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cAMP-specific 3',5'-cyclic phosphodiesterase 4B (EC 3.1.4.53) (DPDE4) (PDE32)

 PDE4B_HUMAN             Reviewed;         736 AA.
Q07343; A5YW33; O15443; Q13945; Q5TEK4; Q5TEK5; Q5TEK6;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
27-SEP-2017, entry version 173.
RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4B;
EC=3.1.4.53;
AltName: Full=DPDE4;
AltName: Full=PDE32;
Name=PDE4B; Synonyms=DPDE4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4B2).
PubMed=8392015; DOI=10.1016/0378-1119(93)90274-7;
Obernolte R., Bhakta S., Alvarez R., Bach C., Mulkins M., Jarnagin K.,
Shelton E.R.;
"The cDNA of a human lymphocyte cyclic-AMP phosphodiesterase (PDE IV)
reveals a multigene family.";
Gene 129:239-247(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE4B1 AND PDE4B2).
TISSUE=Brain;
PubMed=8413254; DOI=10.1128/MCB.13.10.6558;
Bolger G., Michaeli T., Martins T., St John T., Steiner B.,
Rodgers L., Riggs M., Wigler M., Ferguson K.;
"A family of human phosphodiesterases homologous to the dunce learning
and memory gene product of Drosophila melanogaster are potential
targets for antidepressant drugs.";
Mol. Cell. Biol. 13:6558-6571(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4B3).
PubMed=9371714; DOI=10.1042/bj3280549;
Huston E., Lumb S., Russell A., Catterall C., Ross A.H., Steele M.R.,
Bolger G.B., Perry M.J., Owens R.J., Houslay M.D.;
"Molecular cloning and transient expression in COS7 cells of a novel
human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3.";
Biochem. J. 328:549-558(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4B2).
TISSUE=Brain;
PubMed=8384210;
McLaughlin M.M., Cieslinski L.B., Burman M., Torphy T.J., Livi G.P.;
"A low-Km, rolipram-sensitive, cAMP-specific phosphodiesterase from
human brain. Cloning and expression of cDNA, biochemical
characterization of recombinant protein, and tissue distribution of
mRNA.";
J. Biol. Chem. 268:6470-6476(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4B5).
PubMed=17519386; DOI=10.1124/jpet.107.122218;
Cheung Y.F., Kan Z., Garrett-Engele P., Gall I., Murdoch H.,
Baillie G.S., Camargo L.M., Johnson J.M., Houslay M.D., Castle J.C.;
"PDE4B5, a novel, super-short, brain-specific cAMP phosphodiesterase-4
variant whose isoform-specifying N-terminal region is identical to
that of cAMP phosphodiesterase-4D6 (PDE4D6).";
J. Pharmacol. Exp. Ther. 322:600-609(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PDE4B1; PDE4B3 AND
PDE4B5).
TISSUE=Hippocampus, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE4B1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 324-700 IN COMPLEX WITH
METAL IONS, FUNCTION, AND COFACTOR.
PubMed=10846163; DOI=10.1126/science.288.5472.1822;
Xu R.X., Hassell A.M., Vanderwall D., Lambert M.H., Holmes W.D.,
Luther M.A., Rocque W.J., Milburn M.V., Zhao Y., Ke H., Nolte R.T.;
"Atomic structure of PDE4: insights into phosphodiesterase mechanism
and specificity.";
Science 288:1822-1825(2000).
[11]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 324-700 IN COMPLEX WITH AMP;
METAL IONS AND THE INHIBITOR ROLIPRAM, FUNCTION, AND COFACTOR.
PubMed=15003452; DOI=10.1016/j.jmb.2004.01.040;
Xu R.X., Rocque W.J., Lambert M.H., Vanderwall D.E., Luther M.A.,
Nolte R.T.;
"Crystal structures of the catalytic domain of phosphodiesterase 4B
complexed with AMP, 8-Br-AMP, and rolipram.";
J. Mol. Biol. 337:355-365(2004).
[12]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 324-700 IN COMPLEX WITH AMP
AND METAL IONS.
PubMed=15260978; DOI=10.1016/j.molcel.2004.07.005;
Zhang K.Y.J., Card G.L., Suzuki Y., Artis D.R., Fong D., Gillette S.,
Hsieh D., Neiman J., West B.L., Zhang C., Milburn M.V., Kim S.-H.,
Schlessinger J., Bollag G.;
"A glutamine switch mechanism for nucleotide selectivity by
phosphodiesterases.";
Mol. Cell 15:279-286(2004).
[13]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 324-700 IN COMPLEX WITH
METAL IONS AND INHIBITORS.
PubMed=15576036; DOI=10.1016/j.str.2004.10.004;
Card G.L., England B.P., Suzuki Y., Fong D., Powell B., Lee B.,
Luu C., Tabrizizad M., Gillette S., Ibrahim P.N., Artis D.R.,
Bollag G., Milburn M.V., Kim S.-H., Schlessinger J., Zhang K.Y.J.;
"Structural basis for the activity of drugs that inhibit
phosphodiesterases.";
Structure 12:2233-2247(2004).
[14]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 324-700 IN COMPLEX WITH
METAL IONS AND INHIBITORS.
PubMed=15685167; DOI=10.1038/nbt1059;
Card G.L., Blasdel L., England B.P., Zhang C., Suzuki Y., Gillette S.,
Fong D., Ibrahim P.N., Artis D.R., Bollag G., Milburn M.V., Kim S.-H.,
Schlessinger J., Zhang K.Y.J.;
"A family of phosphodiesterase inhibitors discovered by
cocrystallography and scaffold-based drug design.";
Nat. Biotechnol. 23:201-207(2005).
[15]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 324-659 IN COMPLEX WITH
METAL IONS AND THE INHIBITOR NVP.
PubMed=17727341; DOI=10.1042/BJ20070970;
Wang H., Peng M.-S., Chen Y., Geng J., Robinson H., Houslay M.D.,
Cai J., Ke H.;
"Structures of the four subfamilies of phosphodiesterase-4 provide
insight into the selectivity of their inhibitors.";
Biochem. J. 408:193-201(2007).
[16]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 324-675 IN COMPLEX WITH
METAL IONS AND INHIBITOR.
PubMed=18539455; DOI=10.1016/j.bmcl.2008.05.052;
Hamblin J.N., Angell T.D.R., Ballantine S.P., Cook C.M.,
Cooper A.W.J., Dawson J., Delves C.J., Jones P.S., Lindvall M.,
Lucas F.S., Mitchell C.J., Neu M.Y., Ranshaw L.E., Solanke Y.E.,
Somers D.O., Wiseman J.O.;
"Pyrazolopyridines as a novel structural class of potent and selective
PDE4 inhibitors.";
Bioorg. Med. Chem. Lett. 18:4237-4241(2008).
-!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
regulator of many important physiological processes. May be
involved in mediating central nervous system effects of
therapeutic agents ranging from antidepressants to antiasthmatic
and anti-inflammatory agents. {ECO:0000269|PubMed:10846163,
ECO:0000269|PubMed:15003452}.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
adenosine 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000269|PubMed:10846163,
ECO:0000269|PubMed:15003452};
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions. {ECO:0000269|PubMed:10846163,
ECO:0000269|PubMed:15003452};
-!- ENZYME REGULATION: Inhibited by rolipram.
-!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
3',5'-cyclic AMP: step 1/1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=PDE4B1;
IsoId=Q07343-1; Sequence=Displayed;
Name=PDE4B2;
IsoId=Q07343-2; Sequence=VSP_004572;
Name=PDE4B3;
IsoId=Q07343-3; Sequence=VSP_004571;
Name=PDE4B5;
IsoId=Q07343-4; Sequence=VSP_047723, VSP_047724;
Note=Brain-specific isoform.;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, lung and skeletal
muscle.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE4 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35643.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; L12686; AAA35643.1; ALT_INIT; mRNA.
EMBL; L20966; AAA03589.1; -; mRNA.
EMBL; L20971; AAA03593.1; -; mRNA.
EMBL; U85048; AAB96381.1; -; mRNA.
EMBL; M97515; AAA36426.1; -; mRNA.
EMBL; EF595686; ABQ85407.1; -; mRNA.
EMBL; AK289969; BAF82658.1; -; mRNA.
EMBL; AK290006; BAF82695.1; -; mRNA.
EMBL; AK290206; BAF82895.1; -; mRNA.
EMBL; AL592285; CAH70626.1; -; Genomic_DNA.
EMBL; AL109926; CAH70626.1; JOINED; Genomic_DNA.
EMBL; AL357273; CAH70626.1; JOINED; Genomic_DNA.
EMBL; AL359701; CAH70626.1; JOINED; Genomic_DNA.
EMBL; AL592285; CAH70628.1; -; Genomic_DNA.
EMBL; AL109926; CAH70628.1; JOINED; Genomic_DNA.
EMBL; AL357273; CAH70628.1; JOINED; Genomic_DNA.
EMBL; AL359701; CAH70628.1; JOINED; Genomic_DNA.
EMBL; AL357273; CAH73002.1; -; Genomic_DNA.
EMBL; AL109926; CAH73002.1; JOINED; Genomic_DNA.
EMBL; AL359701; CAH73002.1; JOINED; Genomic_DNA.
EMBL; AL592285; CAH73002.1; JOINED; Genomic_DNA.
EMBL; AL357273; CAH73004.1; -; Genomic_DNA.
EMBL; AL109926; CAH73004.1; JOINED; Genomic_DNA.
EMBL; AL359701; CAH73004.1; JOINED; Genomic_DNA.
EMBL; AL592285; CAH73004.1; JOINED; Genomic_DNA.
EMBL; AL109926; CAI21749.1; -; Genomic_DNA.
EMBL; AL357273; CAI21749.1; JOINED; Genomic_DNA.
EMBL; AL359701; CAI21749.1; JOINED; Genomic_DNA.
EMBL; AL592285; CAI21749.1; JOINED; Genomic_DNA.
EMBL; AL109926; CAI21750.1; -; Genomic_DNA.
EMBL; AL359701; CAI21750.1; JOINED; Genomic_DNA.
EMBL; AL109926; CAI21751.1; -; Genomic_DNA.
EMBL; AL357273; CAI21751.1; JOINED; Genomic_DNA.
EMBL; AL359701; CAI21751.1; JOINED; Genomic_DNA.
EMBL; AL592285; CAI21751.1; JOINED; Genomic_DNA.
EMBL; AL359701; CAI23099.1; -; Genomic_DNA.
EMBL; AL109926; CAI23099.1; JOINED; Genomic_DNA.
EMBL; AL357273; CAI23099.1; JOINED; Genomic_DNA.
EMBL; AL592285; CAI23099.1; JOINED; Genomic_DNA.
EMBL; AL359701; CAI23100.1; -; Genomic_DNA.
EMBL; AL109926; CAI23100.1; JOINED; Genomic_DNA.
EMBL; AL359701; CAI23101.1; -; Genomic_DNA.
EMBL; AL109926; CAI23101.1; JOINED; Genomic_DNA.
EMBL; AL357273; CAI23101.1; JOINED; Genomic_DNA.
EMBL; AL592285; CAI23101.1; JOINED; Genomic_DNA.
EMBL; AL513493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL591487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06524.1; -; Genomic_DNA.
EMBL; BC101480; AAI01481.1; -; mRNA.
EMBL; BC105040; AAI05041.1; -; mRNA.
CCDS; CCDS30742.1; -. [Q07343-3]
CCDS; CCDS30743.1; -. [Q07343-2]
CCDS; CCDS632.1; -. [Q07343-1]
CCDS; CCDS72802.1; -. [Q07343-4]
PIR; I61354; I61354.
RefSeq; NP_001032416.1; NM_001037339.2. [Q07343-2]
RefSeq; NP_001032417.1; NM_001037340.2. [Q07343-3]
RefSeq; NP_001032418.1; NM_001037341.1. [Q07343-1]
RefSeq; NP_001284369.1; NM_001297440.1.
RefSeq; NP_001284370.1; NM_001297441.1.
RefSeq; NP_001284371.1; NM_001297442.1. [Q07343-4]
RefSeq; NP_002591.2; NM_002600.3. [Q07343-1]
UniGene; Hs.198072; -.
PDB; 1F0J; X-ray; 1.77 A; A/B=324-700.
PDB; 1JP1; Model; -; A=324-700.
PDB; 1JP2; Model; -; A=324-700.
PDB; 1RO6; X-ray; 2.00 A; A/B=324-700.
PDB; 1RO9; X-ray; 2.13 A; A/B=324-700.
PDB; 1ROR; X-ray; 2.00 A; A/B=324-700.
PDB; 1TB5; X-ray; 2.15 A; A/B=324-700.
PDB; 1XLX; X-ray; 2.19 A; A/B=324-700.
PDB; 1XLZ; X-ray; 2.06 A; A/B=324-700.
PDB; 1XM4; X-ray; 2.31 A; A/B=324-700.
PDB; 1XM6; X-ray; 1.92 A; A/B=324-700.
PDB; 1XMU; X-ray; 2.30 A; A/B=324-700.
PDB; 1XMY; X-ray; 2.40 A; A/B=324-700.
PDB; 1XN0; X-ray; 2.31 A; A/B=324-700.
PDB; 1XOS; X-ray; 2.28 A; A=324-700.
PDB; 1XOT; X-ray; 2.34 A; A/B=324-700.
PDB; 1Y2H; X-ray; 2.40 A; A/B=324-700.
PDB; 1Y2J; X-ray; 2.55 A; A/B=324-700.
PDB; 2CHM; X-ray; 1.60 A; A=450-475.
PDB; 2QYL; X-ray; 1.95 A; A=324-659.
PDB; 3D3P; X-ray; 1.75 A; A=324-675.
PDB; 3FRG; X-ray; 1.70 A; A=324-675.
PDB; 3G45; X-ray; 2.63 A; A/B=241-289, A/B=305-659.
PDB; 3GWT; X-ray; 1.75 A; A=324-675.
PDB; 3HC8; X-ray; 1.79 A; A=451-474.
PDB; 3HDZ; X-ray; 1.80 A; A=451-474.
PDB; 3HMV; X-ray; 2.23 A; A/B=324-700.
PDB; 3KKT; X-ray; 2.48 A; A/B=324-700.
PDB; 3LY2; X-ray; 2.60 A; A/B/C/D/E/F/G/H=324-659.
PDB; 3O0J; X-ray; 1.95 A; A=334-656.
PDB; 3O56; X-ray; 2.42 A; A=324-675.
PDB; 3O57; X-ray; 2.00 A; A=324-675.
PDB; 3W5E; X-ray; 2.30 A; A/B=324-700.
PDB; 3WD9; X-ray; 2.50 A; A/B=324-700.
PDB; 4KP6; X-ray; 1.50 A; A=324-659.
PDB; 4MYQ; X-ray; 1.90 A; A=324-691.
PDB; 4NW7; X-ray; 2.15 A; A=324-691.
PDB; 4WZI; X-ray; 2.58 A; A/B=122-736.
PDB; 4X0F; X-ray; 3.22 A; A/B=122-736.
PDB; 5K6J; X-ray; 1.86 A; A=334-656.
PDBsum; 1F0J; -.
PDBsum; 1JP1; -.
PDBsum; 1JP2; -.
PDBsum; 1RO6; -.
PDBsum; 1RO9; -.
PDBsum; 1ROR; -.
PDBsum; 1TB5; -.
PDBsum; 1XLX; -.
PDBsum; 1XLZ; -.
PDBsum; 1XM4; -.
PDBsum; 1XM6; -.
PDBsum; 1XMU; -.
PDBsum; 1XMY; -.
PDBsum; 1XN0; -.
PDBsum; 1XOS; -.
PDBsum; 1XOT; -.
PDBsum; 1Y2H; -.
PDBsum; 1Y2J; -.
PDBsum; 2CHM; -.
PDBsum; 2QYL; -.
PDBsum; 3D3P; -.
PDBsum; 3FRG; -.
PDBsum; 3G45; -.
PDBsum; 3GWT; -.
PDBsum; 3HC8; -.
PDBsum; 3HDZ; -.
PDBsum; 3HMV; -.
PDBsum; 3KKT; -.
PDBsum; 3LY2; -.
PDBsum; 3O0J; -.
PDBsum; 3O56; -.
PDBsum; 3O57; -.
PDBsum; 3W5E; -.
PDBsum; 3WD9; -.
PDBsum; 4KP6; -.
PDBsum; 4MYQ; -.
PDBsum; 4NW7; -.
PDBsum; 4WZI; -.
PDBsum; 4X0F; -.
PDBsum; 5K6J; -.
ProteinModelPortal; Q07343; -.
SMR; Q07343; -.
BioGrid; 111168; 11.
CORUM; Q07343; -.
ELM; Q07343; -.
IntAct; Q07343; 4.
STRING; 9606.ENSP00000332116; -.
BindingDB; Q07343; -.
ChEMBL; CHEMBL275; -.
DrugBank; DB01647; (R)-Mesopram.
DrugBank; DB04149; (R)-Rolipram.
DrugBank; DB03606; (S)-Rolipram.
DrugBank; DB03349; 8-Bromo-Adenosine-5'-Monophosphate.
DrugBank; DB00131; Adenosine monophosphate.
DrugBank; DB01427; Amrinone.
DrugBank; DB05676; Apremilast.
DrugBank; DB00201; Caffeine.
DrugBank; DB03849; Cilomilast.
DrugBank; DB05219; Crisaborole.
DrugBank; DB00651; Dyphylline.
DrugBank; DB00824; Enprofylline.
DrugBank; DB02660; Filaminast.
DrugBank; DB05266; Ibudilast.
DrugBank; DB01088; Iloprost.
DrugBank; DB01113; Papaverine.
DrugBank; DB00806; Pentoxifylline.
DrugBank; DB01791; Piclamilast.
DrugBank; DB01656; Roflumilast.
DrugBank; DB01954; Rolipram.
DrugBank; DB01412; Theobromine.
DrugBank; DB00277; Theophylline.
GuidetoPHARMACOLOGY; 1301; -.
iPTMnet; Q07343; -.
PhosphoSitePlus; Q07343; -.
BioMuta; PDE4B; -.
DMDM; 729163; -.
PaxDb; Q07343; -.
PeptideAtlas; Q07343; -.
PRIDE; Q07343; -.
Ensembl; ENST00000329654; ENSP00000332116; ENSG00000184588. [Q07343-1]
Ensembl; ENST00000341517; ENSP00000342637; ENSG00000184588. [Q07343-1]
Ensembl; ENST00000371045; ENSP00000360084; ENSG00000184588. [Q07343-2]
Ensembl; ENST00000423207; ENSP00000392947; ENSG00000184588. [Q07343-3]
Ensembl; ENST00000480109; ENSP00000432592; ENSG00000184588. [Q07343-4]
GeneID; 5142; -.
KEGG; hsa:5142; -.
UCSC; uc001dcp.4; human. [Q07343-1]
CTD; 5142; -.
DisGeNET; 5142; -.
EuPathDB; HostDB:ENSG00000184588.17; -.
GeneCards; PDE4B; -.
HGNC; HGNC:8781; PDE4B.
HPA; HPA003005; -.
MIM; 600127; gene.
neXtProt; NX_Q07343; -.
OpenTargets; ENSG00000184588; -.
PharmGKB; PA33129; -.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000118889; -.
HOGENOM; HOG000236297; -.
HOVERGEN; HBG108239; -.
KO; K13293; -.
OMA; TCFDVEN; -.
OrthoDB; EOG091G06CD; -.
PhylomeDB; Q07343; -.
TreeFam; TF314638; -.
BRENDA; 3.1.4.53; 2681.
Reactome; R-HSA-180024; DARPP-32 events.
Reactome; R-HSA-418555; G alpha (s) signalling events.
SIGNOR; Q07343; -.
UniPathway; UPA00762; UER00747.
ChiTaRS; PDE4B; human.
EvolutionaryTrace; Q07343; -.
GeneWiki; PDE4B; -.
GenomeRNAi; 5142; -.
PRO; PR:Q07343; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000184588; -.
CleanEx; HS_PDE4B; -.
ExpressionAtlas; Q07343; baseline and differential.
Genevisible; Q07343; HS.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
GO; GO:0000930; C:gamma-tubulin complex; IEA:Ensembl.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0014069; C:postsynaptic density of dendrite; IEA:Ensembl.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:BHF-UCL.
GO; GO:0030552; F:cAMP binding; IGI:BHF-UCL.
GO; GO:0043015; F:gamma-tubulin binding; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IDA:BHF-UCL.
GO; GO:0035690; P:cellular response to drug; ISS:BHF-UCL.
GO; GO:0071872; P:cellular response to epinephrine stimulus; ISS:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:BHF-UCL.
GO; GO:0050900; P:leukocyte migration; ISS:BHF-UCL.
GO; GO:1901898; P:negative regulation of relaxation of cardiac muscle; ISS:BHF-UCL.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:BHF-UCL.
GO; GO:0001780; P:neutrophil homeostasis; ISS:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:BHF-UCL.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:BHF-UCL.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; ISS:BHF-UCL.
GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; ISS:BHF-UCL.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:BHF-UCL.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR023174; PDEase_CS.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; cAMP; Complete proteome;
Hydrolase; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 736 cAMP-specific 3',5'-cyclic
phosphodiesterase 4B.
/FTId=PRO_0000198809.
NP_BIND 406 410 cAMP.
ACT_SITE 406 406 Proton donor.
METAL 410 410 Divalent metal cation 1.
METAL 446 446 Divalent metal cation 1.
METAL 447 447 Divalent metal cation 1.
METAL 447 447 Divalent metal cation 2.
METAL 564 564 Divalent metal cation 1.
BINDING 447 447 cAMP.
BINDING 564 564 cAMP.
BINDING 615 615 cAMP.
SITE 567 567 Binds AMP, but not cAMP. {ECO:0000250}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:P14646}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000250|UniProtKB:P14646}.
MOD_RES 661 661 Phosphoserine.
{ECO:0000250|UniProtKB:P14646}.
VAR_SEQ 1 211 MKKSRSVMTVMADDNVKDYFECSLSKSYSSSSNTLGIDLWR
GRRCCSGNLQLPPLSQRQSERARTPEGDGISRPTTLPLTTL
PSIAITTVSQECFDVENGPSPGRSPLDPQASSSAGLVLHAT
FPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDL
IVTPFAQVLASLRSVRNNFTILTNLHGTSNKRSPAASQPPV
SRVNPQ -> MKEHGGTFSSTGISGGSGDSAMDSLQPLQPN
YMPVCLFA (in isoform PDE4B2).
{ECO:0000303|PubMed:8384210,
ECO:0000303|PubMed:8392015,
ECO:0000303|PubMed:8413254}.
/FTId=VSP_004572.
VAR_SEQ 1 93 MKKSRSVMTVMADDNVKDYFECSLSKSYSSSSNTLGIDLWR
GRRCCSGNLQLPPLSQRQSERARTPEGDGISRPTTLPLTTL
PSIAITTVSQE -> MTAKDSSKELTASEPEVCIKTFKEQM
HLELELPRLPGNRPTSPKISPRSSPRNSPCFFRKLLVNKSI
RQRRRFTVAHT (in isoform PDE4B3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9371714}.
/FTId=VSP_004571.
VAR_SEQ 1 15 MKKSRSVMTVMADDN -> MPEANYLLSVSWGYI (in
isoform PDE4B5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17519386}.
/FTId=VSP_047723.
VAR_SEQ 16 248 Missing (in isoform PDE4B5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17519386}.
/FTId=VSP_047724.
VARIANT 703 703 S -> C (in dbSNP:rs2227297).
/FTId=VAR_034373.
HELIX 168 183 {ECO:0000244|PDB:4WZI}.
HELIX 217 235 {ECO:0000244|PDB:4WZI}.
HELIX 239 264 {ECO:0000244|PDB:4WZI}.
HELIX 266 279 {ECO:0000244|PDB:4WZI}.
HELIX 324 327 {ECO:0000244|PDB:3G45}.
STRAND 328 330 {ECO:0000244|PDB:3FRG}.
TURN 332 334 {ECO:0000244|PDB:1XMU}.
HELIX 335 342 {ECO:0000244|PDB:4KP6}.
TURN 343 346 {ECO:0000244|PDB:4KP6}.
HELIX 352 358 {ECO:0000244|PDB:4KP6}.
TURN 359 361 {ECO:0000244|PDB:1RO6}.
HELIX 363 374 {ECO:0000244|PDB:4KP6}.
HELIX 377 380 {ECO:0000244|PDB:4KP6}.
HELIX 385 397 {ECO:0000244|PDB:4KP6}.
STRAND 403 407 {ECO:0000244|PDB:4KP6}.
HELIX 408 422 {ECO:0000244|PDB:4KP6}.
HELIX 425 427 {ECO:0000244|PDB:4KP6}.
TURN 428 430 {ECO:0000244|PDB:4KP6}.
HELIX 433 445 {ECO:0000244|PDB:4KP6}.
TURN 446 449 {ECO:0000244|PDB:4KP6}.
HELIX 455 460 {ECO:0000244|PDB:4KP6}.
HELIX 464 468 {ECO:0000244|PDB:4KP6}.
TURN 469 471 {ECO:0000244|PDB:4KP6}.
HELIX 474 486 {ECO:0000244|PDB:4KP6}.
HELIX 490 492 {ECO:0000244|PDB:3FRG}.
TURN 494 497 {ECO:0000244|PDB:4KP6}.
HELIX 500 515 {ECO:0000244|PDB:4KP6}.
HELIX 519 521 {ECO:0000244|PDB:4KP6}.
HELIX 522 534 {ECO:0000244|PDB:4KP6}.
STRAND 540 542 {ECO:0000244|PDB:2QYL}.
HELIX 549 564 {ECO:0000244|PDB:4KP6}.
HELIX 567 569 {ECO:0000244|PDB:4KP6}.
HELIX 572 595 {ECO:0000244|PDB:4KP6}.
HELIX 602 604 {ECO:0000244|PDB:3FRG}.
TURN 606 608 {ECO:0000244|PDB:4KP6}.
HELIX 611 621 {ECO:0000244|PDB:4KP6}.
HELIX 623 633 {ECO:0000244|PDB:4KP6}.
TURN 634 638 {ECO:0000244|PDB:4KP6}.
HELIX 639 654 {ECO:0000244|PDB:4KP6}.
STRAND 656 658 {ECO:0000244|PDB:1RO6}.
STRAND 659 662 {ECO:0000244|PDB:3KKT}.
HELIX 664 666 {ECO:0000244|PDB:3KKT}.
HELIX 671 677 {ECO:0000244|PDB:1F0J}.
SEQUENCE 736 AA; 83343 MW; 208FCE9CD40EF5EB CRC64;
MKKSRSVMTV MADDNVKDYF ECSLSKSYSS SSNTLGIDLW RGRRCCSGNL QLPPLSQRQS
ERARTPEGDG ISRPTTLPLT TLPSIAITTV SQECFDVENG PSPGRSPLDP QASSSAGLVL
HATFPGHSQR RESFLYRSDS DYDLSPKAMS RNSSLPSEQH GDDLIVTPFA QVLASLRSVR
NNFTILTNLH GTSNKRSPAA SQPPVSRVNP QEESYQKLAM ETLEELDWCL DQLETIQTYR
SVSEMASNKF KRMLNRELTH LSEMSRSGNQ VSEYISNTFL DKQNDVEIPS PTQKDREKKK
KQQLMTQISG VKKLMHSSSL NNTSISRFGV NTENEDHLAK ELEDLNKWGL NIFNVAGYSH
NRPLTCIMYA IFQERDLLKT FRISSDTFIT YMMTLEDHYH SDVAYHNSLH AADVAQSTHV
LLSTPALDAV FTDLEILAAI FAAAIHDVDH PGVSNQFLIN TNSELALMYN DESVLENHHL
AVGFKLLQEE HCDIFMNLTK KQRQTLRKMV IDMVLATDMS KHMSLLADLK TMVETKKVTS
SGVLLLDNYT DRIQVLRNMV HCADLSNPTK SLELYRQWTD RIMEEFFQQG DKERERGMEI
SPMCDKHTAS VEKSQVGFID YIVHPLWETW ADLVQPDAQD ILDTLEDNRN WYQSMIPQSP
SPPLDEQNRD CQGLMEKFQF ELTLDEEDSE GPEKEGEGHS YFSSTKTLCV IDPENRDSLG
ETDIDIATED KSPVDT


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