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P23727

- P85A_BOVIN

UniProt

P23727 - P85A_BOVIN

Protein

Phosphatidylinositol 3-kinase regulatory subunit alpha

Gene

PIK3R1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling By similarity.By similarity

    GO - Molecular functioni

    1. ErbB-3 class receptor binding Source: UniProtKB
    2. insulin binding Source: Ensembl
    3. insulin-like growth factor receptor binding Source: UniProtKB
    4. insulin receptor binding Source: UniProtKB
    5. insulin receptor substrate binding Source: UniProtKB
    6. phosphatidylinositol 3-kinase binding Source: BHF-UCL
    7. phosphatidylinositol 3-kinase regulator activity Source: UniProtKB
    8. protein binding Source: IntAct
    9. transmembrane receptor protein tyrosine kinase adaptor activity Source: BHF-UCL

    GO - Biological processi

    1. B cell differentiation Source: Ensembl
    2. cellular response to UV Source: Ensembl
    3. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    4. growth hormone receptor signaling pathway Source: Ensembl
    5. insulin-like growth factor receptor signaling pathway Source: UniProtKB
    6. insulin receptor signaling pathway Source: UniProtKB
    7. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    8. negative regulation of apoptotic process Source: Ensembl
    9. negative regulation of cell-matrix adhesion Source: Ensembl
    10. negative regulation of osteoclast differentiation Source: Ensembl
    11. NFAT protein import into nucleus Source: Ensembl
    12. phosphatidylinositol 3-kinase signaling Source: Ensembl
    13. phosphatidylinositol phosphorylation Source: UniProtKB
    14. positive regulation of cell migration Source: Ensembl
    15. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    16. positive regulation of glucose import Source: BHF-UCL
    17. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    18. positive regulation of tumor necrosis factor production Source: Ensembl
    19. protein phosphorylation Source: Ensembl
    20. regulation of phosphatidylinositol 3-kinase activity Source: BHF-UCL

    Enzyme and pathway databases

    ReactomeiREACT_203011. Signaling by constitutively active EGFR.
    REACT_204114. Signaling by SCF-KIT.
    REACT_204467. PI-3K cascade.
    REACT_204566. Tie2 Signaling.
    REACT_205384. G alpha (12/13) signalling events.
    REACT_205423. Downstream TCR signaling.
    REACT_208171. PIP3 activates AKT signaling.
    REACT_209521. G alpha (q) signalling events.
    REACT_209911. PI3K Cascade.
    REACT_211068. GP1b-IX-V activation signalling.
    REACT_211267. Interleukin-3, 5 and GM-CSF signaling.
    REACT_211504. Nephrin interactions.
    REACT_212750. Downstream signal transduction.
    REACT_213843. Costimulation by the CD28 family.
    REACT_214174. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_214988. DAP12 signaling.
    REACT_215783. Role of phospholipids in phagocytosis.
    REACT_215895. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_217559. CD28 dependent PI3K/Akt signaling.
    REACT_218512. Regulation of signaling by CBL.
    REACT_219098. GPVI-mediated activation cascade.
    REACT_219416. PI3K events in ERBB2 signaling.
    REACT_222082. GAB1 signalosome.
    REACT_222492. PI3K events in ERBB4 signaling.
    REACT_223657. Interleukin receptor SHC signaling.
    REACT_224097. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_225332. PI3K/AKT activation.
    REACT_226907. Signaling by FGFR mutants.
    REACT_227241. Signaling by FGFR1 fusion mutants.
    REACT_227888. Synthesis of PIPs at the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 3-kinase regulatory subunit alpha
    Short name:
    PI3-kinase regulatory subunit alpha
    Short name:
    PI3K regulatory subunit alpha
    Short name:
    PtdIns-3-kinase regulatory subunit alpha
    Alternative name(s):
    Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha
    Short name:
    PI3-kinase subunit p85-alpha
    Short name:
    PtdIns-3-kinase regulatory subunit p85-alpha
    Gene namesi
    Name:PIK3R1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 20

    Subcellular locationi

    GO - Cellular componenti

    1. 1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex Source: UniProtKB
    2. membrane Source: Ensembl
    3. phosphatidylinositol 3-kinase complex Source: BHF-UCL

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 724723Phosphatidylinositol 3-kinase regulatory subunit alphaPRO_0000080757Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei467 – 4671PhosphotyrosineBy similarity
    Modified residuei580 – 5801PhosphotyrosineBy similarity
    Modified residuei608 – 6081Phosphoserine1 Publication

    Post-translational modificationi

    Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation.By similarity
    Phosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated in response to KIT and KITLG/SCF. Phosphorylated on tyrosine residues by TEK/TIE2. Phosphorylated by FGR. Phosphorylated by CSF1R. Phosphorylated by ERBB4. Dephosphorylated by PTPRJ By similarity. Phosphorylated by PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF. The relevance of phosphorylation by PIK3CA is however unclear.By similarity1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP23727.

    Interactioni

    Subunit structurei

    Heterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with phosphorylated LAT, LAX1, TRAT1 and LIME1 upon TCR and/or BCR activation. Interacts with CBLB. The SH2 domains interact with the YTHM motif of phosphorylated INSR in vitro. Also interacts with tyrosine-phosphorylated IGF1R in vitro. Interacts with CD28 and CD3Z upon T-cell activation. Interacts with SOCS7. Interacts with IRS1 and phosphorylated IRS4. Interacts with NISCH, RUFY3 and HCST. Interacts with LYN (via SH3 domain); this enhances enzyme activity. Interacts with AXL, FASLG, FER, FGR, HCK, KIT and BCR. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) By similarity. Interacts with PDGFRA (tyrosine phosphorylated). Interacts with ERBB4 (phosphorylated) By similarity. Interacts with NTRK1 (phosphorylated upon ligand-binding). Interacts with PTK2/FAK1 By similarity. Interacts with PDGFRB (tyrosine phosphorylated). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated).By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Inpp5dQ9ES52-12EBI-520244,EBI-1452545From a different organism.
    KHDRBS1Q076662EBI-520244,EBI-1364From a different organism.
    PDGFRBP096196EBI-520244,EBI-641237From a different organism.
    PIK3CAP328714EBI-520244,EBI-1373130
    RAB5AP203395EBI-520244,EBI-399437From a different organism.

    Protein-protein interaction databases

    BioGridi159569. 1 interaction.
    DIPiDIP-34247N.
    IntActiP23727. 15 interactions.
    MINTiMINT-139236.
    STRINGi9913.ENSBTAP00000014594.

    Structurei

    Secondary structure

    1
    724
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Beta strandi29 – 313
    Helixi37 – 393
    Turni50 – 523
    Beta strandi55 – 606
    Turni61 – 644
    Beta strandi65 – 7814
    Beta strandi331 – 3333
    Turni341 – 3444
    Helixi345 – 3495
    Beta strandi354 – 3574
    Turni362 – 3643
    Beta strandi370 – 3789
    Beta strandi386 – 3883
    Beta strandi393 – 3953
    Turni403 – 4053
    Turni408 – 4114
    Helixi413 – 4153
    Turni418 – 4203
    Helixi617 – 6193
    Helixi621 – 6233
    Beta strandi625 – 6284
    Helixi631 – 6388
    Beta strandi645 – 6506
    Beta strandi652 – 6554
    Beta strandi657 – 6637
    Beta strandi666 – 67510
    Beta strandi678 – 6825
    Beta strandi688 – 6903
    Helixi691 – 70010
    Helixi703 – 7053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BFINMR-A614-724[»]
    1BFJNMR-A614-724[»]
    1OO3NMR-A321-431[»]
    1OO4NMR-A321-431[»]
    1PNJNMR-A1-84[»]
    1QADX-ray1.80A614-724[»]
    2PNANMR-A328-431[»]
    2PNBNMR-A328-431[»]
    2PNINMR-A1-84[»]
    ProteinModelPortaliP23727.
    SMRiP23727. Positions 1-84, 115-309, 328-600, 614-724.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23727.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 7977SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini113 – 301189Rho-GAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini333 – 42896SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini624 – 71895SH2 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The SH3 domain mediates the binding to CBLB.By similarity

    Sequence similaritiesi

    Belongs to the PI3K p85 subunit family.Curated
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
    Contains 2 SH2 domains.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiNOG263689.
    GeneTreeiENSGT00390000010431.
    HOGENOMiHOG000008438.
    HOVERGENiHBG082100.
    InParanoidiP23727.
    KOiK02649.
    OMAiLNGYNET.
    OrthoDBiEOG7BP831.
    TreeFamiTF102033.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    3.30.505.10. 2 hits.
    InterProiIPR001720. PI3kinase_P85.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR10155. PTHR10155. 1 hit.
    PfamiPF00620. RhoGAP. 1 hit.
    PF00017. SH2. 2 hits.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    PRINTSiPR00678. PI3KINASEP85.
    PR00401. SH2DOMAIN.
    SMARTiSM00324. RhoGAP. 1 hit.
    SM00252. SH2. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 2 hits.
    PROSITEiPS50238. RHOGAP. 1 hit.
    PS50001. SH2. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23727-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEAKP    50
    EEIGWLNGYN ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG 100
    PSKTEADSEQ QASTLPDLAE QFAPPDVAPP LLIKLVEAIE KKGLECSTLY 150
    RTQSSSNPAE LRQLLDCDTA SLDLEMFDVH VLADAFKRYL LDLPNPVIPV 200
    AVSSELISLA PEVQSSEEYI QLLKKLIRSP SIPHQYWLTL QYLLKHFFKL 250
    SQTSSKNLLN ARVLSELFSP LLFRFPAASS ENTEHLIKII EILISTEWNE 300
    RQPAPALPPK PPKPTTVANN GMNNNMSLQD AEWYWGDISR EEVNEKLRDT 350
    ADGTFLVRDA STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFNS 400
    VVELINHYRN ESLAQYNPKL DVKLLYPVSK YQQDQVVKED NIEAVGKKLH 450
    EYNTQFQEKS REYDRLYEDY TRTSQEIQMK RTAIEAFNET IKIFEEQCQT 500
    QERYSKEYIE KFKREGNETE IQRIMHNYEK LKSRISEIVD SRRRLEEDLK 550
    KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN 600
    ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE 650
    SSKQGCYACS VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH 700
    TSLVQHNDSL NVTLAYPVYA QQRR 724
    Length:724
    Mass (Da):83,497
    Last modified:November 1, 1991 - v1
    Checksum:iEBDF6E754BBF7321
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61745 mRNA. Translation: AAA79511.1.
    PIRiA38749.
    RefSeqiNP_777000.1. NM_174575.1.
    XP_005221493.1. XM_005221436.1.
    UniGeneiBt.109755.

    Genome annotation databases

    EnsembliENSBTAT00000014594; ENSBTAP00000014594; ENSBTAG00000010989.
    GeneIDi282307.
    KEGGibta:282307.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61745 mRNA. Translation: AAA79511.1 .
    PIRi A38749.
    RefSeqi NP_777000.1. NM_174575.1.
    XP_005221493.1. XM_005221436.1.
    UniGenei Bt.109755.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BFI NMR - A 614-724 [» ]
    1BFJ NMR - A 614-724 [» ]
    1OO3 NMR - A 321-431 [» ]
    1OO4 NMR - A 321-431 [» ]
    1PNJ NMR - A 1-84 [» ]
    1QAD X-ray 1.80 A 614-724 [» ]
    2PNA NMR - A 328-431 [» ]
    2PNB NMR - A 328-431 [» ]
    2PNI NMR - A 1-84 [» ]
    ProteinModelPortali P23727.
    SMRi P23727. Positions 1-84, 115-309, 328-600, 614-724.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 159569. 1 interaction.
    DIPi DIP-34247N.
    IntActi P23727. 15 interactions.
    MINTi MINT-139236.
    STRINGi 9913.ENSBTAP00000014594.

    Proteomic databases

    PRIDEi P23727.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000014594 ; ENSBTAP00000014594 ; ENSBTAG00000010989 .
    GeneIDi 282307.
    KEGGi bta:282307.

    Organism-specific databases

    CTDi 5295.

    Phylogenomic databases

    eggNOGi NOG263689.
    GeneTreei ENSGT00390000010431.
    HOGENOMi HOG000008438.
    HOVERGENi HBG082100.
    InParanoidi P23727.
    KOi K02649.
    OMAi LNGYNET.
    OrthoDBi EOG7BP831.
    TreeFami TF102033.

    Enzyme and pathway databases

    Reactomei REACT_203011. Signaling by constitutively active EGFR.
    REACT_204114. Signaling by SCF-KIT.
    REACT_204467. PI-3K cascade.
    REACT_204566. Tie2 Signaling.
    REACT_205384. G alpha (12/13) signalling events.
    REACT_205423. Downstream TCR signaling.
    REACT_208171. PIP3 activates AKT signaling.
    REACT_209521. G alpha (q) signalling events.
    REACT_209911. PI3K Cascade.
    REACT_211068. GP1b-IX-V activation signalling.
    REACT_211267. Interleukin-3, 5 and GM-CSF signaling.
    REACT_211504. Nephrin interactions.
    REACT_212750. Downstream signal transduction.
    REACT_213843. Costimulation by the CD28 family.
    REACT_214174. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_214988. DAP12 signaling.
    REACT_215783. Role of phospholipids in phagocytosis.
    REACT_215895. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_217559. CD28 dependent PI3K/Akt signaling.
    REACT_218512. Regulation of signaling by CBL.
    REACT_219098. GPVI-mediated activation cascade.
    REACT_219416. PI3K events in ERBB2 signaling.
    REACT_222082. GAB1 signalosome.
    REACT_222492. PI3K events in ERBB4 signaling.
    REACT_223657. Interleukin receptor SHC signaling.
    REACT_224097. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_225332. PI3K/AKT activation.
    REACT_226907. Signaling by FGFR mutants.
    REACT_227241. Signaling by FGFR1 fusion mutants.
    REACT_227888. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    EvolutionaryTracei P23727.
    NextBioi 20806106.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    3.30.505.10. 2 hits.
    InterProi IPR001720. PI3kinase_P85.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR10155. PTHR10155. 1 hit.
    Pfami PF00620. RhoGAP. 1 hit.
    PF00017. SH2. 2 hits.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00678. PI3KINASEP85.
    PR00401. SH2DOMAIN.
    SMARTi SM00324. RhoGAP. 1 hit.
    SM00252. SH2. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 2 hits.
    PROSITEi PS50238. RHOGAP. 1 hit.
    PS50001. SH2. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase."
      Otsu M., Hiles I.D., Goot I., Fry M.J., Ruiz-Larrea F., Panayotou G., Thompson A., Dhand R., Hsuan J., Totty N., Smith A.D., Morgan S.J., Courtneidge S.A., Parker P.J., Waterfield M.D.
      Cell 65:91-104(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes."
      Panayotou G., Bax B., Gout I., Federwisch M., Wroblowski B., Dhand R., Fry M.J., Blundell T.L., Wollmer A., Waterfield M.D.
      EMBO J. 11:4261-4272(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CIRCULAR DICHROISM ANALYSIS, FLUORESCENCE SPECTROSCOPY.
    3. "GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit."
      Kazlauskas A., Kashishian A., Cooper J.A., Valius M.
      Mol. Cell. Biol. 12:2534-2544(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB.
    4. "Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase."
      Booker G.W., Gout I., Downing A.K., Driscoll P.C., Boyd J., Waterfield M.D., Campbell I.D.
      Cell 73:813-822(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-84.
    5. "Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase."
      Booker G.W., Breeze A.L., Downing A.K., Panayotou G., Gout I., Waterfield M.D., Campbell I.D.
      Nature 358:684-687(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 314-431.
    6. "NMR analysis of interactions of a phosphatidylinositol 3'-kinase SH2 domain with phosphotyrosine peptides reveals interdependence of major binding sites."
      Guenther U.L., Liu Y., Sanford D., Bachovchin W.W., Schaffhausen B.
      Biochemistry 35:15570-15581(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 321-434.
    7. "Solution structure of the C-terminal SH2 domain of the p85 alpha regulatory subunit of phosphoinositide 3-kinase."
      Siegal G., Davis B., Kristensen S.M., Sankar A., Linacre J., Stein R.C., Panayotou G., Waterfield M.D., Driscoll P.C.
      J. Mol. Biol. 276:461-478(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 614-724.
    8. "Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo."
      Foukas L.C., Beeton C.A., Jensen J., Phillips W.A., Shepherd P.R.
      Mol. Cell. Biol. 24:966-975(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-608.

    Entry informationi

    Entry nameiP85A_BOVIN
    AccessioniPrimary (citable) accession number: P23727
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 145 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3