Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O76074 (PDE5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

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

Names and origin

Protein namesRecommended name:
cGMP-specific 3',5'-cyclic phosphodiesterase

EC=3.1.4.35
Alternative name(s):
cGMP-binding cGMP-specific phosphodiesterase
Short name=CGB-PDE
Gene names
Name:PDE5A
Synonyms:PDE5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length875 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP.

Catalytic activity

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.

Cofactor

Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.

Enzyme regulation

Sildenafil (Viagra) is a highly selective and potent inhibitor of PDE5A and is effective in the treatment of penile erectile dysfunction. Also inhibited by zaprinast.

Pathway

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

Tissue specificity

Expressed in aortic smooth muscle cells, heart, placenta, skeletal muscle and pancreas and, to a much lesser extent, in brain, liver and lung.

Domain

Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain which contains two homologous allosteric cGMP-binding regions, A and B.

Post-translational modification

Phosphorylation is regulated by binding of cGMP to the two allosteric sites By similarity. Phosphorylation by PRKG1 leads to its activation.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandcGMP
cGMP-binding
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cGMP catabolic process

Inferred from direct assay PubMed 14687666. Source: UniProtKB

negative regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cardiac muscle hypertrophy

Inferred from electronic annotation. Source: Ensembl

positive regulation of oocyte development

Inferred from electronic annotation. Source: Ensembl

relaxation of cardiac muscle

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_function3',5'-cyclic-GMP phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3',5'-cyclic-nucleotide phosphodiesterase activity

Non-traceable author statement Ref.1. Source: UniProtKB

cGMP binding

Traceable author statement PubMed 15938621. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform PDE5A1 (identifier: O76074-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform PDE5A2 (identifier: O76074-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKA → MLPFGDK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 875875cGMP-specific 3',5'-cyclic phosphodiesterase
PRO_0000198823

Regions

Domain164 – 314151GAF 1
Domain346 – 503158GAF 2
Region588 – 853266Catalytic By similarity
Compositional bias10 – 2415Poly-Gln

Sites

Active site6131Proton donor By similarity
Metal binding6171Divalent metal cation 1
Metal binding6531Divalent metal cation 1
Metal binding6541Divalent metal cation 1
Metal binding6541Divalent metal cation 2
Metal binding7641Divalent metal cation 1
Binding site8171cGMP

Amino acid modifications

Modified residue1021Phosphoserine Potential

Natural variations

Alternative sequence1 – 4949MERAG…FVRKA → MLPFGDK in isoform PDE5A2.
VSP_004591
Natural variant931A → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs3733526 [ dbSNP | Ensembl ].
VAR_027775
Natural variant1811S → A.
Corresponds to variant rs17051276 [ dbSNP | Ensembl ].
VAR_027776

Experimental info

Sequence conflict1591I → V in AAP31235. Ref.9
Sequence conflict3101C → G in AAP31235. Ref.9
Sequence conflict3811S → F in AAP31235. Ref.9
Sequence conflict4061K → R in AAP31235. Ref.9
Sequence conflict6421E → G in BAA81667. Ref.4

Secondary structure

..................................................................................................................... 875
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PDE5A1 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 9E30C6C182F13388

FASTA87599,985
        10         20         30         40         50         60 
MERAGPSFGQ QRQQQQPQQQ KQQQRDQDSV EAWLDDHWDF TFSYFVRKAT REMVNAWFAE 

        70         80         90        100        110        120 
RVHTIPVCKE GIRGHTESCS CPLQQSPRAD NSAPGTPTRK ISASEFDRPL RPIVVKDSEG 

       130        140        150        160        170        180 
TVSFLSDSEK KEQMPLTPPR FDHDEGDQCS RLLELVKDIS SHLDVTALCH KIFLHIHGLI 

       190        200        210        220        230        240 
SADRYSLFLV CEDSSNDKFL ISRLFDVAEG STLEEVSNNC IRLEWNKGIV GHVAALGEPL 

       250        260        270        280        290        300 
NIKDAYEDPR FNAEVDQITG YKTQSILCMP IKNHREEVVG VAQAINKKSG NGGTFTEKDE 

       310        320        330        340        350        360 
KDFAAYLAFC GIVLHNAQLY ETSLLENKRN QVLLDLASLI FEEQQSLEVI LKKIAATIIS 

       370        380        390        400        410        420 
FMQVQKCTIF IVDEDCSDSF SSVFHMECEE LEKSSDTLTR EHDANKINYM YAQYVKNTME 

       430        440        450        460        470        480 
PLNIPDVSKD KRFPWTTENT GNVNQQCIRS LLCTPIKNGK KNKVIGVCQL VNKMEENTGK 

       490        500        510        520        530        540 
VKPFNRNDEQ FLEAFVIFCG LGIQNTQMYE AVERAMAKQM VTLEVLSYHA SAAEEETREL 

       550        560        570        580        590        600 
QSLAAAVVPS AQTLKITDFS FSDFELSDLE TALCTIRMFT DLNLVQNFQM KHEVLCRWIL 

       610        620        630        640        650        660 
SVKKNYRKNV AYHNWRHAFN TAQCMFAALK AGKIQNKLTD LEILALLIAA LSHDLDHRGV 

       670        680        690        700        710        720 
NNSYIQRSEH PLAQLYCHSI MEHHHFDQCL MILNSPGNQI LSGLSIEEYK TTLKIIKQAI 

       730        740        750        760        770        780 
LATDLALYIK RRGEFFELIR KNQFNLEDPH QKELFLAMLM TACDLSAITK PWPIQQRIAE 

       790        800        810        820        830        840 
LVATEFFDQG DRERKELNIE PTDLMNREKK NKIPSMQVGF IDAICLQLYE ALTHVSEDCF 

       850        860        870 
PLLDGCRKNR QKWQALAEQQ EKMLINGESG QAKRN 

« Hide

Isoform PDE5A2 [UniParc].

Checksum: 41D0B4B1BAB57D6D
Show »

FASTA83394,805

References

« Hide 'large scale' references
[1]"Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase."
Loughney K., Hill T.R., Florio V.A., Uher L., Rosman G.J., Wolda S.L., Jones B.A., Howard M.L., McAllister-Lucas L.M., Sonnenburg W.K., Francis S.H., Corbin J.D., Beavo J.A., Ferguson K.
Gene 216:139-147(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE5A1 AND PDE5A2), VARIANT VAL-93.
[2]"Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene."
Yanaka N., Kotera J., Ohtsuka A., Akatsuka H., Imai Y., Michibata H., Fujishige K., Kawai E., Takebayashi S., Okumura K., Omori K.
Eur. J. Biochem. 255:391-399(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM PDE5A1), VARIANT VAL-93.
Tissue: Lung and Placenta.
[3]"Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase."
Stacey P., Rulten S., Dapling A., Phillips S.C.
Biochem. Biophys. Res. Commun. 247:249-254(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A1), VARIANT VAL-93.
Tissue: Prostate and Skeletal muscle.
[4]"Molecular cloning and characterization of human cGMP-specific phosphodiesterase 5A2 cDNA."
Kotera J., Imai Y., Omori K.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A2), VARIANT VAL-93.
Tissue: Lung.
[5]"PDE5A splice variants in T84 cells."
Sopory S., Visweswariah S.S.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A2).
Tissue: Colon carcinoma.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE5A1), VARIANT VAL-93.
Tissue: Thalamus.
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 PDE5A1).
[9]"Multiple cyclic nucleotide phosphodiesterases in human trabecular meshwork cells."
Zhou L., Thompson W.J., Potter D.E.
Invest. Ophthalmol. Vis. Sci. 40:1745-1752(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-411.
Tissue: Trabecular meshwork.
[10]"Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation in smooth muscle cells."
Rybalkin S.D., Rybalkina I.G., Feil R., Hofmann F., Beavo J.A.
J. Biol. Chem. 277:3310-3317(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PRKG1.
[11]"Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules."
Sung B.-J., Hwang K.Y., Jeon Y.H., Lee J.I., Heo Y.-S., Kim J.H., Moon J., Yoon J.M., Hyun Y.-L., Kim E., Eum S.J., Park S.-Y., Lee J.-O., Lee T.G., Ro S., Cho J.M.
Nature 425:98-102(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 537-860 IN COMPLEX WITH THE INHIBITORS SILDENAFIL; TADALAFIL AND VARDENAFIL, METAL-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF043731 mRNA. Translation: AAC63967.1.
AF043732 mRNA. Translation: AAC63968.1.
AB001635 Genomic DNA. Translation: BAA33372.2.
D89094 mRNA. Translation: BAA28945.1.
AJ004865 mRNA. Translation: CAA06170.1.
AB015656 mRNA. Translation: BAA81667.1.
AY264918 mRNA. Translation: AAP21809.1.
AK290189 mRNA. Translation: BAF82878.1.
AC093752 Genomic DNA. No translation available.
AC080089 Genomic DNA. No translation available.
BC126233 mRNA. Translation: AAI26234.1.
AY266363 mRNA. Translation: AAP31235.1.
CCDSCCDS34055.1. [O76074-2]
CCDS3713.1. [O76074-1]
PIRJW0106.
RefSeqNP_001074.2. NM_001083.3. [O76074-1]
NP_236914.2. NM_033430.2. [O76074-2]
NP_246273.2. NM_033437.3.
UniGeneHs.647971.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RKPX-ray2.05A535-860[»]
1T9RX-ray2.10A531-875[»]
1T9SX-ray2.00A/B534-858[»]
1TBFX-ray1.30A534-858[»]
1UDTX-ray2.30A537-860[»]
1UDUX-ray2.83A/B537-860[»]
1UHOX-ray2.50A537-860[»]
1XOZX-ray1.37A534-875[»]
1XP0X-ray1.79A534-875[»]
2CHMX-ray1.60A534-656[»]
A682-858[»]
2H40X-ray1.85A535-860[»]
2H42X-ray2.30A/B/C535-860[»]
2H44X-ray1.80A535-860[»]
2XSSX-ray2.50A/B346-509[»]
3B2RX-ray2.07A/B535-860[»]
3BJCX-ray2.00A1-875[»]
3HC8X-ray1.79A536-858[»]
3HDZX-ray1.80A536-657[»]
A682-858[»]
3JWQX-ray2.87A/B/C/D535-786[»]
A/B/C/D827-860[»]
3JWRX-ray2.99A/B535-786[»]
A/B706-860[»]
3LFVX-ray2.80A/B98-518[»]
3MF0X-ray3.10A/B89-518[»]
3SHYX-ray2.65A535-860[»]
3SHZX-ray2.45A535-860[»]
3SIEX-ray1.93A/B535-860[»]
3TGEX-ray1.96A534-656[»]
A682-858[»]
3TGGX-ray1.91A534-858[»]
3TSEX-ray2.14A535-860[»]
3TSFX-ray2.44A535-860[»]
4G2WX-ray2.28A535-860[»]
4G2YX-ray2.40A535-860[»]
4I9ZX-ray2.08A535-860[»]
4IA0X-ray2.17A535-860[»]
ProteinModelPortalO76074.
SMRO76074. Positions 98-860.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114205. 1 interaction.
DIPDIP-46287N.
STRING9606.ENSP00000347046.

Chemistry

BindingDBO76074.
ChEMBLCHEMBL2111340.
DrugBankDB00975. Dipyridamole.
DB00806. Pentoxifylline.
DB00203. Sildenafil.
DB00820. Tadalafil.
DB00277. Theophylline.
DB00862. Vardenafil.
GuidetoPHARMACOLOGY1304.

PTM databases

PhosphoSiteO76074.

Proteomic databases

MaxQBO76074.
PaxDbO76074.
PRIDEO76074.

Protocols and materials databases

DNASU8654.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264805; ENSP00000264805; ENSG00000138735. [O76074-2]
ENST00000354960; ENSP00000347046; ENSG00000138735. [O76074-1]
GeneID8654.
KEGGhsa:8654.
UCSCuc003idf.3. human. [O76074-2]
uc003idg.3. human. [O76074-1]

Organism-specific databases

CTD8654.
GeneCardsGC04M120415.
HGNCHGNC:8784. PDE5A.
HPAHPA004729.
HPA012873.
MIM603310. gene.
neXtProtNX_O76074.
PharmGKBPA33132.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270709.
HOVERGENHBG101207.
InParanoidO76074.
KOK13762.
OMAREHDANK.
OrthoDBEOG7RRF69.
PhylomeDBO76074.
TreeFamTF316499.

Enzyme and pathway databases

BRENDA3.1.4.35. 2681.
ReactomeREACT_604. Hemostasis.
UniPathwayUPA00763; UER00748.

Gene expression databases

ArrayExpressO76074.
BgeeO76074.
CleanExHS_PDE5A.
GenevestigatorO76074.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMSSF55781. SSF55781. 2 hits.
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDE5A. human.
EvolutionaryTraceO76074.
GeneWikiCGMP-specific_phosphodiesterase_type_5.
GenomeRNAi8654.
NextBio32453.
PROO76074.
SOURCESearch...

Entry information

Entry namePDE5A_HUMAN
AccessionPrimary (citable) accession number: O76074
Secondary accession number(s): A0AV69 expand/collapse secondary AC list , A8K2C4, O75026, O75887, Q86UI0, Q86V66, Q9Y6Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM