Protein detail
AKA11
A-kinase anchor protein 11 (AKAP-11) (A-kinase anchor protein 220 kDa) (AKAP 220) (hAKAP220) (Protein kinase A-anchoring protein 11) (PRKA11)
Protein symbol AKA11 | UniProt ID | EVMP score 0.38 |
Frequency 1 | Transmembrane count | Protein classification Plasma proteinsPredicted intracellular proteins |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
A-kinase anchor protein 11 (AKAP-11) (A-kinase anchor protein 220 kDa) (AKAP 220) (hAKAP220) (Protein kinase A-anchoring protein 11) (PRKA11)
Protein Class
Plasma proteinsPredicted intracellular proteins
Protein Function
Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym
AKAP220DKFZp781I12161FLJ11304KIAA0629PPP1R44PRKA11
Gene Description
A-kinase anchoring protein 11
Chromosome
13
Position
42272152-42323261
Frequency
1
EVMP Score
0.38
Fluorescence & Localization
Tissue SpecificgallbladderCell SpecificNeutrophil progenitorsSingle-Nuclei Brain Specificcentral nervous system macrophageBlood Cell Specificclassical monocyteBlood Lineage Specificdendritic cellsSecretome LocationIntracellular and membraneSecretome FunctionEnzyme
Function & Pathway
Protein Function
Predicted intracellular proteins
Cellular Component
Molecular Function
Biological Process
Mediation Categories
Metabolism mediation
Relations & Evidence
Enzyme-Mediated Modification
2 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| AKAP11 | GSK3B | P49841 | T | 1,136 | phosphorylation | SIGNORPhosphoSitePhosphoSite_ProtMapperProtMapper | SIGNOR:26088133 |
| AKAP11 | GSK3B | P49841 | T | 1,140 | phosphorylation | PhosphoSitePhosphoSite_ProtMapperProtMapper |
Ligand-Receptor Signaling
5 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | LOCATE | No | No | No | No | No |
| 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
3 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| AKA11 | Q9UKA4 | IQGA2 | Q13576 | Yes | Yes | No | SIGNOR | SIGNOR:21776420 |
| GSK3B | P49841 | AKA11 | Q9UKA4 | Yes | No | Yes | PhosphoSite_norefPhosphoPointSIGNORProtMapperiPTMnetHPRDHINTSIGNOR_ProtMapperLit-BM-17PhosphoSite_ProtMapper | HPRD:12147701HINT:35271311Lit-BM-17:23602568HINT:12147701HINT:32707033SIGNOR:26088133ProtMapper:26088133Lit-BM-17:12147701 |
| AKA11 | Q9UKA4 | GSK3B | P49841 | Yes | No | Yes | HPRDHINTLit-BM-17SIGNOR | HPRD:12147701HINT:35271311Lit-BM-17:23602568HINT:12147701HINT:32707033SIGNOR:26088133Lit-BM-17:12147701 |
Protein Complex Composition
4 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| AKAP11AKAP3ANKRD26GPR161PRKACGPRKAR1APRKAR1B | O75969P10644P22612P31321Q8N6U8Q9UKA4Q9UPS8 | 0:0:0:0:0:0:0 | hu.MAP | |||
| AKAP11GSK3BPPP1CCUBC | P0CG48P36873P49841Q9UKA4 | 1:1:1:1 | CompleatCFinder | Compleat:HC8483 | ||
| AKAP11CEP68PRKACBPRKAR1APRKAR1B | P10644P22694P31321Q76N32Q9UKA4 | 0:0:0:0:0 | hu.MAP | |||
| AKAP11PPP1CBPRKAR2A | P13861P62140Q9UKA4 | 1:1:1 | CompleatCFinder | Compleat:HC4433 |
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationSize Exclusion Chromatography | Mass spectrometry | 1 | 40689422 |
Sequence, Structure & Domains
Sequences
Length
1,901
Mass
210,512
Sequence
MATFRNNHMKTKASVRKSFSEDVFQSVKSLLQSQKELCSVTAEDCLQQDEHANLTEVTFLGFNEETDAAHIQDLAAVSLELPDILNSLHFCSLNENEIICMKNINKPLDISSDPLNQSHPSGMLCVMRVSPTSPRLRIDFIFSLLSKYATGIRYTLDTFLHQKHQLETTDEDDDDTNQSVSSIEDDFVTAFEHLEEEETSKPYNDGMNITVLRSQCDAASQTVTGHHLETHDLKILISSGQQKSLAKPSTSSVNVLGHKELPSVKTSVTTSISEPWTQRSFYRSSNASDKDSDLQKTFFSSSPAYSSESECSSPSPVIFLDEEGYQKSLKAKLELPKIPVMKDDIEDSDSEVSEFFDSFDQFDELEQTLETCLFNKDPVIGKSSQRKGHKHGKSCMNPQKFKFDRPALPANVRKPTPRKPESPYGNLCDAPDSPRPVKASREDSGLFSPIRSSAFSPLGGCTPAECFCQTDIGGDRIHENHDSVYYTYEDYAKSISCEVLGSVLRTHHTNTLSNINSIKHGENKTVTFKHGNLDQKNKSKNKSLMIKDSIQKFAADLVEKSFGSAFKDLQKGVSSCTNALYHLAIKLTSSVLQMAFDELRRQRAFSLKERAISGLANFLVSEALSNALKDLQYVKKQIFTNTVARFAADLAEELVFEGIMEVCQFSYPQTPASPQCGSFDFEDKVVKLYAKDLSESVIQEAFIELSQVDVTFTTKAAVSVSTDNIKYVSAESVVPSTQAVTFSPSFHNQAIMVTKPVQEYKKEYTVQQALFCTSGIVTSIPVPLAGSALLPYHISSTACQAKAHLSSDDSNSNGDSAQVHIATKNREEKAACLRNICLPSEHNPGNQNDFKPTNDDIEMQSSSKLPNDPAIISNFSAAVVHTIVNETLESMTSLEVTKMVDERTDYLTKSLKEKTPPFSHCDQAVLQCSEASSNKDMFADRLSKSIIKHSIDKSKSVIPNIDKNAVYKESLPVSGEESQLTPEKSPKFPDSQNQLTHCSLSAAKDCVPECKVSMVHGSSLETLPSCPAVTGQKSDLKESAKDQPLKKHNLNSTSLEALSFGQENPFPHSHTFSSTALTCVDGLHVEDKQKVRDRNVIPDTPPSTPLVPSRASSEWDIKKLTKKLKGELAKEFAPATPPSTPHNSSVGSLSENEQNTIEKEEFMLKLMRSLSEEVESSESGELPEVDVKSEHSGKKVQFAEALATHILSLATEMAASHLDNKIIQEPKVKNPCLNVQSQRSVSPTFLNPSDENLKTLCNFAGDLAAEVITEAEKIAKVRNCMLFKQKKNSCYADGDEDYKVEEKLDIEAVVHPREVDPFILSLPPSSCMSGLMYKYPSCESVTDEYAGHLIQILKQEGGNSELIMDQYANRLAYRSVKSGLQEAAKTTKVQCNSRMFPVPSSQVKTNKELLMFSNKEHHQEADKKRQSKRNEGYFCKNQTCERTLDPYRNEVSQLYSFSTSLVHSITKDAKEELTASLVGLPKSLTDSCLFEKSGYEEDNECHVTPELPKSLQPSSQNHRFYHSTGSLNGYGCGDNVVQAVEQYAKKVVDDTLELTLGSTVFRVSETTKSADRVTYAEKLSPLTGQACRYCDLKELHNCTGNSSQHFFRQGSLASSKPASNPKFSSRYQKSRIFHLSVPQIHVNLDKKAVLAEKIVAEAIEKAERELSSTSLAADSGIGQEGASFAESLATETMTAAVTNVGHAVSSSKEIEDFQSTESVSSQQMNLSIGDDSTGSWSNLSFEDEHQDESSSFHHLSESNGNSSSWSSLGLEGDLYEDNLSFPTSDSDGPDDKDEEHEDEVEGLGQDGKTLLITNIDMEPCTVDPQLRIILQWLIASEAEVAELYFHDSANKEFMLLSKQLQEKGWKVGDLLQAVLQYYEVMEKASSEERCKSLFDWLLENA
3D Structural Models
Domain & Motif Annotations
Compositional Bias
1141..1153; Polar residues; 1713..1740; Polar residues; 1747..1756; Basic and acidic residues; 1757..1772; Low complexity; 1787..1801; Acidic 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.
Region
407..443; Disordered; 843..864; Disordered; 971..993; Disordered; 1131..1153; Disordered; 1650..1663; PKA-RII subunit binding domain; 1708..1805; Disordered
Protein Families
AKAP110 family
Sequence Similarities
Belongs to the AKAP110 family.
Clinical Relevance
Antibody
Interaction Protein
ENSG00000005249ENSG00000072062ENSG00000082701ENSG00000101558ENSG00000105723ENSG00000108946ENSG00000124164
Interaction Count
7
Interaction Dataset
biogrid_bioplexbiogrid_opencellintact_biogrid