SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9HCR9

- PDE11_HUMAN

UniProt

Q9HCR9 - PDE11_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A

Gene
PDE11A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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

Enzyme regulationi

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.4 Publications

Kineticsi

  1. KM=3.0 µM for cAMP (isoform 1)3 Publications
  2. KM=1.4 µM for cGMP (isoform 1)
  3. KM=3.0 µM for cAMP (isoform 2)
  4. KM=1.5 µM for cGMP (isoform 2)
  5. KM=3.3 µM for cAMP (isoform 3)
  6. KM=3.7 µM for cGMP (isoform 3)
  7. KM=1.04 µM for cAMP (isoform 4)
  8. 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)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei664 – 6641Proton donor By similarity
Metal bindingi668 – 6681Divalent metal cation 1 By similarity
Metal bindingi704 – 7041Divalent metal cation 1 By similarity
Metal bindingi705 – 7051Divalent metal cation 1 By similarity
Metal bindingi705 – 7051Divalent metal cation 2 By similarity
Metal bindingi708 – 7081Divalent metal cation 2 By similarity
Metal bindingi734 – 7341Divalent metal cation 2 By similarity
Metal bindingi816 – 8161Divalent metal cation 1 By similarity
Binding sitei869 – 8691cAMP or cGMP By similarity

GO - Molecular functioni

  1. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB-EC
  2. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: ProtInc
  3. cAMP binding Source: Ensembl
  4. cGMP binding Source: UniProtKB
  5. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  6. cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  7. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cAMP catabolic process Source: Ensembl
  3. cGMP catabolic process Source: Ensembl
  4. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, cGMP, Metal-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:
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 namesi
Name:PDE11A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:8773. PDE11A.

Subcellular locationi

Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. perikaryon Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Primary pigmented nodular adrenocortical disease 2 (PPNAD2) [MIM:610475]: A rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Adrenal glands show 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. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi355 – 3551D → A: Induces a decrease in enzyme activity due to the inability of cGMP to bind and stimulate enzyme activity. 1 Publication

Keywords - Diseasei

Cushing syndrome

Organism-specific databases

MIMi610475. phenotype.
Orphaneti189439. Primary pigmented nodular adrenocortical disease.
PharmGKBiPA33121.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 933933Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11APRO_0000247040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9HCR9.
PRIDEiQ9HCR9.

PTM databases

PhosphoSiteiQ9HCR9.

Expressioni

Tissue specificityi

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.5 Publications

Gene expression databases

ArrayExpressiQ9HCR9.
BgeeiQ9HCR9.
CleanExiHS_PDE11A.
GenevestigatoriQ9HCR9.

Organism-specific databases

HPAiHPA034560.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000286063.

Structurei

3D structure databases

ProteinModelPortaliQ9HCR9.
SMRiQ9HCR9. Positions 205-911.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini217 – 370154GAF 1Add
BLAST
Domaini402 – 558157GAF 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni640 – 905266Catalytic By similarityAdd
BLAST

Domaini

The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP stimulates enzyme activity.1 Publication

Sequence similaritiesi

Contains 2 GAF domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270709.
HOVERGENiHBG101207.
InParanoidiQ9HCR9.
KOiK13298.
OMAiDYSDLMQ.
OrthoDBiEOG7RRF69.
PhylomeDBiQ9HCR9.
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. 2 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9HCR9-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAASRLDFGE VETFLDRHPE LFEDYLMRKG KQEMVEKWLQ RHSQGQGALG    50
PRPSLAGTSS LAHSTCRGGS SVGGGTGPNG SAHSQPLPGG GDCGGVPLSP 100
SWAGGSRGDG NLQRRASQKE LRKSFARSKA IHVNRTYDEQ VTSRAQEPLS 150
SVRRRALLRK ASSLPPTTAH ILSALLESRV NLPRYPPTAI DYKCHLKKHN 200
ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL FLVEGAAAGK 250
KTLVSKFFDV HAGTPLLPCS STENSNEVQV PWGKGIIGYV GEHGETVNIP 300
DAYQDRRFND EIDKLTGYKT KSLLCMPIRS SDGEIIGVAQ AINKIPEGAP 350
FTEDDEKVMQ MYLPFCGIAI SNAQLFAASR KEYERSRALL EVVNDLFEEQ 400
TDLEKIVKKI MHRAQTLLKC ERCSVLLLED IESPVVKFTK SFELMSPKCS 450
ADAENSFKES MEKSSYSDWL INNSIAELVA STGLPVNISD AYQDPRFDAE 500
ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKPFD DADQRLFEAF 550
VIFCGLGINN TIMYDQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANI 600
PLVSELAIDD IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW 650
LLTVRKNYRM VLYHNWRHAF NVCQLMFAML TTAGFQDILT EVEILAVIVG 700
CLCHDLDHRG TNNAFQAKSG SALAQLYGTS ATLEHHHFNH AVMILQSEGH 750
NIFANLSSKE YSDLMQLLKQ SILATDLTLY FERRTEFFEL VSKGEYDWNI 800
KNHRDIFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE QGDRERLELK 850
LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNVK LKPMLDSVAT 900
NRSKWEELHQ KRLLASTASS SPASVMVAKE DRN 933
Length:933
Mass (Da):104,752
Last modified:May 18, 2010 - v2
Checksum:iB725AE6963D6E799
GO
Isoform 2 (identifier: Q9HCR9-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:683
Mass (Da):78,047
Checksum:i82DD9BB77C941A1C
GO
Isoform 3 (identifier: Q9HCR9-3) [UniParc]FASTAAdd to Basket

Also known as: PDE11A2

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

Show »
Length:575
Mass (Da):65,679
Checksum:iA1DDA7F4BAF43221
GO
Isoform 4 (identifier: Q9HCR9-4) [UniParc]FASTAAdd to Basket

Also known as: PDE11A1

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

Show »
Length:489
Mass (Da):55,700
Checksum:i3E6ED2AAE9CBF03C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti804 – 8041R → H.1 Publication
Corresponds to variant rs75127279 [ dbSNP | Ensembl ].
VAR_027056
Natural varianti867 – 8671R → G.1 Publication
Corresponds to variant rs61306957 [ dbSNP | Ensembl ].
VAR_027057

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 444444Missing in isoform 4. VSP_019898Add
BLAST
Alternative sequencei1 – 358358Missing in isoform 3. VSP_019899Add
BLAST
Alternative sequencei1 – 250250Missing in isoform 2. VSP_019900Add
BLAST
Alternative sequencei251 – 30454KTLVS…PDAYQ → MLKQARRPLFRNVLSATQWK KVKITRLVQISGASLAEKQE KHQDFLIQRQTKTK in isoform 2. VSP_019901Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841R → Q in BAB16371. 1 Publication
Sequence conflicti184 – 1841R → Q in BAB62712. 1 Publication
Sequence conflicti184 – 1841R → Q in AAI12394. 1 Publication
Sequence conflicti184 – 1841R → Q in AAI14432. 1 Publication
Sequence conflicti921 – 9211S → SS in BAB16371. 1 Publication
Sequence conflicti921 – 9211S → SS in BAB16372. 1 Publication
Sequence conflicti921 – 9211S → SS in CAB82573. 1 Publication
Sequence conflicti921 – 9211S → SS in AAG32023. 1 Publication
Sequence conflicti921 – 9211S → SS in CAC15567. 1 Publication
Sequence conflicti921 – 9211S → SS in BAB62712. 1 Publication
Sequence conflicti921 – 9211S → SS in BAB62713. 1 Publication
Sequence conflicti921 – 9211S → SS in BAB62714. 1 Publication
Sequence conflicti921 – 9211S → SS in AAI12394. 1 Publication
Sequence conflicti921 – 9211S → SS in AAI14432. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33334.1. [Q9HCR9-1]
CCDS42785.1. [Q9HCR9-2]
CCDS42786.1. [Q9HCR9-4]
CCDS46459.1. [Q9HCR9-3]
RefSeqiNP_001070664.1. NM_001077196.1. [Q9HCR9-4]
NP_001070665.1. NM_001077197.1. [Q9HCR9-2]
NP_001070826.1. NM_001077358.1. [Q9HCR9-3]
NP_058649.3. NM_016953.3. [Q9HCR9-1]
UniGeneiHs.570273.

Genome annotation databases

EnsembliENST00000286063; ENSP00000286063; ENSG00000128655. [Q9HCR9-1]
ENST00000358450; ENSP00000351232; ENSG00000128655. [Q9HCR9-2]
ENST00000389683; ENSP00000374333; ENSG00000128655. [Q9HCR9-4]
ENST00000409504; ENSP00000386539; ENSG00000128655. [Q9HCR9-3]
ENST00000449286; ENSP00000390599; ENSG00000128655. [Q9HCR9-3]
GeneIDi50940.
KEGGihsa:50940.
UCSCiuc002ulp.3. human. [Q9HCR9-1]
uc002ulr.3. human. [Q9HCR9-2]

Polymorphism databases

DMDMi296439264.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS33334.1. [Q9HCR9-1 ]
CCDS42785.1. [Q9HCR9-2 ]
CCDS42786.1. [Q9HCR9-4 ]
CCDS46459.1. [Q9HCR9-3 ]
RefSeqi NP_001070664.1. NM_001077196.1. [Q9HCR9-4 ]
NP_001070665.1. NM_001077197.1. [Q9HCR9-2 ]
NP_001070826.1. NM_001077358.1. [Q9HCR9-3 ]
NP_058649.3. NM_016953.3. [Q9HCR9-1 ]
UniGenei Hs.570273.

3D structure databases

ProteinModelPortali Q9HCR9.
SMRi Q9HCR9. Positions 205-911.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000286063.

Chemistry

ChEMBLi CHEMBL2717.
GuidetoPHARMACOLOGYi 1311.

PTM databases

PhosphoSitei Q9HCR9.

Polymorphism databases

DMDMi 296439264.

Proteomic databases

PaxDbi Q9HCR9.
PRIDEi Q9HCR9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000286063 ; ENSP00000286063 ; ENSG00000128655 . [Q9HCR9-1 ]
ENST00000358450 ; ENSP00000351232 ; ENSG00000128655 . [Q9HCR9-2 ]
ENST00000389683 ; ENSP00000374333 ; ENSG00000128655 . [Q9HCR9-4 ]
ENST00000409504 ; ENSP00000386539 ; ENSG00000128655 . [Q9HCR9-3 ]
ENST00000449286 ; ENSP00000390599 ; ENSG00000128655 . [Q9HCR9-3 ]
GeneIDi 50940.
KEGGi hsa:50940.
UCSCi uc002ulp.3. human. [Q9HCR9-1 ]
uc002ulr.3. human. [Q9HCR9-2 ]

Organism-specific databases

CTDi 50940.
GeneCardsi GC02M178487.
HGNCi HGNC:8773. PDE11A.
HPAi HPA034560.
MIMi 604961. gene.
610475. phenotype.
neXtProti NX_Q9HCR9.
Orphaneti 189439. Primary pigmented nodular adrenocortical disease.
PharmGKBi PA33121.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270709.
HOVERGENi HBG101207.
InParanoidi Q9HCR9.
KOi K13298.
OMAi DYSDLMQ.
OrthoDBi EOG7RRF69.
PhylomeDBi Q9HCR9.
TreeFami TF316499.

Enzyme and pathway databases

BRENDAi 3.1.4.17. 2681.
Reactomei REACT_19327. G alpha (s) signalling events.
REACT_23767. cGMP effects.

Miscellaneous databases

GeneWikii PDE11A.
GenomeRNAii 50940.
NextBioi 53391.
PROi Q9HCR9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9HCR9.
Bgeei Q9HCR9.
CleanExi HS_PDE11A.
Genevestigatori Q9HCR9.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProi IPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view ]
SUPFAMi SSF55781. SSF55781. 2 hits.
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: DOMAIN, ENZYME REGULATION, MUTAGENESIS OF ASP-355.
  10. Cited for: INVOLVEMENT IN PPNAD2, TISSUE SPECIFICITY, VARIANTS HIS-804 AND GLY-867.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.

Entry informationi

Entry nameiPDE11_HUMAN
AccessioniPrimary (citable) accession number: Q9HCR9
Secondary accession number(s): Q14CD1
, Q53T16, Q96S76, Q9GZY7, Q9HB46, Q9NY45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 18, 2010
Last modified: September 3, 2014
This is version 103 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

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi