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)
Protein symbol AKA10 | UniProt ID | EVMP score 0.50 |
Frequency 3 | Transmembrane count | Protein classification Plasma proteinsPredicted intracellular proteins |
Basic Information
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
Plasma proteinsPredicted intracellular proteins
Protein Function
Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym
D-AKAP2MGC9414PRKA10
Gene Description
A-kinase anchoring protein 10
Chromosome
17
Position
19904302-19978343
Frequency
3
EVMP Score
0.50
Fluorescence & Localization
Cell SpecificLactotrophs
Function & Pathway
Protein Function
Predicted intracellular proteins
Cellular Component
Molecular Function
Biological Process
Reactome
Mediation Categories
Immune mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
4 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
Regulatory Interaction Network
0 records.
Protein Complex Composition
0 records.
Sequence, Structure & Domains
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 Relevance
Antibody