CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039567
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta 
Protein Synonyms/Alias
  
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, 4]
70PGVDFYSKPAGRRTDubiquitination[2, 3, 4, 5, 6]
79AGRRTDLKLLRGLSGubiquitination[2, 6, 7]
201LVEQLPGKLLEHRILubiquitination[1, 2, 3, 4, 5, 6, 7]
241AITRLNLKSTYDAEMubiquitination[2, 3, 4, 5, 6]
267RGPLDFSKDTSGKPVubiquitination[2, 4, 6]
452EYIQYCRKFDIDIRLubiquitination[2, 6]
465RLQLMEQKVVRSDLAubiquitination[2, 4, 6]
496HLQERPVKQTISRQAubiquitination[2]
571RMQPKIQKDPSVLAVubiquitination[6]
617TAVPGSRKHDLVQEAubiquitination[2, 6]
752QVLTCGRKLLGLWPAubiquitination[2, 6, 7]
801FTSPPGDKFSPRYEFubiquitination[2, 3, 6]
818LREEDQRKLKDIMQKubiquitination[2]
837WLTDADKKRLWEKRYubiquitination[2]
999RTGLEEVKQFFALNGubiquitination[2, 4]
1019LSPSLLVKGIVPRDCubiquitination[2, 3, 4, 5, 6, 7]
1037NSNAVPLKLSFQNVDubiquitination[2, 4]
1112PNAETLRKIQVEHGVubiquitination[2]
1124HGVTGSFKDRPLADWubiquitination[1, 2, 4]
1200AQMFGNIKRDRAPFVubiquitination[2]
1355EKIFHPNKGYIYVVKubiquitination[2]
1387EFQELHNKLRLLFPSubiquitination[2]
1454HPLPRDEKAMGTSPAubiquitination[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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] 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
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1606 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
EKRYYCHSEW THMNHQDALG LLHATFPDQE VRRMAVQWIG SLSDAELLDY LPQLVQALKY 900
ECYLDSPLVR FLLKRAVSDL RVTHYFFWLL KDGLKDSQFS IRYQYLLAAL LCCCGKGLRE 960
EFNRQCWLVN ALAKLAQQVR EAAPSARQGI LRTGLEEVKQ FFALNGSCRL PLSPSLLVKG 1020
IVPRDCSYFN SNAVPLKLSF QNVDPLGENI RVIFKCGDDL RQDMLTLQMI RIMSKIWVQE 1080
GLDMRMVIFR CFSTGRGRGM VEMIPNAETL RKIQVEHGVT GSFKDRPLAD WLQKHNPGED 1140
EYEKAVENFI YSCAGCCVAT YVLGICDRHN DNIMLKTTGH MFHIDFGRFL GHAQMFGNIK 1200
RDRAPFVFTS DMAYVINGGD KPSSRFHDFV DLCCQAYNLI RKHTHLFLNL LGLMLSCGIP 1260
ELSDLEDLKY VYDALRPQDT EANATTYFTR LIESSLGSVA TKLNFFIHNL AQMKFTGSDD 1320
RLTLSFASRT HTLKSSGRIS DVFLCRHEKI FHPNKGYIYV VKVMRENTHE ATYIQRTFEE 1380
FQELHNKLRL LFPSSHLPSF PSRFVIGRSR GEAVAERRRE ELNGYIWHLI HAPPEVAECD 1440
LVYTFFHPLP RDEKAMGTSP APKSSDGTWA RPVGKVGGEV KLSISYKNNK LFIMVMHIRG 1500
LQLLQDGNDP DPYVKIYLLP DPQKTTKRKT KVARKTCNPT YNEMLVYDGI PKGDLQQREL 1560
QLSVLSEQGF WENVLLGEVN IRLRELDLAQ EKTGWFALGS RSHGTL 1606 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
 GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
 GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
 GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
 GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro. 
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