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Q61194

- P3C2A_MOUSE

UniProt

Q61194 - P3C2A_MOUSE

Protein

Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha

Gene

Pik3c2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function.3 Publications

    Catalytic activityi

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

    Cofactori

    Calcium or magnesium. Manganese cannot be used By similarity.By similarity

    Enzyme regulationi

    Activated by clathrin By similarity. Only slightly inhibited by wortmannin and LY294002. Activated by insulin.By similarity2 Publications

    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. phosphatidylinositol binding Source: InterPro

    GO - Biological processi

    1. endocytosis Source: UniProtKB
    2. exocytosis Source: UniProtKB-KW
    3. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
    4. phosphatidylinositol-mediated signaling Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Endocytosis, Exocytosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.154. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (EC:2.7.1.154)
    Short name:
    PI3K-C2-alpha
    Short name:
    PtdIns-3-kinase C2 subunit alpha
    Alternative name(s):
    Cpk-m
    Phosphoinositide 3-kinase-C2-alpha
    p170
    Gene namesi
    Name:Pik3c2a
    Synonyms:Cpk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1203729. Pik3c2a.

    Subcellular locationi

    Cell membrane. Golgi apparatus. Cytoplasmic vesicleclathrin-coated vesicle. Nucleus. Cytoplasm By similarity
    Note: Has a preference for membranes containing PtdIns(4,5)P2 or PtdIns(3,4)P2.

    GO - Cellular componenti

    1. clathrin-coated vesicle Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. Golgi apparatus Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB-SubCell
    5. phosphatidylinositol 3-kinase complex Source: RefGenome
    6. plasma membrane Source: UniProtKB
    7. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Chronic renal failure and kidney lesions. Affects podocyte morphology and function.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 16861685Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alphaPRO_0000088796Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei60 – 601PhosphoserineBy similarity
    Modified residuei261 – 2611PhosphoserineBy similarity
    Modified residuei328 – 3281PhosphoserineBy similarity
    Modified residuei339 – 3391PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on Ser-261 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation By similarity. Phosphorylated upon insulin stimulation; which may lead to enzyme activation.By similarity1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ61194.
    PaxDbiQ61194.
    PRIDEiQ61194.

    PTM databases

    PhosphoSiteiQ61194.

    Expressioni

    Tissue specificityi

    Detected in podocytes.1 Publication

    Gene expression databases

    GenevestigatoriQ61194.

    Interactioni

    Subunit structurei

    Interacts with ERBB2 and EGFR. Interacts with clathrin trimers By similarity.By similarity

    Protein-protein interaction databases

    BioGridi202158. 4 interactions.
    IntActiQ61194. 1 interaction.

    Structurei

    Secondary structure

    1
    1686
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1562 – 15709
    Beta strandi1573 – 158210
    Beta strandi1594 – 16029
    Beta strandi1604 – 16063
    Beta strandi1622 – 163110
    Helixi1634 – 16374
    Beta strandi1641 – 16488
    Beta strandi1651 – 16533
    Beta strandi1656 – 16649
    Helixi1665 – 16673
    Beta strandi1674 – 16796

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B3RX-ray2.30A/B1561-1686[»]
    ProteinModelPortaliQ61194.
    SMRiQ61194. Positions 680-1391, 1421-1532, 1561-1682.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61194.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini422 – 51089PI3K-RBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini682 – 841160C2 PI3K-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini861 – 1037177PIK helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini1133 – 1395263PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST
    Domaini1420 – 1536117PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini1557 – 1660104C2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 142141Interaction with clathrin; sufficient to induce clathrin assembyBy similarityAdd
    BLAST
    Regioni1488 – 14936Interaction with PtdIns(4,5)P2-containing membranesBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1606 – 161712Nuclear localization signalBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 C2 PI3K-type 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
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5032.
    HOGENOMiHOG000006920.
    HOVERGENiHBG082099.
    KOiK00923.
    PhylomeDBiQ61194.

    Family and domain databases

    Gene3Di1.10.1070.11. 1 hit.
    1.25.40.70. 1 hit.
    2.60.40.150. 2 hits.
    3.30.1520.10. 1 hit.
    InterProiIPR016024. ARM-type_fold.
    IPR000008. C2_dom.
    IPR011009. Kinase-like_dom.
    IPR001683. Phox.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    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.
    PfamiPF00168. C2. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    PF00792. PI3K_C2. 1 hit.
    PF00794. PI3K_rbd. 1 hit.
    PF00613. PI3Ka. 1 hit.
    PF00787. PX. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    SM00142. PI3K_C2. 1 hit.
    SM00144. PI3K_rbd. 1 hit.
    SM00145. PI3Ka. 1 hit.
    SM00146. PI3Kc. 1 hit.
    SM00312. PX. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    SSF49562. SSF49562. 2 hits.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    PS51547. PI3K_C2. 1 hit.
    PS51546. PI3K_RBD. 1 hit.
    PS51545. PIK_HELICAL. 1 hit.
    PS50195. PX. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q61194-1) [UniParc]FASTAAdd to Basket

    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

    MAQISNNSEF KQCSSSHPEP IRTKDVNKAE ALQMEAEALA KLQKDRQMTD     50
    SPRGFELSSS TRQRTQGFNK QDYDLMVFPE LDSQKRAVDI DVEKLTQAEL 100
    EKILLDDNFE TRKPPALPVT PVLSPSFSTQ LYLRPSGQRG QWPPGLCGPS 150
    TYTLPSTYPS AYSKQATFQN GFSPRMPTFP STESVYLRLP GQSPYFSYPL 200
    TPATPFHPQG SLPVYRPLVS PDMAKLFEKI ASTSEFLKNG KARTDLEIAN 250
    SKASVCNLQI SPKSEDINKF DWLDLDPLSK PKVDYVEVLE HEEEKKDPVL 300
    LAEDPWDAVL LEERSPSCHL ERKVNGKSLS GATVTRSQSL IIRTAQFTKA 350
    QGQVSQKDPN GTSSLPTGSS LLQEFEVQND EVAAFCQSIM KLKTKFPYTD 400
    HCTNPGYLLS PVTVQRNMCG ENASVKVSIE IEGLQLPVTF TCDVSSTVEI 450
    IIMQALCWVH DDLNQVDVGS YILKVCGQEE VLQNNHCLGS HEHIQNCRKW 500
    DTEIKLQLLT LSAMCQNLAR TAEDDEAPVD LNKYLYQIEK PYKEVMTRHP 550
    VEELLDSYHY QVELALQTEN QHRAVDQVIK AVRKICSALD GVETPSVTEA 600
    VKKLKRAVNL PRNKSADVTS LSGSDTRKNS TKGSLNPENP VQVSMDHLTT 650
    AIYDLLRLHA NSSRCSTACP RGSRNIKEAW TATEQLQFTV YAAHGISSNW 700
    VSNYEKYYLI CSLSHNGKDL FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ 750
    ISQLPLESVL HLTLFGVLNQ SSGSSPDSNK QRKGPEALGK VSLTLFDFKR 800
    FLTCGTKLLY LWTSSHTNSI PGAIPKKSYV MERIVLQVDF PSPAFDIIYT 850
    SPQIDRNIIQ QDKLETLESD IKGKLLDIIH RDSSFGLSKE DKVFLWENRY 900
    YCLKHPNCLP KILASAPNWK WANLAKTYSL LHQWPPLCPL AALELLDAKF 950
    ADQEVRSLAV SWMEAISDDE LADLLPQFVQ ALKYEIYLNS SLVRFLLSRA 1000
    LGNIQIAHSL YWLLKDALHD THFGSRYEHV LGALLSVGGK GLREELSKQM 1050
    KLVQLLGGVA EKVRQASGST RQVVLQKSME RVQSFFLRNK CRLPLKPSLV 1100
    AKELNIKSCS FFSSNAMPLK VTMVNADPLG EEINVMFKVG EDLRQDMLAL 1150
    QMIKIMDKIW LKEGLDLRMV IFRCLSTGRD RGMVELVPAS DTLRKIQVEY 1200
    GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD 1250
    RHNDNIMLRS TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN 1300
    GGEKPTIRFQ LFVDLCCQAY NLIRKQTNLF LNLLSLMIPS GLPELTSIQD 1350
    LKYVRDALQP QTTDAEATIF FTRLIESSLG SIATKFNFFI HNLAQLRFSG 1400
    LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK HYIYVVRILR 1450
    EGHLEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA 1500
    AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSAGAV 1550
    PFSPTLGQIG GAVKLSVSYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL 1600
    LPDTHKTSKR KTKISRKTRN PTFNEMLVYS GYSKETLRQR ELQLSVLSAE 1650
    SLRENFFLGG ITLPLKDFNL SKETVKWYQL TAATYL 1686
    Length:1,686
    Mass (Da):190,758
    Last modified:August 30, 2005 - v2
    Checksum:iE390BA7D730F4F87
    GO
    Isoform 2 (identifier: Q61194-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         276-303: Missing.

    Show »
    Length:1,658
    Mass (Da):187,526
    Checksum:i4D18EBC1DDC2A57D
    GO

    Sequence cautioni

    The sequence AAB07682.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401G → V in AK049609. (PubMed:16141072)Curated
    Sequence conflicti668 – 6681A → G in AAC52604. (PubMed:8662856)Curated
    Sequence conflicti954 – 9541E → G in AAC52604. (PubMed:8662856)Curated
    Sequence conflicti1206 – 12083FKD → LR(PubMed:8663140)Curated
    Sequence conflicti1211 – 12122LA → TS(PubMed:8663140)Curated
    Sequence conflicti1218 – 12181Y → N in AAB07682. (PubMed:8663140)Curated
    Sequence conflicti1325 – 13262KQ → T in AAB07682. (PubMed:8663140)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei276 – 30328Missing in isoform 2. 1 PublicationVSP_015254Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U52193 mRNA. Translation: AAC52604.1.
    AK049609 mRNA. No translation available.
    U55772 mRNA. Translation: AAB07682.1. Different initiation.
    CCDSiCCDS52371.1. [Q61194-1]
    PIRiT42642.
    RefSeqiNP_035213.2. NM_011083.2.
    UniGeneiMm.3810.

    Genome annotation databases

    GeneIDi18704.
    KEGGimmu:18704.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U52193 mRNA. Translation: AAC52604.1 .
    AK049609 mRNA. No translation available.
    U55772 mRNA. Translation: AAB07682.1 . Different initiation.
    CCDSi CCDS52371.1. [Q61194-1 ]
    PIRi T42642.
    RefSeqi NP_035213.2. NM_011083.2.
    UniGenei Mm.3810.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B3R X-ray 2.30 A/B 1561-1686 [» ]
    ProteinModelPortali Q61194.
    SMRi Q61194. Positions 680-1391, 1421-1532, 1561-1682.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202158. 4 interactions.
    IntActi Q61194. 1 interaction.

    PTM databases

    PhosphoSitei Q61194.

    Proteomic databases

    MaxQBi Q61194.
    PaxDbi Q61194.
    PRIDEi Q61194.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 18704.
    KEGGi mmu:18704.

    Organism-specific databases

    CTDi 5286.
    MGIi MGI:1203729. Pik3c2a.

    Phylogenomic databases

    eggNOGi COG5032.
    HOGENOMi HOG000006920.
    HOVERGENi HBG082099.
    KOi K00923.
    PhylomeDBi Q61194.

    Enzyme and pathway databases

    BRENDAi 2.7.1.154. 3474.

    Miscellaneous databases

    ChiTaRSi PIK3C2A. mouse.
    EvolutionaryTracei Q61194.
    NextBioi 294759.
    PROi Q61194.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q61194.

    Family and domain databases

    Gene3Di 1.10.1070.11. 1 hit.
    1.25.40.70. 1 hit.
    2.60.40.150. 2 hits.
    3.30.1520.10. 1 hit.
    InterProi IPR016024. ARM-type_fold.
    IPR000008. C2_dom.
    IPR011009. Kinase-like_dom.
    IPR001683. Phox.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    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 PF00168. C2. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    PF00792. PI3K_C2. 1 hit.
    PF00794. PI3K_rbd. 1 hit.
    PF00613. PI3Ka. 1 hit.
    PF00787. PX. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 1 hit.
    SM00142. PI3K_C2. 1 hit.
    SM00144. PI3K_rbd. 1 hit.
    SM00145. PI3Ka. 1 hit.
    SM00146. PI3Kc. 1 hit.
    SM00312. PX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    SSF49562. SSF49562. 2 hits.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    PS51547. PI3K_C2. 1 hit.
    PS51546. PI3K_RBD. 1 hit.
    PS51545. PIK_HELICAL. 1 hit.
    PS50195. PX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cpk is a novel class of Drosophila PtdIns 3-kinase containing a C2 domain."
      Molz L., Chen Y.-W., Hirano M., Williams L.T.
      J. Biol. Chem. 271:13892-13899(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: BALB/c.
    2. "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] OF 1-356 (ISOFORM 1).
      Tissue: Embryonic spinal cord.
    3. "Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain."
      Virbasius J.V., Guilherme A., Czech M.P.
      J. Biol. Chem. 271:13304-13307(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-1686 (ISOFORM 1), FUNCTION, ENZYME REGULATION.
      Tissue: Adipocyte.
    4. "Insulin activates the alpha isoform of class II phosphoinositide 3-kinase."
      Brown R.A., Domin J., Arcaro A., Waterfield M.D., Shepherd P.R.
      J. Biol. Chem. 274:14529-14532(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION.
    5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    6. "Insulin-feedback via PI3K-C2alpha activated PKBalpha/Akt1 is required for glucose-stimulated insulin secretion."
      Leibiger B., Moede T., Uhles S., Barker C.J., Creveaux M., Domin J., Berggren P.-O., Leibiger I.B.
      FASEB J. 24:1824-1837(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ISULIN SECRETION.
    7. "Requirement for class II phosphoinositide 3-kinase C2alpha in maintenance of glomerular structure and function."
      Harris D.P., Vogel P., Wims M., Moberg K., Humphries J., Jhaver K.G., DaCosta C.M., Shadoan M.K., Xu N., Hansen G.M., Balakrishnan S., Domin J., Powell D.R., Oravecz T.
      Mol. Cell. Biol. 31:63-80(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN KIDNEY, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    8. "Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2alpha."
      Liu L., Song X., He D., Komma C., Kita A., Virbasius J.V., Huang G., Bellamy H.D., Miki K., Czech M.P., Zhou G.W.
      J. Biol. Chem. 281:4254-4260(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1561-1686, INTERACTION WITH PHOSPHATIDYLINOSITIDE-CONTAINING MEMBRANES.

    Entry informationi

    Entry nameiP3C2A_MOUSE
    AccessioniPrimary (citable) accession number: Q61194
    Secondary accession number(s): Q61182
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 127 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3