Phosphatidylinositol 3-kinase regulatory subunit alpha

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Reviewed, UniProtKB/Swiss-Prot P23727 (P85A_BOVIN)

Last modified June 16, 2009. Version 96. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Phosphatidylinositol 3-kinase regulatory subunit alpha
Alternative name(s):
    PI3-kinase p85 subunit alpha
    PtdIns-3-kinase p85-alpha
      Short name=PI3K

Gene names

Name:

PIK3R1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	724 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues.
Subunit structure	Heterodimer of a p110 (catalytic) and a p85 (regulatory) subunits. 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 By similarity.
Domain	The SH3 domain mediates the binding to CBLB By similarity.
Post-translational modification	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.
Sequence similarities	Belongs to the PI3K p85 subunit family. Contains 1 Rho-GAP domain. Contains 2 SH2 domains. Contains 1 SH3 domain.

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Ontologies

Keywords
Domain	Repeat SH2 domain SH3 domain
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	insulin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB insulin-like growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB phosphoinositide phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of glucose import Inferred from mutant phenotype. Source: UniProtKB regulation of establishment of protein localization Inferred from mutant phenotype. Source: UniProtKB
Cellular component	1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ErbB-3 class receptor binding Inferred from sequence or structural similarity. Source: UniProtKB insulin receptor binding Inferred from sequence or structural similarity. Source: UniProtKB insulin receptor substrate binding Inferred from sequence or structural similarity. Source: UniProtKB insulin-like growth factor receptor binding Inferred from sequence or structural similarity. Source: UniProtKB phosphoinositide 3-kinase regulator activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Epor	P14753	1	EBI-520244,EBI-617901	From a different organism.
Inpp5d	Q9ES52-1	1	EBI-520244,EBI-1452545	From a different organism.
Inpp5d	Q9ES52-3	1	EBI-520244,EBI-1452551	From a different organism.
Pdgfrb	P05622	1	EBI-520244,EBI-1554855	From a different organism.
PIK3CA	P32871	2	EBI-520244,EBI-1373130
Pik3ca	P42337	1	EBI-520244,EBI-641748	From a different organism.
RAB5A	P20339	2	EBI-520244,EBI-399437	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 724

724

Phosphatidylinositol 3-kinase regulatory subunit alpha

PRO_0000080757

Regions

Domain

3 – 79

SH3

Domain

113 – 301

189

Rho-GAP

Domain

333 – 428

SH2 1

Domain

624 – 718

SH2 2

Amino acid modifications

Modified residue

452

Phosphotyrosine By similarity

Modified residue

467

Phosphotyrosine By similarity

Modified residue

556

Phosphotyrosine By similarity

Modified residue

580

Phosphotyrosine By similarity

Modified residue

607

Phosphotyrosine By similarity

Secondary structure

724

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P23727-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: EBDF6E754BBF7321
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FASTA

724

83,497

        10         20         30         40         50         60 
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEAKP EEIGWLNGYN 

        70         80         90        100        110        120 
ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG PSKTEADSEQ QASTLPDLAE 

       130        140        150        160        170        180 
QFAPPDVAPP LLIKLVEAIE KKGLECSTLY RTQSSSNPAE LRQLLDCDTA SLDLEMFDVH 

       190        200        210        220        230        240 
VLADAFKRYL LDLPNPVIPV AVSSELISLA PEVQSSEEYI QLLKKLIRSP SIPHQYWLTL 

       250        260        270        280        290        300 
QYLLKHFFKL SQTSSKNLLN ARVLSELFSP LLFRFPAASS ENTEHLIKII EILISTEWNE 

       310        320        330        340        350        360 
RQPAPALPPK PPKPTTVANN GMNNNMSLQD AEWYWGDISR EEVNEKLRDT ADGTFLVRDA 

       370        380        390        400        410        420 
STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFNS VVELINHYRN ESLAQYNPKL 

       430        440        450        460        470        480 
DVKLLYPVSK YQQDQVVKED NIEAVGKKLH EYNTQFQEKS REYDRLYEDY TRTSQEIQMK 

       490        500        510        520        530        540 
RTAIEAFNET IKIFEEQCQT QERYSKEYIE KFKREGNETE IQRIMHNYEK LKSRISEIVD 

       550        560        570        580        590        600 
SRRRLEEDLK KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN 

       610        620        630        640        650        660 
ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE SSKQGCYACS 

       670        680        690        700        710        720 
VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH TSLVQHNDSL NVTLAYPVYA 


QQRR

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References

[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: 1707345] [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: 1330535] [Abstract] Cited for: CIRCULAR DICHROISM ANALYSIS, FLUORESCENCE SPECTROSCOPY.
[3]	"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: 7684655] [Abstract] Cited for: STRUCTURE BY NMR OF 1-84.
[4]	"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: 1323062] [Abstract] Cited for: STRUCTURE BY NMR OF 314-431.
[5]	"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: 8952511] [Abstract] Cited for: STRUCTURE BY NMR OF 321-434.
[6]	"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: 9512716] [Abstract] Cited for: STRUCTURE BY NMR OF 614-724.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M61745 mRNA. Translation: AAA79511.1.

IPI

IPI00709792.

PIR

A38749.

RefSeq

NP_777000.1.

UniGene

Bt.91714

3D structure databases

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	[»]

SMR

P23727. Positions 115-309, 325-439.

ModBase

Search...

Protein-protein interaction databases

IntAct

P23727. 12 interactions.

Genome annotation databases

Ensembl

ENSBTAG00000010989. Bos taurus. [Contig view]

GeneID

282307.

KEGG

bta:282307.

Phylogenomic databases

HOVERGEN

P23727.

Family and domain databases

InterPro

IPR001720. PI3kinase_P85.
IPR000198. RhoGAP.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]

Gene3D

G3DSA:1.10.555.10. RhoGAP. 1 hit.
G3DSA:3.30.505.10. SH2. 2 hits.

PANTHER

PTHR10155. PI3kinase_P85. 1 hit.

Pfam

PF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00678. PI3KINASEP85.
PR00401. SH2DOMAIN.

ProDom

PD000093. SH2. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00324. RhoGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]

PROSITE

PS50238. RHOGAP. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

P85A_BOVIN

Accession

Primary (citable) accession number: P23727

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	June 16, 2009
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents