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P23727

- P85A_BOVIN

UniProt

P23727 - P85A_BOVIN

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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

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. 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
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_201946. Interleukin-7 signaling.
REACT_202218. G beta:gamma signalling through PI3Kgamma.
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.
REACT_246299. VEGFA-VEGFR2 Pathway.

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. cell-cell junction Source: Ensembl
  2. membrane Source: Ensembl
  3. phosphatidylinositol 3-kinase complex Source: BHF-UCL
  4. phosphatidylinositol 3-kinase complex, class IA Source: UniProtKB
Complete GO annotation...

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 – 104Combined sources
Beta strandi29 – 313Combined sources
Helixi37 – 393Combined sources
Turni50 – 523Combined sources
Beta strandi55 – 606Combined sources
Turni61 – 644Combined sources
Beta strandi65 – 7814Combined sources
Beta strandi331 – 3333Combined sources
Turni341 – 3444Combined sources
Helixi345 – 3495Combined sources
Beta strandi354 – 3574Combined sources
Turni362 – 3643Combined sources
Beta strandi370 – 3789Combined sources
Beta strandi386 – 3883Combined sources
Beta strandi393 – 3953Combined sources
Turni403 – 4053Combined sources
Turni408 – 4114Combined sources
Helixi413 – 4153Combined sources
Turni418 – 4203Combined sources
Helixi617 – 6193Combined sources
Helixi621 – 6233Combined sources
Beta strandi625 – 6284Combined sources
Helixi631 – 6388Combined sources
Beta strandi645 – 6506Combined sources
Beta strandi652 – 6554Combined sources
Beta strandi657 – 6637Combined sources
Beta strandi666 – 67510Combined sources
Beta strandi678 – 6825Combined sources
Beta strandi688 – 6903Combined sources
Helixi691 – 70010Combined sources
Helixi703 – 7053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEAKP
60 70 80 90 100
EEIGWLNGYN ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG
110 120 130 140 150
PSKTEADSEQ QASTLPDLAE QFAPPDVAPP LLIKLVEAIE KKGLECSTLY
160 170 180 190 200
RTQSSSNPAE LRQLLDCDTA SLDLEMFDVH VLADAFKRYL LDLPNPVIPV
210 220 230 240 250
AVSSELISLA PEVQSSEEYI QLLKKLIRSP SIPHQYWLTL QYLLKHFFKL
260 270 280 290 300
SQTSSKNLLN ARVLSELFSP LLFRFPAASS ENTEHLIKII EILISTEWNE
310 320 330 340 350
RQPAPALPPK PPKPTTVANN GMNNNMSLQD AEWYWGDISR EEVNEKLRDT
360 370 380 390 400
ADGTFLVRDA STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFNS
410 420 430 440 450
VVELINHYRN ESLAQYNPKL DVKLLYPVSK YQQDQVVKED NIEAVGKKLH
460 470 480 490 500
EYNTQFQEKS REYDRLYEDY TRTSQEIQMK RTAIEAFNET IKIFEEQCQT
510 520 530 540 550
QERYSKEYIE KFKREGNETE IQRIMHNYEK LKSRISEIVD SRRRLEEDLK
560 570 580 590 600
KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN
610 620 630 640 650
ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE
660 670 680 690 700
SSKQGCYACS VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH
710 720
TSLVQHNDSL NVTLAYPVYA QQRR
Length:724
Mass (Da):83,497
Last modified:November 1, 1991 - v1
Checksum:iEBDF6E754BBF7321
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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_201946. Interleukin-7 signaling.
REACT_202218. G beta:gamma signalling through PI3Kgamma.
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.
REACT_246299. VEGFA-VEGFR2 Pathway.

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: November 26, 2014
This is version 147 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