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O76083 (PDE9A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A

EC=3.1.4.35
Gene names
Name:PDE9A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Ref.12

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. Ref.12

Enzyme regulation

Inhibited by zaprinast.

Subcellular location

Isoform PDE9A1: Cell projectionruffle membrane. Cytoplasmperinuclear region Ref.5. Golgi apparatus. Endoplasmic reticulum Ref.5.

Isoform PDE9A2: Cell projectionruffle membrane. Cytoplasmperinuclear region Ref.5.

Isoform PDE9A3: Cytoplasm. Endoplasmic reticulum Ref.5.

Isoform PDE9A17: Cytoplasm. Endoplasmic reticulum Ref.5.

Tissue specificity

Expressed in all tissues examined (testis, brain, small intestine, skeletal muscle, heart, lung, thymus, spleen, placenta, kidney, liver, pancreas, ovary and prostate) except blood. Highest levels in brain, heart, kidney, spleen, prostate and colon. Isoform PDE9A12 is found in prostate. Ref.3

Domain

Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE9 subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRIM32Q130493EBI-742764,EBI-742790

Alternative products

This entry describes 16 isoforms produced by alternative splicing. [Align] [Select]
Isoform PDE9A1 (identifier: O76083-1)

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 PDE9A2 (identifier: O76083-2)

The sequence of this isoform differs from the canonical sequence as follows:
     88-147: Missing.
Isoform PDE9A3 (identifier: O76083-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MGSGSSSYRP...DPTMPANSER → MDAFRS
     88-147: Missing.
Isoform PDE9A4 (identifier: O76083-4)

The sequence of this isoform differs from the canonical sequence as follows:
     24-165: VIFSKYCNSS...VLAQVAEQFS → HSVQSETCGHQATL
Isoform PDE9A5 (identifier: O76083-5)

The sequence of this isoform differs from the canonical sequence as follows:
     74-165: TPYKVRPVAI...VLAQVAEQFS → NELILYTSLR...SETCGHQATL
Isoform PDE9A6 (identifier: O76083-6)

Also known as: PDE9A5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR
     88-147: Missing.
Isoform PDE9A7 (identifier: O76083-7)

Also known as: PDE9A8; PDE9A14; PDE9A19; PDE9A20;

The sequence of this isoform differs from the canonical sequence as follows:
     1-207: Missing.
Isoform PDE9A9 (identifier: O76083-8)

The sequence of this isoform differs from the canonical sequence as follows:
     48-73: Missing.
     88-147: Missing.
Isoform PDE9A10 (identifier: O76083-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     161-165: AEQFS → MDAFR
Isoform PDE9A11 (identifier: O76083-10)

Also known as: PDE9A15;

The sequence of this isoform differs from the canonical sequence as follows:
     1-217: Missing.
     218-218: R → M
Isoform PDE9A12 (identifier: O76083-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR
     73-165: Missing.
Isoform PDE9A13 (identifier: O76083-12)

The sequence of this isoform differs from the canonical sequence as follows:
     24-165: VIFSKYCNSS...VLAQVAEQFS → EHDHLPADHR...SETCGHQATL
Isoform PDE9A16 (identifier: O76083-13)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MGSGSSSYRP...DPTMPANSER → MDAFRS
Isoform PDE9A17 (identifier: O76083-14)

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR
Isoform PDE9A18 (identifier: O76083-15)

The sequence of this isoform differs from the canonical sequence as follows:
     48-73: Missing.
Isoform PDE9A21 (identifier: O76083-16)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MGSGSSSYRP...DPTMPANSER → MSSFSIHHSVTCCFYLVRSHGRPTS
     88-147: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
PRO_0000198841

Regions

Nucleotide binding312 – 3165cGMP
Nucleotide binding512 – 5132cGMP
Region288 – 550263Catalytic By similarity

Sites

Active site3121Proton donor
Metal binding3161Divalent metal cation 1
Metal binding3521Divalent metal cation 1
Metal binding3531Divalent metal cation 1
Metal binding3531Divalent metal cation 2
Metal binding4621Divalent metal cation 1
Binding site3531cGMP
Binding site4621cGMP
Binding site4841cGMP

Natural variations

Alternative sequence1 – 217217Missing in isoform PDE9A11.
VSP_017302
Alternative sequence1 – 207207Missing in isoform PDE9A7.
VSP_017303
Alternative sequence1 – 160160Missing in isoform PDE9A10.
VSP_017304
Alternative sequence1 – 7373MGSGS…ANSER → MSSFSIHHSVTCCFYLVRSH GRPTS in isoform PDE9A21.
VSP_038647
Alternative sequence1 – 7373MGSGS…ANSER → MDAFRS in isoform PDE9A3 and isoform PDE9A16.
VSP_004598
Alternative sequence1 – 4646MGSGS…ATGLP → MDAFR in isoform PDE9A6, isoform PDE9A12 and isoform PDE9A17.
VSP_017305
Alternative sequence24 – 165142VIFSK…AEQFS → EHDHLPADHRRRHGLHRPHH AREFRTHSVQSETCGHQATL in isoform PDE9A13.
VSP_017306
Alternative sequence24 – 165142VIFSK…AEQFS → HSVQSETCGHQATL in isoform PDE9A4.
VSP_004600
Alternative sequence48 – 7326Missing in isoform PDE9A9 and isoform PDE9A18.
VSP_017307
Alternative sequence73 – 16593Missing in isoform PDE9A12.
VSP_017308
Alternative sequence74 – 16592TPYKV…AEQFS → NELILYTSLRNLLFLPSKES WASHQHSVQSETCGHQATL in isoform PDE9A5.
VSP_017309
Alternative sequence88 – 14760Missing in isoform PDE9A2, isoform PDE9A3, isoform PDE9A6, isoform PDE9A9 and isoform PDE9A21.
VSP_004599
Alternative sequence161 – 1655AEQFS → MDAFR in isoform PDE9A10.
VSP_017310
Alternative sequence2181R → M in isoform PDE9A11.
VSP_017311

Experimental info

Mutagenesis3121H → A: Completely abolishes catalytic activity. Ref.12
Mutagenesis3561H → A: Reduces catalytic activity, but has no effect on substrate affinity. Ref.12
Sequence conflict791R → G in BAG57446. Ref.6

Secondary structure

................................................... 593
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PDE9A1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: E2731C7C828C0994

FASTA59368,493
        10         20         30         40         50         60 
MGSGSSSYRP KAIYLDIDGR IQKVIFSKYC NSSDIMDLFC IATGLPRNTT ISLLTTDDAM 

        70         80         90        100        110        120 
VSIDPTMPAN SERTPYKVRP VAIKQLSAGV EDKRTTSRGQ SAERPLRDRR VVGLEQPRRE 

       130        140        150        160        170        180 
GAFESGQVEP RPREPQGCYQ EGQRIPPERE ELIQSVLAQV AEQFSRAFKI NELKAEVANH 

       190        200        210        220        230        240 
LAVLEKRVEL EGLKVVEIEK CKSDIKKMRE ELAARSSRTN CPCKYSFLDN HKKLTPRRDV 

       250        260        270        280        290        300 
PTYPKYLLSP ETIEALRKPT FDVWLWEPNE MLSCLEHMYH DLGLVRDFSI NPVTLRRWLF 

       310        320        330        340        350        360 
CVHDNYRNNP FHNFRHCFCV AQMMYSMVWL CSLQEKFSQT DILILMTAAI CHDLDHPGYN 

       370        380        390        400        410        420 
NTYQINARTE LAVRYNDISP LENHHCAVAF QILAEPECNI FSNIPPDGFK QIRQGMITLI 

       430        440        450        460        470        480 
LATDMARHAE IMDSFKEKME NFDYSNEEHM TLLKMILIKC CDISNEVRPM EVAEPWVDCL 

       490        500        510        520        530        540 
LEEYFMQSDR EKSEGLPVAP FMDRDKVTKA TAQIGFIKFV LIPMFETVTK LFPMVEEIML 

       550        560        570        580        590 
QPLWESRDRY EELKRIDDAM KELQKKTDSL TSGATEKSRE RSRDVKNSEG DCA 

« Hide

Isoform PDE9A2 [UniParc].

Checksum: 728ADAAACE0E4D29
Show »

FASTA53361,709
Isoform PDE9A3 [UniParc].

Checksum: DE087DD09AAF4794
Show »

FASTA46654,440
Isoform PDE9A4 [UniParc].

Checksum: BDD6A8F85E591A67
Show »

FASTA46554,096
Isoform PDE9A5 [UniParc].

Checksum: 612A2ECEE7F656B4
Show »

FASTA54062,491
Isoform PDE9A6 (PDE9A5) [UniParc].

Checksum: 1FE4F709AD50C0E6
Show »

FASTA49257,285
Isoform PDE9A7 (PDE9A8) (PDE9A14) (PDE9A19) (PDE9A20) [UniParc].

Checksum: 4120AB778B9746B9
Show »

FASTA38645,290
Isoform PDE9A9 [UniParc].

Checksum: E211E0EB8B67F284
Show »

FASTA50758,933
Isoform PDE9A10 [UniParc].

Checksum: D6036BB3CA9FB7B2
Show »

FASTA43350,713
Isoform PDE9A11 (PDE9A15) [UniParc].

Checksum: BF896546AED87831
Show »

FASTA37644,134
Isoform PDE9A12 [UniParc].

Checksum: E7DA06012931A850
Show »

FASTA45953,489
Isoform PDE9A13 [UniParc].

Checksum: CA53A1793F405CDB
Show »

FASTA49157,350
Isoform PDE9A16 [UniParc].

Checksum: 02A36AE5185CEDF3
Show »

FASTA52661,223
Isoform PDE9A17 [UniParc].

Checksum: F10D41FE319A6D28
Show »

FASTA55264,068
Isoform PDE9A18 [UniParc].

Checksum: 2DFEB16AFCA94F0D
Show »

FASTA56765,717
Isoform PDE9A21 [UniParc].

Checksum: 82275A46E46C4D83
Show »

FASTA48556,554

References

« Hide 'large scale' references
[1]"Isolation and characterization of PDE9A, a novel human cGMP-specific phosphodiesterase."
Fisher D.A., Smith J.F., Pillar J.S., St Denis S.H., Cheng J.B.
J. Biol. Chem. 273:15559-15564(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE9A1).
Tissue: Brain, Prostate and Testis.
[2]"Identification and characterization of a novel cyclic nucleotide phosphodiesterase gene (PDE9A) that maps to 21q22.3: alternative splicing of mRNA transcripts, genomic structure and sequence."
Guipponi M., Scott H.S., Kudoh J., Kawasaki K., Shibuya K., Shintani A., Asakawa S., Chen H., Lalioti M.D., Rossier C., Minoshima S., Shimizu N., Antonarakis S.E.
Hum. Genet. 103:386-392(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS PDE9A1; PDE9A2; PDE9A3 AND PDE9A4).
Tissue: Fetal brain.
[3]"Identification and distribution of different mRNA variants produced by differential splicing in the human phosphodiesterase 9A gene."
Rentero C., Monfort A., Puigdomenech P.
Biochem. Biophys. Res. Commun. 301:686-692(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE9A5; PDE9A6; PDE9A7; PDE9A9; PDE9A10; PDE9A11; PDE9A12; PDE9A13; PDE9A16; PDE9A17 AND PDE9A18), TISSUE SPECIFICITY.
[4]"Identification and characterization of a new human type 9 cGMP-specific phosphodiesterase splice variant (PDE9A5). Differential tissue distribution and subcellular localization of PDE9A variants."
Wang P., Wu P., Egan R.W., Billah M.M.
Gene 314:15-27(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE9A6).
Tissue: Brain, Small intestine and Spleen.
[5]"Specific use of start codons and cellular localization of splice variants of human phosphodiesterase 9A gene."
Rentero C., Puigdomenech P.
BMC Mol. Biol. 7:39-39(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE9A21), SUBCELLULAR LOCATION.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PDE9A1 AND PDE9A3).
[7]"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 PDE9A2).
[8]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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 PDE9A2).
Tissue: Eye.
[11]"Crystal structure of phosphodiesterase 9 shows orientation variation of inhibitor 3-isobutyl-1-methylxanthine binding."
Huai Q., Wang H., Zhang W., Colman R.W., Robinson H., Ke H.
Proc. Natl. Acad. Sci. U.S.A. 101:9624-9629(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 241-566 IN COMPLEX WITH THE INHIBITOR IBMX.
[12]"Structural basis for the catalytic mechanism of human phosphodiesterase 9."
Liu S., Mansour M.N., Dillman K.S., Perez J.R., Danley D.E., Aeed P.A., Simons S.P., Lemotte P.K., Menniti F.S.
Proc. Natl. Acad. Sci. U.S.A. 105:13309-13314(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 242-566 IN COMPLEX WITH MAGNESIUM; MANGANESE; ZINC; GMP AND CGMP, FUNCTION, COFACTOR, MUTAGENESIS OF HIS-312 AND HIS-356.
[13]"Crystal structure of the human phosphodiesterase 9a catalytic domain."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 241-566.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF048837 mRNA. Translation: AAC39778.1.
AB017602 Genomic DNA. Translation: BAA88847.1.
AF067223 mRNA. Translation: AAC26723.1.
AF067224 mRNA. Translation: AAC26724.1.
AF067225 mRNA. Translation: AAC26725.1.
AF067226 mRNA. Translation: AAC26726.1.
AY196299 mRNA. Translation: AAO34685.1.
AY196300 mRNA. Translation: AAO34686.1.
AY196301 mRNA. Translation: AAO34687.1.
AY196302 mRNA. Translation: AAO34688.1.
AY196303 mRNA. Translation: AAO34689.1.
AY196304 mRNA. Translation: AAO34690.1.
AY196305 mRNA. Translation: AAO34691.1.
AY196306 mRNA. Translation: AAO34692.1.
AY196307 mRNA. Translation: AAO34693.1.
AY196308 mRNA. Translation: AAO34694.1.
AY196309 mRNA. Translation: AAO34695.1.
AY196310 mRNA. Translation: AAO34696.1.
AY196311 mRNA. Translation: AAO34697.1.
AY196312 mRNA. Translation: AAO34698.1.
AY196313 mRNA. Translation: AAO34699.1.
AY196314 mRNA. Translation: AAO34700.1.
AY242121 mRNA. Translation: AAO88210.1.
AY701187 mRNA. Translation: AAV84271.1.
AK294112 mRNA. Translation: BAG57446.1.
AK314679 mRNA. Translation: BAG37232.1.
BT007016 mRNA. Translation: AAP35662.1.
AP001747 Genomic DNA. Translation: BAA95552.1.
CH471079 Genomic DNA. Translation: EAX09544.1.
CH471079 Genomic DNA. Translation: EAX09536.1.
CH471079 Genomic DNA. Translation: EAX09537.1.
CH471079 Genomic DNA. Translation: EAX09541.1.
CH471079 Genomic DNA. Translation: EAX09542.1.
CH471079 Genomic DNA. Translation: EAX09546.1.
CH471079 Genomic DNA. Translation: EAX09540.1.
CH471079 Genomic DNA. Translation: EAX09548.1.
CH471079 Genomic DNA. Translation: EAX09549.1.
BC009047 mRNA. Translation: AAH09047.1.
RefSeqNP_001001567.1. NM_001001567.1.
NP_001001568.1. NM_001001568.1.
NP_001001569.1. NM_001001569.1.
NP_001001570.1. NM_001001570.1.
NP_001001571.1. NM_001001571.1.
NP_001001572.1. NM_001001572.1.
NP_001001573.1. NM_001001573.1.
NP_001001574.1. NM_001001574.1.
NP_001001575.1. NM_001001575.1.
NP_001001576.1. NM_001001576.1.
NP_001001577.1. NM_001001577.1.
NP_001001578.1. NM_001001578.1.
NP_001001579.1. NM_001001579.1.
NP_001001580.1. NM_001001580.1.
NP_001001581.1. NM_001001581.1.
NP_001001582.1. NM_001001582.1.
NP_001001583.1. NM_001001583.1.
NP_001001584.1. NM_001001584.2.
NP_001001585.1. NM_001001585.1.
NP_002597.1. NM_002606.2.
UniGeneHs.473927.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HD1X-ray2.23A/B241-566[»]
2YY2X-ray2.80A/B241-566[»]
3DY8X-ray2.15A/B242-566[»]
3DYLX-ray2.70A/B242-566[»]
3DYNX-ray2.10A/B242-566[»]
3DYQX-ray2.50A/B242-566[»]
3DYSX-ray2.30A/B242-566[»]
3JSIX-ray2.72A/B242-566[»]
3JSWX-ray2.30A/B242-566[»]
3K3EX-ray2.70A/B241-566[»]
3K3HX-ray2.50A/B241-566[»]
3N3ZX-ray2.75A/B241-566[»]
3QI3X-ray2.30A/B1-593[»]
3QI4X-ray2.50A/B1-593[»]
4E90X-ray2.50A/B242-566[»]
4G2JX-ray2.40A/B242-566[»]
4G2LX-ray3.00A/B242-566[»]
4GH6X-ray2.70A/B241-566[»]
ProteinModelPortalO76083.
SMRO76083. Positions 242-565.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111178. 3 interactions.
IntActO76083. 2 interactions.
MINTMINT-1444906.

Chemistry

BindingDBO76083.
ChEMBLCHEMBL2363066.
GuidetoPHARMACOLOGY1309.

PTM databases

PhosphoSiteO76083.

Proteomic databases

PaxDbO76083.
PRIDEO76083.

Protocols and materials databases

DNASU5152.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291539; ENSP00000291539; ENSG00000160191. [O76083-1]
ENST00000328862; ENSP00000328699; ENSG00000160191. [O76083-15]
ENST00000335440; ENSP00000335365; ENSG00000160191. [O76083-12]
ENST00000335512; ENSP00000335242; ENSG00000160191. [O76083-2]
ENST00000349112; ENSP00000344730; ENSG00000160191. [O76083-4]
ENST00000380328; ENSP00000369685; ENSG00000160191. [O76083-5]
ENST00000398224; ENSP00000381280; ENSG00000160191. [O76083-3]
ENST00000398225; ENSP00000381281; ENSG00000160191. [O76083-14]
ENST00000398227; ENSP00000381283; ENSG00000160191. [O76083-9]
ENST00000398229; ENSP00000381285; ENSG00000160191. [O76083-11]
ENST00000398232; ENSP00000381287; ENSG00000160191. [O76083-13]
ENST00000398234; ENSP00000381289; ENSG00000160191. [O76083-6]
ENST00000398236; ENSP00000381291; ENSG00000160191. [O76083-8]
GeneID5152.
KEGGhsa:5152.
UCSCuc002zbm.3. human. [O76083-1]
uc002zbn.3. human. [O76083-3]
uc002zbo.3. human. [O76083-5]
uc002zbq.3. human. [O76083-12]
uc002zbt.3. human. [O76083-4]
uc002zbu.3. human. [O76083-11]
uc002zbv.3. human. [O76083-9]
uc002zbw.3. human. [O76083-10]
uc002zbx.3. human. [O76083-2]
uc002zbz.3. human. [O76083-16]
uc002zca.3. human. [O76083-14]
uc002zcb.3. human. [O76083-15]
uc002zcc.3. human. [O76083-6]
uc002zcd.3. human. [O76083-8]
uc002zce.3. human. [O76083-13]
uc010gpf.1. human. [O76083-7]

Organism-specific databases

CTD5152.
GeneCardsGC21P044073.
HGNCHGNC:8795. PDE9A.
HPAHPA011380.
MIM602973. gene.
neXtProtNX_O76083.
PharmGKBPA33143.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268427.
HOVERGENHBG053545.
InParanoidO76083.
KOK13761.
OMAPRAFKIN.
OrthoDBEOG7DFXC4.
PhylomeDBO76083.
TreeFamTF314638.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressO76083.
BgeeO76083.
GenevestigatorO76083.

Family and domain databases

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

Other

ChiTaRSPDE9A. human.
EvolutionaryTraceO76083.
GeneWikiPDE9A.
GenomeRNAi5152.
NextBio19884.
PROO76083.
SOURCESearch...

Entry information

Entry namePDE9A_HUMAN
AccessionPrimary (citable) accession number: O76083
Secondary accession number(s): B2RBI5 expand/collapse secondary AC list , B4DFI5, D3DSJ8, D3DSJ9, O75490, O75491, O95225, Q53Y40, Q5QD39, Q86SF7, Q86SI6, Q86SJ3, Q86WN3, Q86WN4, Q86WN5, Q86WN6, Q86WN7, Q86WN8, Q86WN9, Q86WP0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM