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O35904

- PK3CD_MOUSE

UniProt

O35904 - PK3CD_MOUSE

Protein

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

Gene

Pik3cd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Phosphoinositide-3-kinase (PI3K) that phosphorylates PftdIns(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. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Have a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Have important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function.7 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Activated by growth factors and cytokine receptors through a tyrosine-kinase-dependent mechanism. Activated by RAS. IC87114 inhibits lipid kinase activity and is selective in cells at doses up to 5-10 µM. Among other effects, IC87114 reduces allergic responses, prevents the recruitment of antigen-specific T cells into target tissue, and affects natural killer cell chemotaxis.3 Publications

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

    1. B cell activation Source: MGI
    2. B cell homeostasis Source: MGI
    3. cell differentiation Source: UniProtKB-KW
    4. cell surface receptor signaling pathway Source: MGI
    5. chemotaxis Source: UniProtKB-KW
    6. inflammatory response Source: UniProtKB-KW
    7. innate immune response Source: UniProtKB-KW
    8. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
    9. phosphatidylinositol-mediated signaling Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Adaptive immunity, Chemotaxis, Differentiation, Immunity, Inflammatory response, Innate immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.153. 3474.
    ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    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_210793. Interleukin receptor SHC 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 delta isoform (EC:2.7.1.153)
    Short name:
    PI3-kinase subunit delta
    Short name:
    PI3K-delta
    Short name:
    PI3Kdelta
    Short name:
    PtdIns-3-kinase subunit delta
    Alternative name(s):
    Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta
    Short name:
    PtdIns-3-kinase subunit p110-delta
    Short name:
    p110delta
    Gene namesi
    Name:Pik3cd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1098211. Pik3cd.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. phosphatidylinositol 3-kinase complex Source: RefGenome
    2. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Null mutants are viable and fertile but display defective adaptive and innate immune responses due to signaling defects in multiple cell types including B-, T- and mast and natural killer cells.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi910 – 9101D → A: Inhibits lipid kinase activity. Mice are viable and fertile but display defective adaptive and innate immune responses Signaling defects in B-cells, T-cells, mast cells and natural killer cells. Reduced B and T-cell receptor signaling. Affects development and differentiation of B -ells. Reduced memory T-cell number. Affects B- and T-cell proliferation. Attenuates immune responses in vivo. Induces inflammatory bowel disease development. Lost TCR-induced migration and localization to antigenic tissue. Affects natural killer cell maturation and cytokine production. 4 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10431043Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoformPRO_0000088791Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei523 – 5231PhosphotyrosineBy similarity
    Modified residuei1038 – 10381Phosphoserine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylation on Ser-1038 results in the almost complete inactivation of the lipid kinase activity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO35904.
    PRIDEiO35904.

    PTM databases

    PhosphoSiteiO35904.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed in spleen and lung (at protein level). Isoform 1 is expressed predominantly in leukocytes.1 Publication

    Gene expression databases

    ArrayExpressiO35904.
    BgeeiO35904.
    GenevestigatoriO35904.

    Interactioni

    Subunit structurei

    Heterodimer of a catalytic subunit PIK3CD and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interacts with ERAS and HRAS.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Pik3r1P264502EBI-6470774,EBI-641764

    Protein-protein interaction databases

    BioGridi202161. 2 interactions.
    DIPiDIP-39841N.
    IntActiO35904. 6 interactions.

    Structurei

    Secondary structure

    1
    1043
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi110 – 12112
    Helixi126 – 1305
    Helixi134 – 15421
    Helixi159 – 1668
    Beta strandi189 – 19810
    Beta strandi202 – 2087
    Helixi213 – 22715
    Helixi236 – 2383
    Beta strandi239 – 2435
    Beta strandi252 – 2543
    Helixi256 – 2583
    Helixi260 – 2689
    Beta strandi273 – 2786
    Helixi279 – 28810
    Beta strandi321 – 33111
    Beta strandi340 – 34910
    Beta strandi352 – 3554
    Beta strandi363 – 3653
    Beta strandi370 – 38011
    Helixi381 – 3833
    Beta strandi389 – 3979
    Beta strandi416 – 42611
    Beta strandi430 – 4323
    Beta strandi435 – 4406
    Beta strandi455 – 4573
    Turni465 – 4673
    Beta strandi470 – 4756
    Helixi488 – 4936
    Helixi511 – 5144
    Helixi524 – 5329
    Helixi534 – 5407
    Helixi542 – 5443
    Helixi545 – 5495
    Helixi557 – 56812
    Helixi575 – 5817
    Helixi589 – 59911
    Helixi604 – 61714
    Helixi618 – 6203
    Beta strandi622 – 6254
    Helixi627 – 63812
    Helixi640 – 65112
    Turni652 – 6554
    Helixi657 – 67317
    Helixi675 – 70127
    Turni702 – 7043
    Helixi707 – 71812
    Helixi721 – 7277
    Beta strandi728 – 7325
    Beta strandi735 – 7406
    Helixi745 – 7473
    Beta strandi753 – 7553
    Beta strandi758 – 7636
    Turni765 – 7673
    Helixi768 – 7714
    Beta strandi773 – 7819
    Helixi784 – 80219
    Beta strandi814 – 8185
    Beta strandi821 – 8255
    Beta strandi828 – 8325
    Helixi833 – 8375
    Beta strandi841 – 8433
    Helixi850 – 8523
    Helixi853 – 8619
    Turni863 – 8653
    Helixi866 – 88823
    Beta strandi897 – 9015
    Beta strandi906 – 9083
    Helixi935 – 9417
    Turni942 – 9443
    Helixi949 – 96820
    Helixi970 – 98011
    Helixi981 – 9833
    Beta strandi988 – 9903
    Helixi991 – 100111
    Turni1002 – 10043
    Helixi1007 – 102418

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WXFX-ray1.90A106-1043[»]
    2WXGX-ray2.00A106-1043[»]
    2WXHX-ray1.90A106-1043[»]
    2WXIX-ray2.80A106-1043[»]
    2WXJX-ray2.60A106-1043[»]
    2WXKX-ray2.90A106-1043[»]
    2WXLX-ray1.99A106-1043[»]
    2WXMX-ray2.80A106-1043[»]
    2WXNX-ray2.60A106-1043[»]
    2WXOX-ray2.49A106-1043[»]
    2WXPX-ray2.30A106-1043[»]
    2WXQX-ray2.70A106-1043[»]
    2WXRX-ray2.50A106-1043[»]
    2X38X-ray2.20A106-1043[»]
    4AJWX-ray2.80A/B110-1043[»]
    ProteinModelPortaliO35904.
    SMRiO35904. Positions 20-102, 109-1026.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO35904.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 10590PI3K-ABDPROSITE-ProRule annotationAdd
    BLAST
    Domaini187 – 27892PI3K-RBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini319 – 476158C2 PI3K-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini496 – 673178PIK helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini775 – 1028254PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST

    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.
    KOiK00922.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O35904-1) [UniParc]FASTAAdd to Basket

    Also known as: p110-delta

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPPGVDCPME FWTKEESQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQVLW     50
    HRAQYEPLFH MLSDPEAYVF TCVNQTAEQQ ELEDEQRRLC DIQPFLPVLR 100
    LVAREGDRVK KLINSQISLL IGKGLHEFDS LRDPEVNDFR TKMRQFCEEA 150
    AAHRQQLGWV EWLQYSFPLQ LEPSARGWRA GLLRVSNRAL LVNVKFEGSE 200
    ESFTFQVSTK DMPLALMACA LRKKATVFRQ PLVEQPEEYA LQVNGRHEYL 250
    YGNYPLCHFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR 300
    AKPPPIPAKK PSSVSLWSLE QPFSIELIEG RKVNADERMK LVVQAGLFHG 350
    NEMLCKTVSS SEVNVCSEPV WKQRLEFDIS VCDLPRMARL CFALYAVVEK 400
    AKKARSTKKK SKKADCPIAW ANLMLFDYKD QLKTGERCLY MWPSVPDEKG 450
    ELLNPAGTVR GNPNTESAAA LVIYLPEVAP HPVYFPALEK ILELGRHGER 500
    GRITEEELQL REILERRGSG ELYEHEKDLV WKMRHEVQEH FPEALARLLL 550
    VTKWNKHEDV AQMLYLLCSW PELPVLSALE LLDFSFPDCY VGSFAIKSLR 600
    KLTDDELFQY LLQLVQVLKY ESYLDCELTK FLLGRALANR KIGHFLFWHL 650
    RSEMHVPSVA LRFGLIMEAY CRGSTHHMKV LMKQGEALSK LKALNDFVKV 700
    SSQKTTKPQT KEMMHMCMRQ ETYMEALSHL QSPLDPSTLL EEVCVEQCTF 750
    MDSKMKPLWI MYSSEEAGSA GNVGIIFKNG DDLRQDMLTL QMIQLMDVLW 800
    KQEGLDLRMT PYGCLPTGDR TGLIEVVLHS DTIANIQLNK SNMAATAAFN 850
    KDALLNWLKS KNPGEALDRA IEEFTLSCAG YCVATYVLGI GDRHSDNIMI 900
    RESGQLFHID FGHFLGNFKT KFGINRERVP FILTYDFVHV IQQGKTNNSE 950
    KFERFRGYCE RAYTILRRHG LLFLHLFALM RAAGLPELSC SKDIQYLKDS 1000
    LALGKTEEEA LKHFRVKFNE ALRESWKTKV NWLAHNVSKD NRQ 1043
    Length:1,043
    Mass (Da):119,712
    Last modified:July 27, 2011 - v2
    Checksum:iAD8DE07D8F847795
    GO
    Isoform 2 (identifier: O35904-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         201-212: ESFTFQVSTKDM → VSPSPIPSPSSI
         213-1043: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:212
    Mass (Da):24,355
    Checksum:iF61391FD8427F323
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti122 – 1221G → A in AAC25676. (PubMed:9235916)Curated
    Sequence conflicti584 – 5841F → S in AAC25676. (PubMed:9235916)Curated
    Sequence conflicti651 – 6511R → H in AAC25676. (PubMed:9235916)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei201 – 21212ESFTF…STKDM → VSPSPIPSPSSI in isoform 2. CuratedVSP_044411Add
    BLAST
    Alternative sequencei213 – 1043831Missing in isoform 2. CuratedVSP_044412Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86587 mRNA. Translation: AAC25676.1.
    AF532989 Genomic DNA. Translation: AAN05615.1.
    AL607078 Genomic DNA. Translation: CAM23914.1.
    CU207384 Genomic DNA. Translation: CAQ51667.1.
    CH466594 Genomic DNA. Translation: EDL14872.1.
    CCDSiCCDS51380.1. [O35904-1]
    PIRiT43502.
    RefSeqiNP_001157524.1. NM_001164052.1. [O35904-1]
    XP_006536078.1. XM_006536015.1. [O35904-1]
    XP_006538715.1. XM_006538652.1. [O35904-1]
    UniGeneiMm.229108.

    Genome annotation databases

    EnsembliENSMUST00000105689; ENSMUSP00000101314; ENSMUSG00000039936. [O35904-1]
    GeneIDi18707.
    KEGGimmu:18707.
    UCSCiuc008vwq.1. mouse. [O35904-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86587 mRNA. Translation: AAC25676.1 .
    AF532989 Genomic DNA. Translation: AAN05615.1 .
    AL607078 Genomic DNA. Translation: CAM23914.1 .
    CU207384 Genomic DNA. Translation: CAQ51667.1 .
    CH466594 Genomic DNA. Translation: EDL14872.1 .
    CCDSi CCDS51380.1. [O35904-1 ]
    PIRi T43502.
    RefSeqi NP_001157524.1. NM_001164052.1. [O35904-1 ]
    XP_006536078.1. XM_006536015.1. [O35904-1 ]
    XP_006538715.1. XM_006538652.1. [O35904-1 ]
    UniGenei Mm.229108.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WXF X-ray 1.90 A 106-1043 [» ]
    2WXG X-ray 2.00 A 106-1043 [» ]
    2WXH X-ray 1.90 A 106-1043 [» ]
    2WXI X-ray 2.80 A 106-1043 [» ]
    2WXJ X-ray 2.60 A 106-1043 [» ]
    2WXK X-ray 2.90 A 106-1043 [» ]
    2WXL X-ray 1.99 A 106-1043 [» ]
    2WXM X-ray 2.80 A 106-1043 [» ]
    2WXN X-ray 2.60 A 106-1043 [» ]
    2WXO X-ray 2.49 A 106-1043 [» ]
    2WXP X-ray 2.30 A 106-1043 [» ]
    2WXQ X-ray 2.70 A 106-1043 [» ]
    2WXR X-ray 2.50 A 106-1043 [» ]
    2X38 X-ray 2.20 A 106-1043 [» ]
    4AJW X-ray 2.80 A/B 110-1043 [» ]
    ProteinModelPortali O35904.
    SMRi O35904. Positions 20-102, 109-1026.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202161. 2 interactions.
    DIPi DIP-39841N.
    IntActi O35904. 6 interactions.

    Chemistry

    ChEMBLi CHEMBL2216745.

    PTM databases

    PhosphoSitei O35904.

    Proteomic databases

    PaxDbi O35904.
    PRIDEi O35904.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000105689 ; ENSMUSP00000101314 ; ENSMUSG00000039936 . [O35904-1 ]
    GeneIDi 18707.
    KEGGi mmu:18707.
    UCSCi uc008vwq.1. mouse. [O35904-1 ]

    Organism-specific databases

    CTDi 5293.
    MGIi MGI:1098211. Pik3cd.

    Phylogenomic databases

    eggNOGi COG5032.
    GeneTreei ENSGT00620000087742.
    HOGENOMi HOG000252911.
    HOVERGENi HBG052721.
    KOi K00922.

    Enzyme and pathway databases

    UniPathwayi UPA00220 .
    BRENDAi 2.7.1.153. 3474.
    Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    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_210793. Interleukin receptor SHC signaling.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    ChiTaRSi PIK3CD. mouse.
    EvolutionaryTracei O35904.
    NextBioi 294773.
    PROi O35904.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35904.
    Bgeei O35904.
    Genevestigatori O35904.

    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. "p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes."
      Chantry D., Vojtek A., Kashishian A., Holtzman D.A., Wood C., Gray P.W., Cooper J.A., Hoekstra M.F.
      J. Biol. Chem. 272:19236-19241(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Spleen.
    2. "Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice."
      Okkenhaug K., Bilancio A., Farjot G., Priddle H., Sancho S., Peskett E., Pearce W., Meek S.E., Salpekar A., Waterfield M.D., Smith A.J., Vanhaesebroeck B.
      Science 297:1031-1034(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
      Strain: 129P2.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. 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].
    5. "A crucial role for the p110delta subunit of phosphatidylinositol 3-kinase in B cell development and activation."
      Clayton E., Bardi G., Bell S.E., Chantry D., Downes C.P., Gray A., Humphries L.A., Rawlings D., Reynolds H., Vigorito E., Turner M.
      J. Exp. Med. 196:753-763(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN B-CELLS, DISRUPTION PHENOTYPE.
    6. "Role of Eras in promoting tumor-like properties in mouse embryonic stem cells."
      Takahashi K., Mitsui K., Yamanaka S.
      Nature 423:541-545(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERAS.
    7. Cited for: FUNCTION IN MAST CELLS, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
    8. "T cell development requires the combined activities of the p110gamma and p110delta catalytic isoforms of phosphatidylinositol 3-kinase."
      Webb L.M.C., Vigorito E., Wymann M.P., Hirsch E., Turner M.
      J. Immunol. 175:2783-2787(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN T-CELL DEVELOPMENT.
    9. "T cell receptor-induced phosphoinositide-3-kinase p110delta activity is required for T cell localization to antigenic tissue in mice."
      Jarmin S.J., David R., Ma L., Chai J.-G., Dewchand H., Takesono A., Ridley A.J., Okkenhaug K., Marelli-Berg F.M.
      J. Clin. Invest. 118:1154-1164(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN T-CELL MIGRATION, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
    10. "The p110 delta of PI3K plays a critical role in NK cell terminal maturation and cytokine/chemokine generation."
      Guo H., Samarakoon A., Vanhaesebroeck B., Malarkannan S.
      J. Exp. Med. 205:2419-2435(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NATURAL KILLER CELLS, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
    11. "p110gamma and p110delta isoforms of phosphoinositide 3-kinase differentially regulate natural killer cell migration in health and disease."
      Saudemont A., Garcon F., Yadi H., Roche-Molina M., Kim N., Segonds-Pichon A., Martin-Fontecha A., Okkenhaug K., Colucci F.
      Proc. Natl. Acad. Sci. U.S.A. 106:5795-5800(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NATURAL KILLER CELL MIGRATION, ENZYME REGULATION.
    12. "p37delta is a new isoform of PI3K p110delta that increases cell proliferation and is overexpressed in tumors."
      Fransson S., Uv A., Eriksson H., Andersson M.K., Wettergren Y., Bergo M., Ejeskar K.
      Oncogene 31:3277-3286(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Peripheral blood leukocyte.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 106-1043 IN A COMPLEX WITH IC87114; PIK-39; SW13; SW14; SW30; DL06; DL07; ZSTK474; AS5; GDC-0941; INK654; INK666 AND AS15.

    Entry informationi

    Entry nameiPK3CD_MOUSE
    AccessioniPrimary (citable) accession number: O35904
    Secondary accession number(s): Q8CJ28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 122 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