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Q07343 (PDE4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 4B

EC=3.1.4.53
Alternative name(s):
DPDE4
PDE32
Gene names
Name:PDE4B
Synonyms:DPDE4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.10 Ref.11

Catalytic activity

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.

Cofactor

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. Ref.10 Ref.11

Enzyme regulation

Inhibited by rolipram.

Pathway

Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.

Tissue specificity

Expressed in brain, heart, lung and skeletal muscle.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.

Sequence caution

The sequence AAA35643.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandcAMP
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell receptor signaling pathway

Inferred from mutant phenotype PubMed 17404263. Source: BHF-UCL

cAMP catabolic process

Inferred from direct assay PubMed 17404263. Source: BHF-UCL

cellular response to drug

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to epinephrine stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: BHF-UCL

leukocyte migration

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of relaxation of cardiac muscle

Inferred from sequence or structural similarity. Source: BHF-UCL

neutrophil chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

neutrophil homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interferon-gamma production

Inferred from mutant phenotype PubMed 17404263. Source: BHF-UCL

positive regulation of interleukin-2 production

Inferred from mutant phenotype PubMed 17404263. Source: BHF-UCL

regulation of cardiac muscle cell contraction

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of high voltage-gated calcium channel activity

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentZ disc

Inferred from sequence or structural similarity. Source: BHF-UCL

cell periphery

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from direct assay PubMed 17404263. Source: BHF-UCL

3',5'-cyclic-nucleotide phosphodiesterase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

cAMP binding

Inferred from genetic interaction Ref.2. Source: BHF-UCL

ion channel binding

Inferred from sequence or structural similarity. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform PDE4B1 (identifier: Q07343-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform PDE4B2 (identifier: Q07343-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-211: MKKSRSVMTV...QPPVSRVNPQ → MKEHGGTFSS...PNYMPVCLFA
Isoform PDE4B3 (identifier: Q07343-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: MKKSRSVMTV...SIAITTVSQE → MTAKDSSKEL...QRRRFTVAHT
Isoform PDE4B5 (identifier: Q07343-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MKKSRSVMTVMADDN → MPEANYLLSVSWGYI
     16-248: Missing.
Note: Brain-specific isoform.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 736736cAMP-specific 3',5'-cyclic phosphodiesterase 4B
PRO_0000198809

Regions

Nucleotide binding406 – 4105cAMP

Sites

Active site4061Proton donor
Metal binding4101Divalent metal cation 1
Metal binding4461Divalent metal cation 1
Metal binding4471Divalent metal cation 1
Metal binding4471Divalent metal cation 2
Metal binding5641Divalent metal cation 1
Binding site4471cAMP
Binding site5641cAMP
Binding site6151cAMP
Site5671Binds AMP, but not cAMP By similarity

Natural variations

Alternative sequence1 – 211211MKKSR…RVNPQ → MKEHGGTFSSTGISGGSGDS AMDSLQPLQPNYMPVCLFA in isoform PDE4B2.
VSP_004572
Alternative sequence1 – 9393MKKSR…TVSQE → MTAKDSSKELTASEPEVCIK TFKEQMHLELELPRLPGNRP TSPKISPRSSPRNSPCFFRK LLVNKSIRQRRRFTVAHT in isoform PDE4B3.
VSP_004571
Alternative sequence1 – 1515MKKSR…MADDN → MPEANYLLSVSWGYI in isoform PDE4B5.
VSP_047723
Alternative sequence16 – 248233Missing in isoform PDE4B5.
VSP_047724
Natural variant7031S → C.
Corresponds to variant rs2227297 [ dbSNP | Ensembl ].
VAR_034373

Secondary structure

....................................................................... 736
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PDE4B1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 208FCE9CD40EF5EB

FASTA73683,343
        10         20         30         40         50         60 
MKKSRSVMTV MADDNVKDYF ECSLSKSYSS SSNTLGIDLW RGRRCCSGNL QLPPLSQRQS 

        70         80         90        100        110        120 
ERARTPEGDG ISRPTTLPLT TLPSIAITTV SQECFDVENG PSPGRSPLDP QASSSAGLVL 

       130        140        150        160        170        180 
HATFPGHSQR RESFLYRSDS DYDLSPKAMS RNSSLPSEQH GDDLIVTPFA QVLASLRSVR 

       190        200        210        220        230        240 
NNFTILTNLH GTSNKRSPAA SQPPVSRVNP QEESYQKLAM ETLEELDWCL DQLETIQTYR 

       250        260        270        280        290        300 
SVSEMASNKF KRMLNRELTH LSEMSRSGNQ VSEYISNTFL DKQNDVEIPS PTQKDREKKK 

       310        320        330        340        350        360 
KQQLMTQISG VKKLMHSSSL NNTSISRFGV NTENEDHLAK ELEDLNKWGL NIFNVAGYSH 

       370        380        390        400        410        420 
NRPLTCIMYA IFQERDLLKT FRISSDTFIT YMMTLEDHYH SDVAYHNSLH AADVAQSTHV 

       430        440        450        460        470        480 
LLSTPALDAV FTDLEILAAI FAAAIHDVDH PGVSNQFLIN TNSELALMYN DESVLENHHL 

       490        500        510        520        530        540 
AVGFKLLQEE HCDIFMNLTK KQRQTLRKMV IDMVLATDMS KHMSLLADLK TMVETKKVTS 

       550        560        570        580        590        600 
SGVLLLDNYT DRIQVLRNMV HCADLSNPTK SLELYRQWTD RIMEEFFQQG DKERERGMEI 

       610        620        630        640        650        660 
SPMCDKHTAS VEKSQVGFID YIVHPLWETW ADLVQPDAQD ILDTLEDNRN WYQSMIPQSP 

       670        680        690        700        710        720 
SPPLDEQNRD CQGLMEKFQF ELTLDEEDSE GPEKEGEGHS YFSSTKTLCV IDPENRDSLG 

       730 
ETDIDIATED KSPVDT 

« Hide

Isoform PDE4B2 [UniParc].

Checksum: A4F9FA0C5DB43380
Show »

FASTA56464,352
Isoform PDE4B3 [UniParc].

Checksum: 49618FFEAFF33D30
Show »

FASTA72182,096
Isoform PDE4B5 [UniParc].

Checksum: 23AF122BAF338C42
Show »

FASTA50357,709

References

« Hide 'large scale' references
[1]"The cDNA of a human lymphocyte cyclic-AMP phosphodiesterase (PDE IV) reveals a multigene family."
Obernolte R., Bhakta S., Alvarez R., Bach C., Mulkins M., Jarnagin K., Shelton E.R.
Gene 129:239-247(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4B2).
[2]"A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs."
Bolger G., Michaeli T., Martins T., St John T., Steiner B., Rodgers L., Riggs M., Wigler M., Ferguson K.
Mol. Cell. Biol. 13:6558-6571(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE4B1 AND PDE4B2).
Tissue: Brain.
[3]"Molecular cloning and transient expression in COS7 cells of a novel human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3."
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.
Biochem. J. 328:549-558(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4B3).
[4]"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."
McLaughlin M.M., Cieslinski L.B., Burman M., Torphy T.J., Livi G.P.
J. Biol. Chem. 268:6470-6476(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4B2).
Tissue: Brain.
[5]"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)."
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.
J. Pharmacol. Exp. Ther. 322:600-609(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4B5).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PDE4B1; PDE4B3 AND PDE4B5).
Tissue: Hippocampus and Thalamus.
[7]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE4B1).
Tissue: Brain.
[10]"Atomic structure of PDE4: insights into phosphodiesterase mechanism and specificity."
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.
Science 288:1822-1825(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 324-700 IN COMPLEX WITH METAL IONS, FUNCTION, COFACTOR.
[11]"Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram."
Xu R.X., Rocque W.J., Lambert M.H., Vanderwall D.E., Luther M.A., Nolte R.T.
J. Mol. Biol. 337:355-365(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 324-700 IN COMPLEX WITH AMP; METAL IONS AND THE INHIBITOR ROLIPRAM, FUNCTION, COFACTOR.
[12]"A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases."
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.
Mol. Cell 15:279-286(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 324-700 IN COMPLEX WITH AMP AND METAL IONS.
[13]"Structural basis for the activity of drugs that inhibit phosphodiesterases."
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.
Structure 12:2233-2247(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 324-700 IN COMPLEX WITH METAL IONS AND INHIBITORS.
[14]"A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design."
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.
Nat. Biotechnol. 23:201-207(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 324-700 IN COMPLEX WITH METAL IONS AND INHIBITORS.
[15]"Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors."
Wang H., Peng M.-S., Chen Y., Geng J., Robinson H., Houslay M.D., Cai J., Ke H.
Biochem. J. 408:193-201(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 324-659 IN COMPLEX WITH METAL IONS AND THE INHIBITOR NVP.
[16]"Pyrazolopyridines as a novel structural class of potent and selective PDE4 inhibitors."
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.
Bioorg. Med. Chem. Lett. 18:4237-4241(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 324-675 IN COMPLEX WITH METAL IONS AND INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L12686 mRNA. Translation: AAA35643.1. Different initiation.
L20966 mRNA. Translation: AAA03589.1.
L20971 mRNA. Translation: AAA03593.1.
U85048 mRNA. Translation: AAB96381.1.
M97515 mRNA. Translation: AAA36426.1.
EF595686 mRNA. Translation: ABQ85407.1.
AK289969 mRNA. Translation: BAF82658.1.
AK290006 mRNA. Translation: BAF82695.1.
AK290206 mRNA. Translation: BAF82895.1.
AL592285 expand/collapse EMBL AC list , AL109926, AL357273, AL359701 Genomic DNA. Translation: CAH70626.1.
AL592285 expand/collapse EMBL AC list , AL109926, AL357273, AL359701 Genomic DNA. Translation: CAH70628.1.
AL357273 expand/collapse EMBL AC list , AL109926, AL359701, AL592285 Genomic DNA. Translation: CAH73002.1.
AL357273 expand/collapse EMBL AC list , AL109926, AL359701, AL592285 Genomic DNA. Translation: CAH73004.1.
AL109926 expand/collapse EMBL AC list , AL357273, AL359701, AL592285 Genomic DNA. Translation: CAI21749.1.
AL109926, AL359701 Genomic DNA. Translation: CAI21750.1.
AL109926 expand/collapse EMBL AC list , AL357273, AL359701, AL592285 Genomic DNA. Translation: CAI21751.1.
AL359701 expand/collapse EMBL AC list , AL109926, AL357273, AL592285 Genomic DNA. Translation: CAI23099.1.
AL359701, AL109926 Genomic DNA. Translation: CAI23100.1.
AL359701 expand/collapse EMBL AC list , AL109926, AL357273, AL592285 Genomic DNA. Translation: CAI23101.1.
AL513493 Genomic DNA. No translation available.
AL590783 Genomic DNA. No translation available.
AL591487 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX06524.1.
BC101480 mRNA. Translation: AAI01481.1.
BC105040 mRNA. Translation: AAI05041.1.
PIRI61354.
RefSeqNP_001032416.1. NM_001037339.1.
NP_001032417.1. NM_001037340.1.
NP_001032418.1. NM_001037341.1.
NP_002591.2. NM_002600.3.
XP_005270983.1. XM_005270926.1.
UniGeneHs.198072.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F0JX-ray1.77A/B324-700[»]
1JP1model-A324-700[»]
1JP2model-A324-700[»]
1RO6X-ray2.00A/B324-700[»]
1RO9X-ray2.13A/B324-700[»]
1RORX-ray2.00A/B324-700[»]
1TB5X-ray2.15A/B324-700[»]
1XLXX-ray2.19A/B324-700[»]
1XLZX-ray2.06A/B324-700[»]
1XM4X-ray2.31A/B324-700[»]
1XM6X-ray1.92A/B324-700[»]
1XMUX-ray2.30A/B324-700[»]
1XMYX-ray2.40A/B324-700[»]
1XN0X-ray2.31A/B324-700[»]
1XOSX-ray2.28A324-700[»]
1XOTX-ray2.34A/B324-700[»]
1Y2HX-ray2.40A/B324-700[»]
1Y2JX-ray2.55A/B324-700[»]
2CHMX-ray1.60A450-475[»]
2QYLX-ray1.95A324-659[»]
3D3PX-ray1.75A324-675[»]
3FRGX-ray1.70A324-675[»]
3G45X-ray2.63A/B241-659[»]
3GWTX-ray1.75A324-675[»]
3HC8X-ray1.79A451-474[»]
3HDZX-ray1.80A451-474[»]
3HMVX-ray2.23A/B324-700[»]
3KKTX-ray2.48A/B324-700[»]
3LY2X-ray2.60A/B/C/D/E/F/G/H324-659[»]
3O0JX-ray1.95A334-656[»]
3O56X-ray2.42A324-675[»]
3O57X-ray2.00A324-675[»]
3W5EX-ray2.30A/B324-700[»]
3WD9X-ray2.50A/B324-700[»]
4KP6X-ray1.50A324-659[»]
4MYQX-ray1.90A324-691[»]
ProteinModelPortalQ07343.
SMRQ07343. Positions 335-681.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111168. 5 interactions.
IntActQ07343. 3 interactions.
STRING9606.ENSP00000332116.

Chemistry

BindingDBQ07343.
ChEMBLCHEMBL2093863.
DrugBankDB00131. Adenosine monophosphate.
DB01427. Amrinone.
DB00201. Caffeine.
DB01166. Cilostazol.
DB00651. Dyphylline.
DB00824. Enprofylline.
DB01113. Papaverine.
DB00806. Pentoxifylline.
DB00277. Theophylline.
GuidetoPHARMACOLOGY1301.

PTM databases

PhosphoSiteQ07343.

Polymorphism databases

DMDM729163.

Proteomic databases

PaxDbQ07343.
PRIDEQ07343.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329654; ENSP00000332116; ENSG00000184588. [Q07343-1]
ENST00000341517; ENSP00000342637; ENSG00000184588. [Q07343-1]
ENST00000371045; ENSP00000360084; ENSG00000184588. [Q07343-2]
ENST00000371049; ENSP00000360088; ENSG00000184588. [Q07343-1]
ENST00000423207; ENSP00000392947; ENSG00000184588. [Q07343-3]
ENST00000480109; ENSP00000432592; ENSG00000184588. [Q07343-4]
GeneID5142.
KEGGhsa:5142.
UCSCuc001dcn.3. human. [Q07343-1]
uc001dcp.3. human. [Q07343-3]
uc001dcq.3. human.

Organism-specific databases

CTD5142.
GeneCardsGC01P066339.
HGNCHGNC:8781. PDE4B.
HPAHPA003005.
MIM600127. gene.
neXtProtNX_Q07343.
PharmGKBPA33129.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG122287.
HOGENOMHOG000236297.
HOVERGENHBG108239.
InParanoidQ07343.
KOK01120.
OMATCFDVEN.
OrthoDBEOG7HQNBC.
PhylomeDBQ07343.
TreeFamTF314638.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
UniPathwayUPA00762; UER00747.

Gene expression databases

ArrayExpressQ07343.
BgeeQ07343.
CleanExHS_PDE4B.
GenevestigatorQ07343.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDE4B. human.
EvolutionaryTraceQ07343.
GeneWikiPDE4B.
GenomeRNAi5142.
NextBio19828.
PROQ07343.
SOURCESearch...

Entry information

Entry namePDE4B_HUMAN
AccessionPrimary (citable) accession number: Q07343
Secondary accession number(s): A5YW33 expand/collapse secondary AC list , O15443, Q13945, Q5TEK4, Q5TEK5, Q5TEK6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM