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Q9Z1L0

- PK3CB_RAT

UniProt

Q9Z1L0 - PK3CB_RAT

Protein

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

Gene

Pik3cb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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 By similarity.By similarity

    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: RGD
    2. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: RefGenome
    3. ATP binding Source: UniProtKB-KW
    4. phosphatidylinositol 3-kinase activity Source: RGD
    5. phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: RefGenome

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW
    3. endocytosis Source: UniProtKB-KW
    4. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
    5. phosphatidylinositol-mediated signaling Source: InterPro
    6. phosphatidylinositol phosphorylation Source: RGD

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Autophagy, Cell adhesion, Endocytosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196225. 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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620917. Pik3cb.

    Subcellular locationi

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

    GO - Cellular componenti

    1. brush border membrane Source: RGD
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB-SubCell
    4. phosphatidylinositol 3-kinase complex Source: RGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10701070Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoformPRO_0000088789Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1070 – 10701PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9Z1L0.
    PRIDEiQ9Z1L0.

    PTM databases

    PhosphoSiteiQ9Z1L0.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9Z1L0.

    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 By similarity. Interacts with BECN1, ATG14 and RAB5A By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-204613.
    STRINGi10116.ENSRNOP00000022179.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z1L0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 11590PI3K-ABDPROSITE-ProRule annotationAdd
    BLAST
    Domaini194 – 28592PI3K-RBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini327 – 496170C2 PI3K-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini524 – 701178PIK helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini800 – 1067268PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi410 – 4189Nuclear 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.
    HOGENOMiHOG000252911.
    HOVERGENiHBG052721.
    InParanoidiQ9Z1L0.
    KOiK00922.
    PhylomeDBiQ9Z1L0.

    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.

    Q9Z1L0-1 [UniParc]FASTAAdd to Basket

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    MCFRSIMPPA MADTLDIWAV DSQIASDGSI SVDFLLPTGI YIQLEVPREA     50
    TISYIKQMLW KQVHNYPMFN LLMDIDSYMF ACVNQTAVYE ELEDETRRLC 100
    DVRPFLPVLK LVTRSCDPAE KLDSKIGVLI GKGLHEFDAL KDPEVNEFRR 150
    KMRKFSEDKI QSLVGLSWID WLKHTYPPEH EPSVLENLED KLYGGKLVVA 200
    VHFENSQDVF SFQVSPNLNP IKINELAIQK RLTIRGKEEE ASPCDYVLQV 250
    SGRVEYVFGD HPLIQFQYIR NCVMNRTLPH FILVECCKIK KMYEQEMIAI 300
    EAAINRNSSS LPLPLPPKKT RVISHVWGNN NPFQIVLVKG NKLNTEETVK 350
    VHVRAGLFHG TELLCKTVVS SEISGKNDHI WNEQLEFDIN ICDLPRMARL 400
    CFAVYAVLDK VKTKKSTKTI NPSKYQTIRK AGKVHYPVAW VNTMVFDFKG 450
    QLRSGDVILH SWSSFPDELE EMLNPMGTVQ TNPYAENATA LHIKFPENKK 500
    QPYYYPPFDK IIEKAAEIAS GDSANVSSRG GKKFLAVLKE ILDRDPLSQL 550
    CENEMDLIWT LRQDCRENFP QSLPKLLLSI KWNKLEDVAQ LQALLQIWPK 600
    LPPREALELL DFNYPDQYVR EYAVGCLRQM SDEELSQYLL QLVQVLKYEP 650
    FLDCALSRFL LERALDNRRI GQFLFWHLRS EVHTPAVSIQ FGVILEAYCR 700
    GSVGHMKVLS KQVEALNKLK TLNSLIKLNA MKLNRAKGKE AMHTCLKQSA 750
    YREALSDLQS PLNPCVILSE LYVEKCRYMD SKMKPLWLVY SNRAFGEDAV 800
    GVIFKNGDDL RQDMLTLQML RLMDLLWKEA GLDLRMLPYG CLATGDRSGL 850
    IEVVSTSETI ADIQLNSSNV AATAAFNKDA LLNWLKEYNS GDDLDRAIEE 900
    FTLSCAGYCV ASYVLGIGDR HSDNIMVKKT GQLFHIDFGH ILGNFKSKFG 950
    IKRERVPFIL TYDFIHVIQQ GKTGNTEKFG RFRQCCEDAY LILRRHGNLF 1000
    ITLFALMLTA GLPELTSVKD IQYLKDSLAL GKSEEEALKQ FKQKFDEALR 1050
    ESWTTKVNWM AHTVRKDYRS 1070
    Length:1,070
    Mass (Da):122,608
    Last modified:May 1, 1999 - v1
    Checksum:i4E8EB2333E96E4D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012482 mRNA. Translation: CAA10046.1.
    RefSeqiNP_445933.1. NM_053481.1.
    UniGeneiRn.44268.

    Genome annotation databases

    GeneIDi85243.
    KEGGirno:85243.
    UCSCiRGD:620917. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012482 mRNA. Translation: CAA10046.1 .
    RefSeqi NP_445933.1. NM_053481.1.
    UniGenei Rn.44268.

    3D structure databases

    ProteinModelPortali Q9Z1L0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-204613.
    STRINGi 10116.ENSRNOP00000022179.

    PTM databases

    PhosphoSitei Q9Z1L0.

    Proteomic databases

    PaxDbi Q9Z1L0.
    PRIDEi Q9Z1L0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 85243.
    KEGGi rno:85243.
    UCSCi RGD:620917. rat.

    Organism-specific databases

    CTDi 5291.
    RGDi 620917. Pik3cb.

    Phylogenomic databases

    eggNOGi COG5032.
    HOGENOMi HOG000252911.
    HOVERGENi HBG052721.
    InParanoidi Q9Z1L0.
    KOi K00922.
    PhylomeDBi Q9Z1L0.

    Enzyme and pathway databases

    UniPathwayi UPA00220 .
    Reactomei REACT_196225. Regulation of signaling by CBL.

    Miscellaneous databases

    NextBioi 617306.
    PROi Q9Z1L0.

    Gene expression databases

    Genevestigatori Q9Z1L0.

    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. "Phosphatidylinositol-3 kinase and activation of phosphodiesterase 3B in adipocytes."
      Mulder H., Stenson Holst L., Degerman E.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.

    Entry informationi

    Entry nameiPK3CB_RAT
    AccessioniPrimary (citable) accession number: Q9Z1L0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3