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Protein

Phosphatidylinositol 3-kinase regulatory subunit alpha

Gene

Pik3r1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed:20348926).By similarity1 Publication

GO - Molecular functioni

  • 1-phosphatidylinositol-3-kinase activity Source: MGI
  • ErbB-3 class receptor binding Source: UniProtKB
  • insulin binding Source: MGI
  • insulin-like growth factor receptor binding Source: UniProtKB
  • insulin receptor binding Source: UniProtKB
  • insulin receptor substrate binding Source: UniProtKB
  • neurotrophin TRKA receptor binding Source: MGI
  • phosphatidylinositol 3-kinase regulator activity Source: UniProtKB
  • phosphatidylinositol 3-kinase regulatory subunit binding Source: ParkinsonsUK-UCL
  • protein heterodimerization activity Source: ParkinsonsUK-UCL
  • protein phosphatase binding Source: MGI
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • B cell differentiation Source: MGI
  • cellular glucose homeostasis Source: UniProtKB
  • cellular response to insulin stimulus Source: UniProtKB
  • cellular response to UV Source: MGI
  • extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • growth hormone receptor signaling pathway Source: MGI
  • insulin-like growth factor receptor signaling pathway Source: UniProtKB
  • insulin receptor signaling pathway Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cell adhesion Source: MGI
  • negative regulation of cell-matrix adhesion Source: MGI
  • negative regulation of osteoclast differentiation Source: MGI
  • NFAT protein import into nucleus Source: MGI
  • phosphatidylinositol 3-kinase signaling Source: MGI
  • phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  • phosphatidylinositol phosphorylation Source: UniProtKB
  • positive regulation of cell migration Source: MGI
  • positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
  • positive regulation of glucose import in response to insulin stimulus Source: AgBase
  • positive regulation of RNA splicing Source: UniProtKB
  • positive regulation of transcription factor import into nucleus Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of tumor necrosis factor production Source: MGI
  • protein phosphorylation Source: MGI
  • protein stabilization Source: UniProtKB
  • regulation of establishment of protein localization to plasma membrane Source: MGI
  • regulation of phosphatidylinositol 3-kinase activity Source: GOC
  • regulation of stress fiber assembly Source: MGI
  • response to endoplasmic reticulum stress Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Stress response, Transport

Enzyme and pathway databases

ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1250342. PI3K events in ERBB4 signaling.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1660499. Synthesis of PIPs at the plasma membrane.
R-MMU-180292. GAB1 signalosome.
R-MMU-186763. Downstream signal transduction.
R-MMU-1963642. PI3K events in ERBB2 signaling.
R-MMU-198203. PI3K/AKT activation.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2029485. Role of phospholipids in phagocytosis.
R-MMU-210993. Tie2 Signaling.
R-MMU-2424491. DAP12 signaling.
R-MMU-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-MMU-388841. Costimulation by the CD28 family.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-392451. G beta:gamma signalling through PI3Kgamma.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-430116. GP1b-IX-V activation signalling.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654695. PI-3K cascade:FGFR2.
R-MMU-5654710. PI-3K cascade:FGFR3.
R-MMU-5654720. PI-3K cascade:FGFR4.
R-MMU-912526. Interleukin receptor SHC signaling.
R-MMU-912631. Regulation of signaling by CBL.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:97583. Pik3r1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: MGI
  • cis-Golgi network Source: MGI
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear endoplasmic reticulum membrane Source: MGI
  • phosphatidylinositol 3-kinase complex Source: MGI
  • phosphatidylinositol 3-kinase complex, class IA Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 724723Phosphatidylinositol 3-kinase regulatory subunit alphaPRO_0000080759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei467 – 4671PhosphotyrosineCombined sources
Modified residuei580 – 5801PhosphotyrosineCombined sources
Modified residuei608 – 6081PhosphoserineBy similarity

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.1 Publication
Phosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. Dephosphorylated by PTPRJ. Phosphorylated by PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF. The relevance of phosphorylation by PIK3CA is however unclear. Phosphorylated in response to KIT and KITLG/SCF. Phosphorylated by FGR (By similarity). Phosphorylated by CSF1R. Phosphorylated by ERBB4. Phosphorylated on tyrosine residues by TEK/TIE2.By similarity4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP26450.
MaxQBiP26450.
PaxDbiP26450.
PRIDEiP26450.

PTM databases

iPTMnetiP26450.
PhosphoSiteiP26450.
SwissPalmiP26450.

Expressioni

Gene expression databases

BgeeiP26450.
ExpressionAtlasiP26450. baseline and differential.
GenevisibleiP26450. MM.

Interactioni

Subunit structurei

Interacts with XBP1 isoform 2; the interaction is direct and induces translocation of XBP1 isoform 2 into the nucleus in a ER stress- and/or insulin-dependent but PI3K-independent manner (PubMed:20348926). Interacts with PIK3R2; the interaction is dissociated in an insulin-dependent manner (PubMed:20348926). Heterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with phosphorylated LAT, LAX1 and TRAT1 upon TCR activation. The SH2 domains interact with the YTHM motif of phosphorylated INSR in vitro. Also interacts with tyrosine-phosphorylated IGF1R in vitro. Interacts with IRS1 and phosphorylated IRS4. Interacts with NISCH and RUFY3 (By similarity). Interacts with phosphorylated TOM1L1. Interacts with phosphorylated LIME1 upon TCR or BCR activation. Interacts with CBLB. Interacts with CD28 and CD3Z upon T-cell activation. Interacts with SOCS7 and HCST. Interacts with AXL, FASLG, FGR, HCK, KIT and BCR. Interacts with PTK2/FAK1 (By similarity). Interacts with PDGFRB (tyrosine phosphorylated) (By similarity). Interacts with NTRK1 (phosphorylated upon ligand-binding) (By similarity). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (PubMed:9312046). Interacts with FER. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated) (Probable). Interacts with PDGFRA (tyrosine phosphorylated). Interacts with LYN (via SH3 domain); this enhances enzyme activity. Interacts with ERBB4. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Interacts with FAM83B; activates the PI3K/AKT signaling cascade (By similarity).By similarityCurated17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP03EBI-641764,EBI-375446From a different organism.
Brd7O8866511EBI-641764,EBI-643930
Eif4g2Q624483EBI-641764,EBI-296494
Irs1P355692EBI-641764,EBI-400825
Pik3caP423376EBI-641764,EBI-641748
Pik3cbQ8BTI94EBI-641764,EBI-644672
Pik3cdO35904-22EBI-641764,EBI-6470774
Wasf1Q8R5H62EBI-641764,EBI-774719

GO - Molecular functioni

  • ErbB-3 class receptor binding Source: UniProtKB
  • insulin binding Source: MGI
  • insulin-like growth factor receptor binding Source: UniProtKB
  • insulin receptor binding Source: UniProtKB
  • insulin receptor substrate binding Source: UniProtKB
  • neurotrophin TRKA receptor binding Source: MGI
  • phosphatidylinositol 3-kinase regulatory subunit binding Source: ParkinsonsUK-UCL
  • protein heterodimerization activity Source: ParkinsonsUK-UCL
  • protein phosphatase binding Source: MGI
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi202162. 37 interactions.
DIPiDIP-39593N.
IntActiP26450. 37 interactions.
MINTiMINT-103410.
STRINGi10090.ENSMUSP00000056774.

Structurei

3D structure databases

ProteinModelPortaliP26450.
SMRiP26450. Positions 4-80, 115-309, 322-724.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG4637. Eukaryota.
ENOG410XP6R. LUCA.
GeneTreeiENSGT00390000010431.
HOGENOMiHOG000008438.
HOVERGENiHBG082100.
InParanoidiP26450.
KOiK02649.
OMAiPMLFRFS.
OrthoDBiEOG7BP831.
TreeFamiTF102033.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR032498. PI3K_P85_iSH2.
IPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10155. PTHR10155. 1 hit.
PfamiPF16454. PI3K_P85_iSH2. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PRINTSiPR00401. 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.

P26450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEARP
60 70 80 90 100
EDIGWLNGYN ETTGERGDFP GTYVEYIGRK RISPPTPKPR PPRPLPVAPG
110 120 130 140 150
SSKTEADTEQ QALPLPDLAE QFAPPDVAPP LLIKLLEAIE KKGLECSTLY
160 170 180 190 200
RTQSSSNPAE LRQLLDCDAA SVDLEMIDVH VLADAFKRYL ADLPNPVIPV
210 220 230 240 250
AVYNEMMSLA QELQSPEDCI QLLKKLIRLP NIPHQCWLTL QYLLKHFFKL
260 270 280 290 300
SQASSKNLLN ARVLSEIFSP VLFRFPAASS DNTEHLIKAI EILISTEWNE
310 320 330 340 350
RQPAPALPPK PPKPTTVANN SMNNNMSLQD 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 REYDRLYEEY TRTSQEIQMK RTAIEAFNET IKIFEEQCQT
510 520 530 540 550
QERYSKEYIE KFKREGNEKE IQRIMHNHDK LKSRISEIID 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):83,517
Last modified:July 27, 2011 - v2
Checksum:i9975D7AD8BABBA9C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461Q → P in AAA39886 (PubMed:1849460).Curated
Sequence conflicti510 – 5101E → G in AAA39886 (PubMed:1849460).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60651 mRNA. Translation: AAA39886.1.
CH466567 Genomic DNA. Translation: EDL00772.1.
BC026146 mRNA. Translation: AAH26146.1.
CCDSiCCDS36769.1.
RefSeqiNP_001070963.1. NM_001077495.2.
UniGeneiMm.259333.

Genome annotation databases

EnsembliENSMUST00000055518; ENSMUSP00000056774; ENSMUSG00000041417.
GeneIDi18708.
KEGGimmu:18708.
UCSCiuc007rrt.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60651 mRNA. Translation: AAA39886.1.
CH466567 Genomic DNA. Translation: EDL00772.1.
BC026146 mRNA. Translation: AAH26146.1.
CCDSiCCDS36769.1.
RefSeqiNP_001070963.1. NM_001077495.2.
UniGeneiMm.259333.

3D structure databases

ProteinModelPortaliP26450.
SMRiP26450. Positions 4-80, 115-309, 322-724.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202162. 37 interactions.
DIPiDIP-39593N.
IntActiP26450. 37 interactions.
MINTiMINT-103410.
STRINGi10090.ENSMUSP00000056774.

PTM databases

iPTMnetiP26450.
PhosphoSiteiP26450.
SwissPalmiP26450.

Proteomic databases

EPDiP26450.
MaxQBiP26450.
PaxDbiP26450.
PRIDEiP26450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055518; ENSMUSP00000056774; ENSMUSG00000041417.
GeneIDi18708.
KEGGimmu:18708.
UCSCiuc007rrt.3. mouse.

Organism-specific databases

CTDi5295.
MGIiMGI:97583. Pik3r1.

Phylogenomic databases

eggNOGiKOG4637. Eukaryota.
ENOG410XP6R. LUCA.
GeneTreeiENSGT00390000010431.
HOGENOMiHOG000008438.
HOVERGENiHBG082100.
InParanoidiP26450.
KOiK02649.
OMAiPMLFRFS.
OrthoDBiEOG7BP831.
TreeFamiTF102033.

Enzyme and pathway databases

ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1250342. PI3K events in ERBB4 signaling.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1660499. Synthesis of PIPs at the plasma membrane.
R-MMU-180292. GAB1 signalosome.
R-MMU-186763. Downstream signal transduction.
R-MMU-1963642. PI3K events in ERBB2 signaling.
R-MMU-198203. PI3K/AKT activation.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2029485. Role of phospholipids in phagocytosis.
R-MMU-210993. Tie2 Signaling.
R-MMU-2424491. DAP12 signaling.
R-MMU-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-MMU-388841. Costimulation by the CD28 family.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-392451. G beta:gamma signalling through PI3Kgamma.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-430116. GP1b-IX-V activation signalling.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654695. PI-3K cascade:FGFR2.
R-MMU-5654710. PI-3K cascade:FGFR3.
R-MMU-5654720. PI-3K cascade:FGFR4.
R-MMU-912526. Interleukin receptor SHC signaling.
R-MMU-912631. Regulation of signaling by CBL.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

ChiTaRSiPik3r1. mouse.
NextBioi294779.
PROiP26450.
SOURCEiSearch...

Gene expression databases

BgeeiP26450.
ExpressionAtlasiP26450. baseline and differential.
GenevisibleiP26450. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR032498. PI3K_P85_iSH2.
IPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10155. PTHR10155. 1 hit.
PfamiPF16454. PI3K_P85_iSH2. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PRINTSiPR00401. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of a novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF beta-receptor."
    Escobedo J.A., Navankasattusas S., Kavanaugh W.M., Milfay D., Fried V.A., Williams L.T.
    Cell 65:75-82(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: BALB/cJ.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Tyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction."
    Yu J.C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D., Ruggiero M., Aaronson S.A.
    Mol. Cell. Biol. 11:3780-3785(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDGFRA, ACTIVATION BY PDGFRA.
  5. "Activation of phosphatidylinositol-3' kinase by Src-family kinase SH3 binding to the p85 subunit."
    Pleiman C.M., Hertz W.M., Cambier J.C.
    Science 263:1609-1612(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LYN.
  6. "Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation."
    Bazenet C.E., Gelderloos J.A., Kazlauskas A.
    Mol. Cell. Biol. 16:6926-6936(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDGFRA.
  7. "Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling."
    Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.
    EMBO J. 16:5880-5893(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH CSF1R.
  8. "Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration."
    Jones N., Master Z., Jones J., Bouchard D., Gunji Y., Sasaki H., Daly R., Alitalo K., Dumont D.J.
    J. Biol. Chem. 274:30896-30905(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TEK/TIE2, PHOSPHORYLATION.
  9. "KAP10, a novel transmembrane adapter protein genetically linked to DAP12 but with unique signaling properties."
    Chang C., Dietrich J., Harpur A.G., Lindquist J.A., Haude A., Loke Y.W., King A., Colonna M., Trowsdale J., Wilson M.J.
    J. Immunol. 163:4651-4654(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCST.
  10. "Characterization of a naturally occurring ErbB4 isoform that does not bind or activate phosphatidyl inositol 3-kinase."
    Elenius K., Choi C.J., Paul S., Santiestevan E., Nishi E., Klagsbrun M.
    Oncogene 18:2607-2615(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB4, PHOSPHORYLATION, CATALYTIC ACTIVITY.
  11. "The protein-tyrosine kinase fer associates with signaling complexes containing insulin receptor substrate-1 and phosphatidylinositol 3-kinase."
    Iwanishi M., Czech M.P., Cherniack A.D.
    J. Biol. Chem. 275:38995-39000(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FER.
  12. Cited for: INTERACTION WITH CBLB.
  13. "Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation."
    Hart K.C., Robertson S.C., Donoghue D.J.
    Mol. Biol. Cell 12:931-942(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACTIVATION BY FGFR3, INTERACTION WITH FGFR3, PHOSPHORYLATION.
  14. "Insulin receptor substrate 3 (IRS-3) and IRS-4 impair IRS-1- and IRS-2-mediated signaling."
    Tsuruzoe K., Emkey R., Kriauciunas K.M., Ueki K., Kahn C.R.
    Mol. Cell. Biol. 21:26-38(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRS4.
  15. "Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells."
    Fang D., Liu Y.-C.
    Nat. Immunol. 2:870-875(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD3Z AND CD28, UBIQUITINATION.
  16. "'Srcasm: a novel Src activating and signaling molecule."
    Seykora J.T., Mei L., Dotto G.P., Stein P.L.
    J. Biol. Chem. 277:2812-2822(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOM1L1.
  17. Cited for: INTERACTION WITH SOCS7.
  18. "LIME, a novel transmembrane adaptor protein, associates with p56lck and mediates T cell activation."
    Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.
    J. Exp. Med. 198:1463-1473(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIME1.
  19. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "LIME acts as a transmembrane adapter mediating BCR-dependent B-cell activation."
    Ahn E., Lee H., Yun Y.
    Blood 107:1521-1527(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIME1.
  21. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  22. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung and Spleen.
  24. "The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation."
    Park S.W., Zhou Y., Lee J., Lu A., Sun C., Chung J., Ueki K., Ozcan U.
    Nat. Med. 16:429-437(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PIK3R2 AND XBP1.

Entry informationi

Entry nameiP85A_MOUSE
AccessioniPrimary (citable) accession number: P26450
Secondary accession number(s): Q8K3B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 166 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.