| Tag | Content |
|---|
| CPLM ID | CPLM-016582 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform |
Protein Synonyms/Alias | PI3-kinase subunit beta; PI3K-beta; PI3Kbeta; PtdIns-3-kinase subunit beta; Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta; PtdIns-3-kinase subunit p110-beta; p110beta |
Gene Name | Pik3cb |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1019 | VKDIQYLKDSLALGK | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 20 109 PI3K-ABD.
DOMAIN 188 279 PI3K-RBD.
DOMAIN 323 490 C2 PI3K-type.
DOMAIN 518 695 PIK helical.
DOMAIN 794 1061 PI3K/PI4K.
MOTIF 404 412 Nuclear localization signal (NLS) (By
MOD_RES 1064 1064 Phosphoserine; by autocatalysis. |
Keyword | 3D-structure; ATP-binding; Autophagy; Cell adhesion; Complete proteome; Cytoplasm; Endocytosis; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1064 AA |
Protein Sequence | MPPAMADNLD IWAVDSQIAS DGAISVDFLL PTGIYIQLEV PREATISYIK QMLWKQVHNY 60
PMFNLLMDID SYMFACVNQT AVYEELEDET RRLCDVRPFL PVLKLVTRSC DPAEKLDSKI 120
GVLIGKGLHE FDALKDPEVN EFRRKMRKFS EAKIQSLVGL SWIDWLKHTY PPEHEPSVLE 180
NLEDKLYGGK LVVAVHFENS QDVFSFQVSP NLNPIKINEL AIQKRLTIRG KEDEASPCDY 240
VLQVSGRVEY VFGDHPLIQF QYIRNCVMNR TLPHFILVEC CKIKKMYEQE MIAIEAAINR 300
NSSNLPLPLP PKKTRVISHI WDNNNPFQIT LVKGNKLNTE ETVKVHVRAG LFHGTELLCK 360
TVVSSEISGK NDHIWNEQLE FDINICDLPR MARLCFAVYA VLDKVKTKKS TKTINPSKYQ 420
TIRKAGKVHY PVAWVNTMVF DFKGQLRSGD VILHSWSSFP DELEEMLNPM GTVQTNPYAE 480
NATALHITFP ENKKQPCYYP PFDKIIEKAA ELASGDSANV SSRGGKKFLA VLKEILDRDP 540
LSQLCENEMD LIWTLRQDCR ENFPQSLPKL LLSIKWNKLE DVAQLQALLQ IWPKLPPREA 600
LELLDFNYPD QYVREYAVGC LRQMSDEELS QYLLQLVQVL KYEPFLDCAL SRFLLERALD 660
NRRIGQFLFW HLRSEVHTPA VSVQFGVILE AYCRGSVGHM KVLSKQVEAL NKLKTLNSLI 720
KLNAVKLSRA KGKEAMHTCL KQSAYREALS DLQSPLNPCV ILSELYVEKC KYMDSKMKPL 780
WLVYSSRAFG EDSVGVIFKN GDDLRQDMLT LQMLRLMDLL WKEAGLDLRM LPYGCLATGD 840
RSGLIEVVST SETIADIQLN SSNVAATAAF NKDALLNWLK EYNSGDDLDR AIEEFTLSCA 900
GYCVASYVLG IGDRHSDNIM VKKTGQLFHI DFGHILGNFK SKFGIKRERV PFILTYDFIH 960
VIQQGKTGNT EKFGRFRQCC EDAYLILRRH GNLFITLFAL MLTAGLPELT SVKDIQYLKD 1020
SLALGKSEEE ALKQFKQKFD EALRESWTTK VNWMAHTVRK DYRS 1064 |
Gene Ontology | GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:RefGenome. GO:0005886; C:plasma membrane; IBA:RefGenome. GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IMP:MGI. GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:RefGenome. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IBA:RefGenome. GO:0006914; P:autophagy; IEA:UniProtKB-KW. GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI. GO:0040016; P:embryonic cleavage; IMP:MGI. GO:0006897; P:endocytosis; IEA:UniProtKB-KW. GO:0007156; P:homophilic cell adhesion; IMP:MGI. GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro. GO:0030168; P:platelet activation; IMP:MGI. GO:0001952; P:regulation of cell-matrix adhesion; IMP:MGI. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |