cell size through phosphorylation of upstream binding factor 1 by nuclear phosphatidylinositol 3-kinase."
    Drakas R., Tu X., Baserga R.
    Proc. Natl. Acad. Sci. U.S.A. 101:9272-9276(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRS1.
  5. "A pharmacological map of the PI3-K family defines a role for p110alpha in insulin signaling."
    Knight Z.A., Gonzalez B., Feldman M.E., Zunder E.R., Goldenberg D.D., Williams O., Loewith R., Stokoe D., Balla A., Toth B., Balla T., Weiss W.A., Williams R.L., Shokat K.M.
    Cell 125:733-747(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Critical role for the p110alpha phosphoinositide-3-OH kinase in growth and metabolic regulation."
    Foukas L.C., Claret M., Pearce W., Okkenhaug K., Meek S., Peskett E., Sancho S., Smith A.J.H., Withers D.J., Vanhaesebroeck B.
    Nature 441:366-370(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-933.
  7. "The p110alpha isoform of PI3K is essential for proper growth factor signaling and oncogenic transformation."
    Zhao J.J., Cheng H., Jia S., Wang L., Gjoerup O.V., Mikami A., Roberts T.M.
    Proc. Natl. Acad. Sci. U.S.A. 103:16296-16300(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Binding of ras to phosphoinositide 3-kinase p110alpha is required for ras-driven tumorigenesis in mice."
    Gupta S., Ramjaun A.R., Haiko P., Wang Y., Warne P.H., Nicke B., Nye E., Stamp G., Alitalo K., Downward J.
    Cell 129:957-968(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH HRAS AND KRAS, MUTAGENESIS OF THR-208 AND LYS-227.
  9. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "VEGF-mediated PI3K class IA and PKC signaling in cardiomyogenesis and vasculogenesis of mouse embryonic stem cells."
    Bekhite M.M., Finkensieper A., Binas S., Mueller J., Wetzker R., Figulla H.-R., Sauer H., Wartenberg M.
    J. Cell Sci. 124:1819-1830(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION ON CARDIOMYOGENESIS, FUNCTION ON VASCULOGENESIS.

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 26, 2014
This is version 134 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

External Data

Dasty 3