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Q9Z1L0

- PK3CB_RAT

UniProt

Q9Z1L0 - PK3CB_RAT

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Protein
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
Gene
Pik3cb
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.

Pathwayi

GO - Molecular functioni

  1. 1-phosphatidylinositol-3-kinase activity Source: RGD
  2. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: RefGenome
  3. ATP binding Source: UniProtKB-KW
  4. phosphatidylinositol 3-kinase activity Source: RGD
  5. phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: RefGenome

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. cell adhesion Source: UniProtKB-KW
  3. endocytosis Source: UniProtKB-KW
  4. phosphatidylinositol phosphorylation Source: RGD
  5. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  6. phosphatidylinositol-mediated signaling Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Autophagy, Cell adhesion, Endocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196225. Regulation of signaling by CBL.
UniPathwayiUPA00220.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform (EC:2.7.1.153)
Short name:
PI3-kinase subunit beta
Short name:
PI3K-beta
Short name:
PI3Kbeta
Short name:
PtdIns-3-kinase subunit beta
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 namesi
Name:Pik3cb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620917. Pik3cb.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Interaction with PIK3R2 is required for nuclear localization and export.

GO - Cellular componenti

  1. brush border membrane Source: RGD
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB-SubCell
  4. phosphatidylinositol 3-kinase complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10701070Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
PRO_0000088789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1070 – 10701Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Z1L0.
PRIDEiQ9Z1L0.

PTM databases

PhosphoSiteiQ9Z1L0.

Expressioni

Gene expression databases

GenevestigatoriQ9Z1L0.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

MINTiMINT-204613.
STRINGi10116.ENSRNOP00000022179.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1L0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 11590PI3K-ABD
Add
BLAST
Domaini194 – 28592PI3K-RBD
Add
BLAST
Domaini327 – 496170C2 PI3K-type
Add
BLAST
Domaini524 – 701178PIK helical
Add
BLAST
Domaini800 – 1067268PI3K/PI4K
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi410 – 4189Nuclear localization signal (NLS) By similarity

Domaini

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 similaritiesi

Belongs to the PI3/PI4-kinase family.
Contains 1 PI3K-ABD domain.
Contains 1 PI3K-RBD domain.
Contains 1 PI3K/PI4K domain.
Contains 1 PIK helical domain.

Phylogenomic databases

eggNOGiCOG5032.
HOGENOMiHOG000252911.
HOVERGENiHBG052721.
InParanoidiQ9Z1L0.
KOiK00922.
PhylomeDBiQ9Z1L0.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProiIPR016024. 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]
PANTHERiPTHR10048. PTHR10048. 1 hit.
PfamiPF00454. 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]
SMARTiSM00142. PI3K_C2. 1 hit.
SM00143. PI3K_p85B. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00915. 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]

Sequencei

Sequence statusi: Complete.

Q9Z1L0-1 [UniParc]FASTAAdd to Basket

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MCFRSIMPPA MADTLDIWAV DSQIASDGSI SVDFLLPTGI YIQLEVPREA     50
TISYIKQMLW KQVHNYPMFN LLMDIDSYMF ACVNQTAVYE ELEDETRRLC 100
DVRPFLPVLK LVTRSCDPAE KLDSKIGVLI GKGLHEFDAL KDPEVNEFRR 150
KMRKFSEDKI QSLVGLSWID WLKHTYPPEH EPSVLENLED KLYGGKLVVA 200
VHFENSQDVF SFQVSPNLNP IKINELAIQK RLTIRGKEEE ASPCDYVLQV 250
SGRVEYVFGD HPLIQFQYIR NCVMNRTLPH FILVECCKIK KMYEQEMIAI 300
EAAINRNSSS LPLPLPPKKT RVISHVWGNN NPFQIVLVKG NKLNTEETVK 350
VHVRAGLFHG TELLCKTVVS SEISGKNDHI WNEQLEFDIN ICDLPRMARL 400
CFAVYAVLDK VKTKKSTKTI NPSKYQTIRK AGKVHYPVAW VNTMVFDFKG 450
QLRSGDVILH SWSSFPDELE EMLNPMGTVQ TNPYAENATA LHIKFPENKK 500
QPYYYPPFDK IIEKAAEIAS GDSANVSSRG GKKFLAVLKE ILDRDPLSQL 550
CENEMDLIWT LRQDCRENFP QSLPKLLLSI KWNKLEDVAQ LQALLQIWPK 600
LPPREALELL DFNYPDQYVR EYAVGCLRQM SDEELSQYLL QLVQVLKYEP 650
FLDCALSRFL LERALDNRRI GQFLFWHLRS EVHTPAVSIQ FGVILEAYCR 700
GSVGHMKVLS KQVEALNKLK TLNSLIKLNA MKLNRAKGKE AMHTCLKQSA 750
YREALSDLQS PLNPCVILSE LYVEKCRYMD SKMKPLWLVY SNRAFGEDAV 800
GVIFKNGDDL RQDMLTLQML RLMDLLWKEA GLDLRMLPYG CLATGDRSGL 850
IEVVSTSETI ADIQLNSSNV AATAAFNKDA LLNWLKEYNS GDDLDRAIEE 900
FTLSCAGYCV ASYVLGIGDR HSDNIMVKKT GQLFHIDFGH ILGNFKSKFG 950
IKRERVPFIL TYDFIHVIQQ GKTGNTEKFG RFRQCCEDAY LILRRHGNLF 1000
ITLFALMLTA GLPELTSVKD IQYLKDSLAL GKSEEEALKQ FKQKFDEALR 1050
ESWTTKVNWM AHTVRKDYRS 1070
Length:1,070
Mass (Da):122,608
Last modified:May 1, 1999 - v1
Checksum:i4E8EB2333E96E4D5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ012482 mRNA. Translation: CAA10046.1.
RefSeqiNP_445933.1. NM_053481.1.
UniGeneiRn.44268.

Genome annotation databases

GeneIDi85243.
KEGGirno:85243.
UCSCiRGD:620917. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ012482 mRNA. Translation: CAA10046.1 .
RefSeqi NP_445933.1. NM_053481.1.
UniGenei Rn.44268.

3D structure databases

ProteinModelPortali Q9Z1L0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-204613.
STRINGi 10116.ENSRNOP00000022179.

PTM databases

PhosphoSitei Q9Z1L0.

Proteomic databases

PaxDbi Q9Z1L0.
PRIDEi Q9Z1L0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 85243.
KEGGi rno:85243.
UCSCi RGD:620917. rat.

Organism-specific databases

CTDi 5291.
RGDi 620917. Pik3cb.

Phylogenomic databases

eggNOGi COG5032.
HOGENOMi HOG000252911.
HOVERGENi HBG052721.
InParanoidi Q9Z1L0.
KOi K00922.
PhylomeDBi Q9Z1L0.

Enzyme and pathway databases

UniPathwayi UPA00220 .
Reactomei REACT_196225. Regulation of signaling by CBL.

Miscellaneous databases

NextBioi 617306.
PROi Q9Z1L0.

Gene expression databases

Genevestigatori Q9Z1L0.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProi IPR016024. 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 ]
PANTHERi PTHR10048. PTHR10048. 1 hit.
Pfami 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 ]
SMARTi 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 ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPK3CB_RAT
AccessioniPrimary (citable) accession number: Q9Z1L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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