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Protein

cAMP-specific 3',5'-cyclic phosphodiesterase 4B

Gene

PDE4B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

a divalent metal cation2 PublicationsNote: 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.2 Publications

Enzyme regulationi

Inhibited by rolipram.

Pathway:i3',5'-cyclic AMP degradation

This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. cAMP-specific 3',5'-cyclic phosphodiesterase 4C (PDE4C), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A), cAMP-specific 3',5'-cyclic phosphodiesterase 4A (PDE4A), High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (PDE7A), cAMP-specific 3',5'-cyclic phosphodiesterase 7B (PDE7B), cAMP-specific 3',5'-cyclic phosphodiesterase 4B (PDE4B), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (PDE4D), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (PDE8A), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (PDE8B)
This subpathway is part of the pathway 3',5'-cyclic AMP degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from 3',5'-cyclic AMP, the pathway 3',5'-cyclic AMP degradation and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei406 – 4061Proton donor
Metal bindingi410 – 4101Divalent metal cation 1
Metal bindingi446 – 4461Divalent metal cation 1
Metal bindingi447 – 4471Divalent metal cation 1
Metal bindingi447 – 4471Divalent metal cation 2
Binding sitei447 – 4471cAMP
Metal bindingi564 – 5641Divalent metal cation 1
Binding sitei564 – 5641cAMP
Sitei567 – 5671Binds AMP, but not cAMPBy similarity
Binding sitei615 – 6151cAMP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi406 – 4105cAMP

GO - Molecular functioni

  • 3',5'-cyclic-AMP phosphodiesterase activity Source: BHF-UCL
  • cAMP binding Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.4.53. 2681.
ReactomeiREACT_15334. DARPP-32 events.
REACT_19327. G alpha (s) signalling events.
UniPathwayiUPA00762; UER00747.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 4B (EC:3.1.4.53)
Alternative name(s):
DPDE4
PDE32
Gene namesi
Name:PDE4B
Synonyms:DPDE4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8781. PDE4B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33129.

Chemistry

DrugBankiDB00131. Adenosine monophosphate.
DB01427. Amrinone.
DB00201. Caffeine.
DB00651. Dyphylline.
DB00824. Enprofylline.
DB05266. Ibudilast.
DB01088. Iloprost.
DB00920. Ketotifen.
DB01113. Papaverine.
DB00806. Pentoxifylline.
DB01656. Roflumilast.
DB01412. Theobromine.
DB00277. Theophylline.

Polymorphism and mutation databases

BioMutaiPDE4B.
DMDMi729163.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736cAMP-specific 3',5'-cyclic phosphodiesterase 4BPRO_0000198809Add
BLAST

Proteomic databases

MaxQBiQ07343.
PaxDbiQ07343.
PRIDEiQ07343.

PTM databases

PhosphoSiteiQ07343.

Expressioni

Tissue specificityi

Expressed in brain, heart, lung and skeletal muscle.

Gene expression databases

BgeeiQ07343.
CleanExiHS_PDE4B.
ExpressionAtlasiQ07343. baseline and differential.
GenevisibleiQ07343. HS.

Organism-specific databases

HPAiHPA003005.

Interactioni

Protein-protein interaction databases

BioGridi111168. 9 interactions.
IntActiQ07343. 3 interactions.
STRINGi9606.ENSP00000332116.

Structurei

Secondary structure

1
736
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi168 – 18316Combined sources
Helixi217 – 23519Combined sources
Helixi239 – 26426Combined sources
Helixi266 – 27914Combined sources
Helixi324 – 3274Combined sources
Beta strandi328 – 3303Combined sources
Turni332 – 3343Combined sources
Helixi335 – 3428Combined sources
Turni343 – 3464Combined sources
Helixi352 – 3587Combined sources
Turni359 – 3613Combined sources
Helixi363 – 37412Combined sources
Helixi377 – 3804Combined sources
Helixi385 – 39713Combined sources
Beta strandi403 – 4075Combined sources
Helixi408 – 42215Combined sources
Helixi425 – 4273Combined sources
Turni428 – 4303Combined sources
Helixi433 – 44513Combined sources
Turni446 – 4494Combined sources
Helixi455 – 4606Combined sources
Helixi464 – 4685Combined sources
Turni469 – 4713Combined sources
Helixi474 – 48613Combined sources
Helixi490 – 4923Combined sources
Turni494 – 4974Combined sources
Helixi500 – 51516Combined sources
Helixi519 – 5213Combined sources
Helixi522 – 53413Combined sources
Beta strandi540 – 5423Combined sources
Helixi549 – 56416Combined sources
Helixi567 – 5693Combined sources
Helixi572 – 59524Combined sources
Helixi602 – 6043Combined sources
Turni606 – 6083Combined sources
Helixi611 – 62111Combined sources
Helixi623 – 63311Combined sources
Turni634 – 6385Combined sources
Helixi639 – 65416Combined sources
Beta strandi656 – 6583Combined sources
Beta strandi659 – 6624Combined sources
Helixi664 – 6663Combined sources
Helixi671 – 6777Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/B241-289[»]
A/B305-659[»]
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[»]
4NW7X-ray2.15A324-691[»]
4WZIX-ray2.58A/B122-736[»]
4X0FX-ray3.22A/B122-736[»]
ProteinModelPortaliQ07343.
SMRiQ07343. Positions 335-681.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07343.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG122287.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000236297.
HOVERGENiHBG108239.
KOiK13293.
OMAiTCFDVEN.
OrthoDBiEOG7HQNBC.
PhylomeDBiQ07343.
TreeFamiTF314638.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform PDE4B1 (identifier: Q07343-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKKSRSVMTV MADDNVKDYF ECSLSKSYSS SSNTLGIDLW RGRRCCSGNL
60 70 80 90 100
QLPPLSQRQS ERARTPEGDG ISRPTTLPLT TLPSIAITTV SQECFDVENG
110 120 130 140 150
PSPGRSPLDP QASSSAGLVL HATFPGHSQR RESFLYRSDS DYDLSPKAMS
160 170 180 190 200
RNSSLPSEQH GDDLIVTPFA QVLASLRSVR NNFTILTNLH GTSNKRSPAA
210 220 230 240 250
SQPPVSRVNP QEESYQKLAM ETLEELDWCL DQLETIQTYR SVSEMASNKF
260 270 280 290 300
KRMLNRELTH LSEMSRSGNQ VSEYISNTFL DKQNDVEIPS PTQKDREKKK
310 320 330 340 350
KQQLMTQISG VKKLMHSSSL NNTSISRFGV NTENEDHLAK ELEDLNKWGL
360 370 380 390 400
NIFNVAGYSH NRPLTCIMYA IFQERDLLKT FRISSDTFIT YMMTLEDHYH
410 420 430 440 450
SDVAYHNSLH AADVAQSTHV LLSTPALDAV FTDLEILAAI FAAAIHDVDH
460 470 480 490 500
PGVSNQFLIN TNSELALMYN DESVLENHHL AVGFKLLQEE HCDIFMNLTK
510 520 530 540 550
KQRQTLRKMV IDMVLATDMS KHMSLLADLK TMVETKKVTS SGVLLLDNYT
560 570 580 590 600
DRIQVLRNMV HCADLSNPTK SLELYRQWTD RIMEEFFQQG DKERERGMEI
610 620 630 640 650
SPMCDKHTAS VEKSQVGFID YIVHPLWETW ADLVQPDAQD ILDTLEDNRN
660 670 680 690 700
WYQSMIPQSP SPPLDEQNRD CQGLMEKFQF ELTLDEEDSE GPEKEGEGHS
710 720 730
YFSSTKTLCV IDPENRDSLG ETDIDIATED KSPVDT
Length:736
Mass (Da):83,343
Last modified:February 1, 1995 - v1
Checksum:i208FCE9CD40EF5EB
GO
Isoform PDE4B2 (identifier: Q07343-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-211: MKKSRSVMTV...QPPVSRVNPQ → MKEHGGTFSS...PNYMPVCLFA

Show »
Length:564
Mass (Da):64,352
Checksum:iA4F9FA0C5DB43380
GO
Isoform PDE4B3 (identifier: Q07343-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: MKKSRSVMTV...SIAITTVSQE → MTAKDSSKEL...QRRRFTVAHT

Show »
Length:721
Mass (Da):82,096
Checksum:i49618FFEAFF33D30
GO
Isoform PDE4B5 (identifier: Q07343-4) [UniParc]FASTAAdd to basket

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

Note: Brain-specific isoform.
Show »
Length:503
Mass (Da):57,709
Checksum:i23AF122BAF338C42
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti703 – 7031S → C.
Corresponds to variant rs2227297 [ dbSNP | Ensembl ].
VAR_034373

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 211211MKKSR…RVNPQ → MKEHGGTFSSTGISGGSGDS AMDSLQPLQPNYMPVCLFA in isoform PDE4B2. 3 PublicationsVSP_004572Add
BLAST
Alternative sequencei1 – 9393MKKSR…TVSQE → MTAKDSSKELTASEPEVCIK TFKEQMHLELELPRLPGNRP TSPKISPRSSPRNSPCFFRK LLVNKSIRQRRRFTVAHT in isoform PDE4B3. 2 PublicationsVSP_004571Add
BLAST
Alternative sequencei1 – 1515MKKSR…MADDN → MPEANYLLSVSWGYI in isoform PDE4B5. 2 PublicationsVSP_047723Add
BLAST
Alternative sequencei16 – 248233Missing in isoform PDE4B5. 2 PublicationsVSP_047724Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, AL109926, AL357273, AL359701 Genomic DNA. Translation: CAH70626.1.
AL592285
, AL109926, AL357273, AL359701 Genomic DNA. Translation: CAH70628.1.
AL357273
, AL109926, AL359701, AL592285 Genomic DNA. Translation: CAH73002.1.
AL357273
, AL109926, AL359701, AL592285 Genomic DNA. Translation: CAH73004.1.
AL109926
, AL357273, AL359701, AL592285 Genomic DNA. Translation: CAI21749.1.
AL109926, AL359701 Genomic DNA. Translation: CAI21750.1.
AL109926
, AL357273, AL359701, AL592285 Genomic DNA. Translation: CAI21751.1.
AL359701
, AL109926, AL357273, AL592285 Genomic DNA. Translation: CAI23099.1.
AL359701, AL109926 Genomic DNA. Translation: CAI23100.1.
AL359701
, 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.
CCDSiCCDS30742.1. [Q07343-3]
CCDS30743.1. [Q07343-2]
CCDS632.1. [Q07343-1]
CCDS72802.1. [Q07343-4]
PIRiI61354.
RefSeqiNP_001032416.1. NM_001037339.2. [Q07343-2]
NP_001032417.1. NM_001037340.2. [Q07343-3]
NP_001032418.1. NM_001037341.1. [Q07343-1]
NP_001284369.1. NM_001297440.1.
NP_001284370.1. NM_001297441.1.
NP_001284371.1. NM_001297442.1. [Q07343-4]
NP_002591.2. NM_002600.3. [Q07343-1]
UniGeneiHs.198072.

Genome annotation databases

EnsembliENST00000329654; ENSP00000332116; ENSG00000184588.
ENST00000341517; ENSP00000342637; ENSG00000184588.
ENST00000371045; ENSP00000360084; ENSG00000184588. [Q07343-2]
ENST00000423207; ENSP00000392947; ENSG00000184588. [Q07343-3]
ENST00000480109; ENSP00000432592; ENSG00000184588. [Q07343-4]
GeneIDi5142.
KEGGihsa:5142.
UCSCiuc001dcn.3. human. [Q07343-1]
uc001dcp.3. human. [Q07343-3]
uc001dcq.3. human.
uc009was.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, AL109926, AL357273, AL359701 Genomic DNA. Translation: CAH70626.1.
AL592285
, AL109926, AL357273, AL359701 Genomic DNA. Translation: CAH70628.1.
AL357273
, AL109926, AL359701, AL592285 Genomic DNA. Translation: CAH73002.1.
AL357273
, AL109926, AL359701, AL592285 Genomic DNA. Translation: CAH73004.1.
AL109926
, AL357273, AL359701, AL592285 Genomic DNA. Translation: CAI21749.1.
AL109926, AL359701 Genomic DNA. Translation: CAI21750.1.
AL109926
, AL357273, AL359701, AL592285 Genomic DNA. Translation: CAI21751.1.
AL359701
, AL109926, AL357273, AL592285 Genomic DNA. Translation: CAI23099.1.
AL359701, AL109926 Genomic DNA. Translation: CAI23100.1.
AL359701
, 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.
CCDSiCCDS30742.1. [Q07343-3]
CCDS30743.1. [Q07343-2]
CCDS632.1. [Q07343-1]
CCDS72802.1. [Q07343-4]
PIRiI61354.
RefSeqiNP_001032416.1. NM_001037339.2. [Q07343-2]
NP_001032417.1. NM_001037340.2. [Q07343-3]
NP_001032418.1. NM_001037341.1. [Q07343-1]
NP_001284369.1. NM_001297440.1.
NP_001284370.1. NM_001297441.1.
NP_001284371.1. NM_001297442.1. [Q07343-4]
NP_002591.2. NM_002600.3. [Q07343-1]
UniGeneiHs.198072.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/B241-289[»]
A/B305-659[»]
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[»]
4NW7X-ray2.15A324-691[»]
4WZIX-ray2.58A/B122-736[»]
4X0FX-ray3.22A/B122-736[»]
ProteinModelPortaliQ07343.
SMRiQ07343. Positions 335-681.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111168. 9 interactions.
IntActiQ07343. 3 interactions.
STRINGi9606.ENSP00000332116.

Chemistry

BindingDBiQ07343.
ChEMBLiCHEMBL2111340.
DrugBankiDB00131. Adenosine monophosphate.
DB01427. Amrinone.
DB00201. Caffeine.
DB00651. Dyphylline.
DB00824. Enprofylline.
DB05266. Ibudilast.
DB01088. Iloprost.
DB00920. Ketotifen.
DB01113. Papaverine.
DB00806. Pentoxifylline.
DB01656. Roflumilast.
DB01412. Theobromine.
DB00277. Theophylline.
GuidetoPHARMACOLOGYi1301.

PTM databases

PhosphoSiteiQ07343.

Polymorphism and mutation databases

BioMutaiPDE4B.
DMDMi729163.

Proteomic databases

MaxQBiQ07343.
PaxDbiQ07343.
PRIDEiQ07343.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329654; ENSP00000332116; ENSG00000184588.
ENST00000341517; ENSP00000342637; ENSG00000184588.
ENST00000371045; ENSP00000360084; ENSG00000184588. [Q07343-2]
ENST00000423207; ENSP00000392947; ENSG00000184588. [Q07343-3]
ENST00000480109; ENSP00000432592; ENSG00000184588. [Q07343-4]
GeneIDi5142.
KEGGihsa:5142.
UCSCiuc001dcn.3. human. [Q07343-1]
uc001dcp.3. human. [Q07343-3]
uc001dcq.3. human.
uc009was.3. human.

Organism-specific databases

CTDi5142.
GeneCardsiGC01P066339.
HGNCiHGNC:8781. PDE4B.
HPAiHPA003005.
MIMi600127. gene.
neXtProtiNX_Q07343.
PharmGKBiPA33129.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG122287.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000236297.
HOVERGENiHBG108239.
KOiK13293.
OMAiTCFDVEN.
OrthoDBiEOG7HQNBC.
PhylomeDBiQ07343.
TreeFamiTF314638.

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747.
BRENDAi3.1.4.53. 2681.
ReactomeiREACT_15334. DARPP-32 events.
REACT_19327. G alpha (s) signalling events.

Miscellaneous databases

ChiTaRSiPDE4B. human.
EvolutionaryTraceiQ07343.
GeneWikiiPDE4B.
GenomeRNAii5142.
NextBioi19828.
PROiQ07343.
SOURCEiSearch...

Gene expression databases

BgeeiQ07343.
CleanExiHS_PDE4B.
ExpressionAtlasiQ07343. baseline and differential.
GenevisibleiQ07343. HS.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 324-700 IN COMPLEX WITH AMP AND METAL IONS.
  13. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 324-675 IN COMPLEX WITH METAL IONS AND INHIBITOR.

Entry informationi

Entry nameiPDE4B_HUMAN
AccessioniPrimary (citable) accession number: Q07343
Secondary accession number(s): A5YW33
, O15443, Q13945, Q5TEK4, Q5TEK5, Q5TEK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.