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Q9Z1L0 (PK3CB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1070 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity. Interacts with BECN1, ATG14 and RAB5A By similarity.

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.

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 processAutophagy
Cell adhesion
Endocytosis
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processautophagy

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol phosphorylation

Inferred from direct assay PubMed 12882977. Source: RGD

phosphatidylinositol-3-phosphate biosynthetic process

Inferred from direct assay PubMed 11931646PubMed 12882977. Source: GOC

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbrush border membrane

Inferred from direct assay PubMed 11931646. Source: RGD

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

phosphatidylinositol 3-kinase complex

Inferred from direct assay PubMed 12882977. Source: RGD

   Molecular_function1-phosphatidylinositol-3-kinase activity

Inferred from direct assay PubMed 11931646PubMed 12882977. Source: RGD

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 3-kinase activity

Non-traceable author statement PubMed 12395317. Source: RGD

phosphatidylinositol-4,5-bisphosphate 3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10701070Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
PRO_0000088789

Regions

Domain26 – 11590PI3K-ABD
Domain194 – 28592PI3K-RBD
Domain327 – 496170C2 PI3K-type
Domain524 – 701178PIK helical
Domain800 – 1067268PI3K/PI4K
Motif410 – 4189Nuclear localization signal (NLS) By similarity

Amino acid modifications

Modified residue10701Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z1L0 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4E8EB2333E96E4D5

FASTA1,070122,608
        10         20         30         40         50         60 
MCFRSIMPPA MADTLDIWAV DSQIASDGSI SVDFLLPTGI YIQLEVPREA TISYIKQMLW 

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

       130        140        150        160        170        180 
KLDSKIGVLI GKGLHEFDAL KDPEVNEFRR KMRKFSEDKI QSLVGLSWID WLKHTYPPEH 

       190        200        210        220        230        240 
EPSVLENLED KLYGGKLVVA VHFENSQDVF SFQVSPNLNP IKINELAIQK RLTIRGKEEE 

       250        260        270        280        290        300 
ASPCDYVLQV SGRVEYVFGD HPLIQFQYIR NCVMNRTLPH FILVECCKIK KMYEQEMIAI 

       310        320        330        340        350        360 
EAAINRNSSS LPLPLPPKKT RVISHVWGNN NPFQIVLVKG NKLNTEETVK VHVRAGLFHG 

       370        380        390        400        410        420 
TELLCKTVVS SEISGKNDHI WNEQLEFDIN ICDLPRMARL CFAVYAVLDK VKTKKSTKTI 

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

       490        500        510        520        530        540 
TNPYAENATA LHIKFPENKK QPYYYPPFDK IIEKAAEIAS GDSANVSSRG GKKFLAVLKE 

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

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

       670        680        690        700        710        720 
LERALDNRRI GQFLFWHLRS EVHTPAVSIQ FGVILEAYCR GSVGHMKVLS KQVEALNKLK 

       730        740        750        760        770        780 
TLNSLIKLNA MKLNRAKGKE AMHTCLKQSA YREALSDLQS PLNPCVILSE LYVEKCRYMD 

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

       850        860        870        880        890        900 
CLATGDRSGL IEVVSTSETI ADIQLNSSNV AATAAFNKDA 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 

« Hide

References

[1]"Phosphatidylinositol-3 kinase and activation of phosphodiesterase 3B in adipocytes."
Mulder H., Stenson Holst L., Degerman E.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ012482 mRNA. Translation: CAA10046.1.
RefSeqNP_445933.1. NM_053481.1.
UniGeneRn.44268.

3D structure databases

ProteinModelPortalQ9Z1L0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-204613.
STRING10116.ENSRNOP00000022179.

PTM databases

PhosphoSiteQ9Z1L0.

Proteomic databases

PaxDbQ9Z1L0.
PRIDEQ9Z1L0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID85243.
KEGGrno:85243.
UCSCRGD:620917. rat.

Organism-specific databases

CTD5291.
RGD620917. Pik3cb.

Phylogenomic databases

eggNOGCOG5032.
HOGENOMHOG000252911.
HOVERGENHBG052721.
InParanoidQ9Z1L0.
KOK00922.
PhylomeDBQ9Z1L0.

Enzyme and pathway databases

ReactomeREACT_197471. Cell-Cell communication.
REACT_227097. Immune System.
UniPathwayUPA00220.

Gene expression databases

GenevestigatorQ9Z1L0.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR000008. C2_dom.
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.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00454. 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]
SMARTSM00142. PI3K_C2. 1 hit.
SM00143. PI3K_p85B. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00915. 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]
ProtoNetSearch...

Other

NextBio617306.
PROQ9Z1L0.

Entry information

Entry namePK3CB_RAT
AccessionPrimary (citable) accession number: Q9Z1L0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: June 11, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways