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O08908

- P85B_MOUSE

UniProt

O08908 - P85B_MOUSE

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Protein

Phosphatidylinositol 3-kinase regulatory subunit beta

Gene

Pik3r2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy.By similarity

GO - Molecular functioni

  1. phosphatidylinositol 3-kinase regulator activity Source: InterPro

GO - Biological processi

  1. insulin receptor signaling pathway Source: UniProtKB
  2. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  3. regulation of phosphorylation Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_188185. DAP12 signaling.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198701. Interleukin-7 signaling.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_205300. PI3K/AKT activation.
REACT_210090. Rho GTPase cycle.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_211860. Tie2 Signaling.
REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_225145. Downstream TCR signaling.
REACT_226341. PIP3 activates AKT signaling.
REACT_230639. Downstream signal transduction.
REACT_240139. PI3K Cascade.
REACT_257032. Nephrin interactions.
REACT_257088. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 3-kinase regulatory subunit beta
Short name:
PI3-kinase regulatory subunit beta
Short name:
PI3K regulatory subunit beta
Short name:
PtdIns-3-kinase regulatory subunit beta
Alternative name(s):
Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta
Short name:
PI3-kinase subunit p85-beta
Short name:
PtdIns-3-kinase regulatory subunit p85-beta
Gene namesi
Name:Pik3r2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1098772. Pik3r2.

Subcellular locationi

GO - Cellular componenti

  1. phosphatidylinositol 3-kinase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 722722Phosphatidylinositol 3-kinase regulatory subunit betaPRO_0000080764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei458 – 4581Phosphotyrosine3 Publications
Modified residuei599 – 5991PhosphotyrosineBy similarity
Modified residuei649 – 6491PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylated in response to signaling from activated receptor-type protein kinases. Dephosphorylated by PTPRJ. Dephosphorylated at Tyr-649 by PTPN13. Phosphorylation of Tyr-649 impairs while its dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)-mediated polyubiquitination.By similarity
Ubiquitinated. Polyubiquitination by the SCF(FBXL2) complex probably promotes proteasomal degradation of PIK3R2.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO08908.
PaxDbiO08908.
PRIDEiO08908.

PTM databases

PhosphoSiteiO08908.

Expressioni

Gene expression databases

BgeeiO08908.
ExpressionAtlasiO08908. baseline.
GenevestigatoriO08908.

Interactioni

Subunit structurei

Heterodimer of a regulatory subunit PIK3R2 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL. Interacts with FLT1 (tyrosine-phosphorylated) and FLT4 (tyrosine-phosphorylated) (By similarity). Interacts with NYAP1, NYAP2 and MYO16 (PubMed:21946561). Interacts with FBXL2; PIK3R2 is a substrate of the SCF(FBXL2) complex. Interacts with PTPN13; dephosphorylates PIK3R2 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Brd7O886654EBI-643570,EBI-643930
Pdk2Q9JK423EBI-643570,EBI-643530

Protein-protein interaction databases

BioGridi202163. 4 interactions.
IntActiO08908. 10 interactions.
MINTiMINT-1723872.

Structurei

Secondary structure

1
722
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi448 – 4514Combined sources
Turni452 – 4543Combined sources
Helixi455 – 49642Combined sources
Turni508 – 5103Combined sources
Helixi511 – 55747Combined sources
Helixi559 – 56810Combined sources
Helixi609 – 6113Combined sources
Turni614 – 6163Combined sources
Helixi623 – 6308Combined sources
Beta strandi637 – 6404Combined sources
Beta strandi649 – 6546Combined sources
Beta strandi656 – 66712Combined sources
Beta strandi670 – 6745Combined sources
Helixi683 – 6886Combined sources
Beta strandi691 – 6933Combined sources
Turni696 – 6983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y3AX-ray3.30B423-722[»]
ProteinModelPortaliO08908.
SMRiO08908. Positions 5-82, 111-288, 318-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8077SH3PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 293182Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini324 – 41996SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini616 – 71095SH2 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The SH2 2 domain is required for interaction with FBXL2 and PTPN13.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.
InParanoidiO08908.
KOiK02649.
OMAiHCVIYKT.
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.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10155. PTHR10155. 1 hit.
PfamiPF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
[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.

O08908-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGAEGFQYR AVYPFRRERP EDLELLPGDL LVVSRVALQA LGVADGGERC
60 70 80 90 100
PHNVGWMPGF NERTRQRGDF PGTYVEFLGP VALARPGPRP RGPRPLPARP
110 120 130 140 150
LDGSSESGHI LPDLAEQFSP PDPAPPILVK LVEAIEQAEL DSECYSKPEL
160 170 180 190 200
PATRTDWSLS DLEQWDRTAL YDAVKGFLLA LPAAVVTPEA AAEAYRALRE
210 220 230 240 250
VAGPVGLVLE PPTLPLHQAL TLRFLLQHLG RVARRAPSPD TAVHALASAF
260 270 280 290 300
GPLLLRIPPS GGEGDGSEPV PDFPVLLLER LVQEHVEEQD AAPPALPPKP
310 320 330 340 350
SKAKPAPTAL ANGGSPPSLQ DAEWYWGDIS REEVNERLRD TPDGTFLVRD
360 370 380 390 400
ASSKIQGEYT LTLRKGGNNK LIKVFHRDGH YGFSEPLTFC SVVELISHYR
410 420 430 440 450
HESLAQYNAK LDTRLLYPVS KYQQDQVVKE DSIEAVGAQL KVYHQQYQDK
460 470 480 490 500
SREYDQLYEE YTRTSQELQM KRTAIEAFNE TIKIFEEQGQ TQEKCSKEYL
510 520 530 540 550
ERFRREGNEK EMQRILLNSE RLKSRIAEIH ESRTKLEQDL RAQASDNREI
560 570 580 590 600
DKRMNSLKPD LMQLRKIRDQ YLVWLTQKGA RQRKINEWLG IKNETEDQYS
610 620 630 640 650
LMEDEDALPH HEERTWYVGK INRTQAEEML SGKRDGTFLI RESSQRGCYA
660 670 680 690 700
CSVVVDGDTK HCVIYRTATG FGFAEPYNLY GSLKELVLHY QHASLVQHND
710 720
ALTVTLAHPV RAPGPGPPSA AR
Length:722
Mass (Da):81,266
Last modified:July 27, 2011 - v2
Checksum:iA999FAF9011455FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti433 – 4331I → V in CAA73903. (PubMed:9582025)Curated
Sequence conflicti433 – 4331I → V in AAH06796. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13569 mRNA. Translation: CAA73903.1.
CH466569 Genomic DNA. Translation: EDL28873.1.
BC006796 mRNA. Translation: AAH06796.1.
BC085501 mRNA. Translation: AAH85501.1.
CCDSiCCDS22381.1.
RefSeqiNP_032867.2. NM_008841.2.
UniGeneiMm.12945.

Genome annotation databases

EnsembliENSMUST00000034296; ENSMUSP00000034296; ENSMUSG00000031834.
GeneIDi18709.
KEGGimmu:18709.
UCSCiuc009mbn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13569 mRNA. Translation: CAA73903.1 .
CH466569 Genomic DNA. Translation: EDL28873.1 .
BC006796 mRNA. Translation: AAH06796.1 .
BC085501 mRNA. Translation: AAH85501.1 .
CCDSi CCDS22381.1.
RefSeqi NP_032867.2. NM_008841.2.
UniGenei Mm.12945.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y3A X-ray 3.30 B 423-722 [» ]
ProteinModelPortali O08908.
SMRi O08908. Positions 5-82, 111-288, 318-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202163. 4 interactions.
IntActi O08908. 10 interactions.
MINTi MINT-1723872.

PTM databases

PhosphoSitei O08908.

Proteomic databases

MaxQBi O08908.
PaxDbi O08908.
PRIDEi O08908.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034296 ; ENSMUSP00000034296 ; ENSMUSG00000031834 .
GeneIDi 18709.
KEGGi mmu:18709.
UCSCi uc009mbn.2. mouse.

Organism-specific databases

CTDi 5296.
MGIi MGI:1098772. Pik3r2.

Phylogenomic databases

eggNOGi NOG263689.
GeneTreei ENSGT00390000010431.
HOGENOMi HOG000008438.
HOVERGENi HBG082100.
InParanoidi O08908.
KOi K02649.
OMAi HCVIYKT.
OrthoDBi EOG7BP831.
TreeFami TF102033.

Enzyme and pathway databases

Reactomei REACT_188185. DAP12 signaling.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198701. Interleukin-7 signaling.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_205300. PI3K/AKT activation.
REACT_210090. Rho GTPase cycle.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_211860. Tie2 Signaling.
REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_225145. Downstream TCR signaling.
REACT_226341. PIP3 activates AKT signaling.
REACT_230639. Downstream signal transduction.
REACT_240139. PI3K Cascade.
REACT_257032. Nephrin interactions.
REACT_257088. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

NextBioi 294785.
PROi O08908.
SOURCEi Search...

Gene expression databases

Bgeei O08908.
ExpressionAtlasi O08908. baseline.
Genevestigatori O08908.

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.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR10155. PTHR10155. 1 hit.
Pfami PF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
[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

« Hide 'large scale' publications
  1. "An oncogenic fusion product of the phosphatidylinositol 3-kinase p85beta subunit and HUMORF8, a putative deubiquitinating enzyme."
    Janssen J.W.G., Schleithhoff L., Bartram C.R., Schulz A.S.
    Oncogene 16:1767-1772(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: C57BL/6 and FVB/N.
    Tissue: Brain and Mammary gland.
  4. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "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-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  7. "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-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. "NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling in neurons."
    Yokoyama K., Tezuka T., Kotani M., Nakazawa T., Hoshina N., Shimoda Y., Kakuta S., Sudo K., Watanabe K., Iwakura Y., Yamamoto T.
    EMBO J. 30:4739-4754(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NYAP1; NYAP2 AND MYO16.

Entry informationi

Entry nameiP85B_MOUSE
AccessioniPrimary (citable) accession number: O08908
Secondary accession number(s): Q5U3K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 134 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