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P27986

- P85A_HUMAN

UniProt

P27986 - P85A_HUMAN

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Protein

Phosphatidylinositol 3-kinase regulatory subunit alpha

Gene

PIK3R1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. ErbB-3 class receptor binding Source: UniProtKB
  2. insulin binding Source: UniProtKB
  3. insulin-like growth factor receptor binding Source: UniProtKB
  4. insulin receptor binding Source: UniProtKB
  5. insulin receptor substrate binding Source: BHF-UCL
  6. neurotrophin TRKA receptor binding Source: UniProtKB
  7. phosphatidylinositol 3-kinase binding Source: BHF-UCL
  8. phosphatidylinositol 3-kinase regulator activity Source: UniProtKB
  9. protein phosphatase binding Source: UniProtKB
  10. transmembrane receptor protein tyrosine kinase adaptor activity Source: BHF-UCL

GO - Biological processi

  1. B cell differentiation Source: Ensembl
  2. blood coagulation Source: Reactome
  3. cellular response to UV Source: Ensembl
  4. epidermal growth factor receptor signaling pathway Source: Reactome
  5. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  6. Fc-epsilon receptor signaling pathway Source: Reactome
  7. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  8. fibroblast growth factor receptor signaling pathway Source: Reactome
  9. growth hormone receptor signaling pathway Source: BHF-UCL
  10. innate immune response Source: Reactome
  11. insulin-like growth factor receptor signaling pathway Source: UniProtKB
  12. insulin receptor signaling pathway Source: Reactome
  13. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  14. leukocyte migration Source: Reactome
  15. negative regulation of apoptotic process Source: Ensembl
  16. negative regulation of cell-matrix adhesion Source: Ensembl
  17. negative regulation of osteoclast differentiation Source: Ensembl
  18. neurotrophin TRK receptor signaling pathway Source: Reactome
  19. NFAT protein import into nucleus Source: Ensembl
  20. phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  21. phosphatidylinositol biosynthetic process Source: Reactome
  22. phosphatidylinositol-mediated signaling Source: Reactome
  23. phosphatidylinositol phosphorylation Source: UniProtKB
  24. phospholipid metabolic process Source: Reactome
  25. platelet activation Source: Reactome
  26. positive regulation of cell migration Source: Ensembl
  27. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  28. positive regulation of glucose import Source: BHF-UCL
  29. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  30. positive regulation of tumor necrosis factor production Source: Ensembl
  31. protein phosphorylation Source: Ensembl
  32. regulation of phosphatidylinositol 3-kinase activity Source: BHF-UCL
  33. small molecule metabolic process Source: Reactome
  34. T cell costimulation Source: Reactome
  35. T cell receptor signaling pathway Source: Reactome
  36. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000145675-MONOMER.
ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_115529. Interleukin-7 signaling.
REACT_115852. Signaling by constitutively active EGFR.
REACT_115961. PI3K events in ERBB4 signaling.
REACT_116008. PI3K events in ERBB2 signaling.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_121398. Signaling by FGFR mutants.
REACT_12464. PI3K/AKT activation.
REACT_12555. Downstream TCR signaling.
REACT_12578. GAB1 signalosome.
REACT_12621. Tie2 Signaling.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_147814. DAP12 signaling.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_1695. GPVI-mediated activation cascade.
REACT_17025. Downstream signal transduction.
REACT_18283. G alpha (q) signalling events.
REACT_18407. G alpha (12/13) signalling events.
REACT_19344. Costimulation by the CD28 family.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_21270. PI-3K cascade.
REACT_23787. Regulation of signaling by CBL.
REACT_23832. Nephrin interactions.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23847. GP1b-IX-V activation signalling.
REACT_23891. Interleukin receptor SHC signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_976. PI3K Cascade.
SignaLinkiP27986.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PIK3R1
Synonyms:GRB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:8979. PIK3R1.

Subcellular locationi

GO - Cellular componenti

  1. 1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex Source: UniProtKB
  2. cell-cell junction Source: Ensembl
  3. cytosol Source: Reactome
  4. membrane Source: UniProtKB
  5. phosphatidylinositol 3-kinase complex Source: BHF-UCL
  6. plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti489 – 4891E → 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. 1 Publication
VAR_070221
Natural varianti539 – 5391Missing 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. 1 Publication
VAR_070222
Natural varianti649 – 6491R → W in SHORTS; impairs interaction between PIK3R1 and IRS1 and reduces AKT1-mediated insulin signaling. 1 Publication
VAR_070223

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi269880. phenotype.
615214. phenotype.
Orphaneti33110. Autosomal agammaglobulinemia.
3163. SHORT syndrome.
PharmGKBiPA33312.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 724723Phosphatidylinositol 3-kinase regulatory subunit alphaPRO_0000080758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei467 – 4671PhosphotyrosineBy similarity
Modified residuei580 – 5801Phosphotyrosine1 Publication
Modified residuei608 – 6081PhosphoserineBy similarity

Post-translational modificationi

Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation.2 Publications
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.By similarity3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP27986.
PaxDbiP27986.
PRIDEiP27986.

PTM databases

PhosphoSiteiP27986.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

BgeeiP27986.
CleanExiHS_PIK3R1.
ExpressionAtlasiP27986. baseline and differential.
GenevestigatoriP27986.

Organism-specific databases

HPAiCAB004268.
HPA001216.

Interactioni

Subunit structurei

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).By similarity28 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP08EBI-79464,EBI-375446
ABL2P426842EBI-79464,EBI-1102694
ARP102755EBI-79464,EBI-608057
CBLP226815EBI-79464,EBI-518228
CD28P107478EBI-79464,EBI-4314301
CMIPQ8IY222EBI-79464,EBI-7689652
CRKP461082EBI-79464,EBI-886
CRKLP461092EBI-79464,EBI-910
CTLA4P164103EBI-79464,EBI-1030991
DLGAP4Q9Y2H02EBI-79464,EBI-722139
EGFRP005335EBI-79464,EBI-297353
ERBB2P0462611EBI-79464,EBI-641062
ERBB3P2186040EBI-79464,EBI-720706
ESR1P033726EBI-79464,EBI-78473
FASLGP480232EBI-79464,EBI-495538
FGFR1P113625EBI-79464,EBI-1028277
FLT1P179482EBI-79464,EBI-1026718
FLT3P368882EBI-79464,EBI-3946257
GAB1Q1348033EBI-79464,EBI-517684
GRB2P629933EBI-79464,EBI-401755
HTTP428587EBI-79464,EBI-466029
IGF1RP080694EBI-79464,EBI-475981
INSRP062133EBI-79464,EBI-475899
IRS1P3556812EBI-79464,EBI-517592
Irs1P355702EBI-79464,EBI-520230From a different organism.
IRS2Q9Y4H22EBI-79464,EBI-1049582
KITP1072119EBI-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.
PDGFRBP0961919EBI-79464,EBI-641237
PIK3CAP4233613EBI-79464,EBI-2116585
PLCG2P168852EBI-79464,EBI-617403
PXNP490232EBI-79464,EBI-702209
RAPGEF1Q139052EBI-79464,EBI-976876
RPL13P263732EBI-79464,EBI-356849
RXRAP197938EBI-79464,EBI-78598
SHANK2Q9UPX82EBI-79464,EBI-1570571
SHC1P293533EBI-79464,EBI-78835
SIRT1Q96EB63EBI-79464,EBI-1802965
SOS1Q078893EBI-79464,EBI-297487
SRCP129316EBI-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

Protein-protein interaction databases

BioGridi111313. 133 interactions.
DIPiDIP-119N.
IntActiP27986. 196 interactions.
MINTiMINT-93751.
STRINGi9606.ENSP00000274335.

Structurei

Secondary structure

1
724
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107
Beta strandi29 – 335
Helixi34 – 407
Turni43 – 453
Helixi46 – 483
Helixi50 – 534
Beta strandi55 – 606
Turni61 – 644
Beta strandi65 – 706
Helixi71 – 733
Beta strandi74 – 818
Turni100 – 1023
Helixi118 – 1214
Helixi130 – 14314
Turni147 – 1504
Helixi160 – 1645
Beta strandi167 – 1704
Helixi174 – 1763
Helixi179 – 19113
Beta strandi193 – 1953
Helixi200 – 20910
Helixi210 – 2123
Helixi216 – 22712
Helixi234 – 25219
Helixi254 – 2574
Helixi261 – 27313
Helixi280 – 29516
Helixi323 – 3253
Helixi326 – 3294
Beta strandi334 – 3374
Helixi340 – 3478
Beta strandi354 – 3596
Helixi363 – 3653
Beta strandi367 – 3748
Beta strandi377 – 38610
Beta strandi389 – 3957
Beta strandi398 – 4003
Helixi401 – 41010
Helixi413 – 4153
Helixi418 – 4203
Turni430 – 4323
Helixi433 – 4364
Helixi442 – 51574
Helixi518 – 58770
Helixi591 – 5988
Helixi617 – 6193
Helixi621 – 6233
Beta strandi625 – 6295
Helixi631 – 6388
Beta strandi645 – 6506
Beta strandi652 – 6554
Beta strandi657 – 6637
Beta strandi666 – 67510
Beta strandi678 – 6825
Beta strandi688 – 6903
Helixi691 – 70010
Helixi703 – 7053
Turni708 – 7103
Beta strandi716 – 7194

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4OVUX-ray2.96B322-600[»]
4OVVX-ray3.50B322-600[»]
ProteinModelPortaliP27986.
SMRiP27986. Positions 3-85, 115-309, 322-724.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27986.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7977SH3PROSITE-ProRule annotationAdd
BLAST
Domaini113 – 301189Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini333 – 42896SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini624 – 71895SH2 2PROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the PI3K p85 subunit family.Curated
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 2 SH2 domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG263689.
GeneTreeiENSGT00390000010431.
HOVERGENiHBG082100.
InParanoidiP27986.
KOiK02649.
OMAiLNGYNET.
OrthoDBiEOG7BP831.
PhylomeDBiP27986.
TreeFamiTF102033.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10155. PTHR10155. 1 hit.
PfamiPF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR00678. PI3KINASEP85.
PR00401. SH2DOMAIN.
SMARTiSM00324. RhoGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P27986-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEARP
60 70 80 90 100
EEIGWLNGYN ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG
110 120 130 140 150
SSKTEADVEQ QALTLPDLAE QFAPPDIAPP LLIKLVEAIE KKGLECSTLY
160 170 180 190 200
RTQSSSNLAE LRQLLDCDTP SVDLEMIDVH VLADAFKRYL LDLPNPVIPA
210 220 230 240 250
AVYSEMISLA PEVQSSEEYI QLLKKLIRSP SIPHQYWLTL QYLLKHFFKL
260 270 280 290 300
SQTSSKNLLN ARVLSEIFSP MLFRFSAASS DNTENLIKVI EILISTEWNE
310 320 330 340 350
RQPAPALPPK PPKPTTVANN GMNNNMSLQD AEWYWGDISR EEVNEKLRDT
360 370 380 390 400
ADGTFLVRDA STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFSS
410 420 430 440 450
VVELINHYRN ESLAQYNPKL DVKLLYPVSK YQQDQVVKED NIEAVGKKLH
460 470 480 490 500
EYNTQFQEKS REYDRLYEEY TRTSQEIQMK RTAIEAFNET IKIFEEQCQT
510 520 530 540 550
QERYSKEYIE KFKREGNEKE IQRIMHNYDK LKSRISEIID SRRRLEEDLK
560 570 580 590 600
KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN
610 620 630 640 650
ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE
660 670 680 690 700
SSKQGCYACS VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH
710 720
TSLVQHNDSL NVTLAYPVYA QQRR
Length:724
Mass (Da):83,598
Last modified:November 28, 2006 - v2
Checksum:iB9DAD8416C33140F
GO
Isoform 2 (identifier: P27986-2) [UniParc]FASTAAdd to Basket

Also known as: AS53

The sequence of this isoform differs from the canonical sequence as follows:
     1-270: Missing.
     271-304: MLFRFSAASSDNTENLIKVIEILISTEWNERQPA → MYNTVWNMEDLDLEYAKTDINCGTDLMFYIEMDP

Show »
Length:454
Mass (Da):53,486
Checksum:i33BB0F88AA47CB3F
GO
Isoform 3 (identifier: P27986-3) [UniParc]FASTAAdd to Basket

Also known as: p46

The sequence of this isoform differs from the canonical sequence as follows:
     1-300: Missing.
     301-306: RQPAPA → MHNLQT

Show »
Length:424
Mass (Da):49,965
Checksum:iEF2D6D4D668C62D8
GO
Isoform 4 (identifier: P27986-4) [UniParc]FASTAAdd to Basket

Also known as: p85I

The sequence of this isoform differs from the canonical sequence as follows:
     605-605: D → ENFLSCLPS

Show »
Length:732
Mass (Da):84,474
Checksum:iF4820A783035803A
GO
Isoform 5 (identifier: P27986-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-363: Missing.

Note: No experimental confirmation available.

Show »
Length:361
Mass (Da):42,838
Checksum:i100325CF4D673C4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti330 – 3301D → N in M61906. (PubMed:1849461)Curated
Sequence conflicti460 – 4601S → G in BAG52931. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti326 – 3261M → I Does not affect insulin-stimulated lipid kinase activity. 3 Publications
Corresponds to variant rs3730089 [ dbSNP | Ensembl ].
VAR_010023
Natural varianti409 – 4091R → Q in a patient with severe insulin resistance; lower insulin-stimulated lipid kinase activity compared with wild-type. 1 Publication
VAR_010024
Natural varianti451 – 4511E → K.1 Publication
Corresponds to variant rs17852841 [ dbSNP | Ensembl ].
VAR_029562
Natural varianti489 – 4891E → 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. 1 Publication
VAR_070221
Natural varianti539 – 5391Missing 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. 1 Publication
VAR_070222
Natural varianti649 – 6491R → W in SHORTS; impairs interaction between PIK3R1 and IRS1 and reduces AKT1-mediated insulin signaling. 1 Publication
VAR_070223

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 363363Missing in isoform 5. 1 PublicationVSP_045903Add
BLAST
Alternative sequencei1 – 300300Missing in isoform 3. 1 PublicationVSP_021841Add
BLAST
Alternative sequencei1 – 270270Missing in isoform 2. 3 PublicationsVSP_021842Add
BLAST
Alternative sequencei271 – 30434MLFRF…ERQPA → MYNTVWNMEDLDLEYAKTDI NCGTDLMFYIEMDP in isoform 2. 3 PublicationsVSP_021843Add
BLAST
Alternative sequencei301 – 3066RQPAPA → MHNLQT in isoform 3. 1 PublicationVSP_021844
Alternative sequencei605 – 6051D → ENFLSCLPS in isoform 4. 1 PublicationVSP_021845

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3993.1. [P27986-1]
CCDS3994.1. [P27986-3]
CCDS3995.1. [P27986-2]
CCDS56374.1. [P27986-5]
PIRiA38748.
RefSeqiNP_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]
UniGeneiHs.132225.
Hs.604502.
Hs.734132.

Genome annotation databases

EnsembliENST00000320694; ENSP00000323512; ENSG00000145675. [P27986-3]
ENST00000336483; ENSP00000338554; ENSG00000145675. [P27986-2]
ENST00000521381; ENSP00000428056; ENSG00000145675. [P27986-1]
ENST00000521657; ENSP00000429277; ENSG00000145675. [P27986-1]
ENST00000523872; ENSP00000430098; ENSG00000145675. [P27986-5]
GeneIDi5295.
KEGGihsa:5295.
UCSCiuc003jva.3. human. [P27986-1]
uc003jvc.3. human. [P27986-3]
uc003jvd.3. human. [P27986-2]

Polymorphism databases

DMDMi118572681.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3993.1. [P27986-1 ]
CCDS3994.1. [P27986-3 ]
CCDS3995.1. [P27986-2 ]
CCDS56374.1. [P27986-5 ]
PIRi A38748.
RefSeqi NP_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 ]
UniGenei Hs.132225.
Hs.604502.
Hs.734132.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A0N NMR - A 91-104 [» ]
1AZG NMR - A 91-104 [» ]
1H9O X-ray 1.79 A 617-724 [» ]
1PBW X-ray 2.00 A/B 105-319 [» ]
1PHT X-ray 2.00 A 1-85 [» ]
1PIC NMR - A 617-724 [» ]
1PKS NMR - A 1-79 [» ]
1PKT NMR - A 1-79 [» ]
2IUG X-ray 1.89 A 321-440 [» ]
2IUH X-ray 2.00 A 321-440 [» ]
2IUI X-ray 2.40 A/B 321-440 [» ]
2RD0 X-ray 3.05 B 322-600 [» ]
2V1Y X-ray 2.40 B 431-600 [» ]
3HHM X-ray 2.80 B 322-694 [» ]
3HIZ X-ray 3.30 B 322-694 [» ]
3I5R X-ray 1.70 A 1-83 [» ]
3I5S X-ray 3.00 A/B/C/D 1-83 [» ]
4A55 X-ray 3.50 B 322-600 [» ]
4JPS X-ray 2.20 B 307-593 [» ]
4L1B X-ray 2.59 B 318-615 [» ]
4L23 X-ray 2.50 B 318-615 [» ]
4L2Y X-ray 2.80 B 318-615 [» ]
4OVU X-ray 2.96 B 322-600 [» ]
4OVV X-ray 3.50 B 322-600 [» ]
ProteinModelPortali P27986.
SMRi P27986. Positions 3-85, 115-309, 322-724.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111313. 133 interactions.
DIPi DIP-119N.
IntActi P27986. 196 interactions.
MINTi MINT-93751.
STRINGi 9606.ENSP00000274335.

Chemistry

BindingDBi P27986.
ChEMBLi CHEMBL2111367.
DrugBanki DB01064. Isoprenaline.

PTM databases

PhosphoSitei P27986.

Polymorphism databases

DMDMi 118572681.

Proteomic databases

MaxQBi P27986.
PaxDbi P27986.
PRIDEi P27986.

Protocols and materials databases

DNASUi 5295.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320694 ; ENSP00000323512 ; ENSG00000145675 . [P27986-3 ]
ENST00000336483 ; ENSP00000338554 ; ENSG00000145675 . [P27986-2 ]
ENST00000521381 ; ENSP00000428056 ; ENSG00000145675 . [P27986-1 ]
ENST00000521657 ; ENSP00000429277 ; ENSG00000145675 . [P27986-1 ]
ENST00000523872 ; ENSP00000430098 ; ENSG00000145675 . [P27986-5 ]
GeneIDi 5295.
KEGGi hsa:5295.
UCSCi uc003jva.3. human. [P27986-1 ]
uc003jvc.3. human. [P27986-3 ]
uc003jvd.3. human. [P27986-2 ]

Organism-specific databases

CTDi 5295.
GeneCardsi GC05P067511.
HGNCi HGNC:8979. PIK3R1.
HPAi CAB004268.
HPA001216.
MIMi 171833. gene.
269880. phenotype.
615214. phenotype.
neXtProti NX_P27986.
Orphaneti 33110. Autosomal agammaglobulinemia.
3163. SHORT syndrome.
PharmGKBi PA33312.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG263689.
GeneTreei ENSGT00390000010431.
HOVERGENi HBG082100.
InParanoidi P27986.
KOi K02649.
OMAi LNGYNET.
OrthoDBi EOG7BP831.
PhylomeDBi P27986.
TreeFami TF102033.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000145675-MONOMER.
Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_115529. Interleukin-7 signaling.
REACT_115852. Signaling by constitutively active EGFR.
REACT_115961. PI3K events in ERBB4 signaling.
REACT_116008. PI3K events in ERBB2 signaling.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_121398. Signaling by FGFR mutants.
REACT_12464. PI3K/AKT activation.
REACT_12555. Downstream TCR signaling.
REACT_12578. GAB1 signalosome.
REACT_12621. Tie2 Signaling.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_147814. DAP12 signaling.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_1695. GPVI-mediated activation cascade.
REACT_17025. Downstream signal transduction.
REACT_18283. G alpha (q) signalling events.
REACT_18407. G alpha (12/13) signalling events.
REACT_19344. Costimulation by the CD28 family.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_21270. PI-3K cascade.
REACT_23787. Regulation of signaling by CBL.
REACT_23832. Nephrin interactions.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23847. GP1b-IX-V activation signalling.
REACT_23891. Interleukin receptor SHC signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_976. PI3K Cascade.
SignaLinki P27986.

Miscellaneous databases

ChiTaRSi PIK3R1. human.
EvolutionaryTracei P27986.
GeneWikii PIK3R1.
GenomeRNAii 5295.
NextBioi 20462.
PROi P27986.
SOURCEi Search...

Gene expression databases

Bgeei P27986.
CleanExi HS_PIK3R1.
ExpressionAtlasi P27986. baseline and differential.
Genevestigatori P27986.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
3.30.505.10. 2 hits.
InterProi IPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR10155. PTHR10155. 1 hit.
Pfami PF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
PF07653. SH3_2. 1 hit.
[Graphical view ]
PRINTSi PR00678. PI3KINASEP85.
PR00401. SH2DOMAIN.
SMARTi SM00324. RhoGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEi PS50238. RHOGAP. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiP85A_HUMAN
AccessioniPrimary (citable) accession number: P27986
Secondary accession number(s): B3KT19
, D3DWA0, E7EX19, Q15747, Q4VBZ7, Q53EM6, Q8IXA2, Q8N1C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 28, 2006
Last modified: October 29, 2014
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3