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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 binding Source: IntAct
  7. protein kinase activator activity Source: BHF-UCL
  8. protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

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_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.

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. 1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex Source: Ensembl
  2. lamellipodium Source: MGI
  3. phosphatidylinositol 3-kinase complex Source: MGI
  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 isoform
PRO_0000088786Add
BLAST

Proteomic databases

MaxQBiP42337.
PaxDbiP42337.
PRIDEiP42337.

PTM databases

PhosphoSiteiP42337.

Expressioni

Gene expression databases

ArrayExpressiP42337.
BgeeiP42337.
GenevestigatoriP42337.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CA and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3) By similarity. Interacts with IRS1 in nuclear extracts By similarity. Interacts with RUFY3 By similarity. Interacts with RASD2 By similarity. Interacts with APPL1 By similarity. Interacts with HRAS and KRAS By similarity. Interaction with HRAS/KRAS is required for PI3K pathway signaling and cell proliferation stimulated by EGF and FGF2 By similarity.2 Publications

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

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

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 10590PI3K-ABD
Add
BLAST
Domaini187 – 289103PI3K-RBD
Add
BLAST
Domaini330 – 487158C2 PI3K-type
Add
BLAST
Domaini517 – 694178PIK helical
Add
BLAST
Domaini797 – 1068272PI3K/PI4K
Add
BLAST

Domaini

The PI3K-ABD domain and the PI3K-RBD domain interact with the PI3K/PI4K kinase domain By similarity. The C2 PI3K-type domain may facilitate the recruitment to the plasma membrane By similarity. 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.
Contains 1 PI3K-ABD domain.
Contains 1 PI3K-RBD domain.
Contains 1 PI3K/PI4K domain.
Contains 1 PIK helical domain.

Phylogenomic databases

eggNOGiCOG5032.
GeneTreeiENSGT00620000087742.
HOGENOMiHOG000252911.
HOVERGENiHBG052721.
InParanoidiQ0VGQ5.
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

MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLVTIKHELF     50
REARKYPLHQ LLQDETSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK 100
VIEPVGNREE KILNREIGFV IGMPVCEFDM VKDPEVQDFR RNILNVCKEA 150
VDLRDLNSPH SRAMYVYPPN VESSPELPKH IYNKLDKGQI IVVIWVIVSP 200
NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK LCVLEYQGKY 250
ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPID 300
SFTMPSYSRR ISTATPYMNG ETSTKSLWVI NSALRIKILC ATYVNVNIRD 350
IDKIYVRTGI YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA 400
RLCLSICSVK GRKGAKEEHC PLAWGNINLF DYTDTLVSGK MALNLWPVPH 450
GLEDLLNPIG VTGSNPNKET PCLELEFDWF SSVVKFPDMS VIEEHANWSV 500
SREAGFSYSH TGLSNRLARD NELRENDKEQ LRALCTRDPL SEITEQEKDF 550
LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME 600
LLDCNYPDPM VRSFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV 650
RFLLKKALTN QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK 700
HLNRQVEAME KLINLTDILK QEKKDETQKV QMKFLVEQMR QPDFMDALQG 750
FLSPLNPAHQ LGNLRLEECR IMSSAKRPLW LNWENPDIMS ELLFQNNEII 800
FKNGDDLRQD MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS IGDCVGLIEV 850
VRNSHTIMQI QCKGGLKGAL QFNSHTLHQW LKDKNKGEIY DAAIDLFTRS 900
CAGYCVATFI LGIGDRHNSN IMVKDDGQLF HIDFGHFLDH KKKKFGYKRE 950
RVPFVLTQDF LIVISKGAQE YTKTREFERF QEMCYKAYLA IRQHANLFIN 1000
LFSMMLGSGM PELQSFDDIA YIRKTLALDK TEQEALEYFT KQMNDAHHGG 1050
WTTKMDWIFH TIKQHALN 1068
Length:1,068
Mass (Da):124,412
Last modified:July 27, 2011 - v2
Checksum:iD593283B416ABFD0
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti399 – 3991A → L in AAA18334. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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...

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 ENSGT00620000087742.
HOGENOMi HOG000252911.
HOVERGENi HBG052721.
InParanoidi Q0VGQ5.
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_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.

Miscellaneous databases

ChiTaRSi PIK3CA. mouse.
NextBioi 294769.
PROi P42337.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42337.
Bgeei P42337.
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: September 3, 2014
This is version 131 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

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