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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, Cpk
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

Calcium or magnesium. Manganese cannot be used By similarity.

Enzyme regulationi

Activated by clathrin By similarity. Only slightly inhibited by wortmannin and LY294002. Activated by insulin.2 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. clathrin-coated vesicle Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB
  3. Golgi apparatus Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB-SubCell
  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 – 11Removed By 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-acetylalanine By similarity
Modified residuei60 – 601Phosphoserine By similarity
Modified residuei261 – 2611Phosphoserine By similarity
Modified residuei328 – 3281Phosphoserine By similarity
Modified residuei339 – 3391Phosphoserine By 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.1 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.1 Publication

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 – 15709
Beta strandi1573 – 158210
Beta strandi1594 – 16029
Beta strandi1604 – 16063
Beta strandi1622 – 163110
Helixi1634 – 16374
Beta strandi1641 – 16488
Beta strandi1651 – 16533
Beta strandi1656 – 16649
Helixi1665 – 16673
Beta strandi1674 – 16796

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B3RX-ray2.30A/B1561-1686[»]
ProteinModelPortaliQ61194.
SMRiQ61194. Positions 680-1391, 1421-1532, 1561-1682.

Miscellaneous databases

EvolutionaryTraceiQ61194.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini422 – 51089PI3K-RBDAdd
BLAST
Domaini682 – 841160C2 PI3K-typeAdd
BLAST
Domaini861 – 1037177PIK helicalAdd
BLAST
Domaini1133 – 1395263PI3K/PI4KAdd
BLAST
Domaini1420 – 1536117PXAdd
BLAST
Domaini1557 – 1660104C2Add
BLAST

Region

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

Motif

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

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.
Contains 1 C2 domain.
Contains 1 PI3K-RBD domain.
Contains 1 PI3K/PI4K domain.
Contains 1 PIK helical domain.

Phylogenomic databases

eggNOGiCOG5032.
HOGENOMiHOG000006920.
HOVERGENiHBG082099.
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

MAQISNNSEF KQCSSSHPEP IRTKDVNKAE ALQMEAEALA KLQKDRQMTD     50
SPRGFELSSS TRQRTQGFNK QDYDLMVFPE LDSQKRAVDI DVEKLTQAEL 100
EKILLDDNFE TRKPPALPVT PVLSPSFSTQ LYLRPSGQRG QWPPGLCGPS 150
TYTLPSTYPS AYSKQATFQN GFSPRMPTFP STESVYLRLP GQSPYFSYPL 200
TPATPFHPQG SLPVYRPLVS PDMAKLFEKI ASTSEFLKNG KARTDLEIAN 250
SKASVCNLQI SPKSEDINKF DWLDLDPLSK PKVDYVEVLE HEEEKKDPVL 300
LAEDPWDAVL LEERSPSCHL ERKVNGKSLS GATVTRSQSL IIRTAQFTKA 350
QGQVSQKDPN GTSSLPTGSS LLQEFEVQND EVAAFCQSIM KLKTKFPYTD 400
HCTNPGYLLS PVTVQRNMCG ENASVKVSIE IEGLQLPVTF TCDVSSTVEI 450
IIMQALCWVH DDLNQVDVGS YILKVCGQEE VLQNNHCLGS HEHIQNCRKW 500
DTEIKLQLLT LSAMCQNLAR TAEDDEAPVD LNKYLYQIEK PYKEVMTRHP 550
VEELLDSYHY QVELALQTEN QHRAVDQVIK AVRKICSALD GVETPSVTEA 600
VKKLKRAVNL PRNKSADVTS LSGSDTRKNS TKGSLNPENP VQVSMDHLTT 650
AIYDLLRLHA NSSRCSTACP RGSRNIKEAW TATEQLQFTV YAAHGISSNW 700
VSNYEKYYLI CSLSHNGKDL FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ 750
ISQLPLESVL HLTLFGVLNQ SSGSSPDSNK QRKGPEALGK VSLTLFDFKR 800
FLTCGTKLLY LWTSSHTNSI PGAIPKKSYV MERIVLQVDF PSPAFDIIYT 850
SPQIDRNIIQ QDKLETLESD IKGKLLDIIH RDSSFGLSKE DKVFLWENRY 900
YCLKHPNCLP KILASAPNWK WANLAKTYSL LHQWPPLCPL AALELLDAKF 950
ADQEVRSLAV SWMEAISDDE LADLLPQFVQ ALKYEIYLNS SLVRFLLSRA 1000
LGNIQIAHSL YWLLKDALHD THFGSRYEHV LGALLSVGGK GLREELSKQM 1050
KLVQLLGGVA EKVRQASGST RQVVLQKSME RVQSFFLRNK CRLPLKPSLV 1100
AKELNIKSCS FFSSNAMPLK VTMVNADPLG EEINVMFKVG EDLRQDMLAL 1150
QMIKIMDKIW LKEGLDLRMV IFRCLSTGRD RGMVELVPAS DTLRKIQVEY 1200
GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD 1250
RHNDNIMLRS TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN 1300
GGEKPTIRFQ LFVDLCCQAY NLIRKQTNLF LNLLSLMIPS GLPELTSIQD 1350
LKYVRDALQP QTTDAEATIF FTRLIESSLG SIATKFNFFI HNLAQLRFSG 1400
LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK HYIYVVRILR 1450
EGHLEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA 1500
AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSAGAV 1550
PFSPTLGQIG GAVKLSVSYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL 1600
LPDTHKTSKR KTKISRKTRN PTFNEMLVYS GYSKETLRQR ELQLSVLSAE 1650
SLRENFFLGG ITLPLKDFNL SKETVKWYQL TAATYL 1686
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei276 – 30328Missing in isoform 2. VSP_015254Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401G → V in AK049609. 1 Publication
Sequence conflicti668 – 6681A → G in AAC52604. 1 Publication
Sequence conflicti954 – 9541E → G in AAC52604. 1 Publication
Sequence conflicti1206 – 12083FKD → LR1 Publication
Sequence conflicti1211 – 12122LA → TS1 Publication
Sequence conflicti1218 – 12181Y → N in AAB07682. 1 Publication
Sequence conflicti1325 – 13262KQ → T in AAB07682. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2B3R X-ray 2.30 A/B 1561-1686 [» ]
ProteinModelPortali Q61194.
SMRi Q61194. Positions 680-1391, 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.
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: July 9, 2014
This is version 126 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

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