Q8BTI9 (PK3CB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
Short name=PI3-kinase subunit beta
Short name=PI3K-beta
Short name=PI3Kbeta
Short name=PtdIns-3-kinase subunit beta
EC=2.7.1.153

Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta
Short name=PtdIns-3-kinase subunit p110-beta
Short name=p110beta

Gene names

Name:

Pik3cb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1064 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (Phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.
Pathway	Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis.
Subunit structure	Heterodimer of a catalytic subunit PIK3CB and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interaction with PIK3R2 is required for nuclear localization and nuclear export By similarity. Part of a complex with PIK3R1 and PTEN By similarity. Binding to PTEN may antagonize the lipid kinase activity under normal growth conditions By similarity. Part of a complex involved in autophagosome formation composed of PIK3C3 and PIK3R4. Interacts with BECN1, ATG14 and RAB5A. Ref.8
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Interaction with PIK3R2 is required for nuclear localization and export.
Domain	The inhibitory interactions with PIK3R1 are mediated by the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1; the C2 PI3K-type domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with the nSH2 (N-terminal SH2) region of PIK3R1; and the PI3K/PI4K kinase domain with the cSH2 (C-terminal SH2) region of PIK3R1. The inhibitory interaction between the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1 is weak. The nuclear localization signal (NLS) is required for its function in cell survival By similarity. Ref.9
Post-translational modification	Phosphorylation at Ser-1064 down-regulates lipid kinase activity By similarity.
Disruption phenotype	Mice have defects in autophagosome formation. Have normal bleeding time but are resistant to thrombosis after arterial injury. Mice fail to induce tumors in a model of prostate tumor formation induced by Pten loss. Ref.3 Ref.5 Ref.6 Ref.8
Sequence similarities	Belongs to the PI3/PI4-kinase family. Contains 1 C2 PI3K-type domain. Contains 1 PI3K-ABD domain. Contains 1 PI3K-RBD domain. Contains 1 PI3K/PI4K domain. Contains 1 PIK helical domain.

Ontologies

Keywords
Biological process	Autophagy Cell adhesion Endocytosis
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	autophagy Inferred from electronic annotation. Source: UniProtKB-KW cellular calcium ion homeostasis Inferred from mutant phenotype PubMed 15834429. Source: MGI embryonic cleavage Inferred from mutant phenotype PubMed 11919689. Source: MGI endocytosis Inferred from electronic annotation. Source: UniProtKB-KW homophilic cell adhesion Inferred from mutant phenotype PubMed 15834429. Source: MGI phosphatidylinositol-mediated signaling Inferred from electronic annotation. Source: InterPro platelet activation Inferred from mutant phenotype PubMed 15834429. Source: MGI regulation of cell-matrix adhesion Inferred from mutant phenotype PubMed 15834429. Source: MGI
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell phosphatidylinositol 3-kinase complex Inferred from Biological aspect of Ancestor. Source: RefGenome plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	1-phosphatidylinositol-3-kinase activity Inferred from mutant phenotype PubMed 15834429PubMed 16625210. Source: MGI 1-phosphatidylinositol-4-phosphate 3-kinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-4,5-bisphosphate 3-kinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Pik3r1	P26450	4	EBI-644672,EBI-641764

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1064

1064

Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform

PRO_0000088788

Regions

Domain

20 – 109

90

PI3K-ABD

Domain

188 – 279

92

PI3K-RBD

Domain

323 – 490

168

C2 PI3K-type

Domain

518 – 695

178

PIK helical

Domain

794 – 1061

268

PI3K/PI4K

Motif

404 – 412

9

Nuclear localization signal (NLS) By similarity

Amino acid modifications

Modified residue

1064

1

Phosphoserine; by autocatalysis

Experimental info

Sequence conflict

123

1

L → R in BAC41102. Ref.1

Secondary structure

1

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1064

Helix Strand Turn

Details...

Beta strand

22 – 29

8

Beta strand

35 – 41

7

Helix

46 – 56

11

Helix

57 – 59

3

Turn

61 – 64

4

Helix

69 – 71

3

Beta strand

72 – 81

10

Beta strand

83 – 85

3

Beta strand

91 – 93

3

Helix

94 – 96

3

Beta strand

98 – 101

4

Beta strand

103 – 108

6

Helix

116 – 124

9

Helix

129 – 132

4

Helix

137 – 159

23

Turn

162 – 165

4

Helix

166 – 169

4

Helix

178 – 180

3

Beta strand

186 – 189

4

Beta strand

191 – 197

7

Beta strand

204 – 208

5

Helix

215 – 222

8

Helix

237 – 239

3

Beta strand

240 – 244

5

Beta strand

253 – 255

3

Helix

257 – 259

3

Helix

261 – 268

8

Beta strand

274 – 279

6

Helix

280 – 294

15

Beta strand

325 – 331

7

Beta strand

351 – 353

3

Beta strand

356 – 359

4

Beta strand

369 – 371

3

Beta strand

377 – 387

11

Beta strand

393 – 397

5

Beta strand

434 – 440

7

Beta strand

449 – 452

4

Beta strand

465 – 467

3

Beta strand

486 – 489

4

Beta strand

493 – 495

3

Helix

504 – 512

9

Helix

528 – 533

6

Turn

534 – 537

4

Helix

546 – 554

9

Helix

556 – 562

7

Helix

564 – 566

3

Helix

567 – 573

7

Helix

579 – 590

12

Helix

597 – 600

4

Helix

601 – 604

4

Helix

613 – 622

10

Helix

626 – 642

17

Beta strand

644 – 647

4

Helix

649 – 658

10

Helix

664 – 676

13

Helix

679 – 695

17

Turn

696 – 699

4

Helix

700 – 726

27

Helix

729 – 741

13

Helix

745 – 748

4

Beta strand

750 – 752

3

Beta strand

758 – 760

3

Helix

767 – 769

3

Beta strand

780 – 785

6

Turn

787 – 789

3

Beta strand

790 – 798

9

Helix

805 – 824

20

Beta strand

839 – 841

3

Beta strand

844 – 846

3

Helix

854 – 858

5

Beta strand

859 – 861

3

Turn

863 – 867

5

Helix

874 – 882

9

Helix

886 – 908

23

Turn

916 – 918

3

Beta strand

919 – 921

3

Beta strand

927 – 929

3

Helix

942 – 944

3

Helix

956 – 963

8

Beta strand

970 – 972

3

Helix

975 – 989

15

Helix

991 – 1000

10

Helix

1012 – 1021

10

Helix

1028 – 1044

17

Helix

1046 – 1054

9

Sequences

	Sequence		Length	Mass (Da)
	Q8BTI9 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: EBDF0266BF0A2032	FASTA	1,064	121,711
	10 20 30 40 50 60 MPPAMADNLD IWAVDSQIAS DGAISVDFLL PTGIYIQLEV PREATISYIK QMLWKQVHNY 70 80 90 100 110 120 PMFNLLMDID SYMFACVNQT AVYEELEDET RRLCDVRPFL PVLKLVTRSC DPAEKLDSKI 130 140 150 160 170 180 GVLIGKGLHE FDALKDPEVN EFRRKMRKFS EAKIQSLVGL SWIDWLKHTY PPEHEPSVLE 190 200 210 220 230 240 NLEDKLYGGK LVVAVHFENS QDVFSFQVSP NLNPIKINEL AIQKRLTIRG KEDEASPCDY 250 260 270 280 290 300 VLQVSGRVEY VFGDHPLIQF QYIRNCVMNR TLPHFILVEC CKIKKMYEQE MIAIEAAINR 310 320 330 340 350 360 NSSNLPLPLP PKKTRVISHI WDNNNPFQIT LVKGNKLNTE ETVKVHVRAG LFHGTELLCK 370 380 390 400 410 420 TVVSSEISGK NDHIWNEQLE FDINICDLPR MARLCFAVYA VLDKVKTKKS TKTINPSKYQ 430 440 450 460 470 480 TIRKAGKVHY PVAWVNTMVF DFKGQLRSGD VILHSWSSFP DELEEMLNPM GTVQTNPYAE 490 500 510 520 530 540 NATALHITFP ENKKQPCYYP PFDKIIEKAA ELASGDSANV SSRGGKKFLA VLKEILDRDP 550 560 570 580 590 600 LSQLCENEMD LIWTLRQDCR ENFPQSLPKL LLSIKWNKLE DVAQLQALLQ IWPKLPPREA 610 620 630 640 650 660 LELLDFNYPD QYVREYAVGC LRQMSDEELS QYLLQLVQVL KYEPFLDCAL SRFLLERALD 670 680 690 700 710 720 NRRIGQFLFW HLRSEVHTPA VSVQFGVILE AYCRGSVGHM KVLSKQVEAL NKLKTLNSLI 730 740 750 760 770 780 KLNAVKLSRA KGKEAMHTCL KQSAYREALS DLQSPLNPCV ILSELYVEKC KYMDSKMKPL 790 800 810 820 830 840 WLVYSSRAFG EDSVGVIFKN GDDLRQDMLT LQMLRLMDLL WKEAGLDLRM LPYGCLATGD 850 860 870 880 890 900 RSGLIEVVST SETIADIQLN SSNVAATAAF NKDALLNWLK EYNSGDDLDR AIEEFTLSCA 910 920 930 940 950 960 GYCVASYVLG IGDRHSDNIM VKKTGQLFHI DFGHILGNFK SKFGIKRERV PFILTYDFIH 970 980 990 1000 1010 1020 VIQQGKTGNT EKFGRFRQCC EDAYLILRRH GNLFITLFAL MLTAGLPELT SVKDIQYLKD 1030 1040 1050 1060 SLALGKSEEE ALKQFKQKFD EALRESWTTK VNWMAHTVRK DYRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD. Tissue: Embryo.
[2]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Essential roles of PI(3)K-p110beta in cell growth, metabolism and tumorigenesis." Jia S., Liu Z., Zhang S., Liu P., Zhang L., Lee S.H., Zhang J., Signoretti S., Loda M., Roberts T.M., Zhao J.J. Nature 454:776-779(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]	"The p110beta isoform of phosphoinositide 3-kinase signals downstream of G protein-coupled receptors and is functionally redundant with p110gamma." Guillermet-Guibert J., Bjorklof K., Salpekar A., Gonella C., Ramadani F., Bilancio A., Meek S., Smith A.J.H., Okkenhaug K., Vanhaesebroeck B. Proc. Natl. Acad. Sci. U.S.A. 105:8292-8297(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Genetic evidence for a predominant role of PI3Kbeta catalytic activity in ITAM- and integrin-mediated signaling in platelets." Canobbio I., Stefanini L., Cipolla L., Ciraolo E., Gruppi C., Balduini C., Hirsch E., Torti M. Blood 114:2193-2196(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]	"Deletion of the p110beta isoform of phosphoinositide 3-kinase in platelets reveals its central role in Akt activation and thrombus formation in vitro and in vivo." Martin V., Guillermet-Guibert J., Chicanne G., Cabou C., Jandrot-Perrus M., Plantavid M., Vanhaesebroeck B., Payrastre B., Gratacap M.-P. Blood 115:2008-2013(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]	"Phosphoinositide 3-kinase p110 beta regulates integrin alpha IIb beta 3 avidity and the cellular transmission of contractile forces." Schoenwaelder S.M., Ono A., Nesbitt W.S., Lim J., Jarman K., Jackson S.P. J. Biol. Chem. 285:2886-2896(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive regulator of autophagy." Dou Z., Chattopadhyay M., Pan J.-A., Guerriero J.L., Jiang Y.-P., Ballou L.M., Yue Z., Lin R.Z., Zong W.-X. J. Cell Biol. 191:827-843(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH PIK3C3 AND PIK3R4, INTERACTION WITH BECN1; ATG14 AND RAB5A, DISRUPTION PHENOTYPE.
[9]	"Structure of lipid kinase p110beta/p85beta elucidates an unusual SH2-domain-mediated inhibitory mechanism." Zhang X., Vadas O., Perisic O., Anderson K.E., Clark J., Hawkins P.T., Stephens L.R., Williams R.L. Mol. Cell 41:567-578(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN A COMPLEX WITH PIK3R2 AND GDC-0941, DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK090116 mRNA. Translation: BAC41102.1.
AK154106 mRNA. Translation: BAE32380.1.
CH466560 Genomic DNA. Translation: EDL20998.1.

IPI

IPI00136110.

RefSeq

NP_083370.2. NM_029094.3.

UniGene

Mm.213128.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Y3A	X-ray	3.30	A	1-1064	[»]

ProteinModelPortal

Q8BTI9.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-49395N.

IntAct

Q8BTI9. 6 interactions.

PTM databases

PhosphoSite

Q8BTI9.

Proteomic databases

PaxDb

Q8BTI9.

PRIDE

Q8BTI9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000035037; ENSMUSP00000035037; ENSMUSG00000032462.

GeneID

74769.

KEGG

mmu:74769.

Organism-specific databases

CTD

5291.

MGI

MGI:1922019. Pik3cb.

Phylogenomic databases

eggNOG

COG5032.

GeneTree

ENSGT00620000087742.

HOGENOM

HOG000252911.

HOVERGEN

HBG052721.

InParanoid

Q3U4Q1.

KO

K00922.

OMA

AMHTCLK.

OrthoDB

EOG4ZPDTJ.

Enzyme and pathway databases

UniPathway

UPA00220.

Gene expression databases

ArrayExpress

Q8BTI9.

Bgee

Q8BTI9.

Genevestigator

Q8BTI9.

GermOnline

ENSMUSG00000032462. Mus musculus.

Family and domain databases

Gene3D

1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.

InterPro

IPR016024. ARM-type_fold.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003113. PI3K_adapt-bd_dom.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]

PANTHER

PTHR10048. PTHR10048. 1 hit.

Pfam

PF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF02192. PI3K_p85B. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]

SMART

SM00142. PI3K_C2. 1 hit.
SM00143. PI3K_p85B. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.
SSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51544. PI3K_ABD. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

341596.

SOURCE

Search...

Entry information

Entry name

PK3CB_MOUSE

Accession

Primary (citable) accession number: Q8BTI9
Secondary accession number(s): Q3U4Q1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program