O00329 (PK3CD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
Short name=PI3-kinase subunit delta
Short name=PI3K-delta
Short name=PI3Kdelta
Short name=PtdIns-3-kinase subunit delta
EC=2.7.1.153

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 names

Name:

PIK3CD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1044 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4 Ref.10
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.
Enzyme regulation	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. Ref.10
Pathway	Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis.
Subunit structure	Heterodimer of a catalytic subunit PIK3CD and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interacts with ERAS By similarity. Interacts with HRAS. Ref.4
Subcellular location	Cytoplasm Ref.4.
Tissue specificity	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. Ref.4
Post-translational modification	Autophosphorylation on Ser-1039 results in the almost complete inactivation of the lipid kinase activity.
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 (Ref.12; Ref.11).
Sequence similarities	Belongs to the PI3/PI4-kinase family. Contains 1 C2 PI3K-type domain. Contains 1 PI3K-ABD domain. Contains 1 PI3K-RBD domain. Contains 1 PI3K/PI4K domain. Contains 1 PIK helical domain.

Ontologies

Keywords
Biological process	Adaptive immunity Chemotaxis Differentiation Immunity Inflammatory response Innate immunity
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell activation Traceable author statement Ref.12. Source: UniProtKB B cell chemotaxis Traceable author statement Ref.12. Source: UniProtKB B cell homeostasis Inferred from electronic annotation. Source: Compara B cell receptor signaling pathway Traceable author statement Ref.12. Source: UniProtKB T cell chemotaxis Traceable author statement Ref.12. Source: UniProtKB T cell differentiation Traceable author statement Ref.12. Source: UniProtKB T cell receptor signaling pathway Traceable author statement Ref.12. Source: UniProtKB adaptive immune response Traceable author statement Ref.11. Source: UniProtKB cytokine production Traceable author statement Ref.12. Source: UniProtKB epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome inflammatory response Traceable author statement Ref.11Ref.12. Source: UniProtKB innate immune response Traceable author statement Ref.11Ref.12. Source: UniProtKB mast cell chemotaxis Traceable author statement Ref.12. Source: UniProtKB mast cell degranulation Traceable author statement Ref.12. Source: UniProtKB mast cell differentiation Traceable author statement Ref.12. Source: UniProtKB natural killer cell chemotaxis Traceable author statement Ref.12. Source: UniProtKB natural killer cell differentiation Traceable author statement Ref.12. Source: UniProtKB neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome neutrophil chemotaxis Traceable author statement Ref.12. Source: UniProtKB neutrophil extravasation Traceable author statement Ref.12. Source: UniProtKB phosphatidylinositol 3-kinase cascade Traceable author statement Ref.11. Source: UniProtKB protein phosphorylation Non-traceable author statement Ref.1. Source: UniProtKB respiratory burst involved in defense response Traceable author statement Ref.12. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	phosphatidylinositol 3-kinase complex Non-traceable author statement Ref.1Ref.3. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome
Molecular_function	1-phosphatidylinositol-3-kinase activity Non-traceable author statement Ref.3. Source: UniProtKB 1-phosphatidylinositol-4-phosphate 3-kinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-4,5-bisphosphate 3-kinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HRAS	P01112	2	EBI-718309,EBI-350145

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O00329-1)

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.

Isoform 2 (identifier: O00329-2)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1044	1044	Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform		PRO_0000088790
Regions
	Domain	16 – 105	90	PI3K-ABD
	Domain	187 – 278	92	PI3K-RBD
	Domain	319 – 476	158	C2 PI3K-type
	Domain	497 – 674	178	PIK helical
	Domain	774 – 1041	268	PI3K/PI4K
Amino acid modifications
	Modified residue	524	1	Phosphotyrosine Ref.9
	Modified residue	1039	1	Phosphoserine; by autocatalysis Ref.8 Ref.9
Natural variations
	Alternative sequence	201 – 300	100	ESFTF…VQKPR → VSPCVACGIQAALSMGSTSS VKLLSHPQAPLPQWHQMVFA RCLCMCGAQLNVPPGELHLP GVHQGRAAGADGLCPAEEGH SVPAAAGGAAGRLHAAGERQ in isoform 2.		VSP_044409
	Alternative sequence	302 – 1044	743	Missing in isoform 2.		VSP_044410
Experimental info
	Mutagenesis	894	1	R → P: Abolishes lipid and protein kinase activities. Ref.8
	Mutagenesis	1039	1	S → A: Abolishes autophosphorylation, no effect on lipid kinase activity. Ref.8
	Mutagenesis	1039	1	S → D or E: Abolishes autophosphorylation, reduced lipid kinase activity. Ref.8
	Sequence conflict	253	1	S → N in AAC25677. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p110-delta) [UniParc]. Last modified June 7, 2005. Version 2. Checksum: A38B5D1A1081A3D0	FASTA	1,044	119,479
	10 20 30 40 50 60 MPPGVDCPME FWTKEENQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQLLW HRAQYEPLFH 70 80 90 100 110 120 MLSGPEAYVF TCINQTAEQQ ELEDEQRRLC DVQPFLPVLR LVAREGDRVK KLINSQISLL 130 140 150 160 170 180 IGKGLHEFDS LCDPEVNDFR AKMCQFCEEA AARRQQLGWE AWLQYSFPLQ LEPSAQTWGP 190 200 210 220 230 240 GTLRLPNRAL LVNVKFEGSE ESFTFQVSTK DVPLALMACA LRKKATVFRQ PLVEQPEDYT 250 260 270 280 290 300 LQVNGRHEYL YGSYPLCQFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR 310 320 330 340 350 360 AKPPPIPAKK PSSVSLWSLE QPFRIELIQG SKVNADERMK LVVQAGLFHG NEMLCKTVSS 370 380 390 400 410 420 SEVSVCSEPV WKQRLEFDIN ICDLPRMARL CFALYAVIEK AKKARSTKKK SKKADCPIAW 430 440 450 460 470 480 ANLMLFDYKD QLKTGERCLY MWPSVPDEKG ELLNPTGTVR SNPNTDSAAA LLICLPEVAP 490 500 510 520 530 540 HPVYYPALEK ILELGRHSEC VHVTEEEQLQ LREILERRGS GELYEHEKDL VWKLRHEVQE 550 560 570 580 590 600 HFPEALARLL LVTKWNKHED VAQMLYLLCS WPELPVLSAL ELLDFSFPDC HVGSFAIKSL 610 620 630 640 650 660 RKLTDDELFQ YLLQLVQVLK YESYLDCELT KFLLDRALAN RKIGHFLFWH LRSEMHVPSV 670 680 690 700 710 720 ALRFGLILEA YCRGSTHHMK VLMKQGEALS KLKALNDFVK LSSQKTPKPQ TKELMHLCMR 730 740 750 760 770 780 QEAYLEALSH LQSPLDPSTL LAEVCVEQCT FMDSKMKPLW IMYSNEEAGS GGSVGIIFKN 790 800 810 820 830 840 GDDLRQDMLT LQMIQLMDVL WKQEGLDLRM TPYGCLPTGD RTGLIEVVLR SDTIANIQLN 850 860 870 880 890 900 KSNMAATAAF NKDALLNWLK SKNPGEALDR AIEEFTLSCA GYCVATYVLG IGDRHSDNIM 910 920 930 940 950 960 IRESGQLFHI DFGHFLGNFK TKFGINRERV PFILTYDFVH VIQQGKTNNS EKFERFRGYC 970 980 990 1000 1010 1020 ERAYTILRRH GLLFLHLFAL MRAAGLPELS CSKDIQYLKD SLALGKTEEE ALKHFRVKFN 1030 1040 EALRESWKTK VNWLAHNVSK DNRQ
	Isoform 2 (p37-delta) [UniParc]. Checksum: 18DF7554E3D50988	FASTA	301	33,107
	10 20 30 40 50 60 MPPGVDCPME FWTKEENQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQLLW HRAQYEPLFH 70 80 90 100 110 120 MLSGPEAYVF TCINQTAEQQ ELEDEQRRLC DVQPFLPVLR LVAREGDRVK KLINSQISLL 130 140 150 160 170 180 IGKGLHEFDS LCDPEVNDFR AKMCQFCEEA AARRQQLGWE AWLQYSFPLQ LEPSAQTWGP 190 200 210 220 230 240 GTLRLPNRAL LVNVKFEGSE VSPCVACGIQ AALSMGSTSS VKLLSHPQAP LPQWHQMVFA 250 260 270 280 290 300 RCLCMCGAQL NVPPGELHLP GVHQGRAAGA DGLCPAEEGH SVPAAAGGAA GRLHAAGERQ A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"P110delta, a novel phosphoinositide 3-kinase in leukocytes." Vanhaesebroeck B.A.M., Welham M.J., Kotani K., Stein R., Warne P.H., Zvelebil M.J., Higashi K., Volinia S., Downward J., Waterfield M.D. Proc. Natl. Acad. Sci. U.S.A. 94:4330-4335(1997) [PubMed] [Europe PMC] [Abstract] 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]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-524 AND SER-1039, MASS SPECTROMETRY.
[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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00298410.
RefSeq	NP_005017.3. NM_005026.3.
UniGene	Hs.518451.
3D structure databases
ProteinModelPortal	O00329.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00329. 8 interactions.
STRING	9606.ENSP00000366563.
PTM databases
PhosphoSite	O00329.
Proteomic databases
PaxDb	O00329.
PRIDE	O00329.
Protocols and materials databases
DNASU	5293.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377346; ENSP00000366563; ENSG00000171608.
GeneID	5293.
KEGG	hsa:5293.
UCSC	uc001aqb.4. human.
Organism-specific databases
CTD	5293.
GeneCards	GC01P009711.
HGNC	HGNC:8977. PIK3CD.
HPA	CAB015420.
MIM	602839. gene.
neXtProt	NX_O00329.
PharmGKB	PA33310.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5032.
HOGENOM	HOG000252911.
HOVERGEN	HBG052721.
KO	K00922.
OrthoDB	EOG4XKV67.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000171608-MONOMER.
BRENDA	2.7.1.137. 2681.
Pathway_Interaction_DB	pi3kcipathway. Class I PI3K signaling events. trail_pathway. TRAIL signaling pathway.
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease. REACT_6900. Immune System.
SignaLink	O00329.
UniPathway	UPA00220.
Gene expression databases
ArrayExpress	O00329.
Bgee	O00329.
CleanEx	HS_PIK3CD.
Genevestigator	O00329.
GermOnline	ENSG00000171608. Homo sapiens.
Family and domain databases
Gene3D	1.10.1070.11. 1 hit. 1.25.40.70. 1 hit.
InterPro	IPR016024. ARM-type_fold. IPR008973. C2_Ca/lipid-bd_dom_CaLB. 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. [Graphical view]
PANTHER	PTHR10048. PTHR10048. 1 hit.
Pfam	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]
SMART	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]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF49562. C2_CaLB. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
BindingDB	O00329.
ChEMBL	CHEMBL3130.
ChiTaRS	PIK3CD. human.
GenomeRNAi	5293.
NextBio	20454.
SOURCE	Search...

Entry information

Entry name

PK3CD_HUMAN

Accession

Primary (citable) accession number: O00329
Secondary accession number(s): A6NCG0 , G1FFP1, O15445, Q5SR49

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	June 7, 2005
Last modified:	May 29, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.