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)

Entry name
AKA11
UniProt ID
EVMP confidence score
0.53
Supporting publications (n)
1
Transmembrane count
Protein classification
Plasma proteinsPredicted intracellular proteins
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 (2)
Plasma proteinsPredicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym (6)
AKAP220DKFZp781I12161FLJ11304KIAA0629PPP1R44PRKA11
Gene Description
A-kinase anchoring protein 11
Chromosome
13
Position
42272152-42323261
Supporting publications (n)
1
EVMP confidence score
0.53
Fluorescence & Localization
Tissue SpecificgallbladderCell SpecificNeutrophil progenitorsSingle-Nuclei Brain Specificcentral nervous system macrophageBlood Cell Specificclassical monocyteBlood Lineage Specificdendritic cellsSecretome LocationIntracellular and membraneSecretome FunctionEnzyme
Function & Pathway
Relations & Evidence15

Enzyme-Mediated Modification (2)

2 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
AKAP11GSK3BP49841T1,136phosphorylationSIGNORPhosphoSitePhosphoSite_ProtMapperProtMapperSIGNOR:26088133
AKAP11GSK3BP49841T1,140phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper

Ligand-Receptor Signaling (5)

5 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATE
intracellularintracellularComPPI
intracellularintracellularGO_Intercell
intracellularintracellularUniProt_location
intracellularintracellularOmniPath

Regulatory Interaction Network (3)

3 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
AKA11Q9UKA4IQGA2Q13576YesYesSIGNORSIGNOR:21776420
GSK3BP49841AKA11Q9UKA4YesYesPhosphoSite_norefPhosphoPointSIGNORProtMapperiPTMnetHPRDHINTSIGNOR_ProtMapperLit-BM-17PhosphoSite_ProtMapperHPRD:12147701HINT:35271311Lit-BM-17:23602568HINT:12147701HINT:32707033SIGNOR:26088133ProtMapper:26088133Lit-BM-17:12147701
AKA11Q9UKA4GSK3BP49841YesYesHPRDHINTLit-BM-17SIGNORHPRD:12147701HINT:35271311Lit-BM-17:23602568HINT:12147701HINT:32707033SIGNOR:26088133Lit-BM-17:12147701

Protein Complex Composition (4)

4 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
AKAP11AKAP3ANKRD26GPR161PRKACGPRKAR1APRKAR1BO75969P10644P22612P31321Q8N6U8Q9UKA4Q9UPS80:0:0:0:0:0:0hu.MAP
AKAP11GSK3BPPP1CCUBCP0CG48P36873P49841Q9UKA41:1:1:1CompleatCFinderCompleat:HC8483
AKAP11CEP68PRKACBPRKAR1APRKAR1BP10644P22694P31321Q76N32Q9UKA40:0:0:0:0hu.MAP
AKAP11PPP1CBPRKAR2AP13861P62140Q9UKA41:1:1CompleatCFinderCompleat:HC4433

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry140689422
Sequence, Structure & Domains

Sequences

Length
1,901
Mass
210,512
Sequence
MATFRNNHMKTKASVRKSFSEDVFQSVKSLLQSQKELCSVTAEDCLQQDEHANLTEVTFLGFNEETDAAHIQDLAAVSLELPDILNSLHFCSLNENEIICMKNINKPLDISSDPLNQSHPSGMLCVMRVSPTSPRLRIDFIFSLLSKYATGIRYTLDTFLHQKHQLETTDEDDDDTNQSVSSIEDDFVTAFEHLEEEETSKPYNDGMNITVLRSQCDAASQTVTGHHLETHDLKILISSGQQKSLAKPSTSSVNVLGHKELPSVKTSVTTSISEPWTQRSFYRSSNASDKDSDLQKTFFSSSPAYSSESECSSPSPVIFLDEEGYQKSLKAKLELPKIPVMKDDIEDSDSEVSEFFDSFDQFDELEQTLETCLFNKDPVIGKSSQRKGHKHGKSCMNPQKFKFDRPALPANVRKPTPRKPESPYGNLCDAPDSPRPVKASREDSGLFSPIRSSAFSPLGGCTPAECFCQTDIGGDRIHENHDSVYYTYEDYAKSISCEVLGSVLRTHHTNTLSNINSIKHGENKTVTFKHGNLDQKNKSKNKSLMIKDSIQKFAADLVEKSFGSAFKDLQKGVSSCTNALYHLAIKLTSSVLQMAFDELRRQRAFSLKERAISGLANFLVSEALSNALKDLQYVKKQIFTNTVARFAADLAEELVFEGIMEVCQFSYPQTPASPQCGSFDFEDKVVKLYAKDLSESVIQEAFIELSQVDVTFTTKAAVSVSTDNIKYVSAESVVPSTQAVTFSPSFHNQAIMVTKPVQEYKKEYTVQQALFCTSGIVTSIPVPLAGSALLPYHISSTACQAKAHLSSDDSNSNGDSAQVHIATKNREEKAACLRNICLPSEHNPGNQNDFKPTNDDIEMQSSSKLPNDPAIISNFSAAVVHTIVNETLESMTSLEVTKMVDERTDYLTKSLKEKTPPFSHCDQAVLQCSEASSNKDMFADRLSKSIIKHSIDKSKSVIPNIDKNAVYKESLPVSGEESQLTPEKSPKFPDSQNQLTHCSLSAAKDCVPECKVSMVHGSSLETLPSCPAVTGQKSDLKESAKDQPLKKHNLNSTSLEALSFGQENPFPHSHTFSSTALTCVDGLHVEDKQKVRDRNVIPDTPPSTPLVPSRASSEWDIKKLTKKLKGELAKEFAPATPPSTPHNSSVGSLSENEQNTIEKEEFMLKLMRSLSEEVESSESGELPEVDVKSEHSGKKVQFAEALATHILSLATEMAASHLDNKIIQEPKVKNPCLNVQSQRSVSPTFLNPSDENLKTLCNFAGDLAAEVITEAEKIAKVRNCMLFKQKKNSCYADGDEDYKVEEKLDIEAVVHPREVDPFILSLPPSSCMSGLMYKYPSCESVTDEYAGHLIQILKQEGGNSELIMDQYANRLAYRSVKSGLQEAAKTTKVQCNSRMFPVPSSQVKTNKELLMFSNKEHHQEADKKRQSKRNEGYFCKNQTCERTLDPYRNEVSQLYSFSTSLVHSITKDAKEELTASLVGLPKSLTDSCLFEKSGYEEDNECHVTPELPKSLQPSSQNHRFYHSTGSLNGYGCGDNVVQAVEQYAKKVVDDTLELTLGSTVFRVSETTKSADRVTYAEKLSPLTGQACRYCDLKELHNCTGNSSQHFFRQGSLASSKPASNPKFSSRYQKSRIFHLSVPQIHVNLDKKAVLAEKIVAEAIEKAERELSSTSLAADSGIGQEGASFAESLATETMTAAVTNVGHAVSSSKEIEDFQSTESVSSQQMNLSIGDDSTGSWSNLSFEDEHQDESSSFHHLSESNGNSSSWSSLGLEGDLYEDNLSFPTSDSDGPDDKDEEHEDEVEGLGQDGKTLLITNIDMEPCTVDPQLRIILQWLIASEAEVAELYFHDSANKEFMLLSKQLQEKGWKVGDLLQAVLQYYEVMEKASSEERCKSLFDWLLENA

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 (7)
ENSG00000005249ENSG00000072062ENSG00000082701ENSG00000101558ENSG00000105723ENSG00000108946ENSG00000124164
Interaction Count
7
Interaction Dataset (3)
biogrid_bioplexbiogrid_opencellintact_biogrid
Supporting Publications1
PMIDTitleRelated sentences
38576002Therapy-induced senescent tumor cell-derived extracellular vesicles promote colorectal cancer progression through SERPINE1-mediated NF-κB p65 nuclear translocation.No related sentences available