CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000123
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta 
Protein Synonyms/Alias
 PI3K-C2-beta; PtdIns-3-kinase C2 subunit beta; C2-PI3K; Phosphoinositide 3-kinase-C2-beta 
Gene Name
 PIK3C2B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12QGNGEHWKSLESVGIubiquitination[1, 2]
22ESVGISRKELAMAEAubiquitination[2, 3]
70PGVDFYSKPAGRRTDubiquitination[2, 3, 4]
79AGRRTDLKLLRGLSGubiquitination[2, 5]
201LVEQLPGKLLEHRILubiquitination[1, 2, 3, 4, 5]
241AITRLNLKSTYDAEMubiquitination[2, 3, 4]
267RGPLDFSKDTSGKPVubiquitination[2]
452EYIQYCRKFDIDIRLubiquitination[2]
465RLQLMEQKVVRSDLAubiquitination[2, 3]
496HLQERPVKQTISRQAubiquitination[2]
617TAVPGSRKHDLVQEAubiquitination[2]
752QVLTCGRKLLGLWPAubiquitination[2, 5]
801FTSPPGDKFSPRYEFubiquitination[2, 3]
818LREEDQRKLKDIMQKubiquitination[2]
837WLTDADKKRLWEKRYubiquitination[2]
1027RTGLEEVKQFFALNGubiquitination[2]
1047LSPSLLVKGIVPRDCubiquitination[2, 3, 4, 5]
1065NSNAVPLKLSFQNVDubiquitination[2]
1140PNAETLRKIQVEHGVubiquitination[2]
1152HGVTGSFKDRPLADWubiquitination[1, 2]
1228AQMFGNIKRDRAPFVubiquitination[2]
1383EKIFHPNKGYIYVVKubiquitination[2]
1415EFQELHNKLRLLFPSubiquitination[2]
1482HPLPRDEKAMGTSPAubiquitination[2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
 Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns. Does not phosphorylate PtdIns(4,5)P2. May be involved in EGF and PDGF signaling cascades. 
Sequence Annotation
 DOMAIN 375 463 PI3K-RBD.
 DOMAIN 635 786 C2 PI3K-type.
 DOMAIN 805 981 PIK helical.
 DOMAIN 1079 1343 PI3K/PI4K.
 DOMAIN 1365 1481 PX.
 DOMAIN 1517 1608 C2.
 REGION 2 298 Interaction with GRB2.  
Keyword
 ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Endoplasmic reticulum; Kinase; Membrane; Microsome; Nucleotide-binding; Nucleus; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1634 AA 
Protein Sequence
MSSTQGNGEH WKSLESVGIS RKELAMAEAL QMEYDALSRL RHDKEENRAK QNADPSLISW 60
DEPGVDFYSK PAGRRTDLKL LRGLSGSDPT LNYNSLSPQE GPPNHSTSQG PQPGSDPWPK 120
GSLSGDYLYI FDGSDGGVSS SPGPGDIEGS CKKLSPPPLP PRASIWDTPP LPPRKGSPSS 180
SKISQPSDIN TFSLVEQLPG KLLEHRILEE EEVLGGGGQG RLLGSVDYDG INDAITRLNL 240
KSTYDAEMLR DATRGWKEGR GPLDFSKDTS GKPVARSKTM PPQVPPRTYA SRYGNRKNAT 300
PGKNRRISAA PVGSRPHTVA NGHELFEVSE ERDEEVAAFC HMLDILRSGS DIQDYFLTGY 360
VWSAVTPSPE HLGDEVNLKV TVLCDRLQEA LTFTCNCSST VDLLIYQTLC YTHDDLRNVD 420
VGDFVLKPCG LEEFLQNKHA LGSHEYIQYC RKFDIDIRLQ LMEQKVVRSD LARTVNDDQS 480
PSTLNYLVHL QERPVKQTIS RQALSLLFDT YHNEVDAFLL ADGDFPLKAD RVVQSVKAIC 540
NALAAVETPE ITSALNQLPP CPSRMQPKIQ KDPSVLAVRE NREKVVEALT AAILDLVELY 600
CNTFNADFQT AVPGSRKHDL VQEACHFARS LAFTVYATHR IPIIWATSYE DFYLSCSLSH 660
GGKELCSPLQ TRRAHFSKYL FHLIVWDQQI CFPVQVNRLP RETLLCATLY ALPIPPPGSS 720
SEANKQRRVP EALGWVTTPL FNFRQVLTCG RKLLGLWPAT QENPSARWSA PNFHQPDSVI 780
LQIDFPTSAF DIKFTSPPGD KFSPRYEFGS LREEDQRKLK DIMQKESLYW LTDADKKRLW 840
EKRYYCHSEV SSLPLVLASA PSWEWACLPD IYVLLKQWTH MNHQDALGLL HATFPDQEVR 900
RMAVQWIGSL SDAELLDYLP QLVQALKYEC YLDSPLVRFL LKRAVSDLRV THYFFWLLKD 960
GLKDSQFSIR YQYLLAALLC CCGKGLREEF NRQCWLVNAL AKLAQQVREA APSARQGILR 1020
TGLEEVKQFF ALNGSCRLPL SPSLLVKGIV PRDCSYFNSN AVPLKLSFQN VDPLGENIRV 1080
IFKCGDDLRQ DMLTLQMIRI MSKIWVQEGL DMRMVIFRCF STGRGRGMVE MIPNAETLRK 1140
IQVEHGVTGS FKDRPLADWL QKHNPGEDEY EKAVENFIYS CAGCCVATYV LGICDRHNDN 1200
IMLKTTGHMF HIDFGRFLGH AQMFGNIKRD RAPFVFTSDM AYVINGGDKP SSRFHDFVDL 1260
CCQAYNLIRK HTHLFLNLLG LMLSCGIPEL SDLEDLKYVY DALRPQDTEA NATTYFTRLI 1320
ESSLGSVATK LNFFIHNLAQ MKFTGSDDRL TLSFASRTHT LKSSGRISDV FLCRHEKIFH 1380
PNKGYIYVVK VMRENTHEAT YIQRTFEEFQ ELHNKLRLLF PSSHLPSFPS RFVIGRSRGE 1440
AVAERRREEL NGYIWHLIHA PPEVAECDLV YTFFHPLPRD EKAMGTSPAP KSSDGTWARP 1500
VGKVGGEVKL SISYKNNKLF IMVMHIRGLQ LLQDGNDPDP YVKIYLLPDP QKTTKRKTKV 1560
ARKTCNPTYN EMLVYDGIPK GDLQQRELQL SVLSEQGFWE NVLLGEVNIR LRELDLAQEK 1620
TGWFALGSRS HGTL 1634 
Gene Ontology
 GO:0030139; C:endocytic vesicle; IEA:Compara.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0043231; C:intracellular membrane-bounded organelle; NAS:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:RefGenome.
 GO:0005886; C:plasma membrane; NAS:UniProtKB.
 GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:RefGenome.
 GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; NAS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0001727; F:lipid kinase activity; IEA:Compara.
 GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
 GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
 GO:0043491; P:protein kinase B signaling cascade; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR016024; ARM-type_fold.
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 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. 
Pfam
 PF00168; C2
 PF00454; PI3_PI4_kinase
 PF00792; PI3K_C2
 PF00794; PI3K_rbd
 PF00613; PI3Ka
 PF00787; PX 
SMART
 SM00239; C2
 SM00142; PI3K_C2
 SM00144; PI3K_rbd
 SM00145; PI3Ka
 SM00146; PI3Kc
 SM00312; PX 
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 
PRINTS