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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: 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: phosphatidylinositol phosphate biosynthesis

This protein is involved in the pathway phosphatidylinositol phosphate biosynthesis, which is part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phosphatidylinositol phosphate biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

GO - Biological processi

  • adaptive immune response Source: UniProtKB
  • B cell activation Source: UniProtKB
  • B cell chemotaxis Source: UniProtKB
  • B cell receptor signaling pathway Source: UniProtKB
  • cytokine production Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • innate immune response Source: UniProtKB
  • mast cell chemotaxis Source: UniProtKB
  • mast cell degranulation Source: UniProtKB
  • mast cell differentiation Source: UniProtKB
  • natural killer cell activation Source: UniProtKB
  • natural killer cell chemotaxis Source: UniProtKB
  • natural killer cell differentiation Source: UniProtKB
  • neutrophil chemotaxis Source: UniProtKB
  • neutrophil extravasation Source: UniProtKB
  • phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  • phosphatidylinositol biosynthetic process Source: Reactome
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of cell migration Source: CACAO
  • positive regulation of gene expression Source: CACAO
  • protein phosphorylation Source: UniProtKB
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • respiratory burst involved in defense response Source: UniProtKB
  • signal transduction Source: UniProtKB
  • T cell activation Source: UniProtKB
  • T cell chemotaxis Source: UniProtKB
  • T cell differentiation Source: UniProtKB
  • T cell receptor signaling pathway Source: UniProtKB
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.
2.7.1.153. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-392451. G beta:gamma signalling through PI3Kgamma.
R-HSA-512988. Interleukin-3, 5 and GM-CSF signaling.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-912526. Interleukin receptor SHC signaling.
R-HSA-912631. Regulation of signaling by CBL.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiO00329.
SIGNORiO00329.
UniPathwayiUPA00220.

Chemistry

SwissLipidsiSLP:000000908.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8977. PIK3CD.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Activated PI3K-delta syndrome (APDS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615513
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

MalaCardsiPIK3CD.
MIMi615513. phenotype.
Orphaneti397596. Activated PIK3-delta syndrome.
PharmGKBiPA33310.

Chemistry

ChEMBLiCHEMBL3559703.
DrugBankiDB00201. Caffeine.
GuidetoPHARMACOLOGYi2155.

Polymorphism and mutation databases

BioMutaiPIK3CD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10441044Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoformPRO_0000088790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei524 – 5241PhosphotyrosineCombined sources
Modified residuei1039 – 10391Phosphoserine; by autocatalysisCombined sources1 Publication

Post-translational modificationi

Autophosphorylation on Ser-1039 results in the almost complete inactivation of the lipid kinase activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO00329.
MaxQBiO00329.
PaxDbiO00329.
PRIDEiO00329.

PTM databases

iPTMnetiO00329.
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

BgeeiO00329.
CleanExiHS_PIK3CD.
ExpressionAtlasiO00329. baseline and differential.
GenevisibleiO00329. HS.

Organism-specific databases

HPAiCAB015420.
HPA044953.

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HRASP011122EBI-6470902,EBI-350145

Protein-protein interaction databases

BioGridi111311. 10 interactions.
IntActiO00329. 8 interactions.
STRINGi9606.ENSP00000366563.

Chemistry

BindingDBiO00329.

Structurei

Secondary structure

1
1044
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 257Combined sources
Beta strandi31 – 377Combined sources
Helixi42 – 5312Combined sources
Helixi59 – 613Combined sources
Helixi65 – 673Combined sources
Beta strandi68 – 747Combined sources
Beta strandi79 – 824Combined sources
Helixi89 – 924Combined sources
Beta strandi94 – 10411Combined sources
Helixi108 – 12114Combined sources
Helixi126 – 1305Combined sources
Helixi134 – 15623Combined sources
Helixi159 – 1668Combined sources
Beta strandi192 – 1965Combined sources
Beta strandi203 – 2053Combined sources
Helixi213 – 2219Combined sources
Helixi236 – 2383Combined sources
Beta strandi239 – 2435Combined sources
Beta strandi248 – 2503Combined sources
Helixi256 – 2583Combined sources
Helixi260 – 2689Combined sources
Beta strandi273 – 2786Combined sources
Helixi279 – 2868Combined sources
Beta strandi321 – 33212Combined sources
Beta strandi339 – 34911Combined sources
Beta strandi352 – 3554Combined sources
Beta strandi370 – 38011Combined sources
Turni381 – 3833Combined sources
Beta strandi389 – 3979Combined sources
Beta strandi416 – 42611Combined sources
Beta strandi430 – 4323Combined sources
Beta strandi435 – 4406Combined sources
Turni465 – 4673Combined sources
Beta strandi470 – 4756Combined sources
Helixi488 – 4914Combined sources
Turni492 – 4954Combined sources
Helixi506 – 51510Combined sources
Helixi525 – 5339Combined sources
Helixi535 – 5417Combined sources
Helixi543 – 5453Combined sources
Helixi546 – 5527Combined sources
Helixi558 – 56912Combined sources
Helixi576 – 5827Combined sources
Helixi590 – 60011Combined sources
Helixi605 – 6106Combined sources
Helixi612 – 6187Combined sources
Helixi619 – 6213Combined sources
Beta strandi623 – 6264Combined sources
Helixi628 – 63912Combined sources
Helixi641 – 65212Combined sources
Turni653 – 6564Combined sources
Helixi658 – 67316Combined sources
Helixi676 – 70530Combined sources
Helixi708 – 72013Combined sources
Helixi722 – 7287Combined sources
Beta strandi729 – 7324Combined sources
Beta strandi739 – 7413Combined sources
Turni746 – 7483Combined sources
Beta strandi759 – 7646Combined sources
Beta strandi775 – 7828Combined sources
Helixi785 – 80218Combined sources
Turni803 – 8053Combined sources
Beta strandi815 – 8195Combined sources
Beta strandi822 – 8265Combined sources
Beta strandi829 – 8335Combined sources
Helixi834 – 8396Combined sources
Helixi854 – 8629Combined sources
Helixi865 – 8673Combined sources
Helixi868 – 88821Combined sources
Beta strandi898 – 9025Combined sources
Beta strandi907 – 9093Combined sources
Helixi936 – 9427Combined sources
Turni943 – 9453Combined sources
Helixi950 – 96920Combined sources
Helixi971 – 98111Combined sources
Helixi982 – 9843Combined sources
Helixi992 – 100110Combined sources
Turni1002 – 10054Combined sources
Helixi1008 – 103023Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5DXUX-ray2.64A2-1044[»]
ProteinModelPortaliO00329.
SMRiO00329. Positions 108-1032.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 10590PI3K-ABDPROSITE-ProRule annotationAdd
BLAST
Domaini187 – 27892PI3K-RBDPROSITE-ProRule annotationAdd
BLAST
Domaini319 – 476158C2 PI3K-typePROSITE-ProRule annotationAdd
BLAST
Domaini497 – 674178PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini774 – 1041268PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
Contains 1 C2 PI3K-type domain.PROSITE-ProRule annotation
Contains 1 PI3K-ABD domain.PROSITE-ProRule annotation
Contains 1 PI3K-RBD domain.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 1 PIK helical domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0904. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000252911.
HOVERGENiHBG052721.
InParanoidiO00329.
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. AlignAdd to basket

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

        10         20         30         40         50
MPPGVDCPME FWTKEENQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQLLW
60 70 80 90 100
HRAQYEPLFH MLSGPEAYVF TCINQTAEQQ ELEDEQRRLC DVQPFLPVLR
110 120 130 140 150
LVAREGDRVK KLINSQISLL IGKGLHEFDS LCDPEVNDFR AKMCQFCEEA
160 170 180 190 200
AARRQQLGWE AWLQYSFPLQ LEPSAQTWGP GTLRLPNRAL LVNVKFEGSE
210 220 230 240 250
ESFTFQVSTK DVPLALMACA LRKKATVFRQ PLVEQPEDYT LQVNGRHEYL
260 270 280 290 300
YGSYPLCQFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR
310 320 330 340 350
AKPPPIPAKK PSSVSLWSLE QPFRIELIQG SKVNADERMK LVVQAGLFHG
360 370 380 390 400
NEMLCKTVSS SEVSVCSEPV WKQRLEFDIN ICDLPRMARL CFALYAVIEK
410 420 430 440 450
AKKARSTKKK SKKADCPIAW ANLMLFDYKD QLKTGERCLY MWPSVPDEKG
460 470 480 490 500
ELLNPTGTVR SNPNTDSAAA LLICLPEVAP HPVYYPALEK ILELGRHSEC
510 520 530 540 550
VHVTEEEQLQ LREILERRGS GELYEHEKDL VWKLRHEVQE HFPEALARLL
560 570 580 590 600
LVTKWNKHED VAQMLYLLCS WPELPVLSAL ELLDFSFPDC HVGSFAIKSL
610 620 630 640 650
RKLTDDELFQ YLLQLVQVLK YESYLDCELT KFLLDRALAN RKIGHFLFWH
660 670 680 690 700
LRSEMHVPSV ALRFGLILEA YCRGSTHHMK VLMKQGEALS KLKALNDFVK
710 720 730 740 750
LSSQKTPKPQ TKELMHLCMR QEAYLEALSH LQSPLDPSTL LAEVCVEQCT
760 770 780 790 800
FMDSKMKPLW IMYSNEEAGS GGSVGIIFKN GDDLRQDMLT LQMIQLMDVL
810 820 830 840 850
WKQEGLDLRM TPYGCLPTGD RTGLIEVVLR SDTIANIQLN KSNMAATAAF
860 870 880 890 900
NKDALLNWLK SKNPGEALDR AIEEFTLSCA GYCVATYVLG IGDRHSDNIM
910 920 930 940 950
IRESGQLFHI DFGHFLGNFK TKFGINRERV PFILTYDFVH VIQQGKTNNS
960 970 980 990 1000
EKFERFRGYC ERAYTILRRH GLLFLHLFAL MRAAGLPELS CSKDIQYLKD
1010 1020 1030 1040
SLALGKTEEE ALKHFRVKFN EALRESWKTK VNWLAHNVSK DNRQ
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531S → N in AAC25677 (PubMed:9235916).Curated

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. 1 PublicationVSP_044409Add
BLAST
Alternative sequencei302 – 1044743Missing in isoform 2. 1 PublicationVSP_044410Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_011539883.1. XM_011541581.1. [O00329-1]
UniGeneiHs.518451.

Genome annotation databases

EnsembliENST00000377346; ENSP00000366563; ENSG00000171608. [O00329-1]
GeneIDi5293.
KEGGihsa:5293.
UCSCiuc001aqb.5. 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:
EMBLi
GenBanki
DDBJi
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]
XP_011539883.1. XM_011541581.1. [O00329-1]
UniGeneiHs.518451.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5DXUX-ray2.64A2-1044[»]
ProteinModelPortaliO00329.
SMRiO00329. Positions 108-1032.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111311. 10 interactions.
IntActiO00329. 8 interactions.
STRINGi9606.ENSP00000366563.

Chemistry

BindingDBiO00329.
ChEMBLiCHEMBL3559703.
DrugBankiDB00201. Caffeine.
GuidetoPHARMACOLOGYi2155.
SwissLipidsiSLP:000000908.

PTM databases

iPTMnetiO00329.
PhosphoSiteiO00329.

Polymorphism and mutation databases

BioMutaiPIK3CD.

Proteomic databases

EPDiO00329.
MaxQBiO00329.
PaxDbiO00329.
PRIDEiO00329.

Protocols and materials databases

DNASUi5293.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377346; ENSP00000366563; ENSG00000171608. [O00329-1]
GeneIDi5293.
KEGGihsa:5293.
UCSCiuc001aqb.5. human. [O00329-1]

Organism-specific databases

CTDi5293.
GeneCardsiPIK3CD.
HGNCiHGNC:8977. PIK3CD.
HPAiCAB015420.
HPA044953.
MalaCardsiPIK3CD.
MIMi602839. gene.
615513. phenotype.
neXtProtiNX_O00329.
Orphaneti397596. Activated PIK3-delta syndrome.
PharmGKBiPA33310.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0904. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000252911.
HOVERGENiHBG052721.
InParanoidiO00329.
KOiK00922.
OrthoDBiEOG70CR65.
PhylomeDBiO00329.
TreeFamiTF102031.

Enzyme and pathway databases

UniPathwayiUPA00220.
BioCyciMetaCyc:ENSG00000171608-MONOMER.
BRENDAi2.7.1.137. 2681.
2.7.1.153. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-392451. G beta:gamma signalling through PI3Kgamma.
R-HSA-512988. Interleukin-3, 5 and GM-CSF signaling.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-912526. Interleukin receptor SHC signaling.
R-HSA-912631. Regulation of signaling by CBL.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiO00329.
SIGNORiO00329.

Miscellaneous databases

ChiTaRSiPIK3CD. human.
GeneWikiiP110%CE%B4.
GenomeRNAii5293.
PROiO00329.
SOURCEiSearch...

Gene expression databases

BgeeiO00329.
CleanExiHS_PIK3CD.
ExpressionAtlasiO00329. baseline and differential.
GenevisibleiO00329. HS.

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]
ProtoNetiSearch...

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: June 8, 2016
This is version 159 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 (PubMed:20940048; PubMed:17290298).

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.