Protein detail

AKA10

A-kinase anchor protein 10, mitochondrial (AKAP-10) (Dual specificity A kinase-anchoring protein 2) (D-AKAP-2) (Protein kinase A-anchoring protein 10) (PRKA10)

Entry name
AKA10
UniProt ID
EVMP confidence score
0.50
Supporting publications (n)
3
Transmembrane count
Protein classification
Plasma proteinsPredicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information11
Protein Names
A-kinase anchor protein 10, mitochondrial (AKAP-10) (Dual specificity A kinase-anchoring protein 2) (D-AKAP-2) (Protein kinase A-anchoring protein 10) (PRKA10)
Protein Class (2)
Plasma proteinsPredicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym (3)
D-AKAP2MGC9414PRKA10
Gene Description
A-kinase anchoring protein 10
Chromosome
17
Position
19904302-19978343
Supporting publications (n)
3
EVMP confidence score
0.50
Fluorescence & Localization1
Cell SpecificLactotrophs
Function & Pathway6
Relations & Evidence5

Ligand-Receptor Signaling (4)

4 records.

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

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometry23175372636028467
Sequence, Structure & Domains9

Sequences

Length
662
Mass
73,818
Sequence
MRGAGPSPRQSPRTLRPDPGPAMSFFRRKVKGKEQEKTSDVKSIKASISVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLHDTIVLPYFIQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKKHETTASFLTDSLDKRLEDSGSAQLFMTHSEGIDLNNRTNSTQNHLLLSQECDSAHSLRLEMARAGTHQVSMETQESSSTLTVASRNSPASPLKELSGKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIARICGEDGQVDPNCFVLAQSIVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLTAPGSVGPPDESHPGSSDSSASQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMTFGRVSDLGQFIRESEPEPDVRKSKGSMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDIMQQAQYDQPLEKSTKL

3D Structural Models

Helix
629..653
3D Structure
X-ray crystallography (2)

Domain & Motif Annotations

Compositional Bias
32..43; Basic and acidic residues; 261..280; Polar residues
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 (FT)
125..369; RGS 1; 379..505; RGS 2
Region
1..55; Disordered; 261..282; Disordered; 524..548; Disordered; 634..647; PKA-RII subunit binding
Clinical Relevance1
Antibody
Supporting Publications3
PMIDTitleAbstract
27487081Comparative Proteomic Analysis of Extracellular Vesicles Isolated by Acoustic Trapping or Differential Centrifugation.No abstract available
35763629Proteomic Profiling of Small Extracellular Vesicles Isolated from the Plasma of Vietnamese Patients with Non-Small Cell Lung Cancer Reveals Some Potential Biomarkers.No abstract available
36982312Saliva and Saliva Extracellular Vesicles for Biomarker Candidate Identification-Assay Development and Pilot Study in Amyotrophic Lateral Sclerosis.No abstract available