CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000064
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 cGMP-dependent 3',5'-cyclic phosphodiesterase 
Protein Synonyms/Alias
 Cyclic GMP-stimulated phosphodiesterase; CGS-PDE; cGSPDE 
Gene Name
 PDE2A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
508NILCFPIKNENQEVIubiquitination[1]
880LLQDLFPKAAELYERubiquitination[1]
901HWTKVSHKFTIRGLPubiquitination[1]
Reference
 [1] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
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. 
Sequence Annotation
 DOMAIN 241 377 GAF 1.
 DOMAIN 409 548 GAF 2.
 REGION 633 891 Catalytic (By similarity).
 REGION 656 660 Substrate binding.
 ACT_SITE 656 656 Proton donor (By similarity).
 METAL 660 660 Divalent metal cation 1.
 METAL 696 696 Divalent metal cation 1.
 METAL 697 697 Divalent metal cation 1.
 METAL 697 697 Divalent metal cation 2.
 METAL 808 808 Divalent metal cation 1.
 BINDING 431 431 cGMP (By similarity).
 BINDING 446 446 cGMP (By similarity).
 BINDING 499 499 cGMP (By similarity).
 BINDING 697 697 Substrate.
 BINDING 808 808 Substrate.
 LIPID 2 2 N-myristoyl glycine.
 LIPID 5 5 S-palmitoyl cysteine; in isoform PDE2A3
 LIPID 11 11 S-palmitoyl cysteine; in isoform PDE2A3  
Keyword
 3D-structure; Alternative splicing; cAMP; Cell membrane; cGMP; cGMP-binding; Complete proteome; Hydrolase; Lipoprotein; Membrane; Metal-binding; Myristate; Nucleotide-binding; Palmitate; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 941 AA 
Protein Sequence
MGQACGHSIL CRSQQYPAAR PAEPRGQQVF LKPDEPPPPP QPCADSLQDA LLSLGSVIDI 60
SGLQRAVKEA LSAVLPRVET VYTYLLDGES QLVCEDPPHE LPQEGKVREA IISQKRLGCN 120
GLGFSDLPGK PLARLVAPLA PDTQVLVMPL ADKEAGAVAA VILVHCGQLS DNEEWSLQAV 180
EKHTLVALRR VQVLQQRGPR EAPRAVQNPP EGTAEDQKGG AAYTDRDRKI LQLCGELYDL 240
DASSLQLKVL QYLQQETRAS RCCLLLVSED NLQLSCKVIG DKVLGEEVSF PLTGCLGQVV 300
EDKKSIQLKD LTSEDVQQLQ SMLGCELQAM LCVPVISRAT DQVVALACAF NKLEGDLFTD 360
EDEHVIQHCF HYTSTVLTST LAFQKEQKLK CECQALLQVA KNLFTHLDDV SVLLQEIITE 420
ARNLSNAEIC SVFLLDQNEL VAKVFDGGVV DDESYEIRIP ADQGIAGHVA TTGQILNIPD 480
AYAHPLFYRG VDDSTGFRTR NILCFPIKNE NQEVIGVAEL VNKINGPWFS KFDEDLATAF 540
SIYCGISIAH SLLYKKVNEA QYRSHLANEM MMYHMKVSDD EYTKLLHDGI QPVAAIDSNF 600
ASFTYTPRSL PEDDTSMAIL SMLQDMNFIN NYKIDCPTLA RFCLMVKKGY RDPPYHNWMH 660
AFSVSHFCYL LYKNLELTNY LEDIEIFALF ISCMCHDLDH RGTNNSFQVA SKSVLAALYS 720
SEGSVMERHH FAQAIAILNT HGCNIFDHFS RKDYQRMLDL MRDIILATDL AHHLRIFKDL 780
QKMAEVGYDR NNKQHHRLLL CLLMTSCDLS DQTKGWKTTR KIAELIYKEF FSQGDLEKAM 840
GNRPMEMMDR EKAYIPELQI SFMEHIAMPI YKLLQDLFPK AAELYERVAS NREHWTKVSH 900
KFTIRGLPSN NSLDFLDEEY EVPDLDGTRA PINGCCSLDA E 941 
Gene Ontology
 GO:0030424; C:axon; IEA:Compara.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
 GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
 GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
 GO:0005262; F:calcium channel activity; TAS:UniProtKB.
 GO:0030552; F:cAMP binding; IMP:UniProtKB.
 GO:0030553; F:cGMP binding; IDA:UniProtKB.
 GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB.
 GO:0008144; F:drug binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0006198; P:cAMP catabolic process; IDA:UniProtKB.
 GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
 GO:0071321; P:cellular response to cGMP; IDA:UniProtKB.
 GO:0035690; P:cellular response to drug; IEP:UniProtKB.
 GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
 GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
 GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
 GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
 GO:0046069; P:cGMP catabolic process; IDA:UniProtKB.
 GO:0019934; P:cGMP-mediated signaling; IMP:UniProtKB.
 GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
 GO:0030224; P:monocyte differentiation; IEP:UniProtKB.
 GO:0030818; P:negative regulation of cAMP biosynthetic process; ISS:UniProtKB.
 GO:0033159; P:negative regulation of protein import into nucleus, translocation; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0043116; P:negative regulation of vascular permeability; IMP:UniProtKB.
 GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
 GO:0043117; P:positive regulation of vascular permeability; IMP:UniProtKB.
 GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB. 
Interpro
 IPR003018; GAF.
 IPR003607; HD/PDEase_dom.
 IPR023088; PDEase.
 IPR002073; PDEase_catalytic_dom.
 IPR023174; PDEase_CS. 
Pfam
 PF01590; GAF
 PF00233; PDEase_I 
SMART
 SM00065; GAF
 SM00471; HDc 
PROSITE
 PS00126; PDEASE_I 
PRINTS
 PR00387; PDIESTERASE1.