Adenylate cyclase type 2

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• ATP

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  = 3',5'-cyclic AMP

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + diphosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  10 Publications

  Manual assertion based on experiment inⁱ

  • Ref.1

    "Molecular cloning and characterization of a Ca2+/calmodulin-insensitive adenylyl cyclase from rat brain."
    Feinstein P.G., Schrader K.A., Bakalyar H.A., Tang W.J., Krupinski J., Gilman A.G., Reed R.R.
    Proc. Natl. Acad. Sci. U.S.A. 88:10173-10177(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  • Ref.2

    "A region of adenylyl cyclase 2 critical for regulation by G protein beta gamma subunits."
    Chen J., DeVivo M., Dingus J., Harry A., Li J., Sui J., Carty D.J., Blank J.L., Exton J.H., Stoffel R.H.
    Science 268:1166-1169(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION.
  • Ref.3

    "Identification of new Gbetagamma interaction sites in adenylyl cyclase 2."
    Boran A.D., Chen Y., Iyengar R.
    Cell. Signal. 23:1489-1495(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH THE G PROTEIN BETA AND GAMMA SUBUNIT COMPLEX.
  • Ref.4

    "Muscarinic receptors stimulate AC2 by novel phosphorylation sites, whereas Gbetagamma subunits exert opposing effects depending on the G-protein source."
    Shen J.X., Wachten S., Halls M.L., Everett K.L., Cooper D.M.
    Biochem. J. 447:393-405(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION AT SER-490 AND SER-543, MUTAGENESIS OF SER-490 AND SER-543, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION.
  • Ref.6

    "Non-raft adenylyl cyclase 2 defines a cAMP signaling compartment that selectively regulates IL-6 expression in airway smooth muscle cells: differential regulation of gene expression by AC isoforms."
    Bogard A.S., Birg A.V., Ostrom R.S.
    Naunyn Schmiedebergs Arch. Pharmacol. 387:329-339(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
  • Ref.10

    "Two-metal-ion catalysis in adenylyl cyclase."
    Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.
    Science 285:756-760(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
  • Ref.11

    "Molecular basis for P-site inhibition of adenylyl cyclase."
    Tesmer J.J., Dessauer C.W., Sunahara R.K., Murray L.D., Johnson R.A., Gilman A.G., Sprang S.R.
    Biochemistry 39:14464-14471(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 874-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; MAGNESIUM AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
  • Ref.12

    "Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate."
    Mou T.C., Gille A., Fancy D.A., Seifert R., Sprang S.R.
    J. Biol. Chem. 280:7253-7261(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GNAS, DOMAIN.
  • Ref.13

    "Broad specificity of mammalian adenylyl cyclase for interaction with 2',3'-substituted purine- and pyrimidine nucleotide inhibitors."
    Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R., Sprang S.R.
    Mol. Pharmacol. 70:878-886(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, DOMAIN.
  • Ref.14

    "Structural basis for inhibition of mammalian adenylyl cyclase by calcium."
    Mou T.C., Masada N., Cooper D.M., Sprang S.R.
    Biochemistry 48:3387-3397(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; FORSKOLIN; MAGNESIUM IONS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, DOMAIN.
  EC:4.6.1.1
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  10 Publications

  Manual assertion based on experiment inⁱ

  • Ref.1

    "Molecular cloning and characterization of a Ca2+/calmodulin-insensitive adenylyl cyclase from rat brain."
    Feinstein P.G., Schrader K.A., Bakalyar H.A., Tang W.J., Krupinski J., Gilman A.G., Reed R.R.
    Proc. Natl. Acad. Sci. U.S.A. 88:10173-10177(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  • Ref.2

    "A region of adenylyl cyclase 2 critical for regulation by G protein beta gamma subunits."
    Chen J., DeVivo M., Dingus J., Harry A., Li J., Sui J., Carty D.J., Blank J.L., Exton J.H., Stoffel R.H.
    Science 268:1166-1169(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION.
  • Ref.3

    "Identification of new Gbetagamma interaction sites in adenylyl cyclase 2."
    Boran A.D., Chen Y., Iyengar R.
    Cell. Signal. 23:1489-1495(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH THE G PROTEIN BETA AND GAMMA SUBUNIT COMPLEX.
  • Ref.4

    "Muscarinic receptors stimulate AC2 by novel phosphorylation sites, whereas Gbetagamma subunits exert opposing effects depending on the G-protein source."
    Shen J.X., Wachten S., Halls M.L., Everett K.L., Cooper D.M.
    Biochem. J. 447:393-405(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION AT SER-490 AND SER-543, MUTAGENESIS OF SER-490 AND SER-543, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION.
  • Ref.6

    "Non-raft adenylyl cyclase 2 defines a cAMP signaling compartment that selectively regulates IL-6 expression in airway smooth muscle cells: differential regulation of gene expression by AC isoforms."
    Bogard A.S., Birg A.V., Ostrom R.S.
    Naunyn Schmiedebergs Arch. Pharmacol. 387:329-339(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
  • Ref.10

    "Two-metal-ion catalysis in adenylyl cyclase."
    Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.
    Science 285:756-760(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
  • Ref.11

    "Molecular basis for P-site inhibition of adenylyl cyclase."
    Tesmer J.J., Dessauer C.W., Sunahara R.K., Murray L.D., Johnson R.A., Gilman A.G., Sprang S.R.
    Biochemistry 39:14464-14471(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 874-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; MAGNESIUM AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
  • Ref.12

    "Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate."
    Mou T.C., Gille A., Fancy D.A., Seifert R., Sprang S.R.
    J. Biol. Chem. 280:7253-7261(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GNAS, DOMAIN.
  • Ref.13

    "Broad specificity of mammalian adenylyl cyclase for interaction with 2',3'-substituted purine- and pyrimidine nucleotide inhibitors."
    Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R., Sprang S.R.
    Mol. Pharmacol. 70:878-886(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, DOMAIN.
  • Ref.14

    "Structural basis for inhibition of mammalian adenylyl cyclase by calcium."
    Mou T.C., Masada N., Cooper D.M., Sprang S.R.
    Biochemistry 48:3387-3397(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; FORSKOLIN; MAGNESIUM IONS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, DOMAIN.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  ATP

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  =

  3',5'-cyclic AMP

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  +

  diphosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• adenylate cyclase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.10

    "Two-metal-ion catalysis in adenylyl cyclase."
    Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.
    Science 285:756-760(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
• adenylate cyclase binding Source: BHF-UCLInferred from direct assayⁱ
  • "Heterodimers of adenylyl cyclases 2 and 5 show enhanced functional responses in the presence of Galpha s."
    Baragli A., Grieco M.L., Trieu P., Villeneuve L.R., Hebert T.E.
    Cell. Signal. 20:480-492(2008) [PubMed] [Europe PMC] [Abstract]
• ATP binding Source: UniProtKB-KW
• G-protein beta/gamma-subunit complex binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Gbetagamma that interacts with adenylyl cyclase in opioid tolerance originates from a Gs protein."
    Wang H.Y., Burns L.H.
    J. Neurobiol. 66:1302-1310(2006) [PubMed] [Europe PMC] [Abstract]
• magnesium ion binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Two-metal-ion catalysis in adenylyl cyclase."
    Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.
    Science 285:756-760(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
• manganese ion binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Two-metal-ion catalysis in adenylyl cyclase."
    Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.
    Science 285:756-760(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
• protein heterodimerization activity Source: RGDInferred from sequence orthologyⁱ
  • "Heterodimers of adenylyl cyclases 2 and 5 show enhanced functional responses in the presence of Galpha s."
    Baragli A., Grieco M.L., Trieu P., Villeneuve L.R., Hebert T.E.
    Cell. Signal. 20:480-492(2008) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• adenylate cyclase-activating G protein-coupled receptor signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "A region of adenylyl cyclase 2 critical for regulation by G protein beta gamma subunits."
    Chen J., DeVivo M., Dingus J., Harry A., Li J., Sui J., Carty D.J., Blank J.L., Exton J.H., Stoffel R.H.
    Science 268:1166-1169(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION.
• adenylate cyclase-modulating G protein-coupled receptor signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "Heterodimers of adenylyl cyclases 2 and 5 show enhanced functional responses in the presence of Galpha s."
    Baragli A., Grieco M.L., Trieu P., Villeneuve L.R., Hebert T.E.
    Cell. Signal. 20:480-492(2008) [PubMed] [Europe PMC] [Abstract]
• cAMP biosynthetic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Two-metal-ion catalysis in adenylyl cyclase."
    Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.
    Science 285:756-760(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
• cAMP-mediated signaling Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "A region of adenylyl cyclase 2 critical for regulation by G protein beta gamma subunits."
    Chen J., DeVivo M., Dingus J., Harry A., Li J., Sui J., Carty D.J., Blank J.L., Exton J.H., Stoffel R.H.
    Science 268:1166-1169(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION.
• cellular response to forskolin Source: UniProtKBInferred from direct assayⁱ
  • Ref.1

    "Molecular cloning and characterization of a Ca2+/calmodulin-insensitive adenylyl cyclase from rat brain."
    Feinstein P.G., Schrader K.A., Bakalyar H.A., Tang W.J., Krupinski J., Gilman A.G., Reed R.R.
    Proc. Natl. Acad. Sci. U.S.A. 88:10173-10177(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• adenylate cyclase binding Source: BHF-UCLInferred from direct assayⁱ
  • "Heterodimers of adenylyl cyclases 2 and 5 show enhanced functional responses in the presence of Galpha s."
    Baragli A., Grieco M.L., Trieu P., Villeneuve L.R., Hebert T.E.
    Cell. Signal. 20:480-492(2008) [PubMed] [Europe PMC] [Abstract]
• protein heterodimerization activity Source: RGDInferred from sequence orthologyⁱ
  • "Heterodimers of adenylyl cyclases 2 and 5 show enhanced functional responses in the presence of Galpha s."
    Baragli A., Grieco M.L., Trieu P., Villeneuve L.R., Hebert T.E.
    Cell. Signal. 20:480-492(2008) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL 
        60         70         80         90        100
LIVMGACLAL LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV 
       110        120        130        140        150
FKKLLRVFSL VIWICLVAMG YLFMCFGGTV SAWDQVSFFL FIIFVVYTML 
       160        170        180        190        200
PFNMRDAIIA SILTSSSHTI VLSVYLSATP GAKEHLFWQI LANVIIFICG 
       210        220        230        240        250
NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE RLLLSLLPAH 
       260        270        280        290        300
IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR 
       310        320        330        340        350
LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL 
       360        370        380        390        400
PNHAKNCVKM GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW 
       410        420        430        440        450
QYDVWSHDVT LANHMEAGGV PGRVHISSVT LEHLNGAYKV EEGDGEIRDP 
       460        470        480        490        500
YLKQHLVKTY FVINPKGERR SPQHLFRPRH TLDGAKMRAS VRMTRYLESW 
       510        520        530        540        550
GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR TKSQKKRFEE 
       560        570        580        590        600
ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK 
       610        620        630        640        650
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL 
       660        670        680        690        700
LQCSKKASTS LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL 
       710        720        730        740        750
SNSEETTLPT ANTSNANVSV PDNQASILHA RNLFFLPYFI YSCILGLISC 
       760        770        780        790        800
SVFLRVNYEL KMLIMMVALV GYNTILLHTH AHVLDAYSQV LFQRPGIWKD 
       810        820        830        840        850
LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE REEIETMENL 
       860        870        880        890        900
NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT 
       910        920        930        940        950
ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL 
       960        970        980        990       1000
SAIPSQEHAQ EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI 
      1010       1020       1030       1040       1050
NHGPVIAGVI GAQKPQYDIW GNTVNVASRM DSTGVLDKIQ VTEETSLILQ 
      1060       1070       1080       1090
TLGYTCTCRG IINVKGKGDL KTYFVNTEMS RSLSQSNLAS            

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. SIMILARITY comments
   Index of protein domains and families
2. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references