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P27986 (P85A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 3-kinase regulatory subunit alpha

Short name=PI3-kinase regulatory subunit alpha
Short name=PI3K regulatory subunit alpha
Short name=PtdIns-3-kinase regulatory subunit alpha
Alternative name(s):
Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha
Short name=PI3-kinase subunit p85-alpha
Short name=PtdIns-3-kinase regulatory subunit p85-alpha
Gene names
Name:PIK3R1
Synonyms:GRB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to activated (phosphorylated) protein-Tyr 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. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling. Ref.11 Ref.51 Ref.53

Subunit structure

Heterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with FER. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Interacts with PTK2/FAK1 By similarity. Interacts with phosphorylated TOM1L1. Interacts with phosphorylated LIME1 upon TCR and/or BCR activation. Interacts with SOCS7. Interacts with RUFY3. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts with LYN (via SH3 domain); this enhances enzyme activity By similarity. Interacts with phosphorylated LAT, LAX1 and TRAT1 upon TCR activation. Interacts with CBLB. Interacts with HIV-1 Nef to activate the Nef associated p21-activated kinase (PAK). This interaction depends on the C-terminus of both proteins and leads to increased production of HIV. Interacts with HCV NS5A. 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 IRS1 and phosphorylated IRS4, as well as with NISCH and HCST. Interacts with FASLG, KIT and BCR. Interacts with AXL, FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with FGR and HCK. Interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Interacts with ERBB4 (phosphorylated). Interacts with NTRK1 (phosphorylated upon ligand-binding). Ref.2 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.32 Ref.36 Ref.37 Ref.38 Ref.53

Tissue specificity

Isoform 2 is expressed in skeletal muscle and brain, and at lower levels in kidney and cardiac muscle. Isoform 2 and isoform 4 are present in skeletal muscle (at protein level). Ref.2

Domain

The SH3 domain mediates the binding to CBLB, and to HIV-1 Nef.

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.

Phosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated by CSF1R. Phosphorylated by ERBB4. Phosphorylated on tyrosine residues by TEK/TIE2. Dephosphorylated by PTPRJ. Phosphorylated by PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF. The relevance of phosphorylation by PIK3CA is however unclear By similarity. Phosphorylated in response to KIT and KITLG/SCF. Phosphorylated by FGR. Ref.33 Ref.35

Involvement in disease

Agammaglobulinemia 7, autosomal recessive (AGM7) [MIM:615214]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.42

SHORT syndrome (SHORTS) [MIM:269880]: A rare, multisystem disease characterized by short stature, anomalies of the anterior chamber of the eye, characteristic facial features such as triangular facies, lack of facial fat, and hypoplastic nasal alae with overhanging columella, partial lipodystrophy, hernias, hyperextensibility, and delayed dentition. The clinical phenotype can include insulin resistance, nephrocalcinosis, and hearing deficits. Developmental milestones and cognition are normal.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.57 Ref.58

Sequence similarities

Belongs to the PI3K p85 subunit family.

Contains 1 Rho-GAP domain.

Contains 2 SH2 domains.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dwarfism
   DomainRepeat
SH2 domain
SH3 domain
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from electronic annotation. Source: Ensembl

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

NFAT protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

T cell costimulation

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cellular response to UV

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

growth hormone receptor signaling pathway

Inferred from direct assay PubMed 7782332. Source: BHF-UCL

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Inferred from physical interaction Ref.10. Source: UniProtKB

insulin-like growth factor receptor signaling pathway

Inferred from physical interaction Ref.12. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 7782332. Source: BHF-UCL

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of establishment of protein localization to plasma membrane

Inferred from sequence or structural similarity PubMed 8052599. Source: BHF-UCL

positive regulation of glucose import

Inferred from sequence or structural similarity PubMed 8052599. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of phosphatidylinositol 3-kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_component1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

phosphatidylinositol 3-kinase complex

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionErbB-3 class receptor binding

Inferred from direct assay PubMed 10572067. Source: UniProtKB

insulin binding

Inferred from direct assay PubMed 8440175. Source: UniProtKB

insulin receptor binding

Inferred from physical interaction Ref.13Ref.10. Source: UniProtKB

insulin receptor substrate binding

Inferred from sequence or structural similarity. Source: BHF-UCL

insulin-like growth factor receptor binding

Inferred from physical interaction Ref.12. Source: UniProtKB

neurotrophin TRKA receptor binding

Inferred from physical interaction Ref.30. Source: UniProtKB

phosphatidylinositol 3-kinase binding

Inferred from sequence or structural similarity. Source: BHF-UCL

phosphatidylinositol 3-kinase regulator activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 24705354. Source: IntAct

protein phosphatase binding

Inferred from physical interaction PubMed 14699157. Source: UniProtKB

transmembrane receptor protein tyrosine kinase adaptor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABI1Q8IZP08EBI-79464,EBI-375446
ABL2P426842EBI-79464,EBI-1102694
ARP102755EBI-79464,EBI-608057
CBLP226815EBI-79464,EBI-518228
CD28P107478EBI-79464,EBI-4314301
CMIPQ8IY222EBI-79464,EBI-7689652
CRKLP461092EBI-79464,EBI-910
CTLA4P164103EBI-79464,EBI-1030991
DLGAP4Q9Y2H02EBI-79464,EBI-722139
EGFRP005334EBI-79464,EBI-297353
ERBB2P0462611EBI-79464,EBI-641062
ERBB3P2186040EBI-79464,EBI-720706
ESR1P033726EBI-79464,EBI-78473
FGFR1P113624EBI-79464,EBI-1028277
FLT1P179482EBI-79464,EBI-1026718
FLT3P368882EBI-79464,EBI-3946257
GAB1Q1348033EBI-79464,EBI-517684
GRB2P629933EBI-79464,EBI-401755
HTTP428587EBI-79464,EBI-466029
IGF1RP080693EBI-79464,EBI-475981
INSRP062133EBI-79464,EBI-475899
IRS1P3556812EBI-79464,EBI-517592
Irs1P355702EBI-79464,EBI-520230From a different organism.
IRS2Q9Y4H22EBI-79464,EBI-1049582
KITP1072118EBI-79464,EBI-1379503
LAPTM4BQ86VI4-32EBI-79464,EBI-3267286
LATO435614EBI-79464,EBI-1222766
MAP4K1Q929182EBI-79464,EBI-881
MAPK8P459832EBI-79464,EBI-286483
METP085816EBI-79464,EBI-1039152
NELFBQ8WX922EBI-79464,EBI-347721
Nyap1Q6PFX74EBI-79464,EBI-7447489From a different organism.
Nyap2Q8BM65-43EBI-79464,EBI-7447598From a different organism.
PDGFRBP0961918EBI-79464,EBI-641237
PIK3CAP4233613EBI-79464,EBI-2116585
RAPGEF1Q139052EBI-79464,EBI-976876
RPL13P263732EBI-79464,EBI-356849
RXRAP197938EBI-79464,EBI-78598
SHANK2Q9UPX82EBI-79464,EBI-1570571
SHC1P293533EBI-79464,EBI-78835
SIRT1Q96EB63EBI-79464,EBI-1802965
SOS1Q078892EBI-79464,EBI-297487
SRCP129315EBI-79464,EBI-621482
SSTR2P308745EBI-79464,EBI-6266898
TIRAPP587533EBI-79464,EBI-528644
TLR3O154552EBI-79464,EBI-6116630
TPSAB1Q156612EBI-79464,EBI-1761369
TPX2Q9ULW02EBI-79464,EBI-1037322
VAV3Q9UKW42EBI-79464,EBI-297568
VP3Q991523EBI-79464,EBI-1776808From a different organism.
ZDHHC17Q8IUH52EBI-9090282,EBI-524753

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P27986-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P27986-2)

Also known as: AS53;

The sequence of this isoform differs from the canonical sequence as follows:
     1-270: Missing.
     271-304: MLFRFSAASSDNTENLIKVIEILISTEWNERQPA → MYNTVWNMEDLDLEYAKTDINCGTDLMFYIEMDP
Isoform 3 (identifier: P27986-3)

Also known as: p46;

The sequence of this isoform differs from the canonical sequence as follows:
     1-300: Missing.
     301-306: RQPAPA → MHNLQT
Isoform 4 (identifier: P27986-4)

Also known as: p85I;

The sequence of this isoform differs from the canonical sequence as follows:
     605-605: D → ENFLSCLPS
Isoform 5 (identifier: P27986-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-363: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.43
Chain2 – 724723Phosphatidylinositol 3-kinase regulatory subunit alpha
PRO_0000080758

Regions

Domain3 – 7977SH3
Domain113 – 301189Rho-GAP
Domain333 – 42896SH2 1
Domain624 – 71895SH2 2

Amino acid modifications

Modified residue21N-acetylserine Ref.43
Modified residue4671Phosphotyrosine By similarity
Modified residue5801Phosphotyrosine Ref.40
Modified residue6081Phosphoserine By similarity

Natural variations

Alternative sequence1 – 363363Missing in isoform 5.
VSP_045903
Alternative sequence1 – 300300Missing in isoform 3.
VSP_021841
Alternative sequence1 – 270270Missing in isoform 2.
VSP_021842
Alternative sequence271 – 30434MLFRF…ERQPA → MYNTVWNMEDLDLEYAKTDI NCGTDLMFYIEMDP in isoform 2.
VSP_021843
Alternative sequence301 – 3066RQPAPA → MHNLQT in isoform 3.
VSP_021844
Alternative sequence6051D → ENFLSCLPS in isoform 4.
VSP_021845
Natural variant3261M → I Does not affect insulin-stimulated lipid kinase activity. Ref.5 Ref.55 Ref.56
Corresponds to variant rs3730089 [ dbSNP | Ensembl ].
VAR_010023
Natural variant4091R → Q in a patient with severe insulin resistance; lower insulin-stimulated lipid kinase activity compared with wild-type. Ref.56
VAR_010024
Natural variant4511E → K. Ref.8
Corresponds to variant rs17852841 [ dbSNP | Ensembl ].
VAR_029562
Natural variant4891E → K in SHORTS; there is 70 to 90% reduction in the effect of insulin on AKT1 activation, glycogen synthesis and glucose uptake, indicating severe insulin resistance for both proximal and distal PI3K-dependent signaling. Ref.57
VAR_070221
Natural variant5391Missing in SHORTS; there is 70 to 90% reduction in the effect of insulin on AKT1 activation, glycogen synthesis and glucose uptake, indicating severe insulin resistance for both proximal and distal PI3K-dependent signaling. Ref.57
VAR_070222
Natural variant6491R → W in SHORTS; impairs interaction between PIK3R1 and IRS1 and reduces AKT1-mediated insulin signaling. Ref.58
VAR_070223

Experimental info

Sequence conflict3301D → N in M61906. Ref.1
Sequence conflict4601S → G in BAG52931. Ref.4

Secondary structure

............................................................................................................ 724
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: B9DAD8416C33140F

FASTA72483,598
        10         20         30         40         50         60 
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEARP EEIGWLNGYN 

        70         80         90        100        110        120 
ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG SSKTEADVEQ QALTLPDLAE 

       130        140        150        160        170        180 
QFAPPDIAPP LLIKLVEAIE KKGLECSTLY RTQSSSNLAE LRQLLDCDTP SVDLEMIDVH 

       190        200        210        220        230        240 
VLADAFKRYL LDLPNPVIPA AVYSEMISLA PEVQSSEEYI QLLKKLIRSP SIPHQYWLTL 

       250        260        270        280        290        300 
QYLLKHFFKL SQTSSKNLLN ARVLSEIFSP MLFRFSAASS DNTENLIKVI EILISTEWNE 

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

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

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

       490        500        510        520        530        540 
RTAIEAFNET IKIFEEQCQT QERYSKEYIE KFKREGNEKE IQRIMHNYDK LKSRISEIID 

       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 

« Hide

Isoform 2 (AS53) [UniParc].

Checksum: 33BB0F88AA47CB3F
Show »

FASTA45453,486
Isoform 3 (p46) [UniParc].

Checksum: EF2D6D4D668C62D8
Show »

FASTA42449,965
Isoform 4 (p85I) [UniParc].

Checksum: F4820A783035803A
Show »

FASTA73284,474
Isoform 5 [UniParc].

Checksum: 100325CF4D673C4B
Show »

FASTA36142,838

References

« Hide 'large scale' references
[1]"Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases."
Skolnik E.Y., Margolis B., Mohammadi M., Lowenstein E., Fischer R., Drepps A., Ullrich A., Schlessinger J.
Cell 65:83-90(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Insulin receptor substrate 1 binds two novel splice variants of the regulatory subunit of phosphatidylinositol 3-kinase in muscle and brain."
Antonetti D.A., Algenstaedt P., Kahn C.R.
Mol. Cell. Biol. 16:2195-2203(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), INTERACTION WITH IRS1, TISSUE SPECIFICITY.
Tissue: Skeletal muscle.
[3]Udelhoven M., Kotzka J., Knebel B., Klein E., Krone W., Mueller-Wieland D.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Skeletal muscle.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Brain.
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-326.
Tissue: Brain.
[6]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 1 AND 2), VARIANT LYS-451.
Tissue: Placenta and Skeletal muscle.
[9]"Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor."
Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J., Schlessinger J.
Mol. Cell. Biol. 13:6889-6896(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFRB.
[10]"Direct activation of the phosphatidylinositol 3'-kinase by the insulin receptor."
Van Horn D.J., Myers M.G. Jr., Backer J.M.
J. Biol. Chem. 269:29-32(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSR.
[11]"Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1."
Vainikka S., Joukov V., Wennstrom S., Bergman M., Pelicci P.G., Alitalo K.
J. Biol. Chem. 269:18320-18326(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FGFR4 SIGNALING.
[12]"Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor."
Craparo A., O'Neill T.J., Gustafson T.A.
J. Biol. Chem. 270:15639-15643(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGF1R.
[13]"Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain."
Gustafson T.A., He W., Craparo A., Schaub C.D., O'Neill T.J.
Mol. Cell. Biol. 15:2500-2508(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSR.
[14]"Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors."
Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.
J. Biol. Chem. 271:30942-30949(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFRA.
[15]"Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes."
Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.
J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIT.
[16]"Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site."
Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., Ullrich A., Bartram C.R., Janssen J.W.
Oncogene 14:2619-2631(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXL.
[17]"LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation."
Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.
Cell 92:83-92(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT.
[18]"Characterization of insulin receptor substrate 4 in human embryonic kidney 293 cells."
Fantin V.R., Sparling J.D., Slot J.W., Keller S.R., Lienhard G.E., Lavan B.E.
J. Biol. Chem. 273:10726-10732(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IRS4.
[19]"T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-zeta complex, recruits intracellular signaling proteins to the plasma membrane."
Bruyns E., Marie-Cardine A., Kirchgessner H., Sagolla K., Shevchenko A., Mann M., Autschbach F., Bensussan A., Meuer S., Schraven B.
J. Exp. Med. 188:561-575(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAT1.
[20]"KAP10, a novel transmembrane adapter protein genetically linked to DAP12 but with unique signaling properties."
Chang C., Dietrich J., Harpur A.G., Lindquist J.A., Haude A., Loke Y.W., King A., Colonna M., Trowsdale J., Wilson M.J.
J. Immunol. 163:4651-4654(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCST.
[21]"cbl-b inhibits epidermal growth factor receptor signaling."
Ettenberg S.A., Keane M.M., Nau M.M., Frankel M., Wang L.-M., Pierce J.H., Lipkowitz S.
Oncogene 18:1855-1866(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLB.
[22]"Clustering of beta(2)-integrins on human neutrophils activates dual signaling pathways to PtdIns 3-kinase."
Axelsson L., Hellberg C., Melander F., Smith D., Zheng L., Andersson T.
Exp. Cell Res. 256:257-263(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGR AND HCK.
[23]"Ligand discrimination in signaling through an ErbB4 receptor homodimer."
Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C., Carraway K.L. III
J. Biol. Chem. 275:19803-19807(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4.
[24]"Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells."
Fang D., Wang H.-Y., Fang N., Altman Y., Elly C., Liu Y.-C.
J. Biol. Chem. 276:4872-4878(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLB, UBIQUITINATION.
[25]"Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells."
Fang D., Liu Y.-C.
Nat. Immunol. 2:870-875(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD3Z AND CD28, UBIQUITINATION.
[26]"Insulin receptor substrate 4 associates with the protein IRAS."
Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.
J. Biol. Chem. 277:19439-19447(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NISCH.
[27]"Molecular cloning of a novel gene encoding a membrane-associated adaptor protein (LAX) in lymphocyte signaling."
Zhu M., Janssen E., Leung K., Zhang W.
J. Biol. Chem. 277:46151-46158(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAX1.
[28]"Interaction between Nef and phosphatidylinositol-3-kinase leads to activation of p21-activated kinase and increased production of HIV."
Linnemann T., Zheng Y.-H., Mandic R., Peterlin B.M.
Virology 294:246-255(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 NEF.
[29]"Subversion of cell signaling pathways by hepatitis C virus nonstructural 5A protein via interaction with Grb2 and P85 phosphatidylinositol 3-kinase."
He Y., Nakao H., Tan S.-L., Polyak S.J., Neddermann P., Vijaysri S., Jacobs B.L., Katze M.G.
J. Virol. 76:9207-9217(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV NS5A.
[30]"TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma."
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A., Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A., Mackay A.R.
Cancer Cell 6:347-360(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NTRK1.
[31]"Signal transduction via the stem cell factor receptor/c-Kit."
Ronnstrand L.
Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON INTERACTION WITH KIT AND ROLE IN KIT SIGNALING.
[32]"The c-Fes tyrosine kinase cooperates with the breakpoint cluster region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-dependent manner."
Laurent C.E., Smithgall T.E.
Exp. Cell Res. 299:188-198(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCR.
[33]"The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY FGR.
[34]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase."
Tsuboi N., Utsunomiya T., Roberts R.L., Ito H., Takahashi K., Noda M., Takahashi T.
Biochem. J. 413:193-200(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ.
[36]"System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties."
Kaushansky A., Gordus A., Budnik B.A., Lane W.S., Rush J., MacBeath G.
Chem. Biol. 15:808-817(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4.
[37]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[38]"A novel interaction between fibroblast growth factor receptor 3 and the p85 subunit of phosphoinositide 3-kinase: activation-dependent regulation of ERK by p85 in multiple myeloma cells."
Salazar L., Kashiwada T., Krejci P., Muchowski P., Donoghue D., Wilcox W.R., Thompson L.M.
Hum. Mol. Genet. 18:1951-1961(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFR3.
[39]"Cellular signaling by fibroblast growth factor receptors."
Eswarakumar V.P., Lax I., Schlessinger J.
Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN FGFR1 SIGNALING AND PHOSPHORYLATION.
[40]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[42]"Agammaglobulinemia and absent B lineage cells in a patient lacking the p85? subunit of PI3K."
Conley M.E., Dobbs A.K., Quintana A.M., Bosompem A., Wang Y.D., Coustan-Smith E., Smith A.M., Perez E.E., Murray P.J.
J. Exp. Med. 209:463-470(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AGM7.
[43]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[44]"Crystal structure of P13K SH3 domain at 2.0-A resolution."
Liang J., Chen J.K., Schreiber S.L., Clardy J.
J. Mol. Biol. 257:632-643(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-85.
[45]"Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes."
Nolte R.T., Eck M.J., Schlessinger J., Shoelson S.E., Harrison S.C.
Nat. Struct. Biol. 3:364-373(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 324-434.
[46]"Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit."
Musacchio A., Cantley L.C., Harrison S.C.
Proc. Natl. Acad. Sci. U.S.A. 93:14373-14378(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 115-298.
[47]"NMR trial models: experiences with the colicin immunity protein Im7 and the p85alpha C-terminal SH2-peptide complex."
Pauptit R.A., Dennis C.A., Derbyshire D.J., Breeze A.L., Weston S.A., Rowsell S., Murshudov G.N.
Acta Crystallogr. D 57:1397-1404(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 617-724 IN COMPLEX WITH PDGFRB.
[48]"Structure of the PI3K SH3 domain and analysis of the SH3 family."
Koyama S., Yu H., Dalgarno D.C., Shin T.B., Zydowsky L.D., Schreiber S.L.
Cell 72:945-952(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-79.
[49]"Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase."
Renzoni D.A., Pugh D.J., Siligardi G., Das P., Morton C.J., Rossi C., Waterfield M.D., Campbell I.D., Ladbury J.E.
Biochemistry 35:15646-15653(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 91-104.
[50]"Structure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85 alpha subunit of phosphatidylinositol 3-kinase."
Breeze A.L., Kara B.V., Barratt D.G., Anderson M., Smith J.C., Luke R.W., Best J.R., Cartlidge S.A.
EMBO J. 15:3579-3589(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 617-724.
[51]"Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit."
Miled N., Yan Y., Hon W.C., Perisic O., Zvelebil M., Inbar Y., Schneidman-Duhovny D., Wolfson H.J., Backer J.M., Williams R.L.
Science 317:239-242(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 431-600, FUNCTION.
[52]"The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations."
Huang C.-H., Mandelker D., Schmidt-Kittler O., Samuels Y., Velculescu V.E., Kinzler K.W., Vogelstein B., Gabelli S.B., Amzel L.M.
Science 318:1744-1748(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 322-600.
[53]"A frequent kinase domain mutation that changes the interaction between PI3Kalpha and the membrane."
Mandelker D., Gabelli S.B., Schmidt-Kittler O., Zhu J., Cheong I., Huang C.H., Kinzler K.W., Vogelstein B., Amzel L.M.
Proc. Natl. Acad. Sci. U.S.A. 106:16996-17001(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 322-694, FUNCTION, SUBUNIT.
[54]"Structural studies of the phosphatidylinositol 3-kinase (PI3K) SH3 domain in complex with a peptide ligand: role of the anchor residue in ligand binding."
Batra-Safferling R., Granzin J., Modder S., Hoffmann S., Willbold D.
Biol. Chem. 391:33-42(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-83.
[55]"Identification of a common amino acid polymorphism in the p85alpha regulatory subunit of phosphatidylinositol 3-kinase: effects on glucose disappearance constant, glucose effectiveness, and the insulin sensitivity index."
Hansen T., Andersen C.B., Echwald S.M., Urhammer S.A., Clausen J.O., Vestergaard H., Owens D., Hansen L., Pedersen O.
Diabetes 46:494-501(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ILE-326.
[56]"Natural variants of human p85 alpha phosphoinositide 3-kinase in severe insulin resistance: a novel variant with impaired insulin-stimulated lipid kinase activity."
Baynes K.C.R., Beeton C.A., Panayotou G., Stein R., Soos M., Hansen T., Simpson H., O'Rahilly S., Shepherd P.R., Whitehead J.P.
Diabetologia 43:321-331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-326 AND GLN-409, CHARACTERIZATION OF VARIANTS ILE-326 AND GLN-409.
[57]"PIK3R1 mutations cause syndromic insulin resistance with lipoatrophy."
Thauvin-Robinet C., Auclair M., Duplomb L., Caron-Debarle M., Avila M., St-Onge J., Le Merrer M., Le Luyer B., Heron D., Mathieu-Dramard M., Bitoun P., Petit J.M., Odent S., Amiel J., Picot D., Carmignac V., Thevenon J., Callier P. expand/collapse author list , Laville M., Reznik Y., Fagour C., Nunes M.L., Capeau J., Lascols O., Huet F., Faivre L., Vigouroux C., Riviere J.B.
Am. J. Hum. Genet. 93:141-149(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SHORTS LYS-489 AND ILE-539 DEL.
[58]"SHORT syndrome with partial lipodystrophy due to impaired phosphatidylinositol 3 kinase signaling."
Chudasama K.K., Winnay J., Johansson S., Claudi T., Konig R., Haldorsen I., Johansson B., Woo J.R., Aarskog D., Sagen J.V., Kahn C.R., Molven A., Njolstad P.R.
Am. J. Hum. Genet. 93:150-157(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SHORTS TRP-649.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61906 mRNA. No translation available.
U49349 mRNA. Translation: AAB04140.1.
AF279367 mRNA. Translation: AAO15359.1.
AK094785 mRNA. Translation: BAG52931.1.
AK223613 mRNA. Translation: BAD97333.1.
AC016564 Genomic DNA. No translation available.
AC104120 Genomic DNA. No translation available.
CH471137 Genomic DNA. Translation: EAW51312.1.
CH471137 Genomic DNA. Translation: EAW51313.1.
BC030815 mRNA. Translation: AAH30815.1.
BC094795 mRNA. Translation: AAH94795.1.
CCDSCCDS3993.1. [P27986-1]
CCDS3994.1. [P27986-3]
CCDS3995.1. [P27986-2]
CCDS56374.1. [P27986-5]
PIRA38748.
RefSeqNP_001229395.1. NM_001242466.1. [P27986-5]
NP_852556.2. NM_181504.3. [P27986-2]
NP_852664.1. NM_181523.2. [P27986-1]
NP_852665.1. NM_181524.1. [P27986-3]
XP_005248599.1. XM_005248542.1. [P27986-1]
UniGeneHs.132225.
Hs.604502.
Hs.734132.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0NNMR-A91-104[»]
1AZGNMR-A91-104[»]
1H9OX-ray1.79A617-724[»]
1PBWX-ray2.00A/B105-319[»]
1PHTX-ray2.00A1-85[»]
1PICNMR-A617-724[»]
1PKSNMR-A1-79[»]
1PKTNMR-A1-79[»]
2IUGX-ray1.89A321-440[»]
2IUHX-ray2.00A321-440[»]
2IUIX-ray2.40A/B321-440[»]
2RD0X-ray3.05B322-600[»]
2V1YX-ray2.40B431-600[»]
3HHMX-ray2.80B322-694[»]
3HIZX-ray3.30B322-694[»]
3I5RX-ray1.70A1-83[»]
3I5SX-ray3.00A/B/C/D1-83[»]
4A55X-ray3.50B322-600[»]
4JPSX-ray2.20B307-593[»]
4L1BX-ray2.59B318-615[»]
4L23X-ray2.50B318-615[»]
4L2YX-ray2.80B318-615[»]
ProteinModelPortalP27986.
SMRP27986. Positions 3-85, 115-309, 322-724.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111313. 126 interactions.
DIPDIP-119N.
IntActP27986. 190 interactions.
MINTMINT-93751.
STRING9606.ENSP00000274335.

Chemistry

BindingDBP27986.
ChEMBLCHEMBL2506.
DrugBankDB01064. Isoproterenol.

PTM databases

PhosphoSiteP27986.

Polymorphism databases

DMDM118572681.

Proteomic databases

MaxQBP27986.
PaxDbP27986.
PRIDEP27986.

Protocols and materials databases

DNASU5295.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274335; ENSP00000274335; ENSG00000145675. [P27986-1]
ENST00000320694; ENSP00000323512; ENSG00000145675. [P27986-3]
ENST00000336483; ENSP00000338554; ENSG00000145675. [P27986-2]
ENST00000396611; ENSP00000379855; ENSG00000145675. [P27986-4]
ENST00000521381; ENSP00000428056; ENSG00000145675. [P27986-1]
ENST00000521657; ENSP00000429277; ENSG00000145675. [P27986-1]
ENST00000523872; ENSP00000430098; ENSG00000145675. [P27986-5]
GeneID5295.
KEGGhsa:5295.
UCSCuc003jva.3. human. [P27986-1]
uc003jvc.3. human. [P27986-3]
uc003jvd.3. human. [P27986-2]

Organism-specific databases

CTD5295.
GeneCardsGC05P067511.
HGNCHGNC:8979. PIK3R1.
HPACAB004268.
HPA001216.
MIM171833. gene.
269880. phenotype.
615214. phenotype.
neXtProtNX_P27986.
Orphanet33110. Autosomal agammaglobulinemia.
3163. SHORT syndrome.
PharmGKBPA33312.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263689.
HOVERGENHBG082100.
KOK02649.
OMALNGYNET.
OrthoDBEOG7BP831.
PhylomeDBP27986.
TreeFamTF102033.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000145675-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP27986.

Gene expression databases

ArrayExpressP27986.
BgeeP27986.
CleanExHS_PIK3R1.
GenevestigatorP27986.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
3.30.505.10. 2 hits.
InterProIPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10155. PTHR10155. 1 hit.
PfamPF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR00678. PI3KINASEP85.
PR00401. SH2DOMAIN.
SMARTSM00324. RhoGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEPS50238. RHOGAP. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIK3R1. human.
EvolutionaryTraceP27986.
GeneWikiPIK3R1.
GenomeRNAi5295.
NextBio20462.
PROP27986.
SOURCESearch...

Entry information

Entry nameP85A_HUMAN
AccessionPrimary (citable) accession number: P27986
Secondary accession number(s): B3KT19 expand/collapse secondary AC list , D3DWA0, E7EX19, Q15747, Q4VBZ7, Q53EM6, Q8IXA2, Q8N1C5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM