P27986 (P85A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PIK3R1
Synonyms:	GRB1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	724 AA.
Sequence status	Complete.
Protein existence	Evidence 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.49 Ref.51
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.51
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
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 process	Host-virus interaction
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH2 domain SH3 domain
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from electronic annotation. Source: Compara NFAT protein import into nucleus Inferred from electronic annotation. Source: Compara T cell costimulation Traceable author statement. Source: Reactome T cell receptor signaling pathway Traceable author statement. Source: Reactome cellular response to UV Inferred from electronic annotation. Source: Compara epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome 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 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 leukocyte migration Traceable author statement. Source: Reactome negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of cell-matrix adhesion Inferred from electronic annotation. Source: Compara negative regulation of osteoclast differentiation Inferred from electronic annotation. Source: Compara nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome phosphatidylinositol 3-kinase cascade 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 platelet activation Traceable author statement. Source: Reactome positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara 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: Compara protein phosphorylation Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome
Molecular_function	1-phosphatidylinositol binding Non-traceable author statement. Source: UniProtKB ErbB-3 class receptor binding Inferred from direct assay PubMed 10572067. Source: UniProtKB insulin binding Inferred from direct assay PubMed 8440175. Source: UniProtKB insulin receptor substrate binding Inferred from sequence or structural similarity. Source: BHF-UCL 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 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
ABL2	P42684	2	EBI-79464,EBI-1102694
COBRA1	Q8WX92	2	EBI-79464,EBI-347721
DLGAP4	Q9Y2H0	2	EBI-79464,EBI-722139
ERBB3	P21860	23	EBI-79464,EBI-720706
GRB2	P62993	3	EBI-79464,EBI-401755
LAPTM4B	Q86VI4-3	2	EBI-79464,EBI-3267286
MAP4K1	Q92918	2	EBI-79464,EBI-881
PIK3CA	P42336	2	EBI-79464,EBI-2116585
RAPGEF1	Q13905	2	EBI-79464,EBI-976876
RPL13	P26373	2	EBI-79464,EBI-356849
RXRA	P19793	8	EBI-79464,EBI-78598
SHANK2	Q9UPX8	2	EBI-79464,EBI-1570571
SIRT1	Q96EB6	3	EBI-79464,EBI-1802965
SOS1	Q07889	2	EBI-79464,EBI-297487
TPSAB1	Q15661	2	EBI-79464,EBI-1761369
TPX2	Q9ULW0	2	EBI-79464,EBI-1037322

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 724

724

Phosphatidylinositol 3-kinase regulatory subunit alpha

PRO_0000080758

Regions

Domain

3 – 79

77

SH3

Domain

113 – 301

189

Rho-GAP

Domain

333 – 428

96

SH2 1

Domain

624 – 718

95

SH2 2

Amino acid modifications

Modified residue

467

1

Phosphotyrosine By similarity

Modified residue

580

1

Phosphotyrosine Ref.40

Modified residue

607

1

Phosphotyrosine By similarity

Modified residue

608

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 363

363

Missing in isoform 5.

VSP_045903

Alternative sequence

1 – 300

300

Missing in isoform 3.

VSP_021841

Alternative sequence

1 – 270

270

Missing in isoform 2.

VSP_021842

Alternative sequence

271 – 304

34

MLFRF…ERQPA → MYNTVWNMEDLDLEYAKTDI NCGTDLMFYIEMDP in isoform 2.

VSP_021843

Alternative sequence

301 – 306

6

RQPAPA → MHNLQT in isoform 3.

VSP_021844

Alternative sequence

605

1

D → ENFLSCLPS in isoform 4.

VSP_021845

Natural variant

326

1

M → I Does not affect insulin-stimulated lipid kinase activity. Ref.5 Ref.53 Ref.54
Corresponds to variant rs3730089 [ dbSNP | Ensembl ].

VAR_010023

Natural variant

409

1

R → Q in a patient with severe insulin resistance; lower insulin-stimulated lipid kinase activity compared with wild-type. Ref.54

VAR_010024

Natural variant

451

1

E → K. Ref.8
Corresponds to variant rs17852841 [ dbSNP | Ensembl ].

VAR_029562

Experimental info

Sequence conflict

330

1

D → N in M61906. Ref.1

Sequence conflict

460

1

S → G in BAG52931. Ref.4

Secondary structure

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724

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Beta strand

29 – 33

5

Helix

34 – 40

7

Turn

43 – 45

3

Helix

46 – 48

3

Helix

50 – 53

4

Beta strand

55 – 60

6

Turn

61 – 64

4

Beta strand

65 – 70

6

Helix

71 – 73

3

Beta strand

74 – 81

8

Turn

100 – 102

3

Helix

118 – 121

4

Helix

130 – 143

14

Turn

147 – 150

4

Helix

160 – 164

5

Beta strand

167 – 170

4

Helix

174 – 176

3

Helix

179 – 191

13

Beta strand

193 – 195

3

Helix

200 – 209

10

Helix

210 – 212

3

Helix

216 – 227

12

Helix

234 – 252

19

Helix

254 – 257

4

Helix

261 – 273

13

Helix

280 – 295

16

Helix

326 – 329

4

Beta strand

334 – 337

4

Helix

340 – 347

8

Beta strand

354 – 359

6

Helix

363 – 365

3

Beta strand

367 – 374

8

Beta strand

377 – 386

10

Beta strand

389 – 395

7

Beta strand

398 – 400

3

Helix

401 – 410

10

Helix

413 – 415

3

Helix

418 – 420

3

Turn

430 – 432

3

Helix

439 – 512

74

Turn

513 – 516

4

Helix

518 – 586

69

Helix

591 – 598

8

Helix

617 – 619

3

Helix

621 – 623

3

Beta strand

625 – 629

5

Helix

631 – 638

8

Beta strand

645 – 650

6

Beta strand

652 – 655

4

Beta strand

657 – 663

7

Beta strand

666 – 675

10

Beta strand

678 – 682

5

Beta strand

688 – 690

3

Helix

691 – 700

10

Helix

703 – 705

3

Turn

708 – 710

3

Beta strand

716 – 719

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: B9DAD8416C33140F	FASTA	724	83,598
	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
	Isoform 2 (AS53) [UniParc]. Checksum: 33BB0F88AA47CB3F	FASTA	454	53,486
	10 20 30 40 50 60 MYNTVWNMED LDLEYAKTDI NCGTDLMFYI EMDPPALPPK PPKPTTVANN GMNNNMSLQD 70 80 90 100 110 120 AEWYWGDISR EEVNEKLRDT ADGTFLVRDA STKMHGDYTL TLRKGGNNKL IKIFHRDGKY 130 140 150 160 170 180 GFSDPLTFSS VVELINHYRN ESLAQYNPKL DVKLLYPVSK YQQDQVVKED NIEAVGKKLH 190 200 210 220 230 240 EYNTQFQEKS REYDRLYEEY TRTSQEIQMK RTAIEAFNET IKIFEEQCQT QERYSKEYIE 250 260 270 280 290 300 KFKREGNEKE IQRIMHNYDK LKSRISEIID SRRRLEEDLK KQAAEYREID KRMNSIKPDL 310 320 330 340 350 360 IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN 370 380 390 400 410 420 RNKAENLLRG KRDGTFLVRE SSKQGCYACS VVVDGEVKHC VINKTATGYG FAEPYNLYSS 430 440 450 LKELVLHYQH TSLVQHNDSL NVTLAYPVYA QQRR
	Isoform 3 (p46) [UniParc]. Checksum: EF2D6D4D668C62D8	FASTA	424	49,965
	10 20 30 40 50 60 MHNLQTLPPK PPKPTTVANN GMNNNMSLQD AEWYWGDISR EEVNEKLRDT ADGTFLVRDA 70 80 90 100 110 120 STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFSS VVELINHYRN ESLAQYNPKL 130 140 150 160 170 180 DVKLLYPVSK YQQDQVVKED NIEAVGKKLH EYNTQFQEKS REYDRLYEEY TRTSQEIQMK 190 200 210 220 230 240 RTAIEAFNET IKIFEEQCQT QERYSKEYIE KFKREGNEKE IQRIMHNYDK LKSRISEIID 250 260 270 280 290 300 SRRRLEEDLK KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN 310 320 330 340 350 360 ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE SSKQGCYACS 370 380 390 400 410 420 VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH TSLVQHNDSL NVTLAYPVYA QQRR
	Isoform 4 (p85I) [UniParc]. Checksum: F4820A783035803A	FASTA	732	84,474
	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 ENTEENFLSC LPSQYSLVED DEDLPHHDEK TWNVGSSNRN KAENLLRGKR DGTFLVRESS 670 680 690 700 710 720 KQGCYACSVV VDGEVKHCVI NKTATGYGFA EPYNLYSSLK ELVLHYQHTS LVQHNDSLNV 730 TLAYPVYAQQ RR
	Isoform 5 [UniParc]. Checksum: 100325CF4D673C4B	FASTA	361	42,838
	10 20 30 40 50 60 MHGDYTLTLR KGGNNKLIKI FHRDGKYGFS DPLTFSSVVE LINHYRNESL AQYNPKLDVK 70 80 90 100 110 120 LLYPVSKYQQ DQVVKEDNIE AVGKKLHEYN TQFQEKSREY DRLYEEYTRT SQEIQMKRTA 130 140 150 160 170 180 IEAFNETIKI FEEQCQTQER YSKEYIEKFK REGNEKEIQR IMHNYDKLKS RISEIIDSRR 190 200 210 220 230 240 RLEEDLKKQA AEYREIDKRM NSIKPDLIQL RKTRDQYLMW LTQKGVRQKK LNEWLGNENT 250 260 270 280 290 300 EDQYSLVEDD EDLPHHDEKT WNVGSSNRNK AENLLRGKRD GTFLVRESSK QGCYACSVVV 310 320 330 340 350 360 DGEVKHCVIN KTATGYGFAE PYNLYSSLKE LVLHYQHTSL VQHNDSLNVT LAYPVYAQQR R

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY.
[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]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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.
[54]	"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.
+	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.

IPI

IPI00021448.
IPI00295788.
IPI00333040.
IPI00807573.
IPI00983869.

PIR

A38748.

RefSeq

NP_001229395.1. NM_001242466.1.
NP_852556.2. NM_181504.3.
NP_852664.1. NM_181523.2.
NP_852665.1. NM_181524.1.

UniGene

Hs.132225.
Hs.604502.
Hs.734132.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P27986.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-119N.

IntAct

P27986. 129 interactions.

MINT

MINT-93751.

STRING

9606.ENSP00000274335.

PTM databases

PhosphoSite

P27986.

Polymorphism databases

DMDM

118572681.

Proteomic databases

PaxDb

P27986.

PRIDE

P27986.

Protocols and materials databases

DNASU

5295.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000274335; ENSP00000274335; ENSG00000145675.
ENST00000320694; ENSP00000323512; ENSG00000145675.
ENST00000336483; ENSP00000338554; ENSG00000145675.
ENST00000396611; ENSP00000379855; ENSG00000145675.
ENST00000521381; ENSP00000428056; ENSG00000145675.
ENST00000521657; ENSP00000429277; ENSG00000145675.
ENST00000523872; ENSP00000430098; ENSG00000145675.

GeneID

5295.

KEGG

hsa:5295.

UCSC

uc003jva.3. human.
uc003jvc.3. human.
uc003jvd.3. human.

Organism-specific databases

CTD

5295.

GeneCards

GC05P067511.

HGNC

HGNC:8979. PIK3R1.

HPA

CAB004268.
HPA001216.

MIM

171833. gene.

neXtProt

NX_P27986.

PharmGKB

PA33312.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG263689.

HOVERGEN

HBG082100.

KO

K02649.

OMA

RPEEIGW.

OrthoDB

EOG4GXFM8.

PhylomeDB

P27986.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000145675-MONOMER.

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
arf6cyclingpathway. Arf6 signaling events.
nfkappabatypicalpathway. Atypical NF-kappaB pathway.
bcr_5pathway. BCR signaling pathway.
pi3kcipathway. Class I PI3K signaling events.
epha2_fwdpathway. EPHA2 forward signaling.
ephbfwdpathway. EPHB forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
epopathway. EPO signaling pathway.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
fgf_pathway. FGF signaling pathway.
ifngpathway. IFN-gamma pathway.
igf1_pathway. IGF1 pathway.
il1pathway. IL1-mediated signaling events.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il2_stat5pathway. IL2 signaling events mediated by STAT5.
il2_1pathway. IL2-mediated signaling events.
il23pathway. IL23-mediated signaling events.
il4_2pathway. IL4-mediated signaling events.
il6_7pathway. IL6-mediated signaling events.
insulin_pathway. Insulin Pathway.
avb3_integrin_pathway. Integrins in angiogenesis.
lysophospholipid_pathway. LPA receptor mediated events.
mtor_4pathway. mTOR signaling pathway.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
avb3_opn_pathway. Osteopontin-mediated events.
p75ntrpathway. p75(NTR)-mediated signaling.
a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.
a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.
pdgfrapathway. PDGFR-alpha signaling pathway.
pdgfrbpathway. PDGFR-beta signaling pathway.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
reelinpathway. Reelin signaling pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
ptp1bpathway. Signaling events mediated by PTP1B.
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
hedgehog_2pathway. Signaling events mediated by the Hedgehog family.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
trail_pathway. TRAIL signaling pathway.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.
vegfr1_pathway. VEGFR1 specific signals.
lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P27986.

Bgee

P27986.

CleanEx

HS_PIK3R1.

Genevestigator

P27986.

GermOnline

ENSG00000145675. Homo sapiens.

Family and domain databases

Gene3D

1.10.555.10. 1 hit.
3.30.505.10. 2 hits.

InterPro

IPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

PANTHER

PTHR10155. PTHR10155. 1 hit.

Pfam

PF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]

PRINTS

PR00678. PI3KINASEP85.
PR00401. SH2DOMAIN.

SMART

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

SUPFAM

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

PROSITE

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

ProtoNet

Search...

Other

BindingDB

P27986.

ChEMBL

CHEMBL2506.

ChiTaRS

PIK3R1. human.

DrugBank

DB01064. Isoproterenol.

EvolutionaryTrace

P27986.

GenomeRNAi

5295.

NextBio

20462.

SOURCE

Search...

Entry information

Entry name

P85A_HUMAN

Accession

Primary (citable) accession number: P27986
Secondary accession number(s): B3KT19 , 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:	May 1, 2013
This is version 166 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.