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O35904

- PK3CD_MOUSE

UniProt

O35904 - PK3CD_MOUSE

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Protein

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

Gene

Pik3cd

Organism
Mus musculus (Mouse)
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.7 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. Among other effects, IC87114 reduces allergic responses, prevents the recruitment of antigen-specific T cells into target tissue, and affects natural killer cell chemotaxis.3 Publications

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. B cell activation Source: MGI
  2. B cell homeostasis Source: MGI
  3. cell differentiation Source: UniProtKB-KW
  4. cell surface receptor signaling pathway Source: MGI
  5. chemotaxis Source: UniProtKB-KW
  6. inflammatory response Source: UniProtKB-KW
  7. innate immune response Source: UniProtKB-KW
  8. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  9. phosphatidylinositol-mediated signaling Source: InterPro
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

BRENDAi2.7.1.153. 3474.
ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198634. Regulation of signaling by CBL.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_210793. Interleukin receptor SHC signaling.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_226341. PIP3 activates AKT signaling.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1098211. Pik3cd.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. phosphatidylinositol 3-kinase complex Source: RefGenome
  2. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Null mutants are viable and fertile but display defective adaptive and innate immune responses due to signaling defects in multiple cell types including B-, T- and mast and natural killer cells.5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi910 – 9101D → A: Inhibits lipid kinase activity. Mice are viable and fertile but display defective adaptive and innate immune responses Signaling defects in B-cells, T-cells, mast cells and natural killer cells. Reduced B and T-cell receptor signaling. Affects development and differentiation of B -ells. Reduced memory T-cell number. Affects B- and T-cell proliferation. Attenuates immune responses in vivo. Induces inflammatory bowel disease development. Lost TCR-induced migration and localization to antigenic tissue. Affects natural killer cell maturation and cytokine production. 4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10431043Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoformPRO_0000088791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei523 – 5231PhosphotyrosineBy similarity
Modified residuei1038 – 10381Phosphoserine; by autocatalysisBy similarity

Post-translational modificationi

Autophosphorylation on Ser-1038 results in the almost complete inactivation of the lipid kinase activity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO35904.
PaxDbiO35904.
PRIDEiO35904.

PTM databases

PhosphoSiteiO35904.

Expressioni

Tissue specificityi

Isoform 1 is expressed in spleen and lung (at protein level). Isoform 1 is expressed predominantly in leukocytes.1 Publication

Gene expression databases

BgeeiO35904.
ExpressionAtlasiO35904. baseline and differential.
GenevestigatoriO35904.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Pik3r1P264502EBI-6470774,EBI-641764

Protein-protein interaction databases

BioGridi202161. 2 interactions.
DIPiDIP-39841N.
IntActiO35904. 6 interactions.

Structurei

Secondary structure

1
1043
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi110 – 12112
Helixi126 – 1305
Helixi134 – 15421
Helixi159 – 1668
Beta strandi189 – 19810
Beta strandi202 – 2087
Helixi213 – 22715
Helixi236 – 2383
Beta strandi239 – 2435
Beta strandi252 – 2543
Helixi256 – 2583
Helixi260 – 2689
Beta strandi273 – 2786
Helixi279 – 28810
Beta strandi321 – 33111
Beta strandi340 – 34910
Beta strandi352 – 3554
Beta strandi363 – 3653
Beta strandi370 – 38011
Helixi381 – 3833
Beta strandi389 – 3979
Beta strandi416 – 42611
Beta strandi430 – 4323
Beta strandi435 – 4406
Beta strandi455 – 4573
Turni465 – 4673
Beta strandi470 – 4756
Helixi488 – 4936
Helixi511 – 5144
Helixi524 – 5329
Helixi534 – 5407
Helixi542 – 5443
Helixi545 – 5495
Helixi557 – 56812
Helixi575 – 5817
Helixi589 – 59911
Helixi604 – 61714
Helixi618 – 6203
Beta strandi622 – 6254
Helixi627 – 63812
Helixi640 – 65112
Turni652 – 6554
Helixi657 – 67317
Helixi675 – 70127
Turni702 – 7043
Helixi707 – 71812
Helixi721 – 7277
Beta strandi728 – 7325
Beta strandi735 – 7406
Helixi745 – 7473
Beta strandi753 – 7553
Beta strandi758 – 7636
Turni765 – 7673
Helixi768 – 7714
Beta strandi773 – 7819
Helixi784 – 80219
Beta strandi814 – 8185
Beta strandi821 – 8255
Beta strandi828 – 8325
Helixi833 – 8375
Beta strandi841 – 8433
Helixi850 – 8523
Helixi853 – 8619
Turni863 – 8653
Helixi866 – 88823
Beta strandi897 – 9015
Beta strandi906 – 9083
Helixi935 – 9417
Turni942 – 9443
Helixi949 – 96820
Helixi970 – 98011
Helixi981 – 9833
Beta strandi988 – 9903
Helixi991 – 100111
Turni1002 – 10043
Helixi1007 – 102418

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WXFX-ray1.90A106-1043[»]
2WXGX-ray2.00A106-1043[»]
2WXHX-ray1.90A106-1043[»]
2WXIX-ray2.80A106-1043[»]
2WXJX-ray2.60A106-1043[»]
2WXKX-ray2.90A106-1043[»]
2WXLX-ray1.99A106-1043[»]
2WXMX-ray2.80A106-1043[»]
2WXNX-ray2.60A106-1043[»]
2WXOX-ray2.49A106-1043[»]
2WXPX-ray2.30A106-1043[»]
2WXQX-ray2.70A106-1043[»]
2WXRX-ray2.50A106-1043[»]
2X38X-ray2.20A106-1043[»]
4AJWX-ray2.80A/B110-1043[»]
ProteinModelPortaliO35904.
SMRiO35904. Positions 20-102, 109-1026.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35904.

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
Domaini496 – 673178PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini775 – 1028254PI3K/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

eggNOGiCOG5032.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000252911.
HOVERGENiHBG052721.
InParanoidiO35904.
KOiK00922.

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: O35904) [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 FWTKEESQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQVLW
60 70 80 90 100
HRAQYEPLFH MLSDPEAYVF TCVNQTAEQQ ELEDEQRRLC DIQPFLPVLR
110 120 130 140 150
LVAREGDRVK KLINSQISLL IGKGLHEFDS LRDPEVNDFR TKMRQFCEEA
160 170 180 190 200
AAHRQQLGWV EWLQYSFPLQ LEPSARGWRA GLLRVSNRAL LVNVKFEGSE
210 220 230 240 250
ESFTFQVSTK DMPLALMACA LRKKATVFRQ PLVEQPEEYA LQVNGRHEYL
260 270 280 290 300
YGNYPLCHFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR
310 320 330 340 350
AKPPPIPAKK PSSVSLWSLE QPFSIELIEG RKVNADERMK LVVQAGLFHG
360 370 380 390 400
NEMLCKTVSS SEVNVCSEPV WKQRLEFDIS VCDLPRMARL CFALYAVVEK
410 420 430 440 450
AKKARSTKKK SKKADCPIAW ANLMLFDYKD QLKTGERCLY MWPSVPDEKG
460 470 480 490 500
ELLNPAGTVR GNPNTESAAA LVIYLPEVAP HPVYFPALEK ILELGRHGER
510 520 530 540 550
GRITEEELQL REILERRGSG ELYEHEKDLV WKMRHEVQEH FPEALARLLL
560 570 580 590 600
VTKWNKHEDV AQMLYLLCSW PELPVLSALE LLDFSFPDCY VGSFAIKSLR
610 620 630 640 650
KLTDDELFQY LLQLVQVLKY ESYLDCELTK FLLGRALANR KIGHFLFWHL
660 670 680 690 700
RSEMHVPSVA LRFGLIMEAY CRGSTHHMKV LMKQGEALSK LKALNDFVKV
710 720 730 740 750
SSQKTTKPQT KEMMHMCMRQ ETYMEALSHL QSPLDPSTLL EEVCVEQCTF
760 770 780 790 800
MDSKMKPLWI MYSSEEAGSA GNVGIIFKNG DDLRQDMLTL QMIQLMDVLW
810 820 830 840 850
KQEGLDLRMT PYGCLPTGDR TGLIEVVLHS DTIANIQLNK SNMAATAAFN
860 870 880 890 900
KDALLNWLKS KNPGEALDRA IEEFTLSCAG YCVATYVLGI GDRHSDNIMI
910 920 930 940 950
RESGQLFHID FGHFLGNFKT KFGINRERVP FILTYDFVHV IQQGKTNNSE
960 970 980 990 1000
KFERFRGYCE RAYTILRRHG LLFLHLFALM RAAGLPELSC SKDIQYLKDS
1010 1020 1030 1040
LALGKTEEEA LKHFRVKFNE ALRESWKTKV NWLAHNVSKD NRQ
Length:1,043
Mass (Da):119,712
Last modified:July 27, 2011 - v2
Checksum:iAD8DE07D8F847795
GO
Isoform 2 (identifier: O35904-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     201-212: ESFTFQVSTKDM → VSPSPIPSPSSI
     213-1043: Missing.

Note: No experimental confirmation available.

Show »
Length:212
Mass (Da):24,355
Checksum:iF61391FD8427F323
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221G → A in AAC25676. (PubMed:9235916)Curated
Sequence conflicti584 – 5841F → S in AAC25676. (PubMed:9235916)Curated
Sequence conflicti651 – 6511R → H in AAC25676. (PubMed:9235916)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei201 – 21212ESFTF…STKDM → VSPSPIPSPSSI in isoform 2. CuratedVSP_044411Add
BLAST
Alternative sequencei213 – 1043831Missing in isoform 2. CuratedVSP_044412Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U86587 mRNA. Translation: AAC25676.1.
AF532989 Genomic DNA. Translation: AAN05615.1.
AL607078 Genomic DNA. Translation: CAM23914.1.
CU207384 Genomic DNA. Translation: CAQ51667.1.
CH466594 Genomic DNA. Translation: EDL14872.1.
CCDSiCCDS51380.1. [O35904-1]
PIRiT43502.
RefSeqiNP_001157524.1. NM_001164052.1. [O35904-1]
XP_006536078.1. XM_006536015.1. [O35904-1]
XP_006538715.1. XM_006538652.1. [O35904-1]
UniGeneiMm.229108.

Genome annotation databases

EnsembliENSMUST00000105689; ENSMUSP00000101314; ENSMUSG00000039936. [O35904-1]
GeneIDi18707.
KEGGimmu:18707.
UCSCiuc008vwq.1. mouse. [O35904-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U86587 mRNA. Translation: AAC25676.1 .
AF532989 Genomic DNA. Translation: AAN05615.1 .
AL607078 Genomic DNA. Translation: CAM23914.1 .
CU207384 Genomic DNA. Translation: CAQ51667.1 .
CH466594 Genomic DNA. Translation: EDL14872.1 .
CCDSi CCDS51380.1. [O35904-1 ]
PIRi T43502.
RefSeqi NP_001157524.1. NM_001164052.1. [O35904-1 ]
XP_006536078.1. XM_006536015.1. [O35904-1 ]
XP_006538715.1. XM_006538652.1. [O35904-1 ]
UniGenei Mm.229108.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WXF X-ray 1.90 A 106-1043 [» ]
2WXG X-ray 2.00 A 106-1043 [» ]
2WXH X-ray 1.90 A 106-1043 [» ]
2WXI X-ray 2.80 A 106-1043 [» ]
2WXJ X-ray 2.60 A 106-1043 [» ]
2WXK X-ray 2.90 A 106-1043 [» ]
2WXL X-ray 1.99 A 106-1043 [» ]
2WXM X-ray 2.80 A 106-1043 [» ]
2WXN X-ray 2.60 A 106-1043 [» ]
2WXO X-ray 2.49 A 106-1043 [» ]
2WXP X-ray 2.30 A 106-1043 [» ]
2WXQ X-ray 2.70 A 106-1043 [» ]
2WXR X-ray 2.50 A 106-1043 [» ]
2X38 X-ray 2.20 A 106-1043 [» ]
4AJW X-ray 2.80 A/B 110-1043 [» ]
ProteinModelPortali O35904.
SMRi O35904. Positions 20-102, 109-1026.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202161. 2 interactions.
DIPi DIP-39841N.
IntActi O35904. 6 interactions.

Chemistry

ChEMBLi CHEMBL2216745.

PTM databases

PhosphoSitei O35904.

Proteomic databases

MaxQBi O35904.
PaxDbi O35904.
PRIDEi O35904.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000105689 ; ENSMUSP00000101314 ; ENSMUSG00000039936 . [O35904-1 ]
GeneIDi 18707.
KEGGi mmu:18707.
UCSCi uc008vwq.1. mouse. [O35904-1 ]

Organism-specific databases

CTDi 5293.
MGIi MGI:1098211. Pik3cd.

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00760000119110.
HOGENOMi HOG000252911.
HOVERGENi HBG052721.
InParanoidi O35904.
KOi K00922.

Enzyme and pathway databases

UniPathwayi UPA00220 .
BRENDAi 2.7.1.153. 3474.
Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198634. Regulation of signaling by CBL.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_210793. Interleukin receptor SHC signaling.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_226341. PIP3 activates AKT signaling.

Miscellaneous databases

ChiTaRSi PIK3CD. mouse.
EvolutionaryTracei O35904.
NextBioi 294773.
PROi O35904.
SOURCEi Search...

Gene expression databases

Bgeei O35904.
ExpressionAtlasi O35904. baseline and differential.
Genevestigatori O35904.

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. "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).
    Tissue: Spleen.
  2. "Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice."
    Okkenhaug K., Bilancio A., Farjot G., Priddle H., Sancho S., Peskett E., Pearce W., Meek S.E., Salpekar A., Waterfield M.D., Smith A.J., Vanhaesebroeck B.
    Science 297:1031-1034(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
    Strain: 129P2.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "A crucial role for the p110delta subunit of phosphatidylinositol 3-kinase in B cell development and activation."
    Clayton E., Bardi G., Bell S.E., Chantry D., Downes C.P., Gray A., Humphries L.A., Rawlings D., Reynolds H., Vigorito E., Turner M.
    J. Exp. Med. 196:753-763(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN B-CELLS, DISRUPTION PHENOTYPE.
  6. "Role of Eras in promoting tumor-like properties in mouse embryonic stem cells."
    Takahashi K., Mitsui K., Yamanaka S.
    Nature 423:541-545(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERAS.
  7. Cited for: FUNCTION IN MAST CELLS, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
  8. "T cell development requires the combined activities of the p110gamma and p110delta catalytic isoforms of phosphatidylinositol 3-kinase."
    Webb L.M.C., Vigorito E., Wymann M.P., Hirsch E., Turner M.
    J. Immunol. 175:2783-2787(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T-CELL DEVELOPMENT.
  9. "T cell receptor-induced phosphoinositide-3-kinase p110delta activity is required for T cell localization to antigenic tissue in mice."
    Jarmin S.J., David R., Ma L., Chai J.-G., Dewchand H., Takesono A., Ridley A.J., Okkenhaug K., Marelli-Berg F.M.
    J. Clin. Invest. 118:1154-1164(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T-CELL MIGRATION, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
  10. "The p110 delta of PI3K plays a critical role in NK cell terminal maturation and cytokine/chemokine generation."
    Guo H., Samarakoon A., Vanhaesebroeck B., Malarkannan S.
    J. Exp. Med. 205:2419-2435(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NATURAL KILLER CELLS, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
  11. "p110gamma and p110delta isoforms of phosphoinositide 3-kinase differentially regulate natural killer cell migration in health and disease."
    Saudemont A., Garcon F., Yadi H., Roche-Molina M., Kim N., Segonds-Pichon A., Martin-Fontecha A., Okkenhaug K., Colucci F.
    Proc. Natl. Acad. Sci. U.S.A. 106:5795-5800(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NATURAL KILLER CELL MIGRATION, ENZYME REGULATION.
  12. "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: ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Peripheral blood leukocyte.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 106-1043 IN A COMPLEX WITH IC87114; PIK-39; SW13; SW14; SW30; DL06; DL07; ZSTK474; AS5; GDC-0941; INK654; INK666 AND AS15.

Entry informationi

Entry nameiPK3CD_MOUSE
AccessioniPrimary (citable) accession number: O35904
Secondary accession number(s): Q8CJ28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3