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UniProtKB - 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: 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: phosphatidylinositol phosphate biosynthesis

This protein is involved in the pathway phosphatidylinositol phosphate biosynthesis, which is part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phosphatidylinositol phosphate biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

  • adaptive immune response Source: GO_Central
  • angiogenesis involved in wound healing Source: MGI
  • autophagy Source: UniProtKB-KW
  • cell chemotaxis Source: GO_Central
  • cellular calcium ion homeostasis Source: MGI
  • embryonic cleavage Source: MGI
  • endocytosis Source: UniProtKB-KW
  • endothelial cell proliferation Source: MGI
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: MGI
  • inflammatory response Source: GO_Central
  • innate immune response Source: GO_Central
  • phosphatidylinositol 3-kinase signaling Source: MGI
  • phosphorylation Source: MGI
  • platelet activation Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of neutrophil apoptotic process Source: MGI
  • protein phosphorylation Source: GO_Central
  • regulation of cell-matrix adhesion Source: MGI
  • response to wounding Source: MGI
Complete GO annotation...

Keywordsi

Molecular functionKinase, Transferase
Biological processAutophagy, Cell adhesion, Endocytosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1660499. Synthesis of PIPs at the plasma membrane.
R-MMU-186763. Downstream signal transduction.
R-MMU-198203. PI3K/AKT activation.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2029485. Role of phospholipids in phagocytosis.
R-MMU-210993. Tie2 Signaling.
R-MMU-2424491. DAP12 signaling.
R-MMU-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-MMU-392451. G beta:gamma signalling through PI3Kgamma.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-8853659. RET signaling.
R-MMU-912526. Interleukin receptor SHC signaling.
R-MMU-912631. Regulation of signaling by CBL.
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: 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

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000887881 – 1064Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoformAdd BLAST1064

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei318PhosphoserineCombined sources1
Modified residuei1064Phosphoserine; by autocatalysisBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BTI9.
PaxDbiQ8BTI9.
PRIDEiQ8BTI9.

PTM databases

iPTMnetiQ8BTI9.
PhosphoSitePlusiQ8BTI9.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032462.
ExpressionAtlasiQ8BTI9. baseline and differential.
GenevisibleiQ8BTI9. MM.

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

GO - Molecular functioni

  • insulin receptor substrate binding Source: MGI
Complete GO annotation...

Protein-protein interaction databases

BioGridi217006. 5 interactors.
DIPiDIP-49395N.
IntActiQ8BTI9. 7 interactors.
STRINGi10090.ENSMUSP00000035037.

Chemistry databases

BindingDBiQ8BTI9.

Structurei

Secondary structure

11064
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 29Combined sources8
Beta strandi35 – 41Combined sources7
Helixi46 – 56Combined sources11
Helixi57 – 59Combined sources3
Turni61 – 64Combined sources4
Helixi69 – 71Combined sources3
Beta strandi72 – 81Combined sources10
Beta strandi83 – 85Combined sources3
Beta strandi91 – 93Combined sources3
Helixi94 – 96Combined sources3
Beta strandi98 – 101Combined sources4
Beta strandi103 – 108Combined sources6
Helixi118 – 124Combined sources7
Helixi129 – 133Combined sources5
Helixi137 – 159Combined sources23
Helixi164 – 169Combined sources6
Helixi178 – 180Combined sources3
Helixi182 – 185Combined sources4
Beta strandi186 – 189Combined sources4
Beta strandi191 – 199Combined sources9
Beta strandi204 – 208Combined sources5
Helixi215 – 227Combined sources13
Helixi237 – 239Combined sources3
Beta strandi240 – 244Combined sources5
Beta strandi253 – 255Combined sources3
Turni257 – 259Combined sources3
Helixi261 – 268Combined sources8
Beta strandi274 – 279Combined sources6
Helixi280 – 295Combined sources16
Beta strandi325 – 334Combined sources10
Beta strandi347 – 353Combined sources7
Beta strandi356 – 359Combined sources4
Helixi369 – 371Combined sources3
Beta strandi377 – 384Combined sources8
Turni385 – 387Combined sources3
Beta strandi393 – 398Combined sources6
Beta strandi433 – 440Combined sources8
Beta strandi449 – 454Combined sources6
Beta strandi465 – 467Combined sources3
Beta strandi484 – 489Combined sources6
Beta strandi493 – 495Combined sources3
Helixi502 – 513Combined sources12
Helixi529 – 536Combined sources8
Helixi546 – 554Combined sources9
Helixi556 – 562Combined sources7
Helixi564 – 566Combined sources3
Helixi567 – 570Combined sources4
Helixi579 – 590Combined sources12
Helixi597 – 600Combined sources4
Helixi601 – 604Combined sources4
Helixi611 – 621Combined sources11
Helixi626 – 629Combined sources4
Helixi633 – 642Combined sources10
Beta strandi644 – 647Combined sources4
Helixi649 – 660Combined sources12
Helixi662 – 673Combined sources12
Beta strandi675 – 678Combined sources4
Turni679 – 681Combined sources3
Helixi682 – 695Combined sources14
Turni697 – 699Combined sources3
Helixi700 – 723Combined sources24
Turni724 – 726Combined sources3
Helixi729 – 740Combined sources12
Helixi743 – 749Combined sources7
Beta strandi750 – 753Combined sources4
Beta strandi758 – 762Combined sources5
Helixi767 – 769Combined sources3
Beta strandi780 – 784Combined sources5
Turni787 – 789Combined sources3
Beta strandi795 – 802Combined sources8
Helixi805 – 823Combined sources19
Beta strandi835 – 839Combined sources5
Beta strandi842 – 846Combined sources5
Beta strandi849 – 853Combined sources5
Helixi854 – 858Combined sources5
Beta strandi859 – 861Combined sources3
Turni867 – 870Combined sources4
Helixi874 – 882Combined sources9
Helixi886 – 908Combined sources23
Beta strandi918 – 922Combined sources5
Beta strandi927 – 929Combined sources3
Helixi942 – 944Combined sources3
Helixi956 – 962Combined sources7
Turni963 – 965Combined sources3
Helixi970 – 989Combined sources20
Helixi991 – 1000Combined sources10
Helixi1001 – 1003Combined sources3
Helixi1012 – 1015Combined sources4
Helixi1016 – 1021Combined sources6
Turni1022 – 1025Combined sources4
Helixi1028 – 1044Combined sources17
Helixi1046 – 1058Combined sources13

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 109PI3K-ABDPROSITE-ProRule annotationAdd BLAST90
Domaini188 – 279PI3K-RBDPROSITE-ProRule annotationAdd BLAST92
Domaini323 – 490C2 PI3K-typePROSITE-ProRule annotationAdd BLAST168
Domaini518 – 695PIK helicalPROSITE-ProRule annotationAdd BLAST178
Domaini794 – 1061PI3K/PI4KPROSITE-ProRule annotationAdd BLAST268

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi404 – 412Nuclear localization signal (NLS)By similarity9

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

Phylogenomic databases

eggNOGiKOG0904. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000252911.
HOVERGENiHBG052721.
InParanoidiQ8BTI9.
KOiK00922.
OMAiSLNWASH.
OrthoDBiEOG091G027R.
TreeFamiTF102031.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
2.60.40.150. 1 hit.
InterProiView protein in InterPro
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.
PANTHERiPTHR10048. PTHR10048. 1 hit.
PfamiView protein in Pfam
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.
SMARTiView protein in SMART
SM00142. PI3K_C2. 1 hit.
SM00143. PI3K_p85B. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti123L → R in BAC41102 (PubMed:16141072).Curated1

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.
XP_011241131.1. XM_011242829.2.
XP_011241132.1. XM_011242830.2.
UniGeneiMm.213128.

Genome annotation databases

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

Similar proteinsi

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

Entry informationi

Entry nameiPK3CB_MOUSE
AccessioniPrimary (citable) accession number: Q8BTI9
Secondary accession number(s): Q3U4Q1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 27, 2011
Last modified: July 5, 2017
This is version 126 of the entry and version 2 of the sequence. See 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