dbPAF Protein Information


Tag Content
dbPAF ID dbPAF-0000091
Uniprot Accession O00443; P3C2A_HUMAN; B0LPH2; B4E2G4; Q14CQ9;
Genbank Protein ID NP_002636.2; XP_005253034.1; XP_005253035.1;
Genbank Nucleotide ID NM_002645.2; XM_005252977.1; XM_005252978.3;
Protein Name Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
Protein Synonyms/Alias
Gene Name PIK3C2A
Gene Synonyms/Alias
Organism Homo sapiens(Human)
NCBI Taxa ID 9606
Functional Description
(View all)
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.
Phosphorylation Sites
dbPAF PTMs: 52 (View all)
PositionPeptidesSourceReferences ( PMIDs )
5---MAQISSNSGFKEPhosphoSitePlus22135298
6--MAQISSNSGFKECPhosphoSitePlus22135298
8MAQISSNSGFKECPSPhosphoSitePlus22135298
49LQKDRQVTDNQRGFEPhosphoSitePlus22135298
58NQRGFELSSSTRKKAcurated25627689
59QRGFELSSSTRKKAQcurated25627689
60RGFELSSSTRKKAQVdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PhosphoPep 2.0;PhosphoSitePlus;SysPTM 2.0;UniProt;curated18669648; 16381945; 23193290; 21406692; 18988627; 19060867;
61GFELSSSTRKKAQVYcurated25627689
68TRKKAQVYNKQDYDLPhosphoSitePlus22135298
73QVYNKQDYDLMVFPEdbPTM 3.0;HPRD 9;PhosphoSitePlus;curated20007894; 20068231; 16381945; 23193290; 18988627; 22135298;
108EKLLLDDSFETKKTPdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PHOSIDA;PhosphoPep 2.0;PhosphoSitePlus;SysPTM 2.0;UniProt;curated18669648; 18691976; 19369195; 16381945; 23193290; 20068231;
111LLDDSFETKKTPVLPcurated25627689; 23186163
120KTPVLPVTPILSPSFPhosphoSitePlus22135298
124LPVTPILSPSFSAQLPhosphoSitePlus22135298
126VTPILSPSFSAQLYFPhosphoSitePlus22135298
234FDKIASTSEFLKNGKPhosphoSitePlus22135298
254EITDSKVSNLQVSPKdbPTM 3.0;curated19369195; 16381945; 23193290; 23090842
259KVSNLQVSPKSEDISdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PHOSIDA;PhosphoSitePlus;SysPTM 2.0;UniProt;curated12719431; 18669648; 18691976; 19007248; 19369195; 19690332;
262NLQVSPKSEDISKFDcurated23090842
277WLDLDPLSKPKVDNVcurated26074081
Sequence
(Fasta)
MAQISSNSGF KECPSSHPEP TRAKDVDKEE ALQMEAEALA KLQKDRQVTD NQRGFELSSS 60
TRKKAQVYNK QDYDLMVFPE SDSQKRALDI DVEKLTQAEL EKLLLDDSFE TKKTPVLPVT 120
PILSPSFSAQ LYFRPTIQRG QWPPGLPGPS TYALPSIYPS TYSKQAAFQN GFNPRMPTFP 180
STEPIYLSLP GQSPYFSYPL TPATPFHPQG SLPIYRPVVS TDMAKLFDKI ASTSEFLKNG 240
KARTDLEITD SKVSNLQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA 300
KDPWDAVLLE ERSTANCHLE RKVNGKSLSV ATVTRSQSLN IRTTQLAKAQ GHISQKDPNG 360
TSSLPTGSSL LQEVEVQNEE MAAFCRSITK LKTKFPYTNH RTNPGYLLSP VTAQRNICGE 420
NASVKVSIDI EGFQLPVTFT CDVSSTVEII IMQALCWVHD DLNQVDVGSY VLKVCGQEEV 480
LQNNHCLGSH EHIQNCRKWD TEIRLQLLTF SAMCQNLART AEDDETPVDL NKHLYQIEKP 540
CKEAMTRHPV EELLDSYHNQ VELALQIENQ HRAVDQVIKA VRKICSALDG VETLAITESV 600
KKLKRAVNLP RSKTADVTSL FGGEDTSRSS TRGSLNPENP VQVSINQLTA AIYDLLRLHA 660
NSGRSPTDCA QSSKSVKEAW TTTEQLQFTI FAAHGISSNW VSNYEKYYLI CSLSHNGKDL 720
FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ ISQLPLESVL HLTLFGILNQ SSGSSPDSNK 780
QRKGPEALGK VSLPLFDFKR FLTCGTKLLY LWTSSHTNSV PGTVTKKGYV MERIVLQVDF 840
PSPAFDIIYT TPQVDRSIIQ QHNLETLEND IKGKLLDILH KDSSLGLSKE DKAFLWEKRY 900
YCFKHPNCLP KILASAPNWK WVNLAKTYSL LHQWPALYPL IALELLDSKF ADQEVRSLAV 960
TWIEAISDDE LTDLLPQFVQ ALKYEIYLNS SLVQFLLSRA LGNIQIAHNL YWLLKDALHD 1020
VQFSTRYEHV LGALLSVGGK RLREELLKQT KLVQLLGGVA EKVRQASGSA RQVVLQRSME 1080
RVQSFFQKNK CRLPLKPSLV AKELNIKSCS FFSSNAVPLK VTMVNADPMG EEINVMFKVG 1140
EDLRQDMLAL QMIKIMDKIW LKEGLDLRMV IFKCLSTGRD RGMVELVPAS DTLRKIQVEY 1200
GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD RHNDNIMLRS 1260
TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN GGEKPTIRFQ LFVDLCCQAY 1320
NLIRKQTNLF LNLLSLMIPS GLPELTSIQD LKYVRDALQP QTTDAEATIF FTRLIESSLG 1380
SIATKFNFFI HNLAQLRFSG LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK 1440
HYIYVVRILR EGQIEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA 1500
AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSADAG SFSPTPGQIG 1560
GAVKLSISYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL LPDNHKTSKR KTKISRKTRN 1620
PTFNEMLVYS GYSKETLRQR ELQLSVLSAE SLRENFFLGG VTLPLKDFNL SKETVKWYQL 1680
TAATYL 1687
Keyword

KW-0002--3D-structure
KW-0007--Acetylation
KW-0025--Alternative splicing
KW-0067--ATP-binding
KW-1003--Cell membrane
KW-0181--Complete proteome
KW-0963--Cytoplasm
KW-0968--Cytoplasmic vesicle
KW-0254--Endocytosis
KW-0268--Exocytosis
KW-0333--Golgi apparatus
KW-0418--Kinase
KW-0472--Membrane
KW-0547--Nucleotide-binding
KW-0539--Nucleus
KW-0597--Phosphoprotein
KW-0621--Polymorphism
KW-1185--Reference proteome
KW-0808--Transferase

Interpro

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

PROSITE

PS50004--C2
PS00915--PI3_4_KINASE_1
PS00916--PI3_4_KINASE_2
PS50290--PI3_4_KINASE_3
PS51547--PI3K_C2
PS51546--PI3K_RBD
PS51545--PIK_HELICAL
PS50195--PX

Pfam

PF00168--C2
PF00454--PI3_PI4_kinase
PF00792--PI3K_C2
PF00794--PI3K_rbd
PF00613--PI3Ka
PF00787--PX

Gene Ontology

GO:0030136--C:clathrin-coated vesicle
GO:0005737--C:cytoplasm
GO:0005829--C:cytosol
GO:0070062--C:extracellular exosome
GO:0005794--C:Golgi apparatus
GO:0016020--C:membrane
GO:0005634--C:nucleus
GO:0005942--C:phosphatidylinositol 3-kinase complex
GO:0005886--C:plasma membrane
GO:0031982--C:vesicle
GO:0016303--F:1-phosphatidylinositol-3-kinase activity
GO:0035005--F:1-phosphatidylinositol-4-phosphate 3-kinase activity
GO:0005524--F:ATP binding
GO:0035004--F:phosphatidylinositol 3-kinase activity
GO:0035091--F:phosphatidylinositol binding
GO:0002250--P:adaptive immune response
GO:0060326--P:cell chemotaxis
GO:0048268--P:clathrin coat assembly
GO:0006897--P:endocytosis
GO:0007173--P:epidermal growth factor receptor signaling pathway
GO:0006887--P:exocytosis
GO:0006954--P:inflammatory response
GO:0045087--P:innate immune response
GO:0008286--P:insulin receptor signaling pathway
GO:0071583--P:negative regulation of zinc ion transmembrane transport
GO:0014065--P:phosphatidylinositol 3-kinase signaling
GO:0006661--P:phosphatidylinositol biosynthetic process
GO:0046854--P:phosphatidylinositol phosphorylation
GO:0036092--P:phosphatidylinositol-3-phosphate biosynthetic process
GO:0006644--P:phospholipid metabolic process
GO:0030168--P:platelet activation
GO:0048008--P:platelet-derived growth factor receptor signaling pathway
GO:0006468--P:protein phosphorylation
GO:0044281--P:small molecule metabolic process
GO:0014829--P:vascular smooth muscle contraction