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Reviewed, UniProtKB/Swiss-Prot O00459 (P85B_HUMAN)

Last modified February 9, 2010. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphatidylinositol 3-kinase regulatory subunit beta
      Short name=PtdIns-3-kinase regulatory subunit beta
      Short name=PI3-kinase regulatory subunit beta
      Short name=PI3K regulatory subunit beta
Alternative name(s):
    Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta
      Short name=PtdIns-3-kinase regulatory subunit p85-beta
      Short name=PI3-kinase subunit p85-beta
Gene names
Name: PIK3R2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length728 AA.
Sequence statusComplete.
Protein existenceEvidence 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 p110 (catalytic) and a p85 (regulatory) subunits.

Sequence similarities

Belongs to the PI3K p85 subunit family.

Contains 1 Rho-GAP domain.

Contains 2 SH2 domains.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HCKP086311EBI-346930,EBI-346340

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 728728Phosphatidylinositol 3-kinase regulatory subunit beta
PRO_0000080763

Regions

Domain4 – 8077SH3
Domain109 – 295187Rho-GAP
Domain330 – 42596SH2 1
Domain622 – 71695SH2 2

Amino acid modifications

Modified residue2621Phosphoserine
Modified residue2631Phosphoserine
Modified residue3651Phosphotyrosine Ref.7
Modified residue4641Phosphotyrosine Ref.7 Ref.5 Ref.6 Ref.9
Modified residue4671Phosphotyrosine Ref.7
Modified residue6051Phosphotyrosine Ref.11

Natural variations

Natural variant2341R → S: dbSNP rs2241088. Ref.3
VAR_030679
Natural variant3131P → S: dbSNP rs1011320. Ref.3
VAR_030680

Sequences

Sequence LengthMass (Da)Tools
O00459-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 80C2AF244977346B

FASTA72881,624
        10         20         30         40         50         60 
MAGPEGFQYR ALYPFRRERP EDLELLPGDV LVVSRAALQA LGVAEGGERC PQSVGWMPGL 

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

       130        140        150        160        170        180 
PDVAPPLLVK LVEAIERTGL DSESHYRPEL PAPRTDWSLS DVDQWDTAAL ADGIKSFLLA 

       190        200        210        220        230        240 
LPAPLVTPEA SAEARRALRE AAGPVGPALE PPTLPLHRAL TLRFLLQHLG RVARRAPALG 

       250        260        270        280        290        300 
PAVRALGATF GPLLLRAPPP PSSPPPGGAP DGSEPSPDFP ALLVEKLLQE HLEEQEVAPP 

       310        320        330        340        350        360 
ALPPKPPKAK PAPTVLANGG SPPSLQDAEW YWGDISREEV NEKLRDTPDG TFLVRDASSK 

       370        380        390        400        410        420 
IQGEYTLTLR KGGNNKLIKV FHRDGHYGFS EPLTFCSVVD LINHYRHESL AQYNAKLDTR 

       430        440        450        460        470        480 
LLYPVSKYQQ DQIVKEDSVE AVGAQLKVYH QQYQDKSREY DQLYEEYTRT SQELQMKRTA 

       490        500        510        520        530        540 
IEAFNETIKI FEEQGQTQEK CSKEYLERFR REGNEKEMQR ILLNSERLKS RIAEIHESRT 

       550        560        570        580        590        600 
KLEQQLRAQA SDNREIDKRM NSLKPDLMQL RKIRDQYLVW LTQKGARQKK INEWLGIKNE 

       610        620        630        640        650        660 
TEDQYALMED EDDLPHHEER TWYVGKINRT QAEEMLSGKR DGTFLIRESS QRGCYACSVV 

       670        680        690        700        710        720 
VDGDTKHCVI YRTATGFGFA EPYNLYGSLK ELVLHYQHAS LVQHNDALTV TLAHPVRAPG 


PGPPPAAR 

« Hide

References

« Hide 'large scale' references
[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: 9582025] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Chromosomal localization of human p85 alpha, a subunit of phosphatidylinositol 3-kinase, and its homologue p85 beta."
Volinia S., Patracchini P., Otsu M., Hiles I., Gout I., Calzolari E., Bernardi F., Rooke L., Waterfield M.D.
Oncogene 7:789-793(1992) [PubMed: 1314371] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS SER-234 AND SER-313.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Placenta.
[5]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, MASS SPECTROMETRY.
[7]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-365; TYR-464 AND TYR-467, MASS SPECTROMETRY.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262 AND SER-263, MASS SPECTROMETRY.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-605, MASS SPECTROMETRY.
Tissue: T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80907 mRNA. Translation: CAA56868.1.
AC007192 Genomic DNA. Translation: AAD22671.1.
BC070082 mRNA. Translation: AAH70082.1.
BC090249 mRNA. Translation: AAH90249.1.
IPIIPI00011736.
PIRH59435.
RefSeqNP_005018.1.
UniGeneHs.371344

3D structure databases

SMRO00459. Positions 7-76, 107-258, 324-436, 428-596, 612-718.
ModBaseSearch...

Protein-protein interaction databases

IntActO00459. 3 interactions.
STRINGO00459.

PTM databases

PhosphoSiteO00459.

Proteomic databases

PRIDEO00459.

Genome annotation databases

EnsemblENST00000222254; ENSP00000222254; ENSG00000105647; Homo sapiens. [Genome view]
GeneID5296.
KEGGhsa:5296.
UCSCuc002nia.1. human.

Organism-specific databases

CTD5296.
GeneCardsGC19P018089.
H-InvDBHIX0014905.
HGNCHGNC:8980. PIK3R2.
MIM603157. gene.
PharmGKBPA33313.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG15816.
HOGENOMHBG506175.
HOVERGENO00459.
InParanoidO00459.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000105647-MONOMER.
Pathway_Interaction_DBpi3kcipathway. Class I PI3K signaling events.
trail_pathway. TRAIL signaling pathway.
ReactomeREACT_11044. Signaling by Rho GTPases.
REACT_11061. Signalling by NGF.
REACT_16888. Signaling by PDGF.
REACT_498. Signaling by Insulin receptor.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressO00459.
BgeeO00459.
CleanExHS_PIK3R2.
GenevestigatorO00459.
GermOnlineENSG00000105647. Homo sapiens.

Family and domain databases

InterProIPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
Gene3DG3DSA:1.10.555.10. RhoGAP. 1 hit.
G3DSA:3.30.505.10. SH2. 2 hits.
PANTHERPTHR10155. PI3kinase_P85. 1 hit.
PfamPF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PRINTSPR00678. PI3KINASEP85.
PR00401. SH2DOMAIN.
SMARTSM00324. RhoGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
PROSITEPS50238. RHOGAP. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio20470.
SOURCESearch...

Entry information

Entry nameP85B_HUMAN
AccessionPrimary (citable) accession number: O00459
Secondary accession number(s): Q5EAT5, Q9UPH9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: February 9, 2010
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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