CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014332
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 cGMP-inhibited 3',5'-cyclic phosphodiesterase B 
Protein Synonyms/Alias
 CGIPDE1; Cyclic GMP-inhibited phosphodiesterase B; CGI-PDE B 
Gene Name
 Pde3b 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
525DTTDFLTKPNIILHRubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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 (By similarity). 
Sequence Annotation
 REGION 1 28 Interaction with RAPGEF3 (By similarity).
 REGION 415 439 Interaction with PIK3R6 (By similarity).
 REGION 689 1054 Catalytic (By similarity).
 ACT_SITE 713 713 Proton donor (By similarity).
 METAL 717 717 Divalent metal cation 1 (By similarity).
 METAL 797 797 Divalent metal cation 1 (By similarity).
 METAL 798 798 Divalent metal cation 1 (By similarity).
 METAL 798 798 Divalent metal cation 2 (By similarity).
 METAL 913 913 Divalent metal cation 1 (By similarity).
 MOD_RES 273 273 Phosphoserine; by PKB/AKT1 or PKB/AKT2.
 MOD_RES 421 421 Phosphoserine (By similarity).
 MOD_RES 604 604 Phosphothreonine.  
Keyword
 Angiogenesis; cAMP; cGMP; Coiled coil; Complete proteome; Hydrolase; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1100 AA 
Protein Sequence
MRKDERERDA PAMRSPPPPP ASAASPPESL RNGYVKSCVS PLRQDPPRSF FFHLCRFCNV 60
EPPAASLRAG ARLSLGVLAA FVLAALLGAR PERWAAAAAG LRTLLSACSL SLSPLFSIAC 120
AFFFLTCFLT RAQRGPGRGA GSWWLLALPA CCYLGDFAAW QWWSWLRGEP AAAGRLCLVL 180
SCVGLLTLAP RVRLRHGVLV LLFAGLVWWV SFSGLGALPP ALRPLLSCLV GGAGCLLALG 240
LDHFFHVRGA SPPPRSASTA EEKVPVIRPR RRSSCVSLGE SAAGYYGSGK MFRRPSLPCI 300
SREQMILWDW DLKQWCKPHY QNSGGGNGVD LSVLNEARNM VSDLLIDPSL PPQVISSLRS 360
ISSLMGAFSG SCRPKINSFT PFPGFYPCSE VEDPVEKGDR KLHKGLSGRT SFPTPQLRRS 420
SGASSLLTNE HCSRWDRSSG KRSYQELSVS SHGCHLNGPF SSNLFTIPKQ RSSSVSLTHH 480
AGLRRAGALP SHSLLNSSSH VPVSAGSLTN RSPIGFPDTT DFLTKPNIIL HRSLGSVSSA 540
ADFHQYLRNS DSNLCSSCGH QILKYVSTCE PDGTDHPSEK SGEEDSSVFS KEPLNIVETQ 600
EEETMKKACR ELFLEGDSHL MEEAQQPNID QEVSLDPMLV EDYDSLIEKM NNWNFQIFEL 660
VEKMGEKSGR ILSQVMYTLF QDTGLLETFK IPTQEFMNYF RALENGYRDI PYHNRVHATD 720
VLHAVWYLTT RPIPGLPQIH NNHETETKAD SDGRLGSGQI AYISSKSCCI PDMSYGCLSS 780
NIPALELMAL YVAAAMHDYD HPGRTNAFLV ATNAPQAVLY NDRSVLENHH AASAWNLYLS 840
RPEYNFLLNL DHMEFKRFRF LVIEAILATD LKKHFDFLAE FNAKANDVNS NGIEWSSEND 900
RLLVCQVCIK LADINGPAKD RDLHLRWTEG IVNEFYEQGD EEAALGLPIS PFMDRSSPQL 960
AKLQESFITH IVGPLCNSYD AAGLLPGQWI ETEEGDDTES DDDDDDDDGD GGEELDSDDE 1020
ETEDNLNPKP QRRKGRRRIF CQLMHHLTEN HKIWKEIIEE EEEKCKAEGN KLQVDNASLP 1080
QADEIQVIEE ADEEEEQMFE 1100 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
 GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0016020; C:membrane; IDA:BHF-UCL.
 GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0032869; P:cellular response to insulin stimulus; IEP:BHF-UCL.
 GO:0031018; P:endocrine pancreas development; IDA:MGI.
 GO:0042593; P:glucose homeostasis; IDA:MGI.
 GO:0008152; P:metabolic process; IEA:GOC.
 GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
 GO:0050796; P:regulation of insulin secretion; IDA:MGI.
 GO:0007165; P:signal transduction; IEA:InterPro. 
Interpro
 IPR003607; HD/PDEase_dom.
 IPR002073; PDEase_catalytic_dom.
 IPR023174; PDEase_CS. 
Pfam
 PF00233; PDEase_I 
SMART
 SM00471; HDc 
PROSITE
 PS00126; PDEASE_I 
PRINTS