Reviewed, UniProtKB/Swiss-Prot Q9HCR9 (PDE11_HUMAN)

Names and origin

Protein names

Recommended name:
    Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
    EC=3.1.4.17
    EC=3.1.4.35
Alternative name(s):
    cAMP and cGMP phosphodiesterase 11A

Gene names

Name:

PDE11A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	934 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively. Ref.1 Ref.2 Ref.3
Catalytic activity	Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate. Adenosine 3',5'-cyclic phosphate + H2O = adenosine 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 By similarity.
Enzyme regulation	Inhibited by 3-isobutyl-1-methylxanthine (IBMX), zaprinast and dipyridamole. cGMP acts as an allosteric activator. Weakly inhibited by Sildenafil (Viagra) and Tadalafil (Cialis); however, the fact that the protein is probably absent from testis, suggests that it is not biologically relevant and is not related with erectile dysfunction. Ref.2 Ref.3 Ref.8 Ref.9
Subcellular location	Cytoplasm › cytosol Ref.1.
Tissue specificity	Isoform 1 is present in prostate, pituitary, heart and liver. It is however not present in testis nor in penis, suggesting that weak inhibition by Tadalafil (Cialis) is not relevant (at protein level). Isoform 2 may be expressed in testis. Isoform 4 is expressed in adrenal cortex. Ref.2 Ref.8 Ref.4 Ref.7 Ref.10
Domain	The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP leading to stimulate the enzyme activity. Ref.9
Involvement in disease	Defects in PDE11A are the cause of primary pigmented nodular adrenocortical disease type 2 (PPNAD2) [MIM:610475]. Primary pigmented nodular adrenocortical disease is a rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. PPNAD2 is characterized by adrenal glands with overall normal size and weight, and multiple small yellow-to-dark brown nodules surrounded by a cortex with a uniform appearance. Microscopically, there are moderate diffuse cortical hyperplasia with mostly nonpigmented nodules, multiple capsular deficits and massive circumscribed and infiltrating extra-adrenal cortical excrescences with micronodules. PPNAD2 leads to Cushing syndrome. Ref.10
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. Contains 2 GAF domains.
Biophysicochemical properties	Kinetic parameters: KM=3.0 µM for cAMP (isoform 1) KM=1.4 µM for cGMP (isoform 1) KM=3.0 µM for cAMP (isoform 2) KM=1.5 µM for cGMP (isoform 2) KM=3.3 µM for cAMP (isoform 3) KM=3.7 µM for cGMP (isoform 3) KM=1.04 µM for cAMP (isoform 4) KM=0.52 µM for cGMP (isoform 4) Vmax=3.6 pmol/min/µg enzyme with cAMP as substrate (isoform 4) Vmax=3.9 pmol/min/µg enzyme with cGMP as substrate (isoform 4) Vmax=270 pmol/min/µg enzyme with cAMP as substrate (isoform 1) Vmax=120 pmol/min/µg enzyme with cGMP as substrate (isoform 1)

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Metal-binding cAMP cGMP
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	signal transduction Ref.2 Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9HCR9-1)

Also known as: PDE11A4;

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 2 (identifier: Q9HCR9-2)

Also known as: PDE11A3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-250: Missing.
     251-304: KTLVSKFFDV...ETVNIPDAYQ → MLKQARRPLF...FLIQRQTKTK

Isoform 3 (identifier: Q9HCR9-3)

Also known as: PDE11A2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-358: Missing.

Isoform 4 (identifier: Q9HCR9-4)

Also known as: PDE11A1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-444: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 934	934	Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A		PRO_0000247040
Regions
	Domain	217 – 370	154	GAF 1
	Domain	402 – 558	157	GAF 2
	Region	640 – 905	266	Catalytic By similarity
Sites
	Active site	664	1	Proton donor By similarity
	Metal binding	668	1	Divalent metal cation 1 By similarity
	Metal binding	704	1	Divalent metal cation 1 By similarity
	Metal binding	705	1	Divalent metal cation 1 By similarity
	Metal binding	705	1	Divalent metal cation 2 By similarity
	Metal binding	708	1	Divalent metal cation 2 By similarity
	Metal binding	734	1	Divalent metal cation 2 By similarity
	Metal binding	816	1	Divalent metal cation 1 By similarity
	Binding site	869	1	cAMP or cGMP By similarity
Amino acid modifications
	Modified residue	162	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 444	444	Missing in isoform 4.		VSP_019898
	Alternative sequence	1 – 358	358	Missing in isoform 3.		VSP_019899
	Alternative sequence	1 – 250	250	Missing in isoform 2.		VSP_019900
	Alternative sequence	251 – 304	54	KTLVS…PDAYQ → MLKQARRPLFRNVLSATQWK KVKITRLVQISGASLAEKQE KHQDFLIQRQTKTK in isoform 2.		VSP_019901
	Natural variant	804	1	R → H		VAR_027056
	Natural variant	867	1	R → G		VAR_027057
Experimental info
	Mutagenesis	355	1	D → A: Induces a decrease in enzyme activity due to the inability of cGMP to bind and stimulate enzyme activity. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PDE11A4) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 994675824259447E	FASTA	934	104,811
	10 20 30 40 50 60 MAASRLDFGE VETFLDRHPE LFEDYLMRKG KQEMVEKWLQ RHSQGQGALG PRPSLAGTSS 70 80 90 100 110 120 LAHSTCRGGS SVGGGTGPNG SAHSQPLPGG GDCGGVPLSP SWAGGSRGDG NLQRRASQKE 130 140 150 160 170 180 LRKSFARSKA IHVNRTYDEQ VTSRAQEPLS SVRRRALLRK ASSLPPTTAH ILSALLESRV 190 200 210 220 230 240 NLPQYPPTAI DYKCHLKKHN ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL 250 260 270 280 290 300 FLVEGAAAGK KTLVSKFFDV HAGTPLLPCS STENSNEVQV PWGKGIIGYV GEHGETVNIP 310 320 330 340 350 360 DAYQDRRFND EIDKLTGYKT KSLLCMPIRS SDGEIIGVAQ AINKIPEGAP FTEDDEKVMQ 370 380 390 400 410 420 MYLPFCGIAI SNAQLFAASR KEYERSRALL EVVNDLFEEQ TDLEKIVKKI MHRAQTLLKC 430 440 450 460 470 480 ERCSVLLLED IESPVVKFTK SFELMSPKCS ADAENSFKES MEKSSYSDWL INNSIAELVA 490 500 510 520 530 540 STGLPVNISD AYQDPRFDAE ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKPFD 550 560 570 580 590 600 DADQRLFEAF VIFCGLGINN TIMYDQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANI 610 620 630 640 650 660 PLVSELAIDD IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW LLTVRKNYRM 670 680 690 700 710 720 VLYHNWRHAF NVCQLMFAML TTAGFQDILT EVEILAVIVG CLCHDLDHRG TNNAFQAKSG 730 740 750 760 770 780 SALAQLYGTS ATLEHHHFNH AVMILQSEGH NIFANLSSKE YSDLMQLLKQ SILATDLTLY 790 800 810 820 830 840 FERRTEFFEL VSKGEYDWNI KNHRDIFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE 850 860 870 880 890 900 QGDRERLELK LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNVK LKPMLDSVAT 910 920 930 NRSKWEELHQ KRLLASTASS SSPASVMVAK EDRN
	Isoform 2 (PDE11A3). Checksum: 1E41C4F5199D6B1E	FASTA	684	78,134
	10 20 30 40 50 60 MLKQARRPLF RNVLSATQWK KVKITRLVQI SGASLAEKQE KHQDFLIQRQ TKTKDRRFND 70 80 90 100 110 120 EIDKLTGYKT KSLLCMPIRS SDGEIIGVAQ AINKIPEGAP FTEDDEKVMQ MYLPFCGIAI 130 140 150 160 170 180 SNAQLFAASR KEYERSRALL EVVNDLFEEQ TDLEKIVKKI MHRAQTLLKC ERCSVLLLED 190 200 210 220 230 240 IESPVVKFTK SFELMSPKCS ADAENSFKES MEKSSYSDWL INNSIAELVA STGLPVNISD 250 260 270 280 290 300 AYQDPRFDAE ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKPFD DADQRLFEAF 310 320 330 340 350 360 VIFCGLGINN TIMYDQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANI PLVSELAIDD 370 380 390 400 410 420 IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW LLTVRKNYRM VLYHNWRHAF 430 440 450 460 470 480 NVCQLMFAML TTAGFQDILT EVEILAVIVG CLCHDLDHRG TNNAFQAKSG SALAQLYGTS 490 500 510 520 530 540 ATLEHHHFNH AVMILQSEGH NIFANLSSKE YSDLMQLLKQ SILATDLTLY FERRTEFFEL 550 560 570 580 590 600 VSKGEYDWNI KNHRDIFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE QGDRERLELK 610 620 630 640 650 660 LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNVK LKPMLDSVAT NRSKWEELHQ 670 680 KRLLASTASS SSPASVMVAK EDRN
	Isoform 3 (PDE11A2). Checksum: 3992C4C95A5B0B36	FASTA	576	65,767
	10 20 30 40 50 60 MQMYLPFCGI AISNAQLFAA SRKEYERSRA LLEVVNDLFE EQTDLEKIVK KIMHRAQTLL 70 80 90 100 110 120 KCERCSVLLL EDIESPVVKF TKSFELMSPK CSADAENSFK ESMEKSSYSD WLINNSIAEL 130 140 150 160 170 180 VASTGLPVNI SDAYQDPRFD AEADQISGFH IRSVLCVPIW NSNHQIIGVA QVLNRLDGKP 190 200 210 220 230 240 FDDADQRLFE AFVIFCGLGI NNTIMYDQVK KSWAKQSVAL DVLSYHATCS KAEVDKFKAA 250 260 270 280 290 300 NIPLVSELAI DDIHFDDFSL DVDAMITAAL RMFMELGMVQ KFKIDYETLC RWLLTVRKNY 310 320 330 340 350 360 RMVLYHNWRH AFNVCQLMFA MLTTAGFQDI LTEVEILAVI VGCLCHDLDH RGTNNAFQAK 370 380 390 400 410 420 SGSALAQLYG TSATLEHHHF NHAVMILQSE GHNIFANLSS KEYSDLMQLL KQSILATDLT 430 440 450 460 470 480 LYFERRTEFF ELVSKGEYDW NIKNHRDIFR SMLMTACDLG AVTKPWEISR QVAELVTSEF 490 500 510 520 530 540 FEQGDRERLE LKLTPSAIFD RNRKDELPRL QLEWIDSICM PLYQALVKVN VKLKPMLDSV 550 560 570 ATNRSKWEEL HQKRLLASTA SSSSPASVMV AKEDRN
	Isoform 4 (PDE11A1). Checksum: 28FD77BC040834F4	FASTA	490	55,787
	10 20 30 40 50 60 MSPKCSADAE NSFKESMEKS SYSDWLINNS IAELVASTGL PVNISDAYQD PRFDAEADQI 70 80 90 100 110 120 SGFHIRSVLC VPIWNSNHQI IGVAQVLNRL DGKPFDDADQ RLFEAFVIFC GLGINNTIMY 130 140 150 160 170 180 DQVKKSWAKQ SVALDVLSYH ATCSKAEVDK FKAANIPLVS ELAIDDIHFD DFSLDVDAMI 190 200 210 220 230 240 TAALRMFMEL GMVQKFKIDY ETLCRWLLTV RKNYRMVLYH NWRHAFNVCQ LMFAMLTTAG 250 260 270 280 290 300 FQDILTEVEI LAVIVGCLCH DLDHRGTNNA FQAKSGSALA QLYGTSATLE HHHFNHAVMI 310 320 330 340 350 360 LQSEGHNIFA NLSSKEYSDL MQLLKQSILA TDLTLYFERR TEFFELVSKG EYDWNIKNHR 370 380 390 400 410 420 DIFRSMLMTA CDLGAVTKPW EISRQVAELV TSEFFEQGDR ERLELKLTPS AIFDRNRKDE 430 440 450 460 470 480 LPRLQLEWID SICMPLYQAL VKVNVKLKPM LDSVATNRSK WEELHQKRLL ASTASSSSPA 490 SVMVAKEDRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of two novel phosphodiesterase PDE11A variants showing unique structure and tissue-specific expression." Yuasa K., Kotera J., Fujishige K., Michibata H., Sasaki T., Omori K. J. Biol. Chem. 275:31469-31479(2000) [PubMed: 10906126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Prostate.
[2]	"Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A." Fawcett L., Baxendale R., Stacey P., McGrouther C., Harrow I., Soderling S., Hetman J., Beavo J.A., Phillips S.C. Proc. Natl. Acad. Sci. U.S.A. 97:3702-3707(2000) [PubMed: 10725373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY. Tissue: Skeletal muscle.
[3]	"Cloning and characterisation of two splice variants of human phosphodiesterase 11A." Hetman J.M., Robas N.M., Baxendale R., Fidock M., Phillips S.C., Soderling S.H., Beavo J.A. Proc. Natl. Acad. Sci. U.S.A. 97:12891-12895(2000) [PubMed: 11050148] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[4]	"Genomic organization of the human phosphodiesterase PDE11A gene: evolutionary relatedness with other PDEs containing GAF domains." Yuasa K., Kanoh Y., Okumura K., Omori K. Eur. J. Biochem. 268:168-178(2001) [PubMed: 11121118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 4), TISSUE SPECIFICITY.
[5]	"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. , 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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]	"3',5'-cyclic nucleotide phosphodiesterase 11A: localization in human tissues." Loughney K., Taylor J., Florio V.A. Int. J. Impot. Res. 17:320-325(2005) [PubMed: 15800651] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"Phosphodiesterase 11 (PDE11): is it a player in human testicular function?" Francis S.H. Int. J. Impot. Res. 17:467-468(2005) [PubMed: 16079899] [Abstract] Cited for: ENZYME REGULATION, TISSUE SPECIFICITY.
[9]	"cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11." Gross-Langenhoff M., Hofbauer K., Weber J., Schultz A., Schultz J.E. J. Biol. Chem. 281:2841-2846(2006) [PubMed: 16330539] [Abstract] Cited for: DOMAIN, ENZYME REGULATION, MUTAGENESIS OF ASP-355.
[10]	"A genome-wide scan identifies mutations in the gene encoding phosphodiesterase 11A4 (PDE11A) in individuals with adrenocortical hyperplasia." Horvath A., Boikos S., Giatzakis C., Robinson-White A., Groussin L., Griffin K.J., Stein E., Levine E., Delimpasi G., Hsiao H.P., Keil M., Heyerdahl S., Matyakhina L., Libe R., Fratticci A., Kirschner L.S., Cramer K., Gaillard R.C. , Bertagna X., Carney J.A., Bertherat J., Bossis I., Stratakis C.A. Nat. Genet. 38:794-800(2006) [PubMed: 16767104] [Abstract] Cited for: INVOLVEMENT IN PPNAD2, TISSUE SPECIFICITY, VARIANTS HIS-804 AND GLY-867.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB036704 mRNA. Translation: BAB16371.1. AB038041 mRNA. Translation: BAB16372.1. AJ251509 mRNA. Translation: CAB82573.1. AF281865 mRNA. Translation: AAG32023.1. AJ278682 mRNA. Translation: CAC15567.1. AB048423 Genomic DNA. Translation: BAB62712.1. AB048423 Genomic DNA. Translation: BAB62713.2. AB048423 Genomic DNA. Translation: BAB62714.1. AC073834 Genomic DNA. No translation available. AC073892 Genomic DNA. No translation available. AC083824 Genomic DNA. No translation available. AC011998 Genomic DNA. No translation available. AC012499 Genomic DNA. Translation: AAY14803.1. BC112393 mRNA. Translation: AAI12394.1. BC114431 mRNA. Translation: AAI14432.1.
IPI	IPI00073708. IPI00783388. IPI00784056. IPI00784419.
RefSeq	NP_001070664.1. NP_001070665.1. NP_001070826.1. NP_058649.3.
UniGene	Hs.570273
3D structure databases
SMR	Q9HCR9. Positions 205-570, 589-912.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9HCR9.
PTM databases
PhosphoSite	Q9HCR9.
Proteomic databases
PRIDE	Q9HCR9.
Genome annotation databases
Ensembl	ENST00000286063; ENSP00000286063; ENSG00000128655; Homo sapiens. [Genome view]
GeneID	50940.
KEGG	hsa:50940.
UCSC	uc002ulp.1. human. uc002ulq.1. human. uc002ulr.1. human. uc002uls.1. human.
Organism-specific databases
CTD	50940.
GeneCards	GC02M178201.
HGNC	HGNC:8773. PDE11A.
MIM	604961. gene. 610475. phenotype.
Orphanet	553. Cushing syndrome.
PharmGKB	PA33121.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18192.
HOVERGEN	Q9HCR9.
InParanoid	Q9HCR9.
Enzyme and pathway databases
BRENDA	3.1.4.17. 247. 3.1.4.35. 247.
Reactome	REACT_14797. Signaling by GPCR.
Gene expression databases
ArrayExpress	Q9HCR9.
Bgee	Q9HCR9.
CleanEx	HS_PDE11A.
Genevestigator	Q9HCR9.
GermOnline	ENSG00000128655. Homo sapiens.
Family and domain databases
InterPro	IPR003018. GAF. IPR003607. Metal-dep_PHydrolase_HD_dom. IPR002073. PDEase. [Graphical view]
Pfam	PF01590. GAF. 2 hits. PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00065. GAF. 2 hits. SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	53391.
SOURCE	Search...

Entry information

Entry name

PDE11_HUMAN

Accession

Primary (citable) accession number: Q9HCR9
Secondary accession number(s): Q14CD1 , Q53T16, Q96S76, Q9GZY7, Q9HB46, Q9NY45

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	March 1, 2001
Last modified:	January 19, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.