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Q8BTI9

- PK3CB_MOUSE

UniProt

Q8BTI9 - PK3CB_MOUSE

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Protein

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

Gene

Pik3cb

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. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (Phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors.6 Publications

Catalytic activityi

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

Pathwayi

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

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. cellular calcium ion homeostasis Source: MGI
  3. embryonic cleavage Source: MGI
  4. endocytosis Source: UniProtKB-KW
  5. homophilic cell adhesion via plasma membrane adhesion molecules Source: MGI
  6. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  7. phosphatidylinositol-mediated signaling Source: InterPro
  8. platelet activation Source: MGI
  9. regulation of cell-matrix adhesion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Autophagy, Cell adhesion, Endocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_188185. DAP12 signaling.
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_205300. PI3K/AKT activation.
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_220092. GPVI-mediated activation cascade.
REACT_223974. G beta:gamma signalling through PI3Kgamma.
REACT_225145. Downstream TCR signaling.
REACT_225836. Interleukin-3, 5 and GM-CSF 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.
UniPathwayiUPA00220.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform (EC:2.7.1.153)
Short name:
PI3-kinase subunit beta
Short name:
PI3K-beta
Short name:
PI3Kbeta
Short name:
PtdIns-3-kinase subunit beta
Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta
Short name:
PtdIns-3-kinase subunit p110-beta
Short name:
p110beta
Gene namesi
Name:Pik3cb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1922019. Pik3cb.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Interaction with PIK3R2 is required for nuclear localization and export.

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
  2. phosphatidylinositol 3-kinase complex Source: RefGenome
  3. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice have defects in autophagosome formation. Have normal bleeding time but are resistant to thrombosis after arterial injury. Mice fail to induce tumors in a model of prostate tumor formation induced by Pten loss.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10641064Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoformPRO_0000088788Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1064 – 10641Phosphoserine; by autocatalysisBy similarity

Post-translational modificationi

Phosphorylation at Ser-1064 down-regulates lipid kinase activity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BTI9.
PaxDbiQ8BTI9.
PRIDEiQ8BTI9.

PTM databases

PhosphoSiteiQ8BTI9.

Expressioni

Gene expression databases

BgeeiQ8BTI9.
ExpressionAtlasiQ8BTI9. baseline and differential.
GenevestigatoriQ8BTI9.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CB and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interaction with PIK3R2 is required for nuclear localization and nuclear export (By similarity). Part of a complex with PIK3R1 and PTEN (By similarity). Binding to PTEN may antagonize the lipid kinase activity under normal growth conditions (By similarity). Part of a complex involved in autophagosome formation composed of PIK3C3 and PIK3R4. Interacts with BECN1, ATG14 and RAB5A.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Pik3r1P264504EBI-644672,EBI-641764

Protein-protein interaction databases

BioGridi217006. 3 interactions.
DIPiDIP-49395N.
IntActiQ8BTI9. 6 interactions.

Structurei

Secondary structure

1
1064
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 298Combined sources
Beta strandi35 – 417Combined sources
Helixi46 – 5611Combined sources
Helixi57 – 593Combined sources
Turni61 – 644Combined sources
Helixi69 – 713Combined sources
Beta strandi72 – 8110Combined sources
Beta strandi83 – 853Combined sources
Beta strandi91 – 933Combined sources
Helixi94 – 963Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi103 – 1086Combined sources
Helixi118 – 1247Combined sources
Helixi129 – 1335Combined sources
Helixi137 – 15923Combined sources
Helixi164 – 1696Combined sources
Helixi178 – 1803Combined sources
Helixi182 – 1854Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi191 – 1999Combined sources
Beta strandi204 – 2085Combined sources
Helixi215 – 22713Combined sources
Helixi237 – 2393Combined sources
Beta strandi240 – 2445Combined sources
Beta strandi253 – 2553Combined sources
Turni257 – 2593Combined sources
Helixi261 – 2688Combined sources
Beta strandi274 – 2796Combined sources
Helixi280 – 29516Combined sources
Beta strandi325 – 33410Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi356 – 3594Combined sources
Beta strandi369 – 3713Combined sources
Beta strandi377 – 3848Combined sources
Turni385 – 3873Combined sources
Beta strandi393 – 3986Combined sources
Beta strandi433 – 4408Combined sources
Beta strandi449 – 4546Combined sources
Beta strandi465 – 4673Combined sources
Beta strandi484 – 4896Combined sources
Beta strandi493 – 4953Combined sources
Helixi502 – 51312Combined sources
Helixi529 – 5368Combined sources
Helixi546 – 5549Combined sources
Helixi556 – 5627Combined sources
Helixi564 – 5663Combined sources
Helixi567 – 5704Combined sources
Helixi579 – 59012Combined sources
Helixi597 – 6004Combined sources
Helixi601 – 6044Combined sources
Helixi611 – 62111Combined sources
Helixi626 – 6294Combined sources
Helixi633 – 64210Combined sources
Beta strandi644 – 6474Combined sources
Helixi649 – 66012Combined sources
Helixi662 – 67312Combined sources
Beta strandi675 – 6784Combined sources
Turni679 – 6813Combined sources
Helixi682 – 69514Combined sources
Turni697 – 6993Combined sources
Helixi700 – 72324Combined sources
Turni724 – 7263Combined sources
Helixi729 – 74012Combined sources
Helixi743 – 7497Combined sources
Beta strandi750 – 7534Combined sources
Beta strandi758 – 7625Combined sources
Helixi767 – 7693Combined sources
Beta strandi780 – 7845Combined sources
Turni787 – 7893Combined sources
Beta strandi795 – 8028Combined sources
Helixi805 – 82319Combined sources
Beta strandi835 – 8395Combined sources
Beta strandi842 – 8465Combined sources
Beta strandi849 – 8535Combined sources
Helixi854 – 8585Combined sources
Beta strandi859 – 8613Combined sources
Turni867 – 8704Combined sources
Helixi874 – 8829Combined sources
Helixi886 – 90823Combined sources
Beta strandi918 – 9225Combined sources
Beta strandi927 – 9293Combined sources
Helixi942 – 9443Combined sources
Helixi956 – 9627Combined sources
Turni963 – 9653Combined sources
Helixi970 – 98920Combined sources
Helixi991 – 100010Combined sources
Helixi1001 – 10033Combined sources
Helixi1012 – 10154Combined sources
Helixi1016 – 10216Combined sources
Turni1022 – 10254Combined sources
Helixi1028 – 104417Combined sources
Helixi1046 – 105813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y3AX-ray3.30A1-1064[»]
4BFRX-ray2.80A/B114-1064[»]
ProteinModelPortaliQ8BTI9.
SMRiQ8BTI9. Positions 117-1061.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 10990PI3K-ABDPROSITE-ProRule annotationAdd
BLAST
Domaini188 – 27992PI3K-RBDPROSITE-ProRule annotationAdd
BLAST
Domaini323 – 490168C2 PI3K-typePROSITE-ProRule annotationAdd
BLAST
Domaini518 – 695178PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini794 – 1061268PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi404 – 4129Nuclear localization signal (NLS)By similarity

Domaini

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; the C2 PI3K-type domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with the nSH2 (N-terminal SH2) region of PIK3R1; and the PI3K/PI4K kinase domain with the cSH2 (C-terminal SH2) region of PIK3R1. The inhibitory interaction between the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1 is weak. The nuclear localization signal (NLS) is required for its function in cell survival (By similarity).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.
InParanoidiQ8BTI9.
KOiK00922.
OMAiAMHTCLK.
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]
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.

Q8BTI9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPAMADNLD IWAVDSQIAS DGAISVDFLL PTGIYIQLEV PREATISYIK
60 70 80 90 100
QMLWKQVHNY PMFNLLMDID SYMFACVNQT AVYEELEDET RRLCDVRPFL
110 120 130 140 150
PVLKLVTRSC DPAEKLDSKI GVLIGKGLHE FDALKDPEVN EFRRKMRKFS
160 170 180 190 200
EAKIQSLVGL SWIDWLKHTY PPEHEPSVLE NLEDKLYGGK LVVAVHFENS
210 220 230 240 250
QDVFSFQVSP NLNPIKINEL AIQKRLTIRG KEDEASPCDY VLQVSGRVEY
260 270 280 290 300
VFGDHPLIQF QYIRNCVMNR TLPHFILVEC CKIKKMYEQE MIAIEAAINR
310 320 330 340 350
NSSNLPLPLP PKKTRVISHI WDNNNPFQIT LVKGNKLNTE ETVKVHVRAG
360 370 380 390 400
LFHGTELLCK TVVSSEISGK NDHIWNEQLE FDINICDLPR MARLCFAVYA
410 420 430 440 450
VLDKVKTKKS TKTINPSKYQ TIRKAGKVHY PVAWVNTMVF DFKGQLRSGD
460 470 480 490 500
VILHSWSSFP DELEEMLNPM GTVQTNPYAE NATALHITFP ENKKQPCYYP
510 520 530 540 550
PFDKIIEKAA ELASGDSANV SSRGGKKFLA VLKEILDRDP LSQLCENEMD
560 570 580 590 600
LIWTLRQDCR ENFPQSLPKL LLSIKWNKLE DVAQLQALLQ IWPKLPPREA
610 620 630 640 650
LELLDFNYPD QYVREYAVGC LRQMSDEELS QYLLQLVQVL KYEPFLDCAL
660 670 680 690 700
SRFLLERALD NRRIGQFLFW HLRSEVHTPA VSVQFGVILE AYCRGSVGHM
710 720 730 740 750
KVLSKQVEAL NKLKTLNSLI KLNAVKLSRA KGKEAMHTCL KQSAYREALS
760 770 780 790 800
DLQSPLNPCV ILSELYVEKC KYMDSKMKPL WLVYSSRAFG EDSVGVIFKN
810 820 830 840 850
GDDLRQDMLT LQMLRLMDLL WKEAGLDLRM LPYGCLATGD RSGLIEVVST
860 870 880 890 900
SETIADIQLN SSNVAATAAF NKDALLNWLK EYNSGDDLDR AIEEFTLSCA
910 920 930 940 950
GYCVASYVLG IGDRHSDNIM VKKTGQLFHI DFGHILGNFK SKFGIKRERV
960 970 980 990 1000
PFILTYDFIH VIQQGKTGNT EKFGRFRQCC EDAYLILRRH GNLFITLFAL
1010 1020 1030 1040 1050
MLTAGLPELT SVKDIQYLKD SLALGKSEEE ALKQFKQKFD EALRESWTTK
1060
VNWMAHTVRK DYRS
Length:1,064
Mass (Da):121,711
Last modified:July 27, 2011 - v2
Checksum:iEBDF0266BF0A2032
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231L → R in BAC41102. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090116 mRNA. Translation: BAC41102.1.
AK154106 mRNA. Translation: BAE32380.1.
CH466560 Genomic DNA. Translation: EDL20998.1.
CCDSiCCDS23432.1.
RefSeqiNP_083370.2. NM_029094.3.
UniGeneiMm.213128.

Genome annotation databases

EnsembliENSMUST00000035037; ENSMUSP00000035037; ENSMUSG00000032462.
GeneIDi74769.
KEGGimmu:74769.
UCSCiuc009rdv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090116 mRNA. Translation: BAC41102.1 .
AK154106 mRNA. Translation: BAE32380.1 .
CH466560 Genomic DNA. Translation: EDL20998.1 .
CCDSi CCDS23432.1.
RefSeqi NP_083370.2. NM_029094.3.
UniGenei Mm.213128.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y3A X-ray 3.30 A 1-1064 [» ]
4BFR X-ray 2.80 A/B 114-1064 [» ]
ProteinModelPortali Q8BTI9.
SMRi Q8BTI9. Positions 117-1061.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 217006. 3 interactions.
DIPi DIP-49395N.
IntActi Q8BTI9. 6 interactions.

PTM databases

PhosphoSitei Q8BTI9.

Proteomic databases

MaxQBi Q8BTI9.
PaxDbi Q8BTI9.
PRIDEi Q8BTI9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035037 ; ENSMUSP00000035037 ; ENSMUSG00000032462 .
GeneIDi 74769.
KEGGi mmu:74769.
UCSCi uc009rdv.2. mouse.

Organism-specific databases

CTDi 5291.
MGIi MGI:1922019. Pik3cb.

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00760000119110.
HOGENOMi HOG000252911.
HOVERGENi HBG052721.
InParanoidi Q8BTI9.
KOi K00922.
OMAi AMHTCLK.
OrthoDBi EOG70CR65.
TreeFami TF102031.

Enzyme and pathway databases

UniPathwayi UPA00220 .
Reactomei REACT_188185. DAP12 signaling.
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_205300. PI3K/AKT activation.
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_220092. GPVI-mediated activation cascade.
REACT_223974. G beta:gamma signalling through PI3Kgamma.
REACT_225145. Downstream TCR signaling.
REACT_225836. Interleukin-3, 5 and GM-CSF 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

NextBioi 341596.
PROi Q8BTI9.
SOURCEi Search...

Gene expression databases

Bgeei Q8BTI9.
ExpressionAtlasi Q8BTI9. baseline and differential.
Genevestigatori Q8BTI9.

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 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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Embryo.
  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. "Essential roles of PI(3)K-p110beta in cell growth, metabolism and tumorigenesis."
    Jia S., Liu Z., Zhang S., Liu P., Zhang L., Lee S.H., Zhang J., Signoretti S., Loda M., Roberts T.M., Zhao J.J.
    Nature 454:776-779(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  4. "The p110beta isoform of phosphoinositide 3-kinase signals downstream of G protein-coupled receptors and is functionally redundant with p110gamma."
    Guillermet-Guibert J., Bjorklof K., Salpekar A., Gonella C., Ramadani F., Bilancio A., Meek S., Smith A.J.H., Okkenhaug K., Vanhaesebroeck B.
    Proc. Natl. Acad. Sci. U.S.A. 105:8292-8297(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Genetic evidence for a predominant role of PI3Kbeta catalytic activity in ITAM- and integrin-mediated signaling in platelets."
    Canobbio I., Stefanini L., Cipolla L., Ciraolo E., Gruppi C., Balduini C., Hirsch E., Torti M.
    Blood 114:2193-2196(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Deletion of the p110beta isoform of phosphoinositide 3-kinase in platelets reveals its central role in Akt activation and thrombus formation in vitro and in vivo."
    Martin V., Guillermet-Guibert J., Chicanne G., Cabou C., Jandrot-Perrus M., Plantavid M., Vanhaesebroeck B., Payrastre B., Gratacap M.-P.
    Blood 115:2008-2013(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Phosphoinositide 3-kinase p110 beta regulates integrin alpha IIb beta 3 avidity and the cellular transmission of contractile forces."
    Schoenwaelder S.M., Ono A., Nesbitt W.S., Lim J., Jarman K., Jackson S.P.
    J. Biol. Chem. 285:2886-2896(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive regulator of autophagy."
    Dou Z., Chattopadhyay M., Pan J.-A., Guerriero J.L., Jiang Y.-P., Ballou L.M., Yue Z., Lin R.Z., Zong W.-X.
    J. Cell Biol. 191:827-843(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH PIK3C3 AND PIK3R4, INTERACTION WITH BECN1; ATG14 AND RAB5A, DISRUPTION PHENOTYPE.
  9. "Structure of lipid kinase p110beta/p85beta elucidates an unusual SH2-domain-mediated inhibitory mechanism."
    Zhang X., Vadas O., Perisic O., Anderson K.E., Clark J., Hawkins P.T., Stephens L.R., Williams R.L.
    Mol. Cell 41:567-578(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN A COMPLEX WITH PIK3R2 AND GDC-0941, DOMAIN.

Entry informationi

Entry nameiPK3CB_MOUSE
AccessioniPrimary (citable) accession number: Q8BTI9
Secondary accession number(s): Q3U4Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 100 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3