CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012223
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A 
Protein Synonyms/Alias
 HCP1; TM22 
Gene Name
 PDE7A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
145DDYNGQAKCMLEKVGubiquitination[1]
359LVLQMALKCADICNPubiquitination[1]
374CRTWELSKQWSEKVTubiquitination[1, 2]
379LSKQWSEKVTEEFFHubiquitination[1]
393HQGDIEKKYHLGVSPubiquitination[1]
448LGHVGLNKASWKGLQubiquitination[1]
452GLNKASWKGLQREQSubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May have a role in muscle signal transduction. 
Sequence Annotation
 REGION 187 451 Catalytic (By similarity).
 ACT_SITE 212 212 Proton donor (By similarity).
 METAL 216 216 Divalent metal cation 1.
 METAL 252 252 Divalent metal cation 1.
 METAL 253 253 Divalent metal cation 1.
 METAL 253 253 Divalent metal cation 2.
 METAL 362 362 Divalent metal cation 1.
 MOD_RES 84 84 Phosphoserine (Potential).  
Keyword
 3D-structure; Alternative splicing; cAMP; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 482 AA 
Protein Sequence
MEVCYQLPVL PLDRPVPQHV LSRRGAISFS SSSALFGCPN PRQLSQRRGA ISYDSSDQTA 60
LYIRMLGDVR VRSRAGFESE RRGSHPYIDF RIFHSQSEIE VSVSARNIRR LLSFQRYLRS 120
SRFFRGTAVS NSLNILDDDY NGQAKCMLEK VGNWNFDIFL FDRLTNGNSL VSLTFHLFSL 180
HGLIEYFHLD MMKLRRFLVM IQEDYHSQNP YHNAVHAADV TQAMHCYLKE PKLANSVTPW 240
DILLSLIAAA THDLDHPGVN QPFLIKTNHY LATLYKNTSV LENHHWRSAV GLLRESGLFS 300
HLPLESRQQM ETQIGALILA TDISRQNEYL SLFRSHLDRG DLCLEDTRHR HLVLQMALKC 360
ADICNPCRTW ELSKQWSEKV TEEFFHQGDI EKKYHLGVSP LCDRHTESIA NIQIGFMTYL 420
VEPLFTEWAR FSNTRLSQTM LGHVGLNKAS WKGLQREQSS SEDTDAAFEL NSQLLPQENR 480
LS 482 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
 GO:0007165; P:signal transduction; NAS:UniProtKB. 
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.