Protein detail

AKAP5

A-kinase anchor protein 5 (AKAP-5) (A-kinase anchor protein 79 kDa) (AKAP 79) (H21) (cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein)

Protein symbol
AKAP5
UniProt ID
EVMP score
0.38
Frequency
1
Transmembrane count
Protein classification
Plasma proteinsPredicted intracellular proteinsTransporters
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
A-kinase anchor protein 5 (AKAP-5) (A-kinase anchor protein 79 kDa) (AKAP 79) (H21) (cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein)
Protein Class
Plasma proteinsPredicted intracellular proteinsTransporters
Protein Function
  • Predicted intracellular proteins
  • Transporters:Accessory Factors Involved in Transport
Entrez Gene Symbol
Gene Synonym
AKAP75AKAP79
Gene Description
A-kinase anchoring protein 5
Chromosome
14
Position
64465499-64474503
Frequency
1
EVMP Score
0.38
Fluorescence & Localization
Tissue SpecificliverCell SpecificEpicardial cellsSingle-Nuclei Brain Specificfibroblast
Function & Pathway
Protein Function
  • Predicted intracellular proteins
  • Transporters:Accessory Factors Involved in Transport
Mediation Categories
Fusion and delivery mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

4 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
AKAP5ZDHHC2Q9UIJ5C36palmitoylationSIGNORSIGNOR:25589740
AKAP5ZDHHC2Q9UIJ5C129palmitoylationSIGNORSIGNOR:25589740
AKAP5CAMK2AQ9UQM7S92phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
AKAP5CAMK2AQ9UQM7T87phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper

Ligand-Receptor Signaling

4 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Regulatory Interaction Network

3 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
AKAP5P24588KAPCAP17612YesYesNoSIGNORCui2007HINTCA1WangCA1:8599116HINT:35271311CA1:1512224HINT:32707033HINT:26496610SIGNOR:10939335
ZDHC2Q9UIJ5AKAP5P24588YesYesNoSIGNORSIGNOR:25589740
AKAP5P24588PP2BCP48454YesYesNoSIGNORSIGNOR:20694001

Protein Complex Composition

4 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
AKAP5-PRKAR2A-PPP3CA complexAKAP5PPP3CAPRKAR2AP13861P24588Q082091:1:1CompleatCORUMCompleat:HC884CORUM:51712507994
PKA (RII-alpha and RII-beta)-AKAP5-ADRB1 complexADRB1AKAP5PRKAR2APRKAR2BP08588P13861P24588P313230:0:0:0CORUMCORUM:87816940053
PRKAC-AKAP5-ADRB1 complexADRB1AKAP5PRKACAPRKACBPRKACGP08588P17612P22612P22694P245881:1:1:1:1CompleatCompleat:HC101716940053
AKAP5CALM1P0DP23P245882:2PDBPDB:5nin

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometry136435201
Sequence, Structure & Domains

Sequences

Length
427
Mass
47,088
Sequence
METTISEIHVENKDEKRSAEGSPGAERQKEKASMLCFKRRKKAAKALKPKAGSEAADVARKCPQEAGASDQPEPTRGAWASLKRLVTRRKRSESSKQQKPLEGEMQPAINAEDADLSKKKAKSRLKIPCIKFPRGPKRSNHSKIIEDSDCSIKVQEEAEILDIQTQTPLNDQATKAKSTQDLSEGISRKDGDEVCESNVSNSTTSGEKVISVELGLDNGHSAIQTGTLILEEIETIKEKQDVQPQQASPLETSETDHQQPVLSDVPPLPAIPDQQIVEEASNSTLESAPNGKDYESTEIVAEETKPKDTELSQESDFKENGITEEKSKSEESKRMEPIAIIITDTEISEFDVTKSKNVPKQFLISAENEQVGVFANDNGFEDRTSEQYETLLIETASSLVKNAIQLSIEQLVNEMASDDNKINNLLQ

3D Structural Models

Turn
409..411
Helix
79..83; 393..408
Beta Strand
339..344
3D Structure
NMR spectroscopy (1); X-ray crystallography (2)

Domain & Motif Annotations

Compositional Bias
8..19; Basic and acidic residues; 37..48; Basic residues; 92..102; Basic and acidic residues; 171..182; Polar residues; 242..252; Polar residues; 302..333; Basic and acidic residues
Motif
76..96; AKAP CaM-binding
Domain (CC)
RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.; DOMAIN: The N-terminal region, which is highly basic, is required for interaction with calmodulin.
Region
1..170; Essential to the intracellular anchoring function; 1..122; Disordered; 171..205; Disordered; 239..269; Disordered; 281..333; Disordered; 392..405; PKA-RII subunit binding domain; 410..427; Tethers NFATC2 to CRAC channels
Clinical Relevance
Interaction Protein
ENSG00000005249ENSG00000072062ENSG00000114302
Interaction Count
3
Interaction Dataset
intact_biogridbiogrid_opencell