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Q61194

- P3C2A_MOUSE

UniProt

Q61194 - P3C2A_MOUSE

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Protein

Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha

Gene

Pik3c2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function.3 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate.

Cofactori

Ca2+By similarity, Mg2+By similarityNote: Ca(2+) or Mg(2+). Mn(2+) cannot be used.By similarity

Enzyme regulationi

Activated by clathrin (By similarity). Only slightly inhibited by wortmannin and LY294002. Activated by insulin.By similarity2 Publications

GO - Molecular functioni

  1. 1-phosphatidylinositol-3-kinase activity Source: MGI
  2. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: RefGenome
  3. ATP binding Source: UniProtKB-KW
  4. phosphatidylinositol binding Source: InterPro

GO - Biological processi

  1. endocytosis Source: UniProtKB
  2. exocytosis Source: UniProtKB-KW
  3. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  4. phosphatidylinositol-mediated signaling Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Endocytosis, Exocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.154. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (EC:2.7.1.154)
Short name:
PI3K-C2-alpha
Short name:
PtdIns-3-kinase C2 subunit alpha
Alternative name(s):
Cpk-m
Phosphoinositide 3-kinase-C2-alpha
p170
Gene namesi
Name:Pik3c2a
Synonyms:Cpk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1203729. Pik3c2a.

Subcellular locationi

Cell membrane. Golgi apparatus. Cytoplasmic vesicleclathrin-coated vesicle. Nucleus. Cytoplasm By similarity
Note: Has a preference for membranes containing PtdIns(4,5)P2 or PtdIns(3,4)P2.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. Golgi apparatus Source: UniProtKB-KW
  4. nucleus Source: UniProtKB-KW
  5. phosphatidylinositol 3-kinase complex Source: RefGenome
  6. plasma membrane Source: UniProtKB
  7. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Chronic renal failure and kidney lesions. Affects podocyte morphology and function.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 16861685Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alphaPRO_0000088796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei60 – 601PhosphoserineBy similarity
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei328 – 3281PhosphoserineBy similarity
Modified residuei339 – 3391PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on Ser-261 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation (By similarity). Phosphorylated upon insulin stimulation; which may lead to enzyme activation.By similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61194.
PaxDbiQ61194.
PRIDEiQ61194.

PTM databases

PhosphoSiteiQ61194.

Expressioni

Tissue specificityi

Detected in podocytes.1 Publication

Gene expression databases

GenevestigatoriQ61194.

Interactioni

Subunit structurei

Interacts with ERBB2 and EGFR. Interacts with clathrin trimers (By similarity).By similarity

Protein-protein interaction databases

BioGridi202158. 4 interactions.
IntActiQ61194. 1 interaction.

Structurei

Secondary structure

1
1686
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1562 – 15709Combined sources
Beta strandi1573 – 158210Combined sources
Beta strandi1594 – 16029Combined sources
Beta strandi1604 – 16063Combined sources
Beta strandi1622 – 163110Combined sources
Helixi1634 – 16374Combined sources
Beta strandi1641 – 16488Combined sources
Beta strandi1651 – 16533Combined sources
Beta strandi1656 – 16649Combined sources
Helixi1665 – 16673Combined sources
Beta strandi1674 – 16796Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B3RX-ray2.30A/B1561-1686[»]
ProteinModelPortaliQ61194.
SMRiQ61194. Positions 426-1391, 1421-1532, 1561-1682.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61194.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini422 – 51089PI3K-RBDPROSITE-ProRule annotationAdd
BLAST
Domaini682 – 841160C2 PI3K-typePROSITE-ProRule annotationAdd
BLAST
Domaini861 – 1037177PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini1133 – 1395263PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini1420 – 1536117PXPROSITE-ProRule annotationAdd
BLAST
Domaini1557 – 1660104C2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 142141Interaction with clathrin; sufficient to induce clathrin assembyBy similarityAdd
BLAST
Regioni1488 – 14936Interaction with PtdIns(4,5)P2-containing membranesBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1606 – 161712Nuclear localization signalBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 C2 PI3K-type 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
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5032.
HOGENOMiHOG000006920.
HOVERGENiHBG082099.
InParanoidiQ61194.
KOiK00923.
PhylomeDBiQ61194.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR001683. Phox.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
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.
PfamiPF00168. C2. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
PS50195. PX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q61194-1) [UniParc]FASTAAdd to Basket

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
MAQISNNSEF KQCSSSHPEP IRTKDVNKAE ALQMEAEALA KLQKDRQMTD
60 70 80 90 100
SPRGFELSSS TRQRTQGFNK QDYDLMVFPE LDSQKRAVDI DVEKLTQAEL
110 120 130 140 150
EKILLDDNFE TRKPPALPVT PVLSPSFSTQ LYLRPSGQRG QWPPGLCGPS
160 170 180 190 200
TYTLPSTYPS AYSKQATFQN GFSPRMPTFP STESVYLRLP GQSPYFSYPL
210 220 230 240 250
TPATPFHPQG SLPVYRPLVS PDMAKLFEKI ASTSEFLKNG KARTDLEIAN
260 270 280 290 300
SKASVCNLQI SPKSEDINKF DWLDLDPLSK PKVDYVEVLE HEEEKKDPVL
310 320 330 340 350
LAEDPWDAVL LEERSPSCHL ERKVNGKSLS GATVTRSQSL IIRTAQFTKA
360 370 380 390 400
QGQVSQKDPN GTSSLPTGSS LLQEFEVQND EVAAFCQSIM KLKTKFPYTD
410 420 430 440 450
HCTNPGYLLS PVTVQRNMCG ENASVKVSIE IEGLQLPVTF TCDVSSTVEI
460 470 480 490 500
IIMQALCWVH DDLNQVDVGS YILKVCGQEE VLQNNHCLGS HEHIQNCRKW
510 520 530 540 550
DTEIKLQLLT LSAMCQNLAR TAEDDEAPVD LNKYLYQIEK PYKEVMTRHP
560 570 580 590 600
VEELLDSYHY QVELALQTEN QHRAVDQVIK AVRKICSALD GVETPSVTEA
610 620 630 640 650
VKKLKRAVNL PRNKSADVTS LSGSDTRKNS TKGSLNPENP VQVSMDHLTT
660 670 680 690 700
AIYDLLRLHA NSSRCSTACP RGSRNIKEAW TATEQLQFTV YAAHGISSNW
710 720 730 740 750
VSNYEKYYLI CSLSHNGKDL FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ
760 770 780 790 800
ISQLPLESVL HLTLFGVLNQ SSGSSPDSNK QRKGPEALGK VSLTLFDFKR
810 820 830 840 850
FLTCGTKLLY LWTSSHTNSI PGAIPKKSYV MERIVLQVDF PSPAFDIIYT
860 870 880 890 900
SPQIDRNIIQ QDKLETLESD IKGKLLDIIH RDSSFGLSKE DKVFLWENRY
910 920 930 940 950
YCLKHPNCLP KILASAPNWK WANLAKTYSL LHQWPPLCPL AALELLDAKF
960 970 980 990 1000
ADQEVRSLAV SWMEAISDDE LADLLPQFVQ ALKYEIYLNS SLVRFLLSRA
1010 1020 1030 1040 1050
LGNIQIAHSL YWLLKDALHD THFGSRYEHV LGALLSVGGK GLREELSKQM
1060 1070 1080 1090 1100
KLVQLLGGVA EKVRQASGST RQVVLQKSME RVQSFFLRNK CRLPLKPSLV
1110 1120 1130 1140 1150
AKELNIKSCS FFSSNAMPLK VTMVNADPLG EEINVMFKVG EDLRQDMLAL
1160 1170 1180 1190 1200
QMIKIMDKIW LKEGLDLRMV IFRCLSTGRD RGMVELVPAS DTLRKIQVEY
1210 1220 1230 1240 1250
GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD
1260 1270 1280 1290 1300
RHNDNIMLRS TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN
1310 1320 1330 1340 1350
GGEKPTIRFQ LFVDLCCQAY NLIRKQTNLF LNLLSLMIPS GLPELTSIQD
1360 1370 1380 1390 1400
LKYVRDALQP QTTDAEATIF FTRLIESSLG SIATKFNFFI HNLAQLRFSG
1410 1420 1430 1440 1450
LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK HYIYVVRILR
1460 1470 1480 1490 1500
EGHLEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA
1510 1520 1530 1540 1550
AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSAGAV
1560 1570 1580 1590 1600
PFSPTLGQIG GAVKLSVSYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL
1610 1620 1630 1640 1650
LPDTHKTSKR KTKISRKTRN PTFNEMLVYS GYSKETLRQR ELQLSVLSAE
1660 1670 1680
SLRENFFLGG ITLPLKDFNL SKETVKWYQL TAATYL
Length:1,686
Mass (Da):190,758
Last modified:August 30, 2005 - v2
Checksum:iE390BA7D730F4F87
GO
Isoform 2 (identifier: Q61194-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     276-303: Missing.

Show »
Length:1,658
Mass (Da):187,526
Checksum:i4D18EBC1DDC2A57D
GO

Sequence cautioni

The sequence AAB07682.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401G → V in AK049609. (PubMed:16141072)Curated
Sequence conflicti668 – 6681A → G in AAC52604. (PubMed:8662856)Curated
Sequence conflicti954 – 9541E → G in AAC52604. (PubMed:8662856)Curated
Sequence conflicti1206 – 12083FKD → LR(PubMed:8663140)Curated
Sequence conflicti1211 – 12122LA → TS(PubMed:8663140)Curated
Sequence conflicti1218 – 12181Y → N in AAB07682. (PubMed:8663140)Curated
Sequence conflicti1325 – 13262KQ → T in AAB07682. (PubMed:8663140)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei276 – 30328Missing in isoform 2. 1 PublicationVSP_015254Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52193 mRNA. Translation: AAC52604.1.
AK049609 mRNA. No translation available.
U55772 mRNA. Translation: AAB07682.1. Different initiation.
CCDSiCCDS52371.1. [Q61194-1]
PIRiT42642.
RefSeqiNP_035213.2. NM_011083.2.
UniGeneiMm.3810.

Genome annotation databases

GeneIDi18704.
KEGGimmu:18704.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52193 mRNA. Translation: AAC52604.1 .
AK049609 mRNA. No translation available.
U55772 mRNA. Translation: AAB07682.1 . Different initiation.
CCDSi CCDS52371.1. [Q61194-1 ]
PIRi T42642.
RefSeqi NP_035213.2. NM_011083.2.
UniGenei Mm.3810.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2B3R X-ray 2.30 A/B 1561-1686 [» ]
ProteinModelPortali Q61194.
SMRi Q61194. Positions 426-1391, 1421-1532, 1561-1682.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202158. 4 interactions.
IntActi Q61194. 1 interaction.

PTM databases

PhosphoSitei Q61194.

Proteomic databases

MaxQBi Q61194.
PaxDbi Q61194.
PRIDEi Q61194.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 18704.
KEGGi mmu:18704.

Organism-specific databases

CTDi 5286.
MGIi MGI:1203729. Pik3c2a.

Phylogenomic databases

eggNOGi COG5032.
HOGENOMi HOG000006920.
HOVERGENi HBG082099.
InParanoidi Q61194.
KOi K00923.
PhylomeDBi Q61194.

Enzyme and pathway databases

BRENDAi 2.7.1.154. 3474.

Miscellaneous databases

ChiTaRSi Pik3c2a. mouse.
EvolutionaryTracei Q61194.
NextBioi 294759.
PROi Q61194.
SOURCEi Search...

Gene expression databases

Genevestigatori Q61194.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProi IPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR001683. Phox.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
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 PF00168. C2. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
PF00787. PX. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
SM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00312. PX. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEi PS50004. C2. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
PS50195. PX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cpk is a novel class of Drosophila PtdIns 3-kinase containing a C2 domain."
    Molz L., Chen Y.-W., Hirano M., Williams L.T.
    J. Biol. Chem. 271:13892-13899(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: BALB/c.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-356 (ISOFORM 1).
    Tissue: Embryonic spinal cord.
  3. "Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain."
    Virbasius J.V., Guilherme A., Czech M.P.
    J. Biol. Chem. 271:13304-13307(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-1686 (ISOFORM 1), FUNCTION, ENZYME REGULATION.
    Tissue: Adipocyte.
  4. "Insulin activates the alpha isoform of class II phosphoinositide 3-kinase."
    Brown R.A., Domin J., Arcaro A., Waterfield M.D., Shepherd P.R.
    J. Biol. Chem. 274:14529-14532(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION.
  5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  6. "Insulin-feedback via PI3K-C2alpha activated PKBalpha/Akt1 is required for glucose-stimulated insulin secretion."
    Leibiger B., Moede T., Uhles S., Barker C.J., Creveaux M., Domin J., Berggren P.-O., Leibiger I.B.
    FASEB J. 24:1824-1837(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ISULIN SECRETION.
  7. "Requirement for class II phosphoinositide 3-kinase C2alpha in maintenance of glomerular structure and function."
    Harris D.P., Vogel P., Wims M., Moberg K., Humphries J., Jhaver K.G., DaCosta C.M., Shadoan M.K., Xu N., Hansen G.M., Balakrishnan S., Domin J., Powell D.R., Oravecz T.
    Mol. Cell. Biol. 31:63-80(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN KIDNEY, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  8. "Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2alpha."
    Liu L., Song X., He D., Komma C., Kita A., Virbasius J.V., Huang G., Bellamy H.D., Miki K., Czech M.P., Zhou G.W.
    J. Biol. Chem. 281:4254-4260(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1561-1686, INTERACTION WITH PHOSPHATIDYLINOSITIDE-CONTAINING MEMBRANES.

Entry informationi

Entry nameiP3C2A_MOUSE
AccessioniPrimary (citable) accession number: Q61194
Secondary accession number(s): Q61182
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: November 26, 2014
This is version 129 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3