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O00329

- PK3CD_HUMAN

UniProt

O00329 - PK3CD_HUMAN

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Protein
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
Gene
PIK3CD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Phosphoinositide-3-kinase (PI3K) that phosphorylates PftdIns(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. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Have a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Have important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. Isoform 2 may be involved in stabilizing total RAS levels, resulting in increased ERK phosphorylation and increased PI3K activity.2 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by growth factors and cytokine receptors through a tyrosine-kinase-dependent mechanism. Activated by RAS. IC87114 inhibits lipid kinase activity and is selective in cells at doses up to 5-10 µM. IC87114 blocks T-cell receptor signaling in naive and memory T-cells and reduces cytokine production by memory T-cells.1 Publication

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. B cell chemotaxis Source: UniProtKB
  3. B cell homeostasis Source: Ensembl
  4. B cell receptor signaling pathway Source: UniProtKB
  5. Fc-epsilon receptor signaling pathway Source: Reactome
  6. T cell activation Source: UniProtKB
  7. T cell chemotaxis Source: UniProtKB
  8. T cell differentiation Source: UniProtKB
  9. T cell receptor signaling pathway Source: UniProtKB
  10. adaptive immune response Source: UniProtKB
  11. cytokine production Source: UniProtKB
  12. epidermal growth factor receptor signaling pathway Source: Reactome
  13. fibroblast growth factor receptor signaling pathway Source: Reactome
  14. inflammatory response Source: UniProtKB
  15. innate immune response Source: UniProtKB
  16. mast cell chemotaxis Source: UniProtKB
  17. mast cell degranulation Source: UniProtKB
  18. mast cell differentiation Source: UniProtKB
  19. natural killer cell activation Source: UniProtKB
  20. natural killer cell chemotaxis Source: UniProtKB
  21. natural killer cell differentiation Source: UniProtKB
  22. neurotrophin TRK receptor signaling pathway Source: Reactome
  23. neutrophil chemotaxis Source: UniProtKB
  24. neutrophil extravasation Source: UniProtKB
  25. phosphatidylinositol 3-kinase signaling Source: UniProtKB
  26. phosphatidylinositol biosynthetic process Source: Reactome
  27. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  28. phosphatidylinositol-mediated signaling Source: Reactome
  29. phospholipid metabolic process Source: Reactome
  30. protein phosphorylation Source: UniProtKB
  31. respiratory burst involved in defense response Source: UniProtKB
  32. signal transduction Source: UniProtKB
  33. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Adaptive immunity, Chemotaxis, Differentiation, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000171608-MONOMER.
BRENDAi2.7.1.137. 2681.
ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_23787. Regulation of signaling by CBL.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23891. Interleukin receptor SHC signaling.
REACT_75829. PIP3 activates AKT signaling.
SignaLinkiO00329.
UniPathwayiUPA00220.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform (EC:2.7.1.153)
Short name:
PI3-kinase subunit delta
Short name:
PI3K-delta
Short name:
PI3Kdelta
Short name:
PtdIns-3-kinase subunit delta
Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta
Short name:
PtdIns-3-kinase subunit p110-delta
Short name:
p110delta
Gene namesi
Name:PIK3CD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8977. PIK3CD.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mast cell granule Source: GOC
  3. phosphatidylinositol 3-kinase complex Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Activated PI3K-delta syndrome (APDS) [MIM:615513]: A disorder characterized by recurrent respiratory infections, progressive airway damage, lymphopenia, increased circulating transitional B cells, increased immunoglobulin M, reduced immunoglobulin G2 levels in serum, and impaired vaccine responses.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1021 – 10211E → K in APDS; results in gain of function causing enhanced membrane association and kinase activity. 1 Publication
VAR_070918

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi894 – 8941R → P: Abolishes lipid and protein kinase activities. 1 Publication
Mutagenesisi1039 – 10391S → A: Abolishes autophosphorylation, no effect on lipid kinase activity. 1 Publication
Mutagenesisi1039 – 10391S → D or E: Abolishes autophosphorylation, reduced lipid kinase activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615513. phenotype.
PharmGKBiPA33310.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10441044Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
PRO_0000088790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei524 – 5241Phosphotyrosine1 Publication
Modified residuei1039 – 10391Phosphoserine; by autocatalysis2 Publications

Post-translational modificationi

Autophosphorylation on Ser-1039 results in the almost complete inactivation of the lipid kinase activity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00329.
PaxDbiO00329.
PRIDEiO00329.

PTM databases

PhosphoSiteiO00329.

Expressioni

Tissue specificityi

Isoform 2 is expressed in normal thymus, lung and spleen tissues, and is detected at low levels in normal lysates from colon and ovarian biopsies, at elevated levels in lysates from colorectal tumors and is abundantly expressed in some ovarian tumors (at protein level). Both isoform 1 and isoform 2 are widely expressed. Isoform 1 is expressed predominantly in leukocytes.1 Publication

Gene expression databases

ArrayExpressiO00329.
BgeeiO00329.
CleanExiHS_PIK3CD.
GenevestigatoriO00329.

Organism-specific databases

HPAiCAB015420.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CD and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interacts with ERAS By similarity. Interacts with HRAS.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HRASP011122EBI-718309,EBI-350145

Protein-protein interaction databases

BioGridi111311. 9 interactions.
IntActiO00329. 8 interactions.
STRINGi9606.ENSP00000366563.

Structurei

3D structure databases

ProteinModelPortaliO00329.
SMRiO00329. Positions 20-102, 109-1027.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 10590PI3K-ABD
Add
BLAST
Domaini187 – 27892PI3K-RBD
Add
BLAST
Domaini319 – 476158C2 PI3K-type
Add
BLAST
Domaini497 – 674178PIK helical
Add
BLAST
Domaini774 – 1041268PI3K/PI4K
Add
BLAST

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.
KOiK00922.
OrthoDBiEOG70CR65.
PhylomeDBiO00329.
TreeFamiTF102031.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O00329-1) [UniParc]FASTAAdd to Basket

Also known as: p110-delta

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MPPGVDCPME FWTKEENQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQLLW     50
HRAQYEPLFH MLSGPEAYVF TCINQTAEQQ ELEDEQRRLC DVQPFLPVLR 100
LVAREGDRVK KLINSQISLL IGKGLHEFDS LCDPEVNDFR AKMCQFCEEA 150
AARRQQLGWE AWLQYSFPLQ LEPSAQTWGP GTLRLPNRAL LVNVKFEGSE 200
ESFTFQVSTK DVPLALMACA LRKKATVFRQ PLVEQPEDYT LQVNGRHEYL 250
YGSYPLCQFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR 300
AKPPPIPAKK PSSVSLWSLE QPFRIELIQG SKVNADERMK LVVQAGLFHG 350
NEMLCKTVSS SEVSVCSEPV WKQRLEFDIN ICDLPRMARL CFALYAVIEK 400
AKKARSTKKK SKKADCPIAW ANLMLFDYKD QLKTGERCLY MWPSVPDEKG 450
ELLNPTGTVR SNPNTDSAAA LLICLPEVAP HPVYYPALEK ILELGRHSEC 500
VHVTEEEQLQ LREILERRGS GELYEHEKDL VWKLRHEVQE HFPEALARLL 550
LVTKWNKHED VAQMLYLLCS WPELPVLSAL ELLDFSFPDC HVGSFAIKSL 600
RKLTDDELFQ YLLQLVQVLK YESYLDCELT KFLLDRALAN RKIGHFLFWH 650
LRSEMHVPSV ALRFGLILEA YCRGSTHHMK VLMKQGEALS KLKALNDFVK 700
LSSQKTPKPQ TKELMHLCMR QEAYLEALSH LQSPLDPSTL LAEVCVEQCT 750
FMDSKMKPLW IMYSNEEAGS GGSVGIIFKN GDDLRQDMLT LQMIQLMDVL 800
WKQEGLDLRM TPYGCLPTGD RTGLIEVVLR SDTIANIQLN KSNMAATAAF 850
NKDALLNWLK SKNPGEALDR AIEEFTLSCA GYCVATYVLG IGDRHSDNIM 900
IRESGQLFHI DFGHFLGNFK TKFGINRERV PFILTYDFVH VIQQGKTNNS 950
EKFERFRGYC ERAYTILRRH GLLFLHLFAL MRAAGLPELS CSKDIQYLKD 1000
SLALGKTEEE ALKHFRVKFN EALRESWKTK VNWLAHNVSK DNRQ 1044
Length:1,044
Mass (Da):119,479
Last modified:June 7, 2005 - v2
Checksum:iA38B5D1A1081A3D0
GO
Isoform 2 (identifier: O00329-2) [UniParc]FASTAAdd to Basket

Also known as: p37-delta

The sequence of this isoform differs from the canonical sequence as follows:
     201-300: ESFTFQVSTK...NPAPQVQKPR → VSPCVACGIQ...GRLHAAGERQ
     302-1044: Missing.

Show »
Length:301
Mass (Da):33,107
Checksum:i18DF7554E3D50988
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1021 – 10211E → K in APDS; results in gain of function causing enhanced membrane association and kinase activity. 1 Publication
VAR_070918

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei201 – 300100ESFTF…VQKPR → VSPCVACGIQAALSMGSTSS VKLLSHPQAPLPQWHQMVFA RCLCMCGAQLNVPPGELHLP GVHQGRAAGADGLCPAEEGH SVPAAAGGAAGRLHAAGERQ in isoform 2.
VSP_044409Add
BLAST
Alternative sequencei302 – 1044743Missing in isoform 2.
VSP_044410Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531S → N in AAC25677. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10055 mRNA. Translation: CAA71149.2.
U86453 mRNA. Translation: AAC25677.1.
JN190435 mRNA. Translation: AEK81610.1.
DQ263594 mRNA. Translation: ABB83814.1.
AL691449 Genomic DNA. Translation: CAI15703.1.
BC132919 mRNA. Translation: AAI32920.1.
BC132921 mRNA. Translation: AAI32922.1.
CCDSiCCDS104.1. [O00329-1]
RefSeqiNP_005017.3. NM_005026.3. [O00329-1]
XP_006710749.1. XM_006710686.1. [O00329-1]
XP_006710750.1. XM_006710687.1. [O00329-1]
XP_006710751.1. XM_006710688.1. [O00329-1]
XP_006710752.1. XM_006710689.1. [O00329-1]
UniGeneiHs.518451.

Genome annotation databases

EnsembliENST00000377346; ENSP00000366563; ENSG00000171608. [O00329-1]
GeneIDi5293.
KEGGihsa:5293.
UCSCiuc001aqb.4. human. [O00329-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10055 mRNA. Translation: CAA71149.2 .
U86453 mRNA. Translation: AAC25677.1 .
JN190435 mRNA. Translation: AEK81610.1 .
DQ263594 mRNA. Translation: ABB83814.1 .
AL691449 Genomic DNA. Translation: CAI15703.1 .
BC132919 mRNA. Translation: AAI32920.1 .
BC132921 mRNA. Translation: AAI32922.1 .
CCDSi CCDS104.1. [O00329-1 ]
RefSeqi NP_005017.3. NM_005026.3. [O00329-1 ]
XP_006710749.1. XM_006710686.1. [O00329-1 ]
XP_006710750.1. XM_006710687.1. [O00329-1 ]
XP_006710751.1. XM_006710688.1. [O00329-1 ]
XP_006710752.1. XM_006710689.1. [O00329-1 ]
UniGenei Hs.518451.

3D structure databases

ProteinModelPortali O00329.
SMRi O00329. Positions 20-102, 109-1027.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111311. 9 interactions.
IntActi O00329. 8 interactions.
STRINGi 9606.ENSP00000366563.

Chemistry

BindingDBi O00329.
ChEMBLi CHEMBL2111432.
GuidetoPHARMACOLOGYi 2155.

PTM databases

PhosphoSitei O00329.

Proteomic databases

MaxQBi O00329.
PaxDbi O00329.
PRIDEi O00329.

Protocols and materials databases

DNASUi 5293.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377346 ; ENSP00000366563 ; ENSG00000171608 . [O00329-1 ]
GeneIDi 5293.
KEGGi hsa:5293.
UCSCi uc001aqb.4. human. [O00329-1 ]

Organism-specific databases

CTDi 5293.
GeneCardsi GC01P009711.
HGNCi HGNC:8977. PIK3CD.
HPAi CAB015420.
MIMi 602839. gene.
615513. phenotype.
neXtProti NX_O00329.
PharmGKBi PA33310.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5032.
HOGENOMi HOG000252911.
HOVERGENi HBG052721.
KOi K00922.
OrthoDBi EOG70CR65.
PhylomeDBi O00329.
TreeFami TF102031.

Enzyme and pathway databases

UniPathwayi UPA00220 .
BioCyci MetaCyc:ENSG00000171608-MONOMER.
BRENDAi 2.7.1.137. 2681.
Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_23787. Regulation of signaling by CBL.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23891. Interleukin receptor SHC signaling.
REACT_75829. PIP3 activates AKT signaling.
SignaLinki O00329.

Miscellaneous databases

ChiTaRSi PIK3CD. human.
GeneWikii P110%CE%B4.
GenomeRNAii 5293.
NextBioi 20454.
PROi O00329.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00329.
Bgeei O00329.
CleanExi HS_PIK3CD.
Genevestigatori O00329.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Vanhaesebroeck B.A.M.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 675.
  3. "p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes."
    Chantry D., Vojtek A., Kashishian A., Holtzman D.A., Wood C., Gray P.W., Cooper J.A., Hoekstra M.F.
    J. Biol. Chem. 272:19236-19241(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "p37delta is a new isoform of PI3K p110delta that increases cell proliferation and is overexpressed in tumors."
    Fransson S., Uv A., Eriksson H., Andersson M.K., Wettergren Y., Bergo M., Ejeskar K.
    Oncogene 31:3277-3286(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, INTERACTION WITH HRAS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Peripheral blood leukocyte.
  5. "Variations in the human phosphoinositide-3-kinase p110 gene in children with primary B-cell immunodeficiency of unknown etiology."
    Jou S.-T., Chien Y.-H., Yang Y.-H., Shyur S.-D., Chou C.-C., Chiang B.-L.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "Autophosphorylation of p110 delta phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo."
    Vanhaesebroeck B., Higashi K., Raven C., Welham M., Anderson S., Brennan P., Ward S.G., Waterfield M.D.
    EMBO J. 18:1292-1302(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1031-1040, PHOSPHORYLATION AT SER-1039, MUTAGENESIS OF ARG-894 AND SER-1039.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-524 AND SER-1039, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "PI3K p110delta regulates T-cell cytokine production during primary and secondary immune responses in mice and humans."
    Soond D.R., Bjorgo E., Moltu K., Dale V.Q., Patton D.T., Torgersen K.M., Galleway F., Twomey B., Clark J., Gaston J.S.H., Tasken K., Bunyard P., Okkenhaug K.
    Blood 115:2203-2213(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T-CELLS, ENZYME REGULATION.
  11. "PI3K delta and PI3K gamma: partners in crime in inflammation in rheumatoid arthritis and beyond?"
    Rommel C., Camps M., Ji H.
    Nat. Rev. Immunol. 7:191-201(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  12. "Phosphoinositide 3-kinase delta (PI3Kdelta) in leukocyte signaling and function."
    Fung-Leung W.-P.
    Cell. Signal. 23:603-608(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  13. Cited for: VARIANT APDS LYS-1021, CHARACTERIZATION OF VARIANT APDS LYS-1021.

Entry informationi

Entry nameiPK3CD_HUMAN
AccessioniPrimary (citable) accession number: O00329
Secondary accession number(s): A6NCG0
, G1FFP1, O15445, Q5SR49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 7, 2005
Last modified: September 3, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

IC87114 inhibitor reduces passive cutaneous anaphylaxis, attenuates allergic airway inflammation and hyperresponsiveness and allergen induced rhinitis response. Inhibitors may have therapeutic potential for the treatment of immune system-mediated diseases such as auto-immune diseases, inflammation and allergy (1 Publication; 1 Publication).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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