CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001320
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 cGMP-specific 3',5'-cyclic phosphodiesterase 
Protein Synonyms/Alias
 cGMP-binding cGMP-specific phosphodiesterase; CGB-PDE 
Gene Name
 PDE5A 
Gene Synonyms/Alias
 PDE5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
714EEYKTTLKIIKQAILubiquitination[1]
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] 
Functional Description
 Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'- GMP. 
Sequence Annotation
 DOMAIN 164 314 GAF 1.
 DOMAIN 346 503 GAF 2.
 REGION 588 853 Catalytic (By similarity).
 ACT_SITE 613 613 Proton donor (By similarity).
 METAL 617 617 Divalent metal cation 1.
 METAL 653 653 Divalent metal cation 1.
 METAL 654 654 Divalent metal cation 1.
 METAL 654 654 Divalent metal cation 2.
 METAL 764 764 Divalent metal cation 1.
 BINDING 817 817 cGMP.
 MOD_RES 102 102 Phosphoserine (Potential).  
Keyword
 3D-structure; Allosteric enzyme; Alternative splicing; cGMP; cGMP-binding; Complete proteome; Hydrolase; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 875 AA 
Protein Sequence
MERAGPSFGQ QRQQQQPQQQ KQQQRDQDSV EAWLDDHWDF TFSYFVRKAT REMVNAWFAE 60
RVHTIPVCKE GIRGHTESCS CPLQQSPRAD NSAPGTPTRK ISASEFDRPL RPIVVKDSEG 120
TVSFLSDSEK KEQMPLTPPR FDHDEGDQCS RLLELVKDIS SHLDVTALCH KIFLHIHGLI 180
SADRYSLFLV CEDSSNDKFL ISRLFDVAEG STLEEVSNNC IRLEWNKGIV GHVAALGEPL 240
NIKDAYEDPR FNAEVDQITG YKTQSILCMP IKNHREEVVG VAQAINKKSG NGGTFTEKDE 300
KDFAAYLAFC GIVLHNAQLY ETSLLENKRN QVLLDLASLI FEEQQSLEVI LKKIAATIIS 360
FMQVQKCTIF IVDEDCSDSF SSVFHMECEE LEKSSDTLTR EHDANKINYM YAQYVKNTME 420
PLNIPDVSKD KRFPWTTENT GNVNQQCIRS LLCTPIKNGK KNKVIGVCQL VNKMEENTGK 480
VKPFNRNDEQ FLEAFVIFCG LGIQNTQMYE AVERAMAKQM VTLEVLSYHA SAAEEETREL 540
QSLAAAVVPS AQTLKITDFS FSDFELSDLE TALCTIRMFT DLNLVQNFQM KHEVLCRWIL 600
SVKKNYRKNV AYHNWRHAFN TAQCMFAALK AGKIQNKLTD LEILALLIAA LSHDLDHRGV 660
NNSYIQRSEH PLAQLYCHSI MEHHHFDQCL MILNSPGNQI LSGLSIEEYK TTLKIIKQAI 720
LATDLALYIK RRGEFFELIR KNQFNLEDPH QKELFLAMLM TACDLSAITK PWPIQQRIAE 780
LVATEFFDQG DRERKELNIE PTDLMNREKK NKIPSMQVGF IDAICLQLYE ALTHVSEDCF 840
PLLDGCRKNR QKWQALAEQQ EKMLINGESG QAKRN 875 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:EC.
 GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; NAS:UniProtKB.
 GO:0030553; F:cGMP binding; TAS:UniProtKB.
 GO:0008270; F:zinc ion binding; NAS:UniProtKB.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0046069; P:cGMP catabolic process; IDA:UniProtKB.
 GO:0055118; P:negative regulation of cardiac muscle contraction; IEA:Compara.
 GO:0042130; P:negative regulation of T cell proliferation; IEA:Compara.
 GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IEA:Compara.
 GO:0043406; P:positive regulation of MAP kinase activity; IEA:Compara.
 GO:0060282; P:positive regulation of oocyte development; IEA:Compara.
 GO:0055119; P:relaxation of cardiac muscle; IEA:Compara.
 GO:0007165; P:signal transduction; NAS: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.