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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

  • 1-phosphatidylinositol-3-kinase activity Source: UniProtKB
  • 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: MGI
  • phosphatidylinositol 3-kinase activity Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome

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 biosynthetic process Source: Reactome
  • phosphatidylinositol-mediated signaling Source: Reactome
  • phosphorylation Source: MGI
  • 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.
ZFISH: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-8853659. RET 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 databases

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_0709181021E → K in APDS; results in gain of function causing enhanced membrane association and kinase activity. 1 PublicationCorresponds to variant rs397518423dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi894R → P: Abolishes lipid and protein kinase activities. 1 Publication1
Mutagenesisi1039S → A: Abolishes autophosphorylation, no effect on lipid kinase activity. 1 Publication1
Mutagenesisi1039S → D or E: Abolishes autophosphorylation, reduced lipid kinase activity. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5293.
MalaCardsiPIK3CD.
MIMi615513. phenotype.
OpenTargetsiENSG00000171608.
Orphaneti397596. Activated PIK3-delta syndrome.
PharmGKBiPA33310.

Chemistry databases

ChEMBLiCHEMBL3130.
DrugBankiDB00201. Caffeine.
GuidetoPHARMACOLOGYi2155.

Polymorphism and mutation databases

BioMutaiPIK3CD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000887901 – 1044Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoformAdd BLAST1044

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei315PhosphoserineBy similarity1
Modified residuei524PhosphotyrosineCombined sources1
Modified residuei1039Phosphoserine; by autocatalysisCombined sources1 Publication1

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.
PeptideAtlasiO00329.
PRIDEiO00329.

PTM databases

iPTMnetiO00329.
PhosphoSitePlusiO00329.

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

BgeeiENSG00000171608.
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-718309,EBI-350145

Protein-protein interaction databases

BioGridi111311. 10 interactors.
IntActiO00329. 9 interactors.
STRINGi9606.ENSP00000366563.

Chemistry databases

BindingDBiO00329.

Structurei

Secondary structure

11044
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 25Combined sources7
Beta strandi31 – 37Combined sources7
Helixi42 – 53Combined sources12
Helixi59 – 61Combined sources3
Helixi65 – 67Combined sources3
Beta strandi68 – 74Combined sources7
Beta strandi79 – 82Combined sources4
Helixi89 – 92Combined sources4
Beta strandi94 – 104Combined sources11
Helixi108 – 121Combined sources14
Helixi126 – 130Combined sources5
Helixi134 – 156Combined sources23
Helixi159 – 166Combined sources8
Beta strandi192 – 196Combined sources5
Beta strandi203 – 205Combined sources3
Helixi213 – 221Combined sources9
Helixi236 – 238Combined sources3
Beta strandi239 – 243Combined sources5
Beta strandi248 – 250Combined sources3
Helixi256 – 258Combined sources3
Helixi260 – 268Combined sources9
Beta strandi273 – 278Combined sources6
Helixi279 – 286Combined sources8
Beta strandi321 – 332Combined sources12
Beta strandi339 – 349Combined sources11
Beta strandi352 – 355Combined sources4
Beta strandi370 – 380Combined sources11
Turni381 – 383Combined sources3
Beta strandi389 – 397Combined sources9
Beta strandi416 – 426Combined sources11
Beta strandi430 – 432Combined sources3
Beta strandi435 – 440Combined sources6
Turni465 – 467Combined sources3
Beta strandi470 – 475Combined sources6
Helixi488 – 491Combined sources4
Turni492 – 495Combined sources4
Helixi506 – 515Combined sources10
Helixi525 – 533Combined sources9
Helixi535 – 541Combined sources7
Helixi543 – 545Combined sources3
Helixi546 – 552Combined sources7
Helixi558 – 569Combined sources12
Helixi576 – 582Combined sources7
Helixi590 – 600Combined sources11
Helixi605 – 610Combined sources6
Helixi612 – 618Combined sources7
Helixi619 – 621Combined sources3
Beta strandi623 – 626Combined sources4
Helixi628 – 639Combined sources12
Helixi641 – 652Combined sources12
Turni653 – 656Combined sources4
Helixi658 – 673Combined sources16
Helixi676 – 705Combined sources30
Helixi708 – 720Combined sources13
Helixi722 – 728Combined sources7
Beta strandi729 – 732Combined sources4
Beta strandi739 – 741Combined sources3
Turni746 – 748Combined sources3
Beta strandi759 – 764Combined sources6
Beta strandi775 – 782Combined sources8
Helixi785 – 802Combined sources18
Turni803 – 805Combined sources3
Beta strandi815 – 819Combined sources5
Beta strandi822 – 826Combined sources5
Beta strandi829 – 833Combined sources5
Helixi834 – 839Combined sources6
Helixi854 – 862Combined sources9
Helixi865 – 867Combined sources3
Helixi868 – 888Combined sources21
Beta strandi898 – 902Combined sources5
Beta strandi907 – 909Combined sources3
Helixi936 – 942Combined sources7
Turni943 – 945Combined sources3
Helixi950 – 969Combined sources20
Helixi971 – 981Combined sources11
Helixi982 – 984Combined sources3
Helixi992 – 1001Combined sources10
Turni1002 – 1005Combined sources4
Helixi1008 – 1030Combined sources23

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 105PI3K-ABDPROSITE-ProRule annotationAdd BLAST90
Domaini187 – 278PI3K-RBDPROSITE-ProRule annotationAdd BLAST92
Domaini319 – 476C2 PI3K-typePROSITE-ProRule annotationAdd BLAST158
Domaini497 – 674PIK helicalPROSITE-ProRule annotationAdd BLAST178
Domaini774 – 1041PI3K/PI4KPROSITE-ProRule annotationAdd BLAST268

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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti253S → N in AAC25677 (PubMed:9235916).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0709181021E → K in APDS; results in gain of function causing enhanced membrane association and kinase activity. 1 PublicationCorresponds to variant rs397518423dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044409201 – 300ESFTF…VQKPR → VSPCVACGIQAALSMGSTSS VKLLSHPQAPLPQWHQMVFA RCLCMCGAQLNVPPGELHLP GVHQGRAAGADGLCPAEEGH SVPAAAGGAAGRLHAAGERQ in isoform 2. 1 PublicationAdd BLAST100
Alternative sequenceiVSP_044410302 – 1044Missing in isoform 2. 1 PublicationAdd BLAST743

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_006710750.1. XM_006710687.2. [O00329-1]
XP_006710752.1. XM_006710689.2. [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_006710750.1. XM_006710687.2. [O00329-1]
XP_006710752.1. XM_006710689.2. [O00329-1]
UniGeneiHs.518451.

3D structure databases

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

Protein-protein interaction databases

BioGridi111311. 10 interactors.
IntActiO00329. 9 interactors.
STRINGi9606.ENSP00000366563.

Chemistry databases

BindingDBiO00329.
ChEMBLiCHEMBL3130.
DrugBankiDB00201. Caffeine.
GuidetoPHARMACOLOGYi2155.
SwissLipidsiSLP:000000908.

PTM databases

iPTMnetiO00329.
PhosphoSitePlusiO00329.

Polymorphism and mutation databases

BioMutaiPIK3CD.

Proteomic databases

EPDiO00329.
MaxQBiO00329.
PaxDbiO00329.
PeptideAtlasiO00329.
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.
DisGeNETi5293.
GeneCardsiPIK3CD.
HGNCiHGNC:8977. PIK3CD.
HPAiCAB015420.
HPA044953.
MalaCardsiPIK3CD.
MIMi602839. gene.
615513. phenotype.
neXtProtiNX_O00329.
OpenTargetsiENSG00000171608.
Orphaneti397596. Activated PIK3-delta syndrome.
PharmGKBiPA33310.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00220.
BioCyciMetaCyc:ENSG00000171608-MONOMER.
ZFISH: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-8853659. RET 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

BgeeiENSG00000171608.
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...

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: November 30, 2016
This is version 164 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.