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UniProtKB/Swiss-Prot entry P23727


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name P85A_BOVIN
Primary accession number P23727
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    October 14, 2008 (Entry version 90)
Name and origin of the protein
Protein name Phosphatidylinositol 3-kinase regulatory subunit alpha
Synonyms PI3-kinase p85 subunit alpha
PtdIns-3-kinase p85-alpha
PI3K
Gene name
Name: PIK3R1
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0092-8674(91)90411-Q; PubMed=1707345 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase.";
Cell 65:91-104(1991).
[2]
CIRCULAR DICHROISM ANALYSIS, AND FLUORESCENCE SPECTROSCOPY.
PubMed=1330535 [NCBI, ExPASy, EBI, Israel, Japan]
Panayotou G., Bax B., Gout I., Federwisch M., Wroblowski B., Dhand R., Fry M.J., Blundell T.L., Wollmer A., Waterfield M.D.;
"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.";
EMBO J. 11:4261-4272(1992).
[3]
STRUCTURE BY NMR OF 1-84.
DOI=10.1016/0092-8674(93)90259-S; PubMed=7684655 [NCBI, ExPASy, EBI, Israel, Japan]
Booker G.W., Gout I., Downing A.K., Driscoll P.C., Boyd J., Waterfield M.D., Campbell I.D.;
"Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase.";
Cell 73:813-822(1993).
[4]
STRUCTURE BY NMR OF 314-431.
DOI=10.1038/358684a0; PubMed=1323062 [NCBI, ExPASy, EBI, Israel, Japan]
Booker G.W., Breeze A.L., Downing A.K., Panayotou G., Gout I., Waterfield M.D., Campbell I.D.;
"Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase.";
Nature 358:684-687(1992).
[5]
STRUCTURE BY NMR OF 321-434.
DOI=10.1021/bi961783x; PubMed=8952511 [NCBI, ExPASy, EBI, Israel, Japan]
Guenther U.L., Liu Y., Sanford D., Bachovchin W.W., Schaffhausen B.;
"NMR analysis of interactions of a phosphatidylinositol 3'-kinase SH2 domain with phosphotyrosine peptides reveals interdependence of major binding sites.";
Biochemistry 35:15570-15581(1996).
[6]
STRUCTURE BY NMR OF 614-724.
DOI=10.1006/jmbi.1997.1562; PubMed=9512716 [NCBI, ExPASy, EBI, Israel, Japan]
Siegal G., Davis B., Kristensen S.M., Sankar A., Linacre J., Stein R.C., Panayotou G., Waterfield M.D., Driscoll P.C.;
"Solution structure of the C-terminal SH2 domain of the p85 alpha regulatory subunit of phosphoinositide 3-kinase.";
J. Mol. Biol. 276:461-478(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M61745; AAA79511.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38749; A38749.
RefSeq NP_777000.1; -.
UniGene Bt.91714
3D structure databases
PDB
1BFI; NMR; -; A=614-724.[ExPASy / RCSB / EBI]
1BFJ; NMR; -; A=614-724.[ExPASy / RCSB / EBI]
1OO3; NMR; -; A=321-431.[ExPASy / RCSB / EBI]
1OO4; NMR; -; A=321-431.[ExPASy / RCSB / EBI]
1PNJ; NMR; -; A=1-84.[ExPASy / RCSB / EBI]
1QAD; X-ray; 1.80 A; A=614-724.[ExPASy / RCSB / EBI]
2PNA; NMR; -; A=328-431.[ExPASy / RCSB / EBI]
2PNB; NMR; -; A=328-431.[ExPASy / RCSB / EBI]
2PNI; NMR; -; A=1-84.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BFI; -.
1BFJ; -.
1OO3; -.
1OO4; -.
1PNJ; -.
1QAD; -.
2PNA; -.
2PNB; -.
2PNI; -.
SMR P23727; 115-309, 325-439.
ModBase P23727.
Protein-protein interaction databases
IntAct P23727; -.
Ontologies
GO
GO:0005943; Cellular component: 1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex (inferred from sequence or structural similarity from UniProtKB).
GO:0043125; Molecular function: ErbB-3 class receptor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005158; Molecular function: insulin receptor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0043560; Molecular function: insulin receptor substrate binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005159; Molecular function: insulin-like growth factor receptor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0035014; Molecular function: phosphoinositide 3-kinase regulator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008286; Biological process: insulin receptor signaling pathway (inferred from sequence or structural similarity from UniProtKB).
GO:0048009; Biological process: insulin-like growth factor receptor signaling pathway (inferred from sequence or structural similarity from UniProtKB).
GO:0046854; Biological process: phosphoinositide phosphorylation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001720; PI3kinase_P85.
IPR000198; RhoGAP.
IPR000980; SH2.
IPR001452; SH3.
Graphical view of domain structure.
Gene3D G3DSA:1.10.555.10; RhoGAP; 1.
G3DSA:3.30.505.10; SH2; 2.
PANTHER PTHR10155; PI3kinase_P85; 1.
Pfam PF00620; RhoGAP; 1.
PF00017; SH2; 2.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00678; PI3KINASEP85.
PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
ProDom PD000093; SH2; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00324; RhoGAP; 1.
SM00252; SH2; 2.
SM00326; SH3; 1.
SMART graphical view of domain structure.
PROSITE PS50238; RHOGAP; 1.
PS50001; SH2; 2.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P23727.
Genome annotation databases
Ensembl ENSBTAG00000010989; Bos taurus. [Contig view]
GeneID 282307; -.
KEGG bta:282307; -.
Phylogenomic databases
HOVERGEN P23727; -.
Other
LinkHub P23727; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Phosphoprotein; Repeat; SH2 domain; SH3 domain; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   724  724     Phosphatidylinositol 3-kinase regulatory subunit alpha. PRO_0000080757
DOMAIN   3    79  77     SH3. 
DOMAIN   113   301  189     Rho-GAP. 
DOMAIN   333   428  96     SH2 1. 
DOMAIN   624   718  95     SH2 2. 
MOD_RES   452   452        Phosphotyrosine (By similarity). 
MOD_RES   467   467        Phosphotyrosine (By similarity). 
MOD_RES   556   556        Phosphotyrosine (By similarity). 
MOD_RES   580   580        Phosphotyrosine (By similarity). 
MOD_RES   607   607        Phosphotyrosine (By similarity). 
STRAND   7    10  4      
STRAND   29    31  3      
HELIX   37    39  3      
TURN   50    52  3      
STRAND   55    60  6      
TURN   61    64  4      
STRAND   65    78  14      
TURN   341   344  4      
HELIX   345   349  5      
STRAND   354   357  4      
TURN   362   364  3      
STRAND   370   378  9      
STRAND   393   395  3      
TURN   403   405  3      
TURN   408   411  4      
HELIX   413   415  3      
TURN   418   420  3      
HELIX   617   619  3      
HELIX   621   623  3      
STRAND   625   628  4      
HELIX   631   638  8      
STRAND   645   650  6      
STRAND   657   663  7      
STRAND   666   675  10      
STRAND   678   682  5      
STRAND   688   690  3      
HELIX   691   700  10      
HELIX   703   705  3      
Sequence information
Length: 724 AA [This is the length of the unprocessed precursor] Molecular weight: 83497 Da [This is the MW of the unprocessed precursor] CRC64: EBDF6E754BBF7321 [This is a checksum on the sequence]
        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 

P23727 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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