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

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Q9Z1L0 (PK3CB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1070 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Autophagy Cell adhesion Endocytosis
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	autophagy 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-mediated signaling Inferred from electronic annotation. Source: InterPro
Cellular_component	brush border membrane Inferred from direct assay PubMed 11931646. Source: RGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell phosphatidylinositol 3-kinase complex Inferred from direct assay PubMed 12882977. Source: RGD
Molecular_function	1-phosphatidylinositol-3-kinase activity Inferred from direct assay PubMed 11931646 PubMed 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-4,5-bisphosphate 3-kinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1070

1070

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

PRO_0000088789

Regions

Domain

26 – 115

PI3K-ABD

Domain

194 – 285

PI3K-RBD

Domain

327 – 496

170

C2 PI3K-type

Domain

524 – 701

178

PIK helical

Domain

800 – 1067

268

PI3K/PI4K

Motif

410 – 418

Nuclear localization signal (NLS) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Z1L0 [UniParc].

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

1,070

122,608

        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

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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.
IPI	IPI00208989.
RefSeq	NP_445933.1. NM_053481.1.
UniGene	Rn.44268.
3D structure databases
ProteinModelPortal	Q9Z1L0.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000022179.
PTM databases
PhosphoSite	Q9Z1L0.
Proteomic databases
PaxDb	Q9Z1L0.
PRIDE	Q9Z1L0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	85243.
KEGG	rno:85243.
UCSC	RGD:620917. rat.
Organism-specific databases
CTD	5291.
RGD	620917. Pik3cb.
Phylogenomic databases
eggNOG	COG5032.
HOGENOM	HOG000252911.
HOVERGEN	HBG052721.
InParanoid	Q9Z1L0.
KO	K00922.
OrthoDB	EOG4ZPDTJ.
Enzyme and pathway databases
Reactome	REACT_109781. Immune System. REACT_114732. Cell-Cell communication.
UniPathway	UPA00220.
Gene expression databases
Genevestigator	Q9Z1L0.
GermOnline	ENSRNOG00000016384. Rattus norvegicus.
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	617306.

Entry information

Entry name

PK3CB_RAT

Accession

Primary (citable) accession number: Q9Z1L0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents