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Protein

cGMP-dependent 3',5'-cyclic phosphodiesterase

Gene

PDE2A

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

Functioni

Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes.
Isoform PDE2A2: Regulates Mitochondrial cAMP Levels and Respiration.

Catalytic activityi

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.

Cofactori

a divalent metal cationBy similarityNote: 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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei431 – 4311cGMPBy similarity
Binding sitei446 – 4461cGMPBy similarity
Binding sitei499 – 4991cGMPBy similarity
Active sitei656 – 6561Proton donorBy similarity
Metal bindingi660 – 6601Divalent metal cation 1
Metal bindingi696 – 6961Divalent metal cation 1
Metal bindingi697 – 6971Divalent metal cation 1
Metal bindingi697 – 6971Divalent metal cation 2
Binding sitei697 – 6971Substrate
Metal bindingi808 – 8081Divalent metal cation 1
Binding sitei808 – 8081Substrate

GO - Molecular functioni

  • calcium channel activity Source: UniProtKB
  • cAMP binding Source: UniProtKB
  • cGMP binding Source: UniProtKB
  • cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  • cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  • drug binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: UniProtKB
  • TPR domain binding Source: UniProtKB

GO - Biological processi

  • blood coagulation Source: Reactome
  • calcium ion transmembrane transport Source: GOC
  • cAMP catabolic process Source: UniProtKB
  • cAMP-mediated signaling Source: UniProtKB
  • cellular response to cGMP Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
  • cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
  • cellular response to mechanical stimulus Source: UniProtKB
  • cellular response to transforming growth factor beta stimulus Source: UniProtKB
  • cGMP catabolic process Source: UniProtKB
  • cGMP-mediated signaling Source: UniProtKB
  • establishment of endothelial barrier Source: UniProtKB
  • metabolic process Source: UniProtKB
  • monocyte differentiation Source: UniProtKB
  • negative regulation of cAMP biosynthetic process Source: UniProtKB
  • negative regulation of protein import into nucleus, translocation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of vascular permeability Source: UniProtKB
  • positive regulation of inflammatory response Source: UniProtKB
  • positive regulation of vascular permeability Source: UniProtKB
  • protein targeting to mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.1.4.17. 2681.
ReactomeiREACT_19327. G alpha (s) signalling events.
REACT_23767. cGMP effects.

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-dependent 3',5'-cyclic phosphodiesterase (EC:3.1.4.17)
Alternative name(s):
Cyclic GMP-stimulated phosphodiesterase
Short name:
CGS-PDE
Short name:
cGSPDE
Gene namesi
Name:PDE2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8777. PDE2A.

Subcellular locationi

Isoform PDE2A3 :
Isoform PDE2A2 :
Isoform PDE2A1 :

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • membrane raft Source: Ensembl
  • mitochondrial matrix Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • presynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33125.

Chemistry

DrugBankiDB00201. Caffeine.
DB08811. Tofisopam.

Polymorphism and mutation databases

BioMutaiPDE2A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 941940cGMP-dependent 3',5'-cyclic phosphodiesterasePRO_0000198796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine2 Publications
Lipidationi5 – 51S-palmitoyl cysteine; in isoform PDE2A31 Publication
Lipidationi11 – 111S-palmitoyl cysteine; in isoform PDE2A31 Publication

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

MaxQBiO00408.
PaxDbiO00408.
PRIDEiO00408.

PTM databases

PhosphoSiteiO00408.

Expressioni

Tissue specificityi

Expressed in brain and to a lesser extent in heart, placenta, lung, skeletal muscle, kidney and pancreas.

Gene expression databases

BgeeiO00408.
CleanExiHS_PDE2A.
ExpressionAtlasiO00408. baseline and differential.
GenevisibleiO00408. HS.

Organism-specific databases

HPAiCAB009752.

Interactioni

Subunit structurei

Homodimer.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIPO001706EBI-1785967,EBI-704197

Protein-protein interaction databases

BioGridi111164. 3 interactions.
DIPiDIP-40269N.
IntActiO00408. 3 interactions.
STRINGi9606.ENSP00000334910.

Structurei

Secondary structure

1
941
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi226 – 23611Combined sources
Helixi242 – 25615Combined sources
Beta strandi262 – 2676Combined sources
Beta strandi271 – 2799Combined sources
Beta strandi282 – 29110Combined sources
Beta strandi294 – 2963Combined sources
Helixi297 – 3026Combined sources
Helixi308 – 3103Combined sources
Helixi313 – 32311Combined sources
Beta strandi330 – 3367Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi342 – 35514Combined sources
Helixi362 – 40342Combined sources
Turni410 – 4123Combined sources
Helixi413 – 42513Combined sources
Beta strandi427 – 4359Combined sources
Beta strandi437 – 4437Combined sources
Beta strandi446 – 4483Combined sources
Beta strandi456 – 4605Combined sources
Helixi464 – 4729Combined sources
Beta strandi476 – 4794Combined sources
Beta strandi502 – 5065Combined sources
Beta strandi510 – 5123Combined sources
Beta strandi516 – 52813Combined sources
Turni531 – 5344Combined sources
Helixi535 – 57036Combined sources
Turni571 – 5733Combined sources
Helixi580 – 5878Combined sources
Helixi593 – 5953Combined sources
Turni598 – 6014Combined sources
Helixi607 – 6093Combined sources
Helixi612 – 6143Combined sources
Helixi615 – 62511Combined sources
Helixi628 – 6314Combined sources
Helixi636 – 64813Combined sources
Beta strandi654 – 6574Combined sources
Helixi658 – 67518Combined sources
Helixi677 – 6793Combined sources
Helixi683 – 69513Combined sources
Turni696 – 6994Combined sources
Helixi705 – 7106Combined sources
Helixi714 – 7196Combined sources
Turni720 – 7223Combined sources
Helixi725 – 73814Combined sources
Turni741 – 7433Combined sources
Turni745 – 7484Combined sources
Helixi751 – 76616Combined sources
Helixi770 – 78617Combined sources
Helixi793 – 80816Combined sources
Helixi810 – 8134Combined sources
Helixi816 – 83924Combined sources
Helixi846 – 8483Combined sources
Turni850 – 8523Combined sources
Helixi855 – 86511Combined sources
Helixi867 – 87711Combined sources
Helixi879 – 8813Combined sources
Helixi882 – 89817Combined sources
Helixi899 – 9024Combined sources
Beta strandi904 – 9063Combined sources
Helixi914 – 9163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z1LX-ray1.70A578-919[»]
3IBJX-ray3.02A/B215-900[»]
3ITMX-ray2.49A/B/C/D579-919[»]
3ITUX-ray1.58A/B/C/D579-919[»]
4C1IX-ray2.40A/B/C/D578-921[»]
4D08X-ray1.90A/B/C/D578-921[»]
4D09X-ray2.50A/B/C/D578-921[»]
4HTXX-ray1.90A/B/C/D578-919[»]
4HTZX-ray2.00A/B/C/D578-919[»]
4JIBX-ray1.72A/B/C/D579-919[»]
ProteinModelPortaliO00408.
SMRiO00408. Positions 223-916.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00408.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini241 – 377137GAF 1Add
BLAST
Domaini409 – 548140GAF 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni633 – 891259CatalyticBy similarityAdd
BLAST
Regioni656 – 6605Substrate binding

Domaini

GAF 1 functions as a dimerization domain, whereas GAF 2 binds cGMP, which causes activation of the catalytic activity of the enzyme.By similarity

Sequence similaritiesi

Contains 2 GAF domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270709.
GeneTreeiENSGT00760000119066.
HOGENOMiHOG000007068.
HOVERGENiHBG053540.
KOiK18283.
OMAiRAPINGC.
OrthoDBiEOG767393.
PhylomeDBiO00408.
TreeFamiTF316499.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom-like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 3 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms.

Isoform PDE2A3 (identifier: O00408-1) [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
MGQACGHSIL CRSQQYPAAR PAEPRGQQVF LKPDEPPPPP QPCADSLQDA
60 70 80 90 100
LLSLGSVIDI SGLQRAVKEA LSAVLPRVET VYTYLLDGES QLVCEDPPHE
110 120 130 140 150
LPQEGKVREA IISQKRLGCN GLGFSDLPGK PLARLVAPLA PDTQVLVMPL
160 170 180 190 200
ADKEAGAVAA VILVHCGQLS DNEEWSLQAV EKHTLVALRR VQVLQQRGPR
210 220 230 240 250
EAPRAVQNPP EGTAEDQKGG AAYTDRDRKI LQLCGELYDL DASSLQLKVL
260 270 280 290 300
QYLQQETRAS RCCLLLVSED NLQLSCKVIG DKVLGEEVSF PLTGCLGQVV
310 320 330 340 350
EDKKSIQLKD LTSEDVQQLQ SMLGCELQAM LCVPVISRAT DQVVALACAF
360 370 380 390 400
NKLEGDLFTD EDEHVIQHCF HYTSTVLTST LAFQKEQKLK CECQALLQVA
410 420 430 440 450
KNLFTHLDDV SVLLQEIITE ARNLSNAEIC SVFLLDQNEL VAKVFDGGVV
460 470 480 490 500
DDESYEIRIP ADQGIAGHVA TTGQILNIPD AYAHPLFYRG VDDSTGFRTR
510 520 530 540 550
NILCFPIKNE NQEVIGVAEL VNKINGPWFS KFDEDLATAF SIYCGISIAH
560 570 580 590 600
SLLYKKVNEA QYRSHLANEM MMYHMKVSDD EYTKLLHDGI QPVAAIDSNF
610 620 630 640 650
ASFTYTPRSL PEDDTSMAIL SMLQDMNFIN NYKIDCPTLA RFCLMVKKGY
660 670 680 690 700
RDPPYHNWMH AFSVSHFCYL LYKNLELTNY LEDIEIFALF ISCMCHDLDH
710 720 730 740 750
RGTNNSFQVA SKSVLAALYS SEGSVMERHH FAQAIAILNT HGCNIFDHFS
760 770 780 790 800
RKDYQRMLDL MRDIILATDL AHHLRIFKDL QKMAEVGYDR NNKQHHRLLL
810 820 830 840 850
CLLMTSCDLS DQTKGWKTTR KIAELIYKEF FSQGDLEKAM GNRPMEMMDR
860 870 880 890 900
EKAYIPELQI SFMEHIAMPI YKLLQDLFPK AAELYERVAS NREHWTKVSH
910 920 930 940
KFTIRGLPSN NSLDFLDEEY EVPDLDGTRA PINGCCSLDA E
Length:941
Mass (Da):105,717
Last modified:July 1, 1997 - v1
Checksum:i9797609B487FD64E
GO
Isoform PDE2A1 (identifier: O00408-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQ → MRRQPAASLDPLAKEPGPPGSRDDRLE

Note: Soluble form.
Show »
Length:920
Mass (Da):103,478
Checksum:iCF77ED12741349C0
GO
Isoform PDE2A2 (identifier: O00408-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MGQACGHSILCRSQQYPAARPAEP → MVLVLHHILIAVVQFLR

Note: Contains a transit peptide at positions 1-17.
Show »
Length:934
Mass (Da):105,147
Checksum:i2C1E4885AD13F504
GO
Isoform PDE2A4 (identifier: O00408-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MGQACGHSILCRSQQYPAARPAEP → MKKQRIQEGKSLAHR

Show »
Length:932
Mass (Da):104,955
Checksum:i9F5CE92BA3C2E2E5
GO
Isoform 5 (identifier: O00408-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MGQACGHSILCRSQQYPAARPAEP → MVLVLHHILIAVVQFLR
     109-357: Missing.

Note: No experimental confirmation available.
Show »
Length:685
Mass (Da):78,177
Checksum:iA6087394B98221C3
GO
Isoform 6 (identifier: O00408-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQ → MRRQPAASLDPLAKEPGPPGSRDDRLE
     750-807: SRKDYQRMLD...LLLCLLMTSC → PLRTTTILMV...DPRTGRQAQV
     808-941: Missing.

Note: No experimental confirmation available.
Show »
Length:786
Mass (Da):87,235
Checksum:i33190E63C6351001
GO

Sequence cautioni

The sequence AAS75515.1 differs from that shown. Reason: Frameshift at position 48. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381P → L in AAS75513 (Ref. 2) Curated
Sequence conflicti99 – 991H → R in BAG35343 (PubMed:14702039).Curated
Sequence conflicti213 – 2131T → A in AAS75513 (Ref. 2) Curated
Sequence conflicti664 – 6641V → A in AAS75513 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241T → I.
Corresponds to variant rs341047 [ dbSNP | Ensembl ].
VAR_024170

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848MGQAC…ADSLQ → MRRQPAASLDPLAKEPGPPG SRDDRLE in isoform PDE2A1 and isoform 6. 2 PublicationsVSP_055315Add
BLAST
Alternative sequencei1 – 2424MGQAC…RPAEP → MVLVLHHILIAVVQFLR in isoform PDE2A2 and isoform 5. 2 PublicationsVSP_055316Add
BLAST
Alternative sequencei1 – 2424MGQAC…RPAEP → MKKQRIQEGKSLAHR in isoform PDE2A4. 1 PublicationVSP_055317Add
BLAST
Alternative sequencei109 – 357249Missing in isoform 5. 1 PublicationVSP_055318Add
BLAST
Alternative sequencei750 – 80758SRKDY…LMTSC → PLRTTTILMVGLGPGGYRGP RKKLPEGQLSALQRGALGRS RMGLMGRRDPRTGRQAQV in isoform 6. 1 PublicationVSP_055319Add
BLAST
Alternative sequencei808 – 941134Missing in isoform 6. 1 PublicationVSP_055320Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67733 mRNA. Translation: AAC51320.1.
AY495087 mRNA. Translation: AAS75513.1.
AY495088 mRNA. Translation: AAS75514.1.
AY495089 mRNA. Translation: AAS75515.1. Frameshift.
AK092278 mRNA. Translation: BAG52517.1.
AK131525 mRNA. Translation: BAD18664.1.
AK312434 mRNA. Translation: BAG35343.1.
AP003065 Genomic DNA. No translation available.
AP005019 Genomic DNA. No translation available.
CCDSiCCDS44670.1. [O00408-3]
CCDS53678.1. [O00408-4]
CCDS73345.1. [O00408-2]
CCDS8216.1. [O00408-1]
RefSeqiNP_001137311.1. NM_001143839.3. [O00408-3]
NP_001139681.1. NM_001146209.2. [O00408-4]
NP_001230713.1. NM_001243784.1. [O00408-2]
NP_002590.1. NM_002599.4. [O00408-1]
UniGeneiHs.503163.

Genome annotation databases

EnsembliENST00000334456; ENSP00000334910; ENSG00000186642.
ENST00000376450; ENSP00000365633; ENSG00000186642. [O00408-5]
ENST00000444035; ENSP00000411657; ENSG00000186642. [O00408-2]
ENST00000540345; ENSP00000446399; ENSG00000186642. [O00408-4]
ENST00000544570; ENSP00000442256; ENSG00000186642. [O00408-3]
GeneIDi5138.
KEGGihsa:5138.
UCSCiuc010rrb.2. human. [O00408-4]
uc010rrc.2. human. [O00408-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67733 mRNA. Translation: AAC51320.1.
AY495087 mRNA. Translation: AAS75513.1.
AY495088 mRNA. Translation: AAS75514.1.
AY495089 mRNA. Translation: AAS75515.1. Frameshift.
AK092278 mRNA. Translation: BAG52517.1.
AK131525 mRNA. Translation: BAD18664.1.
AK312434 mRNA. Translation: BAG35343.1.
AP003065 Genomic DNA. No translation available.
AP005019 Genomic DNA. No translation available.
CCDSiCCDS44670.1. [O00408-3]
CCDS53678.1. [O00408-4]
CCDS73345.1. [O00408-2]
CCDS8216.1. [O00408-1]
RefSeqiNP_001137311.1. NM_001143839.3. [O00408-3]
NP_001139681.1. NM_001146209.2. [O00408-4]
NP_001230713.1. NM_001243784.1. [O00408-2]
NP_002590.1. NM_002599.4. [O00408-1]
UniGeneiHs.503163.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z1LX-ray1.70A578-919[»]
3IBJX-ray3.02A/B215-900[»]
3ITMX-ray2.49A/B/C/D579-919[»]
3ITUX-ray1.58A/B/C/D579-919[»]
4C1IX-ray2.40A/B/C/D578-921[»]
4D08X-ray1.90A/B/C/D578-921[»]
4D09X-ray2.50A/B/C/D578-921[»]
4HTXX-ray1.90A/B/C/D578-919[»]
4HTZX-ray2.00A/B/C/D578-919[»]
4JIBX-ray1.72A/B/C/D579-919[»]
ProteinModelPortaliO00408.
SMRiO00408. Positions 223-916.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111164. 3 interactions.
DIPiDIP-40269N.
IntActiO00408. 3 interactions.
STRINGi9606.ENSP00000334910.

Chemistry

BindingDBiO00408.
ChEMBLiCHEMBL2652.
DrugBankiDB00201. Caffeine.
DB08811. Tofisopam.
GuidetoPHARMACOLOGYi1297.

PTM databases

PhosphoSiteiO00408.

Polymorphism and mutation databases

BioMutaiPDE2A.

Proteomic databases

MaxQBiO00408.
PaxDbiO00408.
PRIDEiO00408.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334456; ENSP00000334910; ENSG00000186642.
ENST00000376450; ENSP00000365633; ENSG00000186642. [O00408-5]
ENST00000444035; ENSP00000411657; ENSG00000186642. [O00408-2]
ENST00000540345; ENSP00000446399; ENSG00000186642. [O00408-4]
ENST00000544570; ENSP00000442256; ENSG00000186642. [O00408-3]
GeneIDi5138.
KEGGihsa:5138.
UCSCiuc010rrb.2. human. [O00408-4]
uc010rrc.2. human. [O00408-1]

Organism-specific databases

CTDi5138.
GeneCardsiGC11M072287.
HGNCiHGNC:8777. PDE2A.
HPAiCAB009752.
MIMi602658. gene.
neXtProtiNX_O00408.
PharmGKBiPA33125.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG270709.
GeneTreeiENSGT00760000119066.
HOGENOMiHOG000007068.
HOVERGENiHBG053540.
KOiK18283.
OMAiRAPINGC.
OrthoDBiEOG767393.
PhylomeDBiO00408.
TreeFamiTF316499.

Enzyme and pathway databases

BRENDAi3.1.4.17. 2681.
ReactomeiREACT_19327. G alpha (s) signalling events.
REACT_23767. cGMP effects.

Miscellaneous databases

ChiTaRSiPDE2A. human.
EvolutionaryTraceiO00408.
GeneWikiiPDE2A.
GenomeRNAii5138.
NextBioi19812.
PROiO00408.
SOURCEiSearch...

Gene expression databases

BgeeiO00408.
CleanExiHS_PDE2A.
ExpressionAtlasiO00408. baseline and differential.
GenevisibleiO00408. HS.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom-like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 3 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]
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Publicationsi

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  1. "Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase."
    Rosman G.J., Martins T.J., Sonnenburg W.K., Beavo J.A., Ferguson K., Loughney K.
    Gene 191:89-95(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A3).
    Tissue: Fetal brain and Hippocampus.
  2. "Human PDE2A1, PDE2A2 and PDE2A4."
    Bugaj-Gaweda B., De Vivo M., Wang D.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A4), NUCLEOTIDE SEQUENCE [MRNA] OF 1-27 (ISOFORM PDE2A1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-55 (ISOFORM PDE2A2).
  3. "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 PDE2A3; 5 AND 6).
    Tissue: Adrenal gland, Brain and Tongue.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Dual acylation of PDE2A splice variant 3: targeting to synaptic membranes."
    Russwurm C., Zoidl G., Koesling D., Russwurm M.
    J. Biol. Chem. 284:25782-25790(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-5 AND CYS-11, SUBCELLULAR LOCATION (ISOFORMS PDE2A1 AND PDE2A3).
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
    Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
    Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  8. Cited for: FUNCTION (ISOFORM PDE2A2), SUBCELLULAR LOCATION (ISOFORM PDE2A2).
  9. "Structural determinants for inhibitor specificity and selectivity in PDE2A using the wheat germ in vitro translation system."
    Iffland A., Kohls D., Low S., Luan J., Zhang Y., Kothe M., Cao Q., Kamath A.V., Ding Y.H., Ellenberger T.
    Biochemistry 44:8312-8325(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 578-919 IN COMPLEX WITH METAL IONS AND PHOSPHATE, FUNCTION.
  10. "Mechanism for the allosteric regulation of phosphodiesterase 2A deduced from the X-ray structure of a near full-length construct."
    Pandit J., Forman M.D., Fennell K.F., Dillman K.S., Menniti F.S.
    Proc. Natl. Acad. Sci. U.S.A. 106:18225-18230(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 215-919 IN COMPLEX WITH METAL IONS AND THE INHIBITOR IBMX, SUBUNIT, FUNCTION.
  11. "X-ray crystal structure of phosphodiesterase 2 in complex with a highly selective, nanomolar inhibitor reveals a binding-induced pocket important for selectivity."
    Zhu J., Yang Q., Dai D., Huang Q.
    J. Am. Chem. Soc. 135:11708-11711(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 578-919 IN COMPLEX WITH INHIBITOR.

Entry informationi

Entry nameiPDE2A_HUMAN
AccessioniPrimary (citable) accession number: O00408
Secondary accession number(s): B2R646
, B3KRV5, E9PGI1, F6W5Z0, Q5J791, Q5J792, Q5J793, Q6ZMR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: July 22, 2015
This is version 137 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

Miscellaneous

cGMP binds at an allosteric activator site.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.