CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011605
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 cAMP-specific 3',5'-cyclic phosphodiesterase 4D 
Protein Synonyms/Alias
 DPDE3; PDE43 
Gene Name
 PDE4D 
Gene Synonyms/Alias
 DPDE3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
48EKSKTARKSVSPKLSubiquitination[1]
53ARKSVSPKLSPVISPubiquitination[1]
78LLSSNIPKQRRFTVAubiquitination[1]
140SDYDLSPKSMSRNSSubiquitination[1]
323SIPRFGVKTEQEDVLsumoylation[2]
Reference
 [1] 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]
 [2] Selective SUMO modification of cAMP-specific phosphodiesterase-4D5 (PDE4D5) regulates the functional consequences of phosphorylation by PKA and ERK.
 Li X, Vadrevu S, Dunlop A, Day J, Advant N, Troeger J, Klussmann E, Jaffrey E, Hay RT, Adams DR, Houslay MD, Baillie GS.
 Biochem J. 2010 Apr 28;428(1):55-65. [PMID: 20196770] 
Functional Description
 Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. 
Sequence Annotation
 NP_BIND 462 466 cAMP.
 ACT_SITE 462 462 Proton donor (By similarity).
 METAL 466 466 Divalent metal cation 1.
 METAL 502 502 Divalent metal cation 1.
 METAL 503 503 Divalent metal cation 1.
 METAL 503 503 Divalent metal cation 2.
 METAL 620 620 Divalent metal cation 1.
 BINDING 503 503 cAMP.
 BINDING 620 620 cAMP.
 BINDING 671 671 cAMP.
 MOD_RES 190 190 Phosphoserine (By similarity).
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 301 301 Phosphoserine.
 CROSSLNK 387 387 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; cAMP; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Hydrolase; Isopeptide bond; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 809 AA 
Protein Sequence
MAQQTSPDTL TVPEVDNPHC PNPWLNEDLV KSLRENLLQH EKSKTARKSV SPKLSPVISP 60
RNSPRLLRRM LLSSNIPKQR RFTVAHTCFD VDNGTSAGRS PLDPMTSPGS GLILQANFVH 120
SQRRESFLYR SDSDYDLSPK SMSRNSSIAS DIHGDDLIVT PFAQVLASLR TVRNNFAALT 180
NLQDRAPSKR SPMCNQPSIN KATITEEAYQ KLASETLEEL DWCLDQLETL QTRHSVSEMA 240
SNKFKRMLNR ELTHLSEMSR SGNQVSEFIS NTFLDKQHEV EIPSPTQKEK EKKKRPMSQI 300
SGVKKLMHSS SLTNSSIPRF GVKTEQEDVL AKELEDVNKW GLHVFRIAEL SGNRPLTVIM 360
HTIFQERDLL KTFKIPVDTL ITYLMTLEDH YHADVAYHNN IHAADVVQST HVLLSTPALE 420
AVFTDLEILA AIFASAIHDV DHPGVSNQFL INTNSELALM YNDSSVLENH HLAVGFKLLQ 480
EENCDIFQNL TKKQRQSLRK MVIDIVLATD MSKHMNLLAD LKTMVETKKV TSSGVLLLDN 540
YSDRIQVLQN MVHCADLSNP TKPLQLYRQW TDRIMEEFFR QGDRERERGM EISPMCDKHN 600
ASVEKSQVGF IDYIVHPLWE TWADLVHPDA QDILDTLEDN REWYQSTIPQ SPSPAPDDPE 660
EGRQGQTEKF QFELTLEEDG ESDTEKDSGS QVEEDTSCSD SKTLCTQDSE STEIPLDEQV 720
EEEAVGEEEE SQPEACVIDD RSPDT 745 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
 GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:ProtInc.
 GO:0030552; F:cAMP binding; IDA:UniProtKB.
 GO:0008144; F:drug binding; IPI:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007568; P:aging; IEA:Compara.
 GO:0006198; P:cAMP catabolic process; IMP:UniProtKB.
 GO:0071222; P:cellular response to lipopolysaccharide; IEA:Compara.
 GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
 GO:0035264; P:multicellular organism growth; IEA:Compara.
 GO:0030593; P:neutrophil chemotaxis; IEA:Compara.
 GO:0007165; P:signal transduction; IEA:InterPro.
 GO:0006939; P:smooth muscle contraction; IEA:Compara. 
Interpro
 IPR003607; HD/PDEase_dom.
 IPR023088; PDEase.
 IPR002073; PDEase_catalytic_dom.
 IPR023174; PDEase_CS. 
Pfam
 PF00233; PDEase_I 
SMART
 SM00471; HDc 
PROSITE
 PS00126; PDEASE_I 
PRINTS
 PR00387; PDIESTERASE1.