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Q08499

- PDE4D_HUMAN

UniProt

Q08499 - PDE4D_HUMAN

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Protein

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

Gene
PDE4D, DPDE3
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

Catalytic activityi

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

Cofactori

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. Activated by phosphatidic acid.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei462 – 4621Proton donor By similarity
Metal bindingi466 – 4661Divalent metal cation 1
Metal bindingi502 – 5021Divalent metal cation 1
Metal bindingi503 – 5031Divalent metal cation 1
Metal bindingi503 – 5031Divalent metal cation 2
Binding sitei503 – 5031cAMP
Metal bindingi620 – 6201Divalent metal cation 1
Binding sitei620 – 6201cAMP
Sitei623 – 6231Binds AMP, but not cAMP
Binding sitei671 – 6711cAMP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi462 – 4665cAMP

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: BHF-UCL
  2. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  3. ATPase binding Source: BHF-UCL
  4. beta-2 adrenergic receptor binding Source: BHF-UCL
  5. cAMP binding Source: BHF-UCL
  6. drug binding Source: UniProtKB
  7. enzyme binding Source: BHF-UCL
  8. ion channel binding Source: BHF-UCL
  9. metal ion binding Source: UniProtKB-KW
  10. protein binding Source: IntAct
  11. scaffold protein binding Source: BHF-UCL
  12. ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  1. adrenergic receptor signaling pathway Source: BHF-UCL
  2. adrenergic receptor signaling pathway involved in positive regulation of heart rate Source: BHF-UCL
  3. aging Source: Ensembl
  4. cAMP catabolic process Source: BHF-UCL
  5. cAMP-mediated signaling Source: BHF-UCL
  6. cellular response to cAMP Source: BHF-UCL
  7. cellular response to epinephrine stimulus Source: BHF-UCL
  8. cellular response to lipopolysaccharide Source: Ensembl
  9. establishment of endothelial barrier Source: UniProtKB
  10. multicellular organism growth Source: Ensembl
  11. negative regulation of heart contraction Source: BHF-UCL
  12. negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  13. negative regulation of relaxation of cardiac muscle Source: BHF-UCL
  14. neutrophil chemotaxis Source: Ensembl
  15. positive regulation of interferon-gamma production Source: BHF-UCL
  16. positive regulation of interleukin-2 production Source: BHF-UCL
  17. positive regulation of interleukin-5 production Source: BHF-UCL
  18. regulation of cardiac muscle cell contraction Source: BHF-UCL
  19. regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  20. regulation of heart rate Source: BHF-UCL
  21. regulation of receptor activity Source: BHF-UCL
  22. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  23. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  24. smooth muscle contraction Source: Ensembl
  25. T cell receptor signaling pathway Source: BHF-UCL
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.
SignaLinkiQ08499.
UniPathwayiUPA00762; UER00747.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 4D (EC:3.1.4.53)
Alternative name(s):
DPDE3
PDE43
Gene namesi
Name:PDE4D
Synonyms:DPDE3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:8783. PDE4D.

Subcellular locationi

Apical cell membrane. Cytoplasm By similarity. Membrane By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
Note: Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome By similarity. Colocalized with SHANK2 to the apical membrane of colonic crypt cells.1 Publication

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB-SubCell
  2. calcium channel complex Source: BHF-UCL
  3. cytosol Source: BHF-UCL
  4. membrane Source: BHF-UCL
  5. microtubule organizing center Source: UniProtKB-SubCell
  6. voltage-gated calcium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Genetic variations in PDE4D might be associated with susceptibility to stroke. 1 Publication states that association with stroke has to be considered with caution.
Acrodysostosis 2, with or without hormone resistance (ACRDYS2) [MIM:614613]: A pleiotropic disorder characterized by skeletal, endocrine, and neurological abnormalities. Skeletal features include brachycephaly, midface hypoplasia with a small upturned nose, brachydactyly, and lumbar spinal stenosis. Endocrine abnormalities include hypothyroidism and hypogonadism in males and irregular menses in females. Developmental disability is a common finding but is variable in severity and can be associated with significant behavioral problems.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti190 – 1901S → A in ACRDYS2. 1 Publication
VAR_068242
Natural varianti225 – 2251P → T in ACRDYS2. 2 Publications
VAR_068243
Natural varianti226 – 2261F → S in ACRDYS2. 1 Publication
VAR_068244
Natural varianti227 – 2271A → S in ACRDYS2. 1 Publication
VAR_069448
Natural varianti228 – 2281Q → E in ACRDYS2. 1 Publication
VAR_069449
Natural varianti301 – 3011S → T in ACRDYS2. 1 Publication
VAR_069450
Natural varianti304 – 3041A → V in ACRDYS2. 1 Publication
VAR_069451
Natural varianti329 – 3291V → A in ACRDYS2. 1 Publication
VAR_069452
Natural varianti587 – 5871T → P in ACRDYS2. 1 Publication
VAR_068245
Natural varianti590 – 5901E → A in ACRDYS2. 2 Publications
VAR_069453
Natural varianti673 – 6731G → D in ACRDYS2. 1 Publication
VAR_069454
Natural varianti678 – 6781I → T in ACRDYS2. 1 Publication
VAR_069455

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi503 – 5031D → N: Abolishes catalytic activity.
Mutagenesisi527 – 5271D → R: Abolishes homodimerization. 1 Publication
Mutagenesisi563 – 5631R → D: Abolishes homodimerization. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614613. phenotype.
Orphaneti950. Acrodysostosis.
280651. Acrodysostosis with multiple hormone resistance.
PharmGKBiPA33130.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 809809cAMP-specific 3',5'-cyclic phosphodiesterase 4DPRO_0000198814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991Phosphoserine1 Publication
Modified residuei301 – 3011Phosphoserine1 Publication
Cross-linki387 – 387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

Long isoforms that share a conserved PKA phosphorylation site in the N-terminus are activated by PKA through phosphorylation By similarity. Isoform 3 and isoform 7 are activated by phosphorylation (in vitro), but not isoform 6. Isoform N3 and isoform 12 are phosphorylated on Ser-49, Ser-51, Ser-55 and Ser-59.2 Publications
Sumoylation of long isoforms by PIAS4 augments their activation by PKA phosphorylation and represses their inhibition by ERK phosphorylation.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ08499.
PaxDbiQ08499.
PRIDEiQ08499.

PTM databases

PhosphoSiteiQ08499.

Expressioni

Tissue specificityi

Expressed in colonic epithelial cells (at protein level). Widespread; most abundant in skeletal muscle. Isoform 6 is detected in brain. Isoform 8 is detected in brain, placenta, lung and kidney. Isoform 7 is detected in heart and skeletal muscle.2 Publications

Gene expression databases

ArrayExpressiQ08499.
BgeeiQ08499.
GenevestigatoriQ08499.

Organism-specific databases

HPAiHPA045895.

Interactioni

Subunit structurei

Homodimer for the long isoforms. Isoforms with truncated N-termini are monomeric. Isoform 3 is part of a ternary complex containing PRKAR2A, PRKAR2B and AKAP9. Interacts with PDE4DIP. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) By similarity. Isoform 5, isoform N3 and isoform 12 bind GNB2L1 via their unique N-terminus. Binds ARRB2. Interacts (via N-terminal region) with SHANK2 (via proline-rich region); the interaction is increased in a PKA-dependent manner.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Adcy2P267693EBI-8095525,EBI-1027877From a different organism.
ZDHHC17Q8IUH52EBI-9090666,EBI-524753

Protein-protein interaction databases

BioGridi111170. 32 interactions.
DIPiDIP-29709N.
DIP-41115N.
IntActiQ08499. 10 interactions.
MINTiMINT-92262.

Structurei

Secondary structure

1
809
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi328 – 3369
Beta strandi383 – 3864
Helixi389 – 3979
Helixi398 – 4003
Helixi408 – 4147
Helixi419 – 43012
Helixi433 – 4364
Helixi441 – 45313
Beta strandi460 – 4634
Helixi464 – 47815
Helixi481 – 4833
Turni484 – 4863
Helixi489 – 50113
Turni502 – 5054
Helixi511 – 5166
Helixi520 – 5256
Helixi530 – 54112
Helixi542 – 5443
Turni545 – 5473
Turni550 – 5534
Helixi556 – 57116
Helixi575 – 5773
Helixi578 – 59013
Beta strandi598 – 6003
Helixi605 – 62016
Helixi623 – 6253
Helixi628 – 65225
Turni658 – 6603
Beta strandi662 – 6643
Helixi667 – 67711
Helixi679 – 68911
Turni690 – 6945
Helixi695 – 71016

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E9KNMR-A-[»]
1MKDX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L388-715[»]
1OYNX-ray2.00A/B/C/D381-740[»]
1PTWX-ray2.30A/B/C/D381-740[»]
1Q9MX-ray2.30A/B/C/D381-740[»]
1TB7X-ray1.63A/B388-715[»]
1TBBX-ray1.60A/B388-715[»]
1XOMX-ray1.55A/B388-715[»]
1XONX-ray1.72A/B388-715[»]
1XOQX-ray1.83A/B388-715[»]
1XORX-ray1.54A/B388-715[»]
1Y2BX-ray1.40A/B388-715[»]
1Y2CX-ray1.67A/B388-715[»]
1Y2DX-ray1.70A/B388-715[»]
1Y2EX-ray2.10A/B388-715[»]
1Y2KX-ray1.36A/B388-715[»]
1ZKNX-ray2.10A/B/C/D381-714[»]
2FM0X-ray2.00A/B/C/D381-741[»]
2FM5X-ray2.03A/B/C/D381-741[»]
2PW3X-ray1.56A/B388-714[»]
2QYNX-ray1.57A/B388-715[»]
3G4GX-ray2.30A/B/C/D299-347[»]
A/B/C/D360-714[»]
3G4IX-ray1.90A/B/C/D380-753[»]
3G4KX-ray1.95A/B/C/D380-753[»]
3G4LX-ray2.50A/B/C/D380-753[»]
3G58X-ray2.05A/B/C/D380-753[»]
3IADX-ray2.65A/B/C/D326-339[»]
A/B/C/D380-714[»]
3IAKX-ray2.80A388-715[»]
3K4SX-ray2.05A388-715[»]
3SL3X-ray2.10A/B/C/D381-741[»]
3SL4X-ray1.90A/B/C/D381-741[»]
3SL5X-ray2.65A/B/C/D381-714[»]
3SL6X-ray2.44A/B/C/D381-741[»]
3SL8X-ray2.60A/B/C/D381-741[»]
3V9BX-ray2.10A/B/C/D381-740[»]
ProteinModelPortaliQ08499.
SMRiQ08499. Positions 327-739.

Miscellaneous databases

EvolutionaryTraceiQ08499.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 8847Pro-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG122287.
HOVERGENiHBG108239.
InParanoidiQ08499.
KOiK01120.
OMAiYENSSAD.
OrthoDBiEOG7HQNBC.
PhylomeDBiQ08499.
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 (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. Align

Isoform 4 (identifier: Q08499-1) [UniParc]FASTAAdd to Basket

Also known as: hPDE4D4

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

MEAEGSSAPA RAGSGEGSDS AGGATLKAPK HLWRHEQHHQ YPLRQPQFRL    50
LHPHHHLPPP PPPSPQPQPQ CPLQPPPPPP LPPPPPPPGA ARGRYASSGA 100
TGRVRHRGYS DTERYLYCRA MDRTSYAVET GHRPGLKKSR MSWPSSFQGL 150
RRFDVDNGTS AGRSPLDPMT SPGSGLILQA NFVHSQRRES FLYRSDSDYD 200
LSPKSMSRNS SIASDIHGDD LIVTPFAQVL ASLRTVRNNF AALTNLQDRA 250
PSKRSPMCNQ PSINKATITE EAYQKLASET LEELDWCLDQ LETLQTRHSV 300
SEMASNKFKR MLNRELTHLS EMSRSGNQVS EFISNTFLDK QHEVEIPSPT 350
QKEKEKKKRP MSQISGVKKL MHSSSLTNSS IPRFGVKTEQ EDVLAKELED 400
VNKWGLHVFR IAELSGNRPL TVIMHTIFQE RDLLKTFKIP VDTLITYLMT 450
LEDHYHADVA YHNNIHAADV VQSTHVLLST PALEAVFTDL EILAAIFASA 500
IHDVDHPGVS NQFLINTNSE LALMYNDSSV LENHHLAVGF KLLQEENCDI 550
FQNLTKKQRQ SLRKMVIDIV LATDMSKHMN LLADLKTMVE TKKVTSSGVL 600
LLDNYSDRIQ VLQNMVHCAD LSNPTKPLQL YRQWTDRIME EFFRQGDRER 650
ERGMEISPMC DKHNASVEKS QVGFIDYIVH PLWETWADLV HPDAQDILDT 700
LEDNREWYQS TIPQSPSPAP DDPEEGRQGQ TEKFQFELTL EEDGESDTEK 750
DSGSQVEEDT SCSDSKTLCT QDSESTEIPL DEQVEEEAVG EEEESQPEAC 800
VIDDRSPDT 809
Length:809
Mass (Da):91,115
Last modified:December 1, 2000 - v2
Checksum:i7A4773DD3A044F57
GO
Isoform 3 (identifier: Q08499-2) [UniParc]FASTAAdd to Basket

Also known as: hPDE4D3

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: MEAEGSSAPA...WPSSFQGLRR → MMHVNNFPFRRHSWIC

Note: Contains a phosphoserine at position 53. Activated by phosphorylation at Ser-53. Mutagenesis of Ser-53 abolishes activation.

Show »
Length:673
Mass (Da):76,467
Checksum:iBDC04171BA91A297
GO
Isoform 10 (identifier: Q08499-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-205: Missing.

Show »
Length:604
Mass (Da):68,607
Checksum:i446D0C31C86399AB
GO
Isoform 1 (identifier: Q08499-4) [UniParc]FASTAAdd to Basket

Also known as: hPDE4D1

The sequence of this isoform differs from the canonical sequence as follows:
     1-269: MEAEGSSAPA...QPSINKATIT → MKEQPSCAGT...TESPFPCLFA

Show »
Length:584
Mass (Da):66,376
Checksum:iC1761886FF962102
GO
Isoform 2 (identifier: Q08499-5) [UniParc]FASTAAdd to Basket

Also known as: hPDE4D2

The sequence of this isoform differs from the canonical sequence as follows:
     1-302: Missing.

Show »
Length:507
Mass (Da):57,792
Checksum:i6C07C949952EE5DF
GO
Isoform 5 (identifier: Q08499-6) [UniParc]FASTAAdd to Basket

Also known as: hPDE4D5

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: MEAEGSSAPA...WPSSFQGLRR → MAQQTSPDTL...QRRFTVAHTC

Note: Contains a phosphoserine at position 59. Contains a phosphoserine at position 63.

Show »
Length:745
Mass (Da):84,428
Checksum:iD136AE2B7132DAAC
GO
Isoform N3 (identifier: Q08499-7) [UniParc]FASTAAdd to Basket

Also known as: PDE4DN3

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: MEAEGSSAPA...WPSSFQGLRR → MAQQTSPDTL...QRRFTVAHTC
     270-279: EEAYQKLASE → GLYNGIIAFL
     280-809: Missing.

Note: Contains a phosphoserine at position 59. Contains a phosphoserine at position 63.

Show »
Length:215
Mass (Da):23,839
Checksum:i255EF7985DB75353
GO
Isoform 6 (identifier: Q08499-8) [UniParc]FASTAAdd to Basket

Also known as: PDE4D6

The sequence of this isoform differs from the canonical sequence as follows:
     1-291: Missing.
     292-306: ETLQTRHSVSEMASN → MPEANYLLSVSWGYI

Show »
Length:518
Mass (Da):59,113
Checksum:i069F18EB90BAAF4B
GO
Isoform 8 (identifier: Q08499-9) [UniParc]FASTAAdd to Basket

Also known as: PDE4D8

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.
     123-152: RTSYAVETGHRPGLKKSRMSWPSSFQGLRR → MAFVWDPLGATVPGPSTRAKSRLRFSKSYS

Show »
Length:687
Mass (Da):77,705
Checksum:i90B1ED110D7ED77C
GO
Isoform 9 (identifier: Q08499-10) [UniParc]FASTAAdd to Basket

Also known as: PDE4D9

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: Missing.
     131-152: GHRPGLKKSRMSWPSSFQGLRR → MSIIMKPRSRSTSSLRTAEAVC

Show »
Length:679
Mass (Da):76,816
Checksum:iD35B0A2D975C5705
GO
Isoform 7 (identifier: Q08499-11) [UniParc]FASTAAdd to Basket

Also known as: PDE4D7

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
     62-152: PPSPQPQPQC...WPSSFQGLRR → MKRNTCDLLS...IAITSAESSG

Show »
Length:748
Mass (Da):84,662
Checksum:iD10CF5036B1EA7C8
GO
Isoform 12 (identifier: Q08499-12) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: MEAEGSSAPA...WPSSFQGLRR → MAQQTSPDTL...QRRFTVAHTC
     270-283: EEAYQKLASETLEE → GSWMELNPYTLLDM
     284-809: Missing.

Note: Contains a phosphoserine at position 59. Contains a phosphoserine at position 63.

Show »
Length:219
Mass (Da):24,429
Checksum:i04C84B400D6F7D2C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti190 – 1901S → A in ACRDYS2. 1 Publication
VAR_068242
Natural varianti225 – 2251P → T in ACRDYS2. 2 Publications
VAR_068243
Natural varianti226 – 2261F → S in ACRDYS2. 1 Publication
VAR_068244
Natural varianti227 – 2271A → S in ACRDYS2. 1 Publication
VAR_069448
Natural varianti228 – 2281Q → E in ACRDYS2. 1 Publication
VAR_069449
Natural varianti301 – 3011S → T in ACRDYS2. 1 Publication
VAR_069450
Natural varianti304 – 3041A → V in ACRDYS2. 1 Publication
VAR_069451
Natural varianti329 – 3291V → A in ACRDYS2. 1 Publication
VAR_069452
Natural varianti587 – 5871T → P in ACRDYS2. 1 Publication
VAR_068245
Natural varianti590 – 5901E → A in ACRDYS2. 2 Publications
VAR_069453
Natural varianti673 – 6731G → D in ACRDYS2. 1 Publication
VAR_069454
Natural varianti678 – 6781I → T in ACRDYS2. 1 Publication
VAR_069455

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 302302Missing in isoform 2. VSP_004580Add
BLAST
Alternative sequencei1 – 291291Missing in isoform 6. VSP_012383Add
BLAST
Alternative sequencei1 – 269269MEAEG…KATIT → MKEQPSCAGTGHPMAGYGRM APFELASGPVKRLRTESPFP CLFA in isoform 1. VSP_004579Add
BLAST
Alternative sequencei1 – 205205Missing in isoform 10. VSP_004578Add
BLAST
Alternative sequencei1 – 152152MEAEG…QGLRR → MMHVNNFPFRRHSWIC in isoform 3. VSP_004577Add
BLAST
Alternative sequencei1 – 152152MEAEG…QGLRR → MAQQTSPDTLTVPEVDNPHC PNPWLNEDLVKSLRENLLQH EKSKTARKSVSPKLSPVISP RNSPRLLRRMLLSSNIPKQR RFTVAHTC in isoform 5, isoform N3 and isoform 12. VSP_012384Add
BLAST
Alternative sequencei1 – 130130Missing in isoform 9. VSP_012385Add
BLAST
Alternative sequencei1 – 122122Missing in isoform 8. VSP_012386Add
BLAST
Alternative sequencei1 – 6161Missing in isoform 7. VSP_012387Add
BLAST
Alternative sequencei62 – 15291PPSPQ…QGLRR → MKRNTCDLLSRSKSASEETL HSSNEEEDPFRGMEPYLVRR LSCRNIQLPPLAFRQLEQAD LKSESENIQRPTSLPLKILP LIAITSAESSG in isoform 7. VSP_012388Add
BLAST
Alternative sequencei123 – 15230RTSYA…QGLRR → MAFVWDPLGATVPGPSTRAK SRLRFSKSYS in isoform 8. VSP_012389Add
BLAST
Alternative sequencei131 – 15222GHRPG…QGLRR → MSIIMKPRSRSTSSLRTAEA VC in isoform 9. VSP_012390Add
BLAST
Alternative sequencei270 – 28314EEAYQ…ETLEE → GSWMELNPYTLLDM in isoform 12. VSP_023326Add
BLAST
Alternative sequencei270 – 27910EEAYQKLASE → GLYNGIIAFL in isoform N3. VSP_012391
Alternative sequencei280 – 809530Missing in isoform N3. VSP_012392Add
BLAST
Alternative sequencei284 – 809526Missing in isoform 12. VSP_023327Add
BLAST
Alternative sequencei292 – 30615ETLQT…EMASN → MPEANYLLSVSWGYI in isoform 6. VSP_012393Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti510 – 5101S → F in AAH36319. 1 Publication
Sequence conflicti549 – 5491D → G in AAN10119. 1 Publication
Sequence conflicti644 – 6441R → P1 Publication
Sequence conflicti769 – 7691C → R in AAA97890. 1 Publication
Sequence conflicti769 – 7691C → R in AAA97891. 1 Publication
Sequence conflicti769 – 7691C → R in AAA97892. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20970 mRNA. Translation: AAA03592.1.
L20969 mRNA. Translation: AAC00042.1.
U02882 mRNA. Translation: AAC13745.1.
U50157 mRNA. Translation: AAA97890.1.
U50158 mRNA. Translation: AAA97891.1.
U50159 mRNA. Translation: AAA97892.1.
AF012074 mRNA. Translation: AAC00070.1.
AF012073 mRNA. Translation: AAC00069.1.
AJ250854 mRNA. Translation: CAC03757.1.
AF536975 mRNA. Translation: AAN10117.1.
AF536976 mRNA. Translation: AAN10118.1.
AF536977 mRNA. Translation: AAN10119.1.
AY388960 mRNA. Translation: AAQ90404.1.
AY245866 mRNA. Translation: AAP75760.1.
AY245867 mRNA. Translation: AAP75761.1.
BT007398 mRNA. Translation: AAP36062.1.
BC008390 mRNA. Translation: AAH08390.1.
BC036319 mRNA. Translation: AAH36319.1.
CCDSiCCDS47213.1. [Q08499-1]
CCDS54858.1. [Q08499-2]
CCDS54859.1. [Q08499-11]
CCDS56369.1. [Q08499-8]
CCDS56370.1. [Q08499-5]
CCDS56371.1. [Q08499-10]
CCDS56372.1. [Q08499-9]
CCDS56373.1. [Q08499-6]
PIRiI61358.
RefSeqiNP_001098101.1. NM_001104631.1. [Q08499-1]
NP_001159371.1. NM_001165899.1. [Q08499-11]
NP_001184147.1. NM_001197218.1. [Q08499-6]
NP_001184148.1. NM_001197219.1. [Q08499-9]
NP_001184149.1. NM_001197220.1. [Q08499-10]
NP_001184150.1. NM_001197221.1. [Q08499-5]
NP_001184151.1. NM_001197222.1.
NP_001184152.1. NM_001197223.1. [Q08499-8]
NP_006194.2. NM_006203.4. [Q08499-2]
XP_005248595.1. XM_005248538.2. [Q08499-2]
XP_005248598.1. XM_005248541.2. [Q08499-5]
UniGeneiHs.117545.

Genome annotation databases

EnsembliENST00000309641; ENSP00000308485; ENSG00000113448. [Q08499-7]
ENST00000317118; ENSP00000321739; ENSG00000113448. [Q08499-8]
ENST00000340635; ENSP00000345502; ENSG00000113448. [Q08499-1]
ENST00000358923; ENSP00000351800; ENSG00000113448. [Q08499-5]
ENST00000360047; ENSP00000353152; ENSG00000113448.
ENST00000405755; ENSP00000384806; ENSG00000113448. [Q08499-9]
ENST00000502484; ENSP00000423094; ENSG00000113448. [Q08499-11]
ENST00000502575; ENSP00000425917; ENSG00000113448. [Q08499-12]
ENST00000503258; ENSP00000425605; ENSG00000113448. [Q08499-10]
ENST00000507116; ENSP00000424852; ENSG00000113448. [Q08499-6]
ENST00000546160; ENSP00000442734; ENSG00000113448. [Q08499-11]
GeneIDi5144.
KEGGihsa:5144.
UCSCiuc003jrs.2. human. [Q08499-8]
uc003jrt.2. human. [Q08499-1]
uc003jru.3. human. [Q08499-4]
uc003jrv.2. human. [Q08499-10]
uc003jrw.2. human. [Q08499-9]
uc003jrz.3. human. [Q08499-6]
uc003jsb.3. human. [Q08499-11]
uc003jsc.3. human. [Q08499-12]

Polymorphism databases

DMDMi12644392.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

phosphodiesterase 4D, cAMP-specific (phosphodiesterase E3 dunce homolog, Drosophila) (PDE4D)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20970 mRNA. Translation: AAA03592.1 .
L20969 mRNA. Translation: AAC00042.1 .
U02882 mRNA. Translation: AAC13745.1 .
U50157 mRNA. Translation: AAA97890.1 .
U50158 mRNA. Translation: AAA97891.1 .
U50159 mRNA. Translation: AAA97892.1 .
AF012074 mRNA. Translation: AAC00070.1 .
AF012073 mRNA. Translation: AAC00069.1 .
AJ250854 mRNA. Translation: CAC03757.1 .
AF536975 mRNA. Translation: AAN10117.1 .
AF536976 mRNA. Translation: AAN10118.1 .
AF536977 mRNA. Translation: AAN10119.1 .
AY388960 mRNA. Translation: AAQ90404.1 .
AY245866 mRNA. Translation: AAP75760.1 .
AY245867 mRNA. Translation: AAP75761.1 .
BT007398 mRNA. Translation: AAP36062.1 .
BC008390 mRNA. Translation: AAH08390.1 .
BC036319 mRNA. Translation: AAH36319.1 .
CCDSi CCDS47213.1. [Q08499-1 ]
CCDS54858.1. [Q08499-2 ]
CCDS54859.1. [Q08499-11 ]
CCDS56369.1. [Q08499-8 ]
CCDS56370.1. [Q08499-5 ]
CCDS56371.1. [Q08499-10 ]
CCDS56372.1. [Q08499-9 ]
CCDS56373.1. [Q08499-6 ]
PIRi I61358.
RefSeqi NP_001098101.1. NM_001104631.1. [Q08499-1 ]
NP_001159371.1. NM_001165899.1. [Q08499-11 ]
NP_001184147.1. NM_001197218.1. [Q08499-6 ]
NP_001184148.1. NM_001197219.1. [Q08499-9 ]
NP_001184149.1. NM_001197220.1. [Q08499-10 ]
NP_001184150.1. NM_001197221.1. [Q08499-5 ]
NP_001184151.1. NM_001197222.1.
NP_001184152.1. NM_001197223.1. [Q08499-8 ]
NP_006194.2. NM_006203.4. [Q08499-2 ]
XP_005248595.1. XM_005248538.2. [Q08499-2 ]
XP_005248598.1. XM_005248541.2. [Q08499-5 ]
UniGenei Hs.117545.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E9K NMR - A - [» ]
1MKD X-ray 2.90 A/B/C/D/E/F/G/H/I/J/K/L 388-715 [» ]
1OYN X-ray 2.00 A/B/C/D 381-740 [» ]
1PTW X-ray 2.30 A/B/C/D 381-740 [» ]
1Q9M X-ray 2.30 A/B/C/D 381-740 [» ]
1TB7 X-ray 1.63 A/B 388-715 [» ]
1TBB X-ray 1.60 A/B 388-715 [» ]
1XOM X-ray 1.55 A/B 388-715 [» ]
1XON X-ray 1.72 A/B 388-715 [» ]
1XOQ X-ray 1.83 A/B 388-715 [» ]
1XOR X-ray 1.54 A/B 388-715 [» ]
1Y2B X-ray 1.40 A/B 388-715 [» ]
1Y2C X-ray 1.67 A/B 388-715 [» ]
1Y2D X-ray 1.70 A/B 388-715 [» ]
1Y2E X-ray 2.10 A/B 388-715 [» ]
1Y2K X-ray 1.36 A/B 388-715 [» ]
1ZKN X-ray 2.10 A/B/C/D 381-714 [» ]
2FM0 X-ray 2.00 A/B/C/D 381-741 [» ]
2FM5 X-ray 2.03 A/B/C/D 381-741 [» ]
2PW3 X-ray 1.56 A/B 388-714 [» ]
2QYN X-ray 1.57 A/B 388-715 [» ]
3G4G X-ray 2.30 A/B/C/D 299-347 [» ]
A/B/C/D 360-714 [» ]
3G4I X-ray 1.90 A/B/C/D 380-753 [» ]
3G4K X-ray 1.95 A/B/C/D 380-753 [» ]
3G4L X-ray 2.50 A/B/C/D 380-753 [» ]
3G58 X-ray 2.05 A/B/C/D 380-753 [» ]
3IAD X-ray 2.65 A/B/C/D 326-339 [» ]
A/B/C/D 380-714 [» ]
3IAK X-ray 2.80 A 388-715 [» ]
3K4S X-ray 2.05 A 388-715 [» ]
3SL3 X-ray 2.10 A/B/C/D 381-741 [» ]
3SL4 X-ray 1.90 A/B/C/D 381-741 [» ]
3SL5 X-ray 2.65 A/B/C/D 381-714 [» ]
3SL6 X-ray 2.44 A/B/C/D 381-741 [» ]
3SL8 X-ray 2.60 A/B/C/D 381-741 [» ]
3V9B X-ray 2.10 A/B/C/D 381-740 [» ]
ProteinModelPortali Q08499.
SMRi Q08499. Positions 327-739.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111170. 32 interactions.
DIPi DIP-29709N.
DIP-41115N.
IntActi Q08499. 10 interactions.
MINTi MINT-92262.

Chemistry

BindingDBi Q08499.
ChEMBLi CHEMBL2111340.
DrugBanki DB00131. Adenosine monophosphate.
DB00651. Dyphylline.
GuidetoPHARMACOLOGYi 1303.

PTM databases

PhosphoSitei Q08499.

Polymorphism databases

DMDMi 12644392.

Proteomic databases

MaxQBi Q08499.
PaxDbi Q08499.
PRIDEi Q08499.

Protocols and materials databases

DNASUi 5144.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309641 ; ENSP00000308485 ; ENSG00000113448 . [Q08499-7 ]
ENST00000317118 ; ENSP00000321739 ; ENSG00000113448 . [Q08499-8 ]
ENST00000340635 ; ENSP00000345502 ; ENSG00000113448 . [Q08499-1 ]
ENST00000358923 ; ENSP00000351800 ; ENSG00000113448 . [Q08499-5 ]
ENST00000360047 ; ENSP00000353152 ; ENSG00000113448 .
ENST00000405755 ; ENSP00000384806 ; ENSG00000113448 . [Q08499-9 ]
ENST00000502484 ; ENSP00000423094 ; ENSG00000113448 . [Q08499-11 ]
ENST00000502575 ; ENSP00000425917 ; ENSG00000113448 . [Q08499-12 ]
ENST00000503258 ; ENSP00000425605 ; ENSG00000113448 . [Q08499-10 ]
ENST00000507116 ; ENSP00000424852 ; ENSG00000113448 . [Q08499-6 ]
ENST00000546160 ; ENSP00000442734 ; ENSG00000113448 . [Q08499-11 ]
GeneIDi 5144.
KEGGi hsa:5144.
UCSCi uc003jrs.2. human. [Q08499-8 ]
uc003jrt.2. human. [Q08499-1 ]
uc003jru.3. human. [Q08499-4 ]
uc003jrv.2. human. [Q08499-10 ]
uc003jrw.2. human. [Q08499-9 ]
uc003jrz.3. human. [Q08499-6 ]
uc003jsb.3. human. [Q08499-11 ]
uc003jsc.3. human. [Q08499-12 ]

Organism-specific databases

CTDi 5144.
GeneCardsi GC05M058302.
HGNCi HGNC:8783. PDE4D.
HPAi HPA045895.
MIMi 600129. gene.
614613. phenotype.
neXtProti NX_Q08499.
Orphaneti 950. Acrodysostosis.
280651. Acrodysostosis with multiple hormone resistance.
PharmGKBi PA33130.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG122287.
HOVERGENi HBG108239.
InParanoidi Q08499.
KOi K01120.
OMAi YENSSAD.
OrthoDBi EOG7HQNBC.
PhylomeDBi Q08499.
TreeFami TF314638.

Enzyme and pathway databases

UniPathwayi UPA00762 ; UER00747 .
BRENDAi 3.1.4.53. 2681.
Reactomei REACT_15334. DARPP-32 events.
REACT_19327. G alpha (s) signalling events.
SignaLinki Q08499.

Miscellaneous databases

ChiTaRSi PDE4D. human.
EvolutionaryTracei Q08499.
GeneWikii PDE4D.
GenomeRNAii 5144.
NextBioi 19846.
PROi Q08499.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q08499.
Bgeei Q08499.
Genevestigatori Q08499.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
InterProi IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 3 AND 4).
  2. "Identification of cyclic AMP-phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells."
    Nemoz G., Zhang R.B., Sette C., Conti M.
    FEBS Lett. 384:97-102(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4).
  3. "Isolation of a cDNA encoding a human rolipram-sensitive cyclic AMP phosphodiesterase (PDE IVD)."
    Baecker P.A., Obernolte R., Bach C., Yee C., Shelton E.R.
    Gene 138:253-256(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
    Tissue: Heart.
  4. "Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene."
    Bolger G.B., Erdogan S., Jones R.E., Loughney K., Scotland G., Hoffmann R., Wilkinson I., Farrell C., Houslay M.D.
    Biochem. J. 328:539-548(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 10), SEQUENCE REVISION (ISOFORM 1).
  5. "Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-alpha1."
    Miro X., Casacuberta J.M., Gutierrez-Lopez M.D., Landazuri M.O., Puigdomenech P.
    Biochem. Biophys. Res. Commun. 274:415-421(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N3), ALTERNATIVE SPLICING.
    Tissue: Umbilical vein endothelial cell.
  6. "Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7."
    Wang D., Deng C., Bugaj-Gaweda B., Kwan M., Gunwaldsen C., Leonard C., Xin X., Hu Y., Unterbeck A., De Vivo M.
    Cell. Signal. 15:883-891(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 7; 8 AND 9), PHOSPHORYLATION, TISSUE SPECIFICITY.
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7 AND 9), INVOLVEMENT IN SUSCEPTIBILITY TO STROKE.
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12).
  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] (ISOFORMS 6 AND 12).
    Tissue: Brain and Testis.
  10. "Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5."
    Bolger G.B., McCahill A., Yarwood S.J., Steele M.S., Warwicker J., Houslay M.D.
    BMC Biochem. 3:24-24(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GNB2L1.
  11. "The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins."
    Bolger G.B., McCahill A., Huston E., Cheung Y.F., McSorley T., Baillie G.S., Houslay M.D.
    J. Biol. Chem. 278:49230-49238(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2, SUBCELLULAR LOCATION.
  12. "The oligomerization state determines regulatory properties and inhibitor sensitivity of type 4 cAMP-specific phosphodiesterases."
    Richter W., Conti M.
    J. Biol. Chem. 279:30338-30348(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION OF LONG ISOFORMS, ENZYME REGULATION BY ROLIPRAM AND PHOSPHATIDIC ACID, PHOSPHORYLATION AT SER-53 (ISOFORM 3).
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Many hypotheses but no replication for the association between PDE4D and stroke."
    Rosand J., Bayley N., Rost N., de Bakker P.I.W.
    Nat. Genet. 38:1091-1092(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF INVOLVEMENT IN STROKE.
  15. "Dynamic regulation of cystic fibrosis transmembrane conductance regulator by competitive interactions of molecular adaptors."
    Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M., Lee M.G.
    J. Biol. Chem. 282:10414-10422(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHANK2, TISSUE SPECIFICITY.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-63 (ISOFORMS 12; 5 AND N3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Selective SUMO modification of cAMP-specific phosphodiesterase-4D5 (PDE4D5) regulates the functional consequences of phosphorylation by PKA and ERK."
    Li X., Vadrevu S., Dunlop A., Day J., Advant N., Troeger J., Klussmann E., Jaffrey E., Hay R.T., Adams D.R., Houslay M.D., Baillie G.S.
    Biochem. J. 428:55-65(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-387 BY PIAS4.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299 AND SER-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Crystal structure of phosphodiesterase 4D and inhibitor complex."
    Lee M.E., Markowitz J., Lee J.-O., Lee H.
    FEBS Lett. 530:53-58(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 388-715 IN COMPLEX WITH THE INHIBITOR ZARDAVERINE AND DIVALENT METAL IONS, MUTAGENESIS OF ASP-527 AND ARG-563.
  22. "The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis."
    Huai Q., Colicelli J., Ke H.
    Biochemistry 42:13220-13226(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 381-739 IN COMPLEX WITH CAMP AND DIVALENT METAL IONS.
  23. "Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity."
    Huai Q., Wang H., Sun Y., Kim H.Y., Liu Y., Ke H.
    Structure 11:865-873(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 381-739 IN COMPLEX WITH INHIBITOR.
  24. "Crystal structures of phosphodiesterases 4 and 5 in complex with inhibitor 3-isobutyl-1-methylxanthine suggest a conformation determinant of inhibitor selectivity."
    Huai Q., Liu Y., Francis S.H., Corbin J.D., Ke H.
    J. Biol. Chem. 279:13095-13101(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 381-714 IN COMPLEX WITH METAL IONS AND INHIBITOR.
  25. "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 (2.0 ANGSTROMS) OF 380-756 IN COMPLEX WITH AMP; METAL IONS AND THE INHIBITOR ROLIPRAM.
  26. Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 388-715 IN COMPLEX WITH AMP; METAL IONS AND THE INHIBITOR ROLIPRAM, FUNCTION, COFACTOR.
  27. Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 388-715 IN COMPLEX WITH METAL IONS AND INHIBITORS, FUNCTION, COFACTOR.
  28. "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 (1.36 ANGSTROMS) OF 388-715 IN COMPLEX WITH METAL IONS AND INHIBITORS.
  29. "Enantiomer discrimination illustrated by the high resolution crystal structures of type 4 phosphodiesterase."
    Huai Q., Sun Y., Wang H., Macdonald D., Aspiotis R., Robinson H., Huang Z., Ke H.
    J. Med. Chem. 49:1867-1873(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 381-741 IN COMPLEX WITH METAL IONS AND INHIBITORS.
  30. "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 (1.57 ANGSTROMS) OF 388-715 IN COMPLEX WITH METAL IONS AND THE INHIBITOR NVP.
  31. "1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1."
    Smith K.J., Baillie G.S., Hyde E.I., Li X., Houslay T.M., McCahill A., Dunlop A.J., Bolger G.B., Klussmann E., Adams D.R., Houslay M.D.
    Cell. Signal. 19:2612-2624(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF N-TERMINUS OF ISOFORM 5/N3/12, INTERACTION WITH GNB2L1.
  32. "The molecular basis for different recognition of substrates by phosphodiesterase families 4 and 10."
    Wang H., Robinson H., Ke H.
    J. Mol. Biol. 371:302-307(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 388-714 OF MUTANT ASN-503 IN COMPLEX WITH CAMP AND METAL IONS.
  33. Cited for: VARIANTS ACRDYS2 ALA-190; THR-225; SER-226 AND PRO-587.
  34. Cited for: VARIANTS ACRDYS2 GLU-228; ALA-590 AND ASP-673.
  35. Cited for: VARIANTS ACRDYS2 SER-227 AND ALA-590.
  36. Cited for: VARIANTS ACRDYS2 THR-225; THR-301; VAL-304; ALA-329 AND THR-678.

Entry informationi

Entry nameiPDE4D_HUMAN
AccessioniPrimary (citable) accession number: Q08499
Secondary accession number(s): O43433
, Q13549, Q13550, Q13551, Q7Z2L8, Q8IV84, Q8IVA9, Q8IVD2, Q8IVD3, Q96HL4, Q9HCX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: September 3, 2014
This is version 159 of the entry and version 2 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 5
    Human chromosome 5: 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

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