O35904 (PK3CD_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1043 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. Ref.2 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
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. Among other effects, IC87114 reduces allergic responses, prevents the recruitment of antigen-specific T cells into target tissue, and affects natural killer cell chemotaxis. Ref.7 Ref.9 Ref.11
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 and HRAS. Ref.6
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Isoform 1 is expressed in spleen and lung (at protein level). Isoform 1 is expressed predominantly in leukocytes. Ref.12
Post-translational modification	Autophosphorylation on Ser-1038 results in the almost complete inactivation of the lipid kinase activity By similarity.
Disruption phenotype	Null mutants are viable and fertile but display defective adaptative and innate immune responses due to signaling defects in multiple cell types including B-, T- and mast and natural killer cells. Ref.2 Ref.5 Ref.7 Ref.9 Ref.10
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell activation Inferred from mutant phenotype Ref.5. Source: MGI B cell homeostasis Inferred from mutant phenotype Ref.5. Source: MGI cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cell surface receptor signaling pathway Inferred from mutant phenotype Ref.5. Source: MGI chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-mediated signaling Inferred from electronic annotation. Source: InterPro
Cellular_component	phosphatidylinositol 3-kinase complex Inferred from Biological aspect of Ancestor. Source: RefGenome plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	1-phosphatidylinositol-3-kinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome 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
Pik3r1	P26450	2	EBI-6470774,EBI-641764

Alternative products

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

Isoform 1 (identifier: O35904-1)

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: O35904-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1043

1043

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

PRO_0000088791

Regions

Domain

16 – 105

90

PI3K-ABD

Domain

187 – 278

92

PI3K-RBD

Domain

319 – 476

158

C2 PI3K-type

Domain

496 – 673

178

PIK helical

Domain

775 – 1028

254

PI3K/PI4K

Amino acid modifications

Modified residue

523

1

Phosphotyrosine By similarity

Modified residue

1038

1

Phosphoserine; by autocatalysis By similarity

Natural variations

Alternative sequence

201 – 212

12

ESFTF…STKDM → VSPSPIPSPSSI in isoform 2.

VSP_044411

Alternative sequence

213 – 1043

831

Missing in isoform 2.

VSP_044412

Experimental info

Mutagenesis

910

1

D → A: Inhibits lipid kinase activity. Mice are viable and fertile but display defective adaptative 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. Ref.2 Ref.7 Ref.9 Ref.10

Sequence conflict

122

1

G → A in AAC25676. Ref.1

Sequence conflict

584

1

F → S in AAC25676. Ref.1

Sequence conflict

651

1

R → H in AAC25676. Ref.1

Secondary structure

1

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1043

Helix Strand Turn

Details...

Helix

110 – 121

12

Helix

126 – 130

5

Helix

134 – 154

21

Helix

159 – 166

8

Beta strand

189 – 198

10

Beta strand

202 – 208

7

Helix

213 – 227

15

Helix

236 – 238

3

Beta strand

239 – 243

5

Beta strand

252 – 254

3

Helix

256 – 258

3

Helix

260 – 268

9

Beta strand

273 – 278

6

Helix

279 – 288

10

Beta strand

321 – 331

11

Beta strand

340 – 349

10

Beta strand

352 – 355

4

Beta strand

363 – 365

3

Beta strand

370 – 380

11

Helix

381 – 383

3

Beta strand

389 – 397

9

Beta strand

416 – 426

11

Beta strand

430 – 432

3

Beta strand

435 – 440

6

Beta strand

455 – 457

3

Turn

465 – 467

3

Beta strand

470 – 475

6

Helix

488 – 493

6

Helix

511 – 514

4

Helix

524 – 532

9

Helix

534 – 540

7

Helix

542 – 544

3

Helix

545 – 549

5

Helix

557 – 568

12

Helix

575 – 581

7

Helix

589 – 599

11

Helix

604 – 617

14

Helix

618 – 620

3

Beta strand

622 – 625

4

Helix

627 – 638

12

Helix

640 – 651

12

Turn

652 – 655

4

Helix

657 – 673

17

Helix

675 – 701

27

Turn

702 – 704

3

Helix

707 – 718

12

Helix

721 – 727

7

Beta strand

728 – 732

5

Beta strand

735 – 740

6

Helix

745 – 747

3

Beta strand

753 – 755

3

Beta strand

758 – 763

6

Turn

765 – 767

3

Helix

768 – 771

4

Beta strand

773 – 781

9

Helix

784 – 802

19

Beta strand

814 – 818

5

Beta strand

821 – 825

5

Beta strand

828 – 832

5

Helix

833 – 837

5

Beta strand

841 – 843

3

Helix

850 – 852

3

Helix

853 – 861

9

Turn

863 – 865

3

Helix

866 – 888

23

Beta strand

897 – 901

5

Beta strand

906 – 908

3

Helix

935 – 941

7

Turn

942 – 944

3

Helix

949 – 968

20

Helix

970 – 980

11

Helix

981 – 983

3

Beta strand

988 – 990

3

Helix

991 – 1001

11

Turn

1002 – 1004

3

Helix

1007 – 1024

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p110-delta) [UniParc]. Last modified July 27, 2011. Version 2. Checksum: AD8DE07D8F847795	FASTA	1,043	119,712
	10 20 30 40 50 60 MPPGVDCPME FWTKEESQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQVLW HRAQYEPLFH 70 80 90 100 110 120 MLSDPEAYVF TCVNQTAEQQ ELEDEQRRLC DIQPFLPVLR LVAREGDRVK KLINSQISLL 130 140 150 160 170 180 IGKGLHEFDS LRDPEVNDFR TKMRQFCEEA AAHRQQLGWV EWLQYSFPLQ LEPSARGWRA 190 200 210 220 230 240 GLLRVSNRAL LVNVKFEGSE ESFTFQVSTK DMPLALMACA LRKKATVFRQ PLVEQPEEYA 250 260 270 280 290 300 LQVNGRHEYL YGNYPLCHFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR 310 320 330 340 350 360 AKPPPIPAKK PSSVSLWSLE QPFSIELIEG RKVNADERMK LVVQAGLFHG NEMLCKTVSS 370 380 390 400 410 420 SEVNVCSEPV WKQRLEFDIS VCDLPRMARL CFALYAVVEK AKKARSTKKK SKKADCPIAW 430 440 450 460 470 480 ANLMLFDYKD QLKTGERCLY MWPSVPDEKG ELLNPAGTVR GNPNTESAAA LVIYLPEVAP 490 500 510 520 530 540 HPVYFPALEK ILELGRHGER GRITEEELQL REILERRGSG ELYEHEKDLV WKMRHEVQEH 550 560 570 580 590 600 FPEALARLLL VTKWNKHEDV AQMLYLLCSW PELPVLSALE LLDFSFPDCY VGSFAIKSLR 610 620 630 640 650 660 KLTDDELFQY LLQLVQVLKY ESYLDCELTK FLLGRALANR KIGHFLFWHL RSEMHVPSVA 670 680 690 700 710 720 LRFGLIMEAY CRGSTHHMKV LMKQGEALSK LKALNDFVKV SSQKTTKPQT KEMMHMCMRQ 730 740 750 760 770 780 ETYMEALSHL QSPLDPSTLL EEVCVEQCTF MDSKMKPLWI MYSSEEAGSA GNVGIIFKNG 790 800 810 820 830 840 DDLRQDMLTL QMIQLMDVLW KQEGLDLRMT PYGCLPTGDR TGLIEVVLHS DTIANIQLNK 850 860 870 880 890 900 SNMAATAAFN KDALLNWLKS KNPGEALDRA IEEFTLSCAG YCVATYVLGI GDRHSDNIMI 910 920 930 940 950 960 RESGQLFHID FGHFLGNFKT KFGINRERVP FILTYDFVHV IQQGKTNNSE KFERFRGYCE 970 980 990 1000 1010 1020 RAYTILRRHG LLFLHLFALM RAAGLPELSC SKDIQYLKDS LALGKTEEEA LKHFRVKFNE 1030 1040 ALRESWKTKV NWLAHNVSKD NRQ
	Isoform 2 [UniParc]. Checksum: F61391FD8427F323	FASTA	212	24,355
	10 20 30 40 50 60 MPPGVDCPME FWTKEESQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQVLW HRAQYEPLFH 70 80 90 100 110 120 MLSDPEAYVF TCVNQTAEQQ ELEDEQRRLC DIQPFLPVLR LVAREGDRVK KLINSQISLL 130 140 150 160 170 180 IGKGLHEFDS LRDPEVNDFR TKMRQFCEEA AAHRQQLGWV EWLQYSFPLQ LEPSARGWRA 190 200 210 GLLRVSNRAL LVNVKFEGSE VSPSPIPSPS SI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]	"Essential role for the p110delta phosphoinositide 3-kinase in the allergic response." Ali K., Bilancio A., Thomas M., Pearce W., Gilfillan A.M., Tkaczyk C., Kuehn N., Gray A., Giddings J., Peskett E., Fox R., Bruce I., Walker C., Sawyer C., Okkenhaug K., Finan P., Vanhaesebroeck B. Nature 431:1007-1011(2004) [PubMed] [Europe PMC] [Abstract] 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]	"The p110 delta structure: mechanisms for selectivity and potency of new PI(3)K inhibitors." Berndt A., Miller S., Williams O., Le D.D., Houseman B.T., Pacold J.I., Gorrec F., Hon W.-C., Liu Y., Rommel C., Gaillard P., Ruckle T., Schwarz M.K., Shokat K.M., Shaw J.P., Williams R.L. Nat. Chem. Biol. 6:117-124(2010) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00649628.

PIR

T43502.

RefSeq

NP_001157524.1. NM_001164052.1.

UniGene

Mm.229108.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O35904.

SMR

O35904. Positions 20-102, 109-1026.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39841N.

IntAct

O35904. 3 interactions.

PTM databases

PhosphoSite

O35904.

Proteomic databases

PaxDb

O35904.

PRIDE

O35904.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000105689; ENSMUSP00000101314; ENSMUSG00000039936.

GeneID

18707.

KEGG

mmu:18707.

Organism-specific databases

CTD

5293.

MGI

MGI:1098211. Pik3cd.

Phylogenomic databases

eggNOG

COG5032.

GeneTree

ENSGT00620000087742.

HOGENOM

HOG000252911.

HOVERGEN

HBG052721.

KO

K00922.

Enzyme and pathway databases

BRENDA

2.7.1.153. 3474.

UniPathway

UPA00220.

Gene expression databases

ArrayExpress

O35904.

Bgee

O35904.

Genevestigator

O35904.

GermOnline

ENSMUSG00000039936. Mus musculus.

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

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Other

ChiTaRS

PIK3CD. mouse.

EvolutionaryTrace

O35904.

NextBio

294773.

SOURCE

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Entry information

Entry name

PK3CD_MOUSE

Accession

Primary (citable) accession number: O35904
Secondary accession number(s): Q8CJ28

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program