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Q8BTI9

- PK3CB_MOUSE

UniProt

Q8BTI9 - PK3CB_MOUSE

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
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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
    6. protein binding Source: IntAct

    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 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

    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_225145. Downstream TCR signaling.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_226341. PIP3 activates AKT signaling.
    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-SubCell
    2. phosphatidylinositol 3-kinase complex Source: RefGenome
    3. plasma membrane Source: RefGenome

    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

    ArrayExpressiQ8BTI9.
    BgeeiQ8BTI9.
    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 – 298
    Beta strandi35 – 417
    Helixi46 – 5611
    Helixi57 – 593
    Turni61 – 644
    Helixi69 – 713
    Beta strandi72 – 8110
    Beta strandi83 – 853
    Beta strandi91 – 933
    Helixi94 – 963
    Beta strandi98 – 1014
    Beta strandi103 – 1086
    Helixi118 – 1247
    Helixi129 – 1335
    Helixi137 – 15923
    Helixi164 – 1696
    Helixi178 – 1803
    Helixi182 – 1854
    Beta strandi186 – 1894
    Beta strandi191 – 1999
    Beta strandi204 – 2085
    Helixi215 – 22713
    Helixi237 – 2393
    Beta strandi240 – 2445
    Beta strandi253 – 2553
    Turni257 – 2593
    Helixi261 – 2688
    Beta strandi274 – 2796
    Helixi280 – 29516
    Beta strandi325 – 33410
    Beta strandi347 – 3537
    Beta strandi356 – 3594
    Beta strandi369 – 3713
    Beta strandi377 – 3848
    Turni385 – 3873
    Beta strandi393 – 3986
    Beta strandi433 – 4408
    Beta strandi449 – 4546
    Beta strandi465 – 4673
    Beta strandi484 – 4896
    Beta strandi493 – 4953
    Helixi502 – 51312
    Helixi529 – 5368
    Helixi546 – 5549
    Helixi556 – 5627
    Helixi564 – 5663
    Helixi567 – 5704
    Helixi579 – 59012
    Helixi597 – 6004
    Helixi601 – 6044
    Helixi611 – 62111
    Helixi626 – 6294
    Helixi633 – 64210
    Beta strandi644 – 6474
    Helixi649 – 66012
    Helixi662 – 67312
    Beta strandi675 – 6784
    Turni679 – 6813
    Helixi682 – 69514
    Turni697 – 6993
    Helixi700 – 72324
    Turni724 – 7263
    Helixi729 – 74012
    Helixi743 – 7497
    Beta strandi750 – 7534
    Beta strandi758 – 7625
    Helixi767 – 7693
    Beta strandi780 – 7845
    Turni787 – 7893
    Beta strandi795 – 8028
    Helixi805 – 82319
    Beta strandi835 – 8395
    Beta strandi842 – 8465
    Beta strandi849 – 8535
    Helixi854 – 8585
    Beta strandi859 – 8613
    Turni867 – 8704
    Helixi874 – 8829
    Helixi886 – 90823
    Beta strandi918 – 9225
    Beta strandi927 – 9293
    Helixi942 – 9443
    Helixi956 – 9627
    Turni963 – 9653
    Helixi970 – 98920
    Helixi991 – 100010
    Helixi1001 – 10033
    Helixi1012 – 10154
    Helixi1016 – 10216
    Turni1022 – 10254
    Helixi1028 – 104417
    Helixi1046 – 105813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00620000087742.
    HOGENOMiHOG000252911.
    HOVERGENiHBG052721.
    InParanoidiQ3U4Q1.
    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

    MPPAMADNLD IWAVDSQIAS DGAISVDFLL PTGIYIQLEV PREATISYIK     50
    QMLWKQVHNY PMFNLLMDID SYMFACVNQT AVYEELEDET RRLCDVRPFL 100
    PVLKLVTRSC DPAEKLDSKI GVLIGKGLHE FDALKDPEVN EFRRKMRKFS 150
    EAKIQSLVGL SWIDWLKHTY PPEHEPSVLE NLEDKLYGGK LVVAVHFENS 200
    QDVFSFQVSP NLNPIKINEL AIQKRLTIRG KEDEASPCDY VLQVSGRVEY 250
    VFGDHPLIQF QYIRNCVMNR TLPHFILVEC CKIKKMYEQE MIAIEAAINR 300
    NSSNLPLPLP PKKTRVISHI WDNNNPFQIT LVKGNKLNTE ETVKVHVRAG 350
    LFHGTELLCK TVVSSEISGK NDHIWNEQLE FDINICDLPR MARLCFAVYA 400
    VLDKVKTKKS TKTINPSKYQ TIRKAGKVHY PVAWVNTMVF DFKGQLRSGD 450
    VILHSWSSFP DELEEMLNPM GTVQTNPYAE NATALHITFP ENKKQPCYYP 500
    PFDKIIEKAA ELASGDSANV SSRGGKKFLA VLKEILDRDP LSQLCENEMD 550
    LIWTLRQDCR ENFPQSLPKL LLSIKWNKLE DVAQLQALLQ IWPKLPPREA 600
    LELLDFNYPD QYVREYAVGC LRQMSDEELS QYLLQLVQVL KYEPFLDCAL 650
    SRFLLERALD NRRIGQFLFW HLRSEVHTPA VSVQFGVILE AYCRGSVGHM 700
    KVLSKQVEAL NKLKTLNSLI KLNAVKLSRA KGKEAMHTCL KQSAYREALS 750
    DLQSPLNPCV ILSELYVEKC KYMDSKMKPL WLVYSSRAFG EDSVGVIFKN 800
    GDDLRQDMLT LQMLRLMDLL WKEAGLDLRM LPYGCLATGD RSGLIEVVST 850
    SETIADIQLN SSNVAATAAF NKDALLNWLK EYNSGDDLDR AIEEFTLSCA 900
    GYCVASYVLG IGDRHSDNIM VKKTGQLFHI DFGHILGNFK SKFGIKRERV 950
    PFILTYDFIH VIQQGKTGNT EKFGRFRQCC EDAYLILRRH GNLFITLFAL 1000
    MLTAGLPELT SVKDIQYLKD SLALGKSEEE ALKQFKQKFD EALRESWTTK 1050
    VNWMAHTVRK DYRS 1064
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 ENSGT00620000087742.
    HOGENOMi HOG000252911.
    HOVERGENi HBG052721.
    InParanoidi Q3U4Q1.
    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_225145. Downstream TCR signaling.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    NextBioi 341596.
    PROi Q8BTI9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BTI9.
    Bgeei Q8BTI9.
    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

    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: October 1, 2014
    This is version 98 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