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
26775013Proteomic characterization of circulating extracellular vesicles identifies novel serum myeloma associated markers.No abstract available
30071318Changes in the urinary extracellular vesicle proteome are associated with nephronophthisis-related ciliopathies.No abstract available
31320591Exosomes regulate neurogenesis and circuit assembly.No abstract available
31508500Proteomic profiling of extracellular vesicles allows for human breast cancer subtyping.No abstract available
32795414Extracellular Vesicle and Particle Biomarkers Define Multiple Human Cancers.Among traditional exosome markers, CD9, HSPA8, ALIX, and HSP90AB1 represent pan-EVP markers, while ACTB, MSN, and RAP1B are novel pan-EVP markers.
33709510Unbiased proteomic profiling of host cell extracellular vesicle composition and dynamics upon HIV-1 infection.No abstract available
38225453Deep proteomic analysis of obstetric antiphospholipid syndrome by DIA-MS of extracellular vesicle enriched fractions.No abstract available
38490958Proteomic analysis of ascitic extracellular vesicles describes tumour microenvironment and predicts patient survival in ovarian cancer.No abstract available
38731868The Deep Proteomics Approach Identified Extracellular Vesicular Proteins Correlated to Extracellular Matrix in Type One and Two Endometrial Cancer.No abstract available
39290459Urinary extracellular vesicles as a monitoring tool for renal damage in patients not meeting criteria for chronic kidney disease.No abstract available
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