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O00329 (PK3CD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1044 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processAdaptive immunity
Chemotaxis
Differentiation
Immunity
Inflammatory response
Innate immunity
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB 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: Ensembl

B cell receptor signaling pathway

Traceable author statement Ref.12. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

T cell activation

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 activation

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 signaling

Traceable author statement Ref.11. Source: UniProtKB

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol-3-phosphate biosynthetic process

Non-traceable author statement Ref.3. Source: GOC

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

protein phosphorylation

Non-traceable author statement Ref.1. Source: UniProtKB

respiratory burst involved in defense response

Traceable author statement Ref.12. Source: UniProtKB

signal transduction

Non-traceable author statement Ref.1. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mast cell granule

Traceable author statement Ref.12. Source: GOC

phosphatidylinositol 3-kinase complex

Non-traceable author statement Ref.1Ref.3. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_function1-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 3-kinase activity

Traceable author statement Ref.11. Source: UniProtKB

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

HRASP011122EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10441044Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
PRO_0000088790

Regions

Domain16 – 10590PI3K-ABD
Domain187 – 27892PI3K-RBD
Domain319 – 476158C2 PI3K-type
Domain497 – 674178PIK helical
Domain774 – 1041268PI3K/PI4K

Amino acid modifications

Modified residue5241Phosphotyrosine Ref.9
Modified residue10391Phosphoserine; by autocatalysis Ref.8 Ref.9

Natural variations

Alternative sequence201 – 300100ESFTF…VQKPR → VSPCVACGIQAALSMGSTSS VKLLSHPQAPLPQWHQMVFA RCLCMCGAQLNVPPGELHLP GVHQGRAAGADGLCPAEEGH SVPAAAGGAAGRLHAAGERQ in isoform 2.
VSP_044409
Alternative sequence302 – 1044743Missing in isoform 2.
VSP_044410

Experimental info

Mutagenesis8941R → P: Abolishes lipid and protein kinase activities. Ref.8
Mutagenesis10391S → A: Abolishes autophosphorylation, no effect on lipid kinase activity. Ref.8
Mutagenesis10391S → D or E: Abolishes autophosphorylation, reduced lipid kinase activity. Ref.8
Sequence conflict2531S → N in AAC25677. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p110-delta) [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: A38B5D1A1081A3D0

FASTA1,044119,479
        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 

« Hide

Isoform 2 (p37-delta) [UniParc].

Checksum: 18DF7554E3D50988
Show »

FASTA30133,107

References

« Hide '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. expand/collapse author list , 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, 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.
+Additional computationally mapped references.

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.
RefSeqNP_005017.3. NM_005026.3.
UniGeneHs.518451.

3D structure databases

ProteinModelPortalO00329.
SMRO00329. Positions 20-102, 109-1027.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111311. 8 interactions.
IntActO00329. 8 interactions.
STRING9606.ENSP00000366563.

Chemistry

BindingDBO00329.
ChEMBLCHEMBL2111432.
GuidetoPHARMACOLOGY2155.

PTM databases

PhosphoSiteO00329.

Proteomic databases

PaxDbO00329.
PRIDEO00329.

Protocols and materials databases

DNASU5293.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377346; ENSP00000366563; ENSG00000171608. [O00329-1]
GeneID5293.
KEGGhsa:5293.
UCSCuc001aqb.4. human. [O00329-1]

Organism-specific databases

CTD5293.
GeneCardsGC01P009711.
HGNCHGNC:8977. PIK3CD.
HPACAB015420.
MIM602839. gene.
neXtProtNX_O00329.
PharmGKBPA33310.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5032.
HOGENOMHOG000252911.
HOVERGENHBG052721.
KOK00922.
OrthoDBEOG70CR65.
PhylomeDBO00329.
TreeFamTF102031.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000171608-MONOMER.
BRENDA2.7.1.137. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkO00329.
UniPathwayUPA00220.

Gene expression databases

ArrayExpressO00329.
BgeeO00329.
CleanExHS_PIK3CD.
GenevestigatorO00329.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProIPR016024. 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.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00454. 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]
SMARTSM00142. PI3K_C2. 1 hit.
SM00143. PI3K_p85B. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00915. 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]
ProtoNetSearch...

Other

ChiTaRSPIK3CD. human.
GeneWikiP110%CE%B4.
GenomeRNAi5293.
NextBio20454.
PROO00329.
SOURCESearch...

Entry information

Entry namePK3CD_HUMAN
AccessionPrimary (citable) accession number: O00329
Secondary accession number(s): A6NCG0 expand/collapse secondary AC list , G1FFP1, O15445, Q5SR49
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM