Protein detail

PLAK2

PALM2-AKAP2 fusion protein (A-kinase anchor protein 2) (AKAP-2) (AKAP-KL) (Paralemmin A kinase anchor protein) (Paralemmin-2) (Protein kinase A-anchoring protein 2) (PRKA2)

Entry name
PLAK2
UniProt ID
EVMP confidence score
0.72
Supporting publications (n)
17
Transmembrane count
Protein classification
Predicted 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
PALM2-AKAP2 fusion protein (A-kinase anchor protein 2) (AKAP-2) (AKAP-KL) (Paralemmin A kinase anchor protein) (Paralemmin-2) (Protein kinase A-anchoring protein 2) (PRKA2)
Protein Class
Predicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym
PALM2-AKAP2
Gene Description
PALM2 and AKAP2 fusion
Chromosome
9
Position
109498325-110172512
Supporting publications (n)
17
EVMP confidence score
0.72
Fluorescence & Localization1
Cell SpecificAdipocytes
Function & Pathway5
Protein Function
Predicted intracellular proteins
Mediation Categories
Fusion and delivery mediation
Relations & Evidence6

Ligand-Receptor Signaling (5)

5 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
plasma_membraneplasma_membraneUniProt_locationNoNoNoNoNo
apical_cell_membraneplasma_membraneUniProt_locationNoNoNoNoNo
plasma_membraneplasma_membraneOmniPathNoNoNoNoNo

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometryWestern blotting138716512
Sequence, Structure & Domains9

Sequences

Length
1,103
Mass
122,071
Sequence
MAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQKGFSSTDGDAVNYISSQLPDLPILCSRTAEPSPGQDGTSRAAGVGWENVLLKEGESASNATETSGPDMTIKKPPQLSEDDIWLKSEGDNYSATLLEPAASSLSPDHKNMEIEVSVAECKSVPGITSTPHPMDHPSAFYSPPHNGLLTDHHESLDNDVAREIRYLDEVLEANCCDSAVDGTYNGTSSPEPGAVVLVGGLSPPVHEATQPEPTERTASRQAPPHIELSNSSPDPMAEAERTNGHSPSQPRDALGDSLQVPVSPSSTTSSRCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEDDEHEKEQYCIRKVRPSEEMLELEKERRELIRSQAVKKNPGIAAKWWNPPQEKTIEEQLDEEHLESHKKYKERKERRAQQEQLLLQKQLQQQQQQPPSQLCTAPASSHERASMIDKAKEDIVTEQIDFSAARKQFQLMENSRQAVAKGQSTPRLFSIKPFYRPLGSVNSDKPLTNPRPPSVGGPPEDSGASAAKGQKSPGALETPSAAGSQGNTASQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDDDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETTNALQENSLADFSLPQTPQTDNPSEGRGEGVSKSFSDHGFYSPSSTLGDSPLVDDPLEYQAGLLVQNAIQQAIAEQVDKAVSKTSRDGAEQQGPEATVEEAEAAAFGSEKPQSMFEPPQVSSPVQEKRDVLPKILPAEDRALRERGPPQPLPAVQPSGPINMEETRPEGSYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVLQSTQSPRTKNAPSLPSRTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGTQRPKNLMQTLMEDYETHKSKRRERMDDSSYTSKLLSCKVTSEVLEATRVNRRKSALALRWEAGIYANQEEEDNE
Alternative Products
Event=Alternative splicing; Named isoforms=7; Name=3; Synonyms=PALM2-AKAP2; IsoId=Q9Y2D5-4; Sequence=Displayed; Name=1; IsoId=Q9Y2D5-3; Sequence=VSP_062014, VSP_062022; Name=2; IsoId=Q9Y2D5-5; Sequence=VSP_062015, VSP_062022; Name=4; IsoId=Q9Y2D5-6; Sequence=VSP_062022; Name=5; IsoId=Q9Y2D5-7; Sequence=VSP_062015; Name=6; Synonyms=Palm2, Paralemmin-2; IsoId=Q9Y2D5-8; Sequence=VSP_062018, VSP_062020, VSP_062021; Name=7; IsoId=Q9Y2D5-9; Sequence=VSP_062016, VSP_062017, VSP_062019
Alternative Sequence
1..231; Missing (in isoform 1); 1..194; MAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQKGFSSTDGDAVNYISSQLPDLPILCSRTAEPSPGQDGTSRAAGVGWENVLLKEGESASNATETSGPDMTIK -> MRWPQPGAAARLPPESPGPPESPGPPEREAAAARRWTGAEPQDCAPGSGRPE (in isoform 2 and isoform 5); 1; M -> MEM (in isoform 7); 132..377; DAVNYISSQLPDLPILCSRTAEPSPGQDGTSRAAGVGWENVLLKEGESASNATETSGPDMTIKKPPQLSEDDIWLKSEGDNYSATLLEPAASSLSPDHKNMEIEVSVAECKSVPGITSTPHPMDHPSAFYSPPHNGLLTDHHESLDNDVAREIRYLDEVLEANCCDSAVDGTYNGTSSPEPGAVVLVGGLSPPVHEATQPEPTERTASRQAPPHIELSNSSPDPMAEAERTNGHSPSQPRDALGDS -> AVYAMEINVEKDKQTGETKILSTSTIGPEGVHQKGVKVYDDGTKVVYEVRSGGTVVENGVHKLSTKDVEELIQKAGQSSLGGGHVSERTVIADGSLSHPKEHMLCKEAKLEMVHKSRKDHSSGNPGQQAQAPSAAGPEANLDQPVTMIFMGYQNIEDEEETKKVLGYDETIKAELVLIDEDDEKSLREKTVTDVSTIDGNAAELVSGRPVSDTTEPSSPEGKEESLATEPAPGTQKKKRCQCCVVM (in isoform 7); 166..630; GVGWENVLLKEGESASNATETSGPDMTIKKPPQLSEDDIWLKSEGDNYSATLLEPAASSLSPDHKNMEIEVSVAECKSVPGITSTPHPMDHPSAFYSPPHNGLLTDHHESLDNDVAREIRYLDEVLEANCCDSAVDGTYNGTSSPEPGAVVLVGGLSPPVHEATQPEPTERTASRQAPPHIELSNSSPDPMAEAERTNGHSPSQPRDALGDSLQVPVSPSSTTSSRCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEDDEHEKEQYCIRKVRPSEEMLELEKERRELIRSQAVKKNPGIAAKWWNPPQEKTIEEQLDEEHLESHKKYKERKERRAQQEQLLLQKQLQQQQQQPPSQLCTAPASSHERASMIDKAKEDIVTEQIDFSAARKQFQLMENSRQAVAKGQSTPRLFSIKPFYRPLGSVNSDKPLTNPRPPSVGGPPEDSGASAAKGQKSPGALET -> AVYAMEINVEKDKQTGETKILSTSTIGPEGVHQKGVKVYDDGTKVVYEVRSGGTVVENGVHKLSTKDVEELIQKAGQSSLGGGHVSERTVIADGSLSHPKEHMLCKEAKLEMVHKSRKDHSSGNPGQQAQA (in isoform 6); 378..1103; Missing (in isoform 7); 636..745; SQGNTASQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDDDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETTNALQ -> PEANLDQPVTMIFMGYQNIEDEEETKKVLGYDETIKAELVLIDEDDEKSLREKTVTDVSTIDGNAAELVSGRPVSDTTEPSSPEGKEESLATEPAPGTQKKKRCQCCVVM (in isoform 6); 746..1103; Missing (in isoform 6); 1058..1071; SYTSKLLSCKVTSE -> S (in isoform 2, isoform 1 and isoform 4)

Domain & Motif Annotations

Compositional Bias
179..189; Polar residues; 380..392; Low complexity; 490..505; Basic and acidic residues; 506..521; Low complexity; 522..531; Polar residues; 533..544; Basic and acidic residues; 566..579; Polar residues; 633..643; Polar residues; 745..763; Polar residues; 817..829; Basic and acidic residues; 865..886; Basic and acidic residues; 976..990; Polar residues
Coiled Coil
444..521; 941..979
Domain (CC)
The 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
178..197; Disordered; 304..396; Disordered; 483..544; Disordered; 566..662; Disordered; 745..794; Disordered; 797..810; PKA-RII subunit binding domain; 817..907; Disordered; 962..1035; Disordered
Clinical Relevance1
Supporting Publications16
PMIDTitleAbstract
39949490CRISPR-dCas9 Activation of TSG-6 in MSCs Modulates the Cargo of MSC-Derived Extracellular Vesicles and Attenuates Inflammatory Responses in Human Intervertebral Disc Cells In Vitro.No abstract available
40091455Potential Role of Menstrual Fluid-Derived Small Extracellular Vesicle Proteins in Endometriosis Pathogenesiss.No abstract available
40098346Toward Identification of Markers for Brain-Derived Extracellular Vesicles in Cerebrospinal Fluid: A Large-Scale, Unbiased Analysis Using Proximity Extension Assays.No abstract available
40311616Integrative proteomic profiling of tumor and plasma extracellular vesicles identifies a diagnostic biomarker panel for colorectal cancer.No abstract available
40928027Familial Alzheimer's disease mutation identifies novel role of SORLA in release of neurotrophic exosomes.No abstract available
41227296Extracellular Vesicles Profiling in Acute Myeloid Leukemia Cell Lines: A Proteomic Characterization.No abstract available
Page 2 of 2Previous