| Tag | Content |
|---|
| CPLM ID | CPLM-000971 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A |
Protein Synonyms/Alias | |
Gene Name | PDE8A |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 268 | GEVPINEKKADLLDT | ubiquitination | [1] |
|
Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development. |
Sequence Annotation | DOMAIN 213 283 PAS.
DOMAIN 287 329 PAC.
REGION 531 813 Catalytic (By similarity).
ACT_SITE 556 556 Proton donor (By similarity).
METAL 560 560 Divalent metal cation 1.
METAL 596 596 Divalent metal cation 1.
METAL 597 597 Divalent metal cation 1.
METAL 597 597 Divalent metal cation 2.
METAL 726 726 Divalent metal cation 1.
MOD_RES 20 20 Phosphoserine.
MOD_RES 359 359 Phosphoserine; by PKA.
MOD_RES 457 457 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; cAMP; Complete proteome; Hydrolase; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 829 AA |
Protein Sequence | MGCAPSIHIS ERLVAEDAPS PAAPPLSSGG PRLPQGQKTA ALPRTRGAGL LESELRDGSG 60
KKVAVADVQF GPMRFHQDQL QVLLVFTKED NQCNGFCRAC EKAGFKCTVT KEAQAVLACF 120
LDKHHDIIII DHRNPRQLDA EALCRSIRSS KLSENTVIVG VVRRVDREEL SVMPFISAGF 180
TRRYVENPNI MACYNELLQL EFGEVRSQLK LRACNSVFTA LENSEDAIEI TSEDRFIQYA 240
NPAFETTMGY QSGELIGKEL GEVPINEKKA DLLDTINSCI RIGKEWQGIY YAKKKNGDNI 300
QQNVKIIPVI GQGGKIRHYV SIIRVCNGNN KAEKISECVQ SDTHTDNQTG KHKDRRKGSL 360
DVKAVASRAT EVSSQRRHSS MARIHSMTIE APITKVINII NAAQESSPMP VTEALDRVLE 420
ILRTTELYSP QFGAKDDDPH ANDLVGGLMS DGLRRLSGNE YVLSTKNTQM VSSNIITPIS 480
LDDVPPRIAR AMENEEYWDF DIFELEAATH NRPLIYLGLK MFARFGICEF LHCSESTLRS 540
WLQIIEANYH SSNPYHNSTH SADVLHATAY FLSKERIKET LDPIDEVAAL IAATIHDVDH 600
PGRTNSFLCN AGSELAILYN DTAVLESHHA ALAFQLTTGD DKCNIFKNME RNDYRTLRQG 660
IIDMVLATEM TKHFEHVNKF VNSINKPLAT LEENGETDKN QEVINTMLRT PENRTLIKRM 720
LIKCADVSNP CRPLQYCIEW AARISEEYFS QTDEEKQQGL PVVMPVFDRN TCSIPKSQIS 780
FIDYFITDMF DAWDAFVDLP DLMQHLDNNF KYWKGLDEMK LRNLRPPPE 829 |
Gene Ontology | GO:0005829; C:cytosol; TAS:Reactome. GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:Compara. GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; NAS:UniProtKB. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro. GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway. GO:0009187; P:cyclic nucleotide metabolic process; NAS:UniProtKB. GO:0035556; P:intracellular signal transduction; IEA:GOC. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |