[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8246984 [NCBI, ExPASy, EBI, Israel, Japan] Hu P., Mondino A., Skolnik E.Y., Schlessinger J.; "Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85."; Mol. Cell. Biol. 13:7677-7688(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=11016459 [NCBI, ExPASy, EBI, Israel, Japan] Kossila M., Sinkovic M., Karkkainen P., Laukkanen M.O., Miettinen R., Rissanen J., Kekalainen P., Kuusisto J., Yla-Herttuala S., Laakso M.; "Gene encoding the catalytic subunit p110beta of human phosphatidylinositol 3-kinase: cloning, genomic structure, and screening for variants in patients with type 2 diabetes."; Diabetes 49:1740-1743(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

Comments

FUNCTION: Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2.
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: Heterodimer of a p110 (catalytic) and a p85 (regulatory) subunit.
TISSUE SPECIFICITY: Expressed ubiquitously.
SIMILARITY: Belongs to the PI3/PI4-kinase family.
SIMILARITY: Contains 1 PI3K/PI4K domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S67334; AAB29081.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297549; CAC21449.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297550; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297551; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297552; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297553; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297554; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297555; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297556; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297557; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297558; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297559; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297560; CAC21449.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC114432; AAI14433.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00031388; -.

A54600; A54600.

NP_006210.1; -.

3D structure databases

HSSP

P48736; 1E8Y. [HSSP ENTRY / PDB]

ModBase

P42338.

PTM databases

PhosphoSite

P42338; -.

Enzyme and pathway databases

BRENDA

2.7.1.137; 247.

Pathway_Interaction_DB

pi3kcipathway; Class I PI3K signaling events.
lysophospholipid_pathway; LPA receptor mediated events.
trail_pathway; TRAIL signaling pathway.

Reactome

REACT_11061; Signalling by NGF.
REACT_498; Signaling by Insulin receptor.
REACT_604; Hemostasis.
REACT_6900; Signaling in Immune system.

Organism-specific databases

GC03M139855; -.

HIX0030788; -.

HGNC:8976; PIK3CB.

602925; gene. [NCBI / EBI]

PharmGKB

PA33309; -.

Gene expression databases

P42338; -.

P42338; -.

HS_PIK3CB; -.

ENSG00000051382; Homo sapiens.

Ontologies

GO:0005942;	Cellular component: phosphoinositide 3-kinase complex (inferred from electronic annotation from InterPro).
GO:0016303;	Molecular function: 1-phosphatidylinositol-3-kinase activity (traceable author statement from ProtInc).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0046934;	Molecular function: phosphatidylinositol-4,5-bisphosphate 3-kinase activity (inferred from electronic annotation from EC).
GO:0000187;	Biological process: activation of MAPK activity (traceable author statement from ProtInc).
GO:0006935;	Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0007186;	Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
GO:0046854;	Biological process: phosphoinositide phosphorylation (inferred from electronic annotation from InterPro).
GO:0048015;	Biological process: phosphoinositide-mediated signaling (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000403; PI3/4_kinase_cat.
IPR018936; PI3/4_kinase_CS.
IPR002420; PI3K_C2.
IPR003113; PI3K_p85_bd.
IPR000341; PI3K_ras_bd.
IPR001263; PI3Ka.
IPR015433; PI_Kinase.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.1070.11; PI3/4_kinase_cat; 1.
G3DSA:1.25.40.70; PI3Ka; 1.

PANTHER

PTHR10048; PI_Kinase; 1.

Pfam

PF00454; PI3_PI4_kinase; 1.
PF00792; PI3K_C2; 1.
PF02192; PI3K_p85B; 1.
PF00794; PI3K_rbd; 1.
PF00613; PI3Ka; 1.
Pfam graphical view of domain structure.

SMART

SM00142; PI3K_C2; 1.
SM00143; PI3K_p85B; 1.
SM00144; PI3K_rbd; 1.
SM00145; PI3Ka; 1.
SM00146; PI3Kc; 1.
SMART graphical view of domain structure.

PROSITE

PS00915; PI3_4_KINASE_1; 1.
PS00916; PI3_4_KINASE_2; 1.
PS50290; PI3_4_KINASE_3; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

P42338; -.

PRIDE

P42338; -.

Genome annotation databases

Ensembl

ENSG00000051382; Homo sapiens. [Contig view]

GeneID

5291; -.

KEGG

hsa:5291; -.

Phylogenomic databases

HOGENOM

P42338; -.

HOVERGEN

P42338; -.

OMA

P42338; VKGNKLN.

Other

NextBio

20446; -.

SOURCE

PIK3CB; Homo sapiens.

ProtoNet

P42338.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Kinase; Nucleotide-binding; Polymorphism; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1070`	`1070`	`Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform.`	`PRO_0000088787`
`DOMAIN`	`800 1050`	`251`	`PI3K/PI4K.`
`VARIANT`	`672 672`	`1`	`Q -> H (in dbSNP:rs2230462 [NCBI]).`	`VAR_050530`

Sequence information

Length: 1070 AA [This is the length of the unprocessed precursor]

Molecular weight: 122762 Da [This is the MW of the unprocessed precursor]

CRC64: 81135FE93452C00E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MCFSFIMPPA MADILDIWAV DSQIASDGSI PVDFLLPTGI YIQLEVPREA TISYIKQMLW 

        70         80         90        100        110        120 
KQVHNYPMFN LLMDIDSYMF ACVNQTAVYE ELEDETRRLC DVRPFLPVLK LVTRSCDPGE 

       130        140        150        160        170        180 
KLDSKIGVLI GKGLHEFDSL KDPEVNEFRR KMRKFSEEKI LSLVGLSWMD WLKQTYPPEH 

       190        200        210        220        230        240 
EPSIPENLED KLYGGKLIVA VHFENCQDVF SFQVSPNMNP IKVNELAIQK RLTIHGKEDE 

       250        260        270        280        290        300 
VSPYDYVLQV SGRVEYVFGD HPLIQFQYIR NCVMNRALPH FILVECCKIK KMYEQEMIAI 

       310        320        330        340        350        360 
EAAINRNSSN LPLPLPPKKT RIISHVWENN NPFQIVLVKG NKLNTEETVK VHVRAGLFHG 

       370        380        390        400        410        420 
TELLCKTIVS SEVSGKNDHI WNEPLEFDIN ICDLPRMARL CFAVYAVLDK VKTKKSTKTI 

       430        440        450        460        470        480 
NPSKYQTIRK AGKVHYPVAW VNTMVFDFKG QLRTGDIILH SWSSFPDELE EMLNPMGTVQ 

       490        500        510        520        530        540 
TNPYTENATA LHVKFPENKK QPYYYPPFDK IIEKAAEIAS SDSANVSSRG GKKFLPVLKE 

       550        560        570        580        590        600 
ILDRDPLSQL CENEMDLIWT LRQDCREIFP QSLPKLLLSI KWNKLEDVAQ LQALLQIWPK 

       610        620        630        640        650        660 
LPPREALELL DFNYPDQYVR EYAVGCLRQM SDEELSQYLL QLVQVLKYEP FLDCALSRFL 

       670        680        690        700        710        720 
LERALGNRRI GQFLFWHLRS EVHIPAVSVQ FGVILEAYCR GSVGHMKVLS KQVEALNKLK 

       730        740        750        760        770        780 
TLNSLIKLNA VKLNRAKGKE AMHTCLKQSA YREALSDLQS PLNPCVILSE LYVEKCKYMD 

       790        800        810        820        830        840 
SKMKPLWLVY NNKVFGEDSV GVIFKNGDDL RQDMLTLQML RLMDLLWKEA GLDLRMLPYG 

       850        860        870        880        890        900 
CLATGDRSGL IEVVSTSETI ADIQLNSSNV AAAAAFNKDA LLNWLKEYNS GDDLDRAIEE 

       910        920        930        940        950        960 
FTLSCAGYCV ASYVLGIGDR HSDNIMVKKT GQLFHIDFGH ILGNFKSKFG IKRERVPFIL 

       970        980        990       1000       1010       1020 
TYDFIHVIQQ GKTGNTEKFG RFRQCCEDAY LILRRHGNLF ITLFALMLTA GLPELTSVKD 

      1030       1040       1050       1060       1070 
IQYLKDSLAL GKSEEEALKQ FKQKFDEALR ESWTTKVNWM AHTVRKDYRS

P42338 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools