CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012076
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 cGMP-inhibited 3',5'-cyclic phosphodiesterase B 
Protein Synonyms/Alias
 CGIPDE1; CGIP1; Cyclic GMP-inhibited phosphodiesterase B; CGI-PDE B 
Gene Name
 PDE3B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33SLRNGYVKSCVSPLRubiquitination[1]
285LSSAAEEKVPVIRPRubiquitination[1]
312ASYYGSCKIFRRPSLubiquitination[1]
339WDLKQWYKPHYQNSGubiquitination[1, 2, 3]
419EIEDPAEKGDRKLNKubiquitination[1, 4]
546DTADFLNKPSVILQRubiquitination[1, 5]
585SCGHQMLKYVSTSESubiquitination[1]
601GTDCCSGKSGEEENIubiquitination[1]
611EEENIFSKESFKLMEubiquitination[1, 5]
627QQEEETEKKDSRKLFubiquitination[1]
628QEEETEKKDSRKLFQubiquitination[1]
943ADINGPAKVRDLHLKubiquitination[1, 5]
Reference
 [1] 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]
 [2] 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]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [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
 Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis. 
Sequence Annotation
 REGION 1 25 Interaction with RAPGEF3.
 REGION 436 460 Interaction with PIK3R6.
 REGION 713 1072 Catalytic (By similarity).
 ACT_SITE 737 737 Proton donor (By similarity).
 METAL 741 741 Divalent metal cation 1.
 METAL 821 821 Divalent metal cation 1.
 METAL 822 822 Divalent metal cation 1.
 METAL 822 822 Divalent metal cation 2.
 METAL 937 937 Divalent metal cation 1.
 MOD_RES 295 295 Phosphoserine; by PKB/AKT1 or PKB/AKT2
 MOD_RES 442 442 Phosphoserine.
 MOD_RES 625 625 Phosphothreonine (By similarity).  
Keyword
 3D-structure; Angiogenesis; cAMP; cGMP; Complete proteome; Hydrolase; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1112 AA 
Protein Sequence
MRRDERDAKA MRSLQPPDGA GSPPESLRNG YVKSCVSPLR QDPPRGFFFH LCRFCNVELR 60
PPPASPQQPR RCSPFCRARL SLGALAAFVL ALLLGAEPES WAAGAAWLRT LLSVCSHSLS 120
PLFSIACAFF FLTCFLTRTK RGPGPGRSCG SWWLLALPAC CYLGDFLVWQ WWSWPWGDGD 180
AGSAAPHTPP EAAAGRLLLV LSCVGLLLTL AHPLRLRHCV LVLLLASFVW WVSFTSLGSL 240
PSALRPLLSG LVGGAGCLLA LGLDHFFQIR EAPLHPRLSS AAEEKVPVIR PRRRSSCVSL 300
GETAASYYGS CKIFRRPSLP CISREQMILW DWDLKQWYKP HYQNSGGGNG VDLSVLNEAR 360
NMVSDLLTDP SLPPQVISSL RSISSLMGAF SGSCRPKINP LTPFPGFYPC SEIEDPAEKG 420
DRKLNKGLNR NSLPTPQLRR SSGTSGLLPV EQSSRWDRNN GKRPHQEFGI SSQGCYLNGP 480
FNSNLLTIPK QRSSSVSLTH HVGLRRAGVL SSLSPVNSSN HGPVSTGSLT NRSPIEFPDT 540
ADFLNKPSVI LQRSLGNAPN TPDFYQQLRN SDSNLCNSCG HQMLKYVSTS ESDGTDCCSG 600
KSGEEENIFS KESFKLMETQ QEEETEKKDS RKLFQEGDKW LTEEAQSEQQ TNIEQEVSLD 660
LILVEEYDSL IEKMSNWNFP IFELVEKMGE KSGRILSQVM YTLFQDTGLL EIFKIPTQQF 720
MNYFRALENG YRDIPYHNRI HATDVLHAVW YLTTRPVPGL QQIHNGCGTG NETDSDGRIN 780
HGRIAYISSK SCSNPDESYG CLSSNIPALE LMALYVAAAM HDYDHPGRTN AFLVATNAPQ 840
AVLYNDRSVL ENHHAASAWN LYLSRPEYNF LLHLDHVEFK RFRFLVIEAI LATDLKKHFD 900
FLAEFNAKAN DVNSNGIEWS NENDRLLVCQ VCIKLADING PAKVRDLHLK WTEGIVNEFY 960
EQGDEEANLG LPISPFMDRS SPQLAKLQES FITHIVGPLC NSYDAAGLLP GQWLEAEEDN 1020
DTESGDDEDG EELDTEDEEM ENNLNPKPPR RKSRRRIFCQ LMHHLTENHK IWKEIVEEEE 1080
KCKADGNKLQ VENSSLPQAD EIQVIEEADE EE 1112 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
 GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
 GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:BHF-UCL.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0016020; C:membrane; IDA:BHF-UCL.
 GO:0004119; F:cGMP-inhibited cyclic-nucleotide phosphodiesterase activity; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0043422; F:protein kinase B binding; ISS:BHF-UCL.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0006198; P:cAMP catabolic process; IEP:BHF-UCL.
 GO:0031018; P:endocrine pancreas development; IEA:Compara.
 GO:0042593; P:glucose homeostasis; IEA:Compara.
 GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
 GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
 GO:0043951; P:negative regulation of cAMP-mediated signaling; IC:BHF-UCL.
 GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IC:BHF-UCL.
 GO:0050995; P:negative regulation of lipid catabolic process; IMP:BHF-UCL.
 GO:0050796; P:regulation of insulin secretion; IEA:Compara. 
Interpro
 IPR003607; HD/PDEase_dom.
 IPR002073; PDEase_catalytic_dom.
 IPR023174; PDEase_CS. 
Pfam
 PF00233; PDEase_I 
SMART
 SM00471; HDc 
PROSITE
 PS00126; PDEASE_I 
PRINTS