Phosphatidylinositol 3-kinase regulatory subunit beta

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P23726 (P85B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 103. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

PIK3R2

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

Protein attributes

Sequence length	724 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Subunit structure	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.
Post-translational modification	Phosphorylated in response to signaling from activated receptor-type protein kinases. Dephosphorylated by PTPRJ By similarity.
Sequence similarities	Belongs to the PI3K p85 subunit family. Contains 1 Rho-GAP domain. Contains 2 SH2 domains. Contains 1 SH3 domain.

Ontologies

Keywords
Domain	Repeat SH2 domain SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of anti-apoptosis Inferred from sequence or structural similarity. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	phosphatidylinositol 3-kinase complex Inferred from electronic annotation. Source: InterPro
Molecular function	phosphatidylinositol 3-kinase regulator activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PIK3CA	P32871	3	EBI-1555978,EBI-1373130

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 724

724

Phosphatidylinositol 3-kinase regulatory subunit beta

PRO_0000080762

Regions

Domain

4 – 80

SH3

Domain

109 – 291

183

Rho-GAP

Domain

326 – 421

SH2 1

Domain

618 – 712

SH2 2

Amino acid modifications

Modified residue

259

Phosphoserine By similarity

Modified residue

361

Phosphotyrosine By similarity

Modified residue

460

Phosphotyrosine By similarity

Modified residue

463

Phosphotyrosine By similarity

Modified residue

601

Phosphotyrosine By similarity

Secondary structure

724

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23726 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 9D2BA8B6DB087098
Show »

FASTA

724

81,060

        10         20         30         40         50         60 
MAGPEGFQYR ALYPFRRERP EDLELLPGDV LVVSRAALQA LGVAEGNERC PQSVGWMPGL 

        70         80         90        100        110        120 
NERTRQRGDF PGTYVEFLGP VALARPGPRP RGPRPLPARP RDGPPEPGLT LPDLPEQFSP 

       130        140        150        160        170        180 
PDVAPPILVK LVEAIERTGL DSYRPEPPAV RTDWSLSDVE QWDAAALSDG VKGFLLALPA 

       190        200        210        220        230        240 
PLVTPEAAAE AHRALREAAG PVGPALEPPT LPLHHALTLR FLLQHLGRVA GRAPAPGPAV 

       250        260        270        280        290        300 
RALGATFGPL LLRAPPPPSP PPGGAPDGTE PTPDFPALLV EKLLQEHLEE QEVAPPALPP 

       310        320        330        340        350        360 
KPPKTKPAPT GLANGGSPPS LQDAEWYWGD ISREEVNEKL RDTPDGTFLV RDASSKIQGE 

       370        380        390        400        410        420 
YTLTLRKGGN NKLIKVFHRD GHYGFSEPLT FCSVVDLITH YRHESLAQYN AKLDTRLLYP 

       430        440        450        460        470        480 
VSKYQQDQIV KEDSVEAVGA QLKVYHQQYQ DKSREYDQLY EEYTRTSQEL QMKRTAIEAF 

       490        500        510        520        530        540 
NETIKIFEEQ GQTQEKCSKE YLERFRREGN EKEMQRILLN SERLKSRIAE IHESRTKLEQ 

       550        560        570        580        590        600 
ELRAQASDNR EIDKRMNSLK PDLMQLRKIR DQYLVWLTQK GARQKKINEW LGIKNETEDQ 

       610        620        630        640        650        660 
YSLMEDEDDL PHHEERTWYV GKINRTQAEE MLSGKRDGTF LIRESSQRGC YACSVVVDGD 

       670        680        690        700        710        720 
TKHCVIYRTA TGFGFAEPYN LYGSLKELVL HYQHASLVQH NDALTVTLAH PVRAPGPGPP 


PAAR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' 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]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus.
[3]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M61746 mRNA. Translation: AAA79510.1.
BC118113 mRNA. Translation: AAI18114.1.

IPI

IPI00710112.

PIR

B38749.

RefSeq

NP_777001.1. NM_174576.2.

UniGene

Bt.515.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3L4Q	X-ray	2.30	C/D	424-593	[»]

ProteinModelPortal

P23726.

SMR

P23726. Positions 4-86, 320-592, 608-714.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39878N.

IntAct

P23726. 1 interaction.

MINT

MINT-1348098.

STRING

P23726.

Proteomic databases

PRIDE

P23726.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000003033; ENSBTAP00000003033; ENSBTAG00000002350.

GeneID

282308.

KEGG

bta:282308.

Organism-specific databases

CTD

5296.

Phylogenomic databases

eggNOG

maNOG04646.

GeneTree

ENSGT00390000010431.

HOVERGEN

HBG082100.

InParanoid

P23726.

OMA

DEDDLPH.

OrthoDB

EOG49GKG4.

PhylomeDB

P23726.

Family and domain databases

InterPro

IPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]

Gene3D

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

K02649.

PANTHER

PTHR10155. PI3kinase_P85. 1 hit.

Pfam

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

PRINTS

PR00678. PI3KINASEP85.
PR00401. SH2DOMAIN.

SMART

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

SUPFAM

SSF48350. Rho_GAP. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

P85B_BOVIN

Accession

Primary (citable) accession number: P23726
Secondary accession number(s): Q17QY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	November 16, 2011
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents