CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038701
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 cGMP-inhibited 3',5'-cyclic phosphodiesterase B 
Protein Synonyms/Alias
  
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]
1063IIEEEEEKCKAEGNKacetylation[2]
1065EEEEEKCKAEGNKLQacetylation[2]
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]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Hydrolase; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1099 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 EEATLGLPIS PFMDRSSPQL 960
AKLQESFITH IVGPLCNSYD AAGLLPGQWI ETEEGDDTES DDDDDDDDGG GEELDSDDEE 1020
TEDNLNPKPQ RRKGRRRIFC QLMHHLTENH KIWKEIIEEE EEKCKAEGNK LQVDNASLPQ 1080
ADEIQVIEEA DEEEEQMFE 1099 
Gene Ontology
 GO:0032045; C:guanyl-nucleotide exchange factor complex; IEA:Compara.
 GO:0016020; C:membrane; IEA:Compara.
 GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006198; P:cAMP catabolic process; IEA:Compara.
 GO:0031018; P:endocrine pancreas development; IDA:MGI.
 GO:0042593; P:glucose homeostasis; IDA:MGI.
 GO:0016525; P:negative regulation of angiogenesis; IEA:Compara.
 GO:0007162; P:negative regulation of cell adhesion; IEA:Compara.
 GO:0050995; P:negative regulation of lipid catabolic process; IEA:Compara.
 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