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 0.60 |
Supporting publications (n) 16 | Transmembrane count | Protein classification Predicted intracellular proteins |
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.70High >= 0.60Medium >= 0.40Low >= 0.30Basic Information
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
Ensembl
Entrez Gene Symbol
Gene Synonym
PALM2-AKAP2
Gene Description
PALM2 and AKAP2 fusion
Chromosome
9
Position
109498325-110172512
Supporting publications (n)
16
EVMP confidence score
0.60
Fluorescence & Localization
Cell SpecificAdipocytes
Function & Pathway
Protein Function
Predicted intracellular proteins
Cellular Component (2)
Molecular Function
Biological Process (3)
Mediation Categories
Fusion and delivery mediation
Relations & Evidence6
Ligand-Receptor Signaling (5)
5 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | |||||
| intracellular | intracellular | OmniPath | |||||
| plasma_membrane | plasma_membrane | UniProt_location | |||||
| apical_cell_membrane | plasma_membrane | UniProt_location | |||||
| plasma_membrane | plasma_membrane | OmniPath |
Isolation & Detection Technology (1)
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationSize Exclusion Chromatography | Mass spectrometryWestern blotting | 1 | 38716512 |
Sequence, Structure & Domains
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
Supporting Publications16
| PMID | Title | Related sentences |
|---|---|---|
| 26775013 | Proteomic characterization of circulating extracellular vesicles identifies novel serum myeloma associated markers. | No related sentences available |
| 30071318 | Changes in the urinary extracellular vesicle proteome are associated with nephronophthisis-related ciliopathies. | No related sentences available |
| 31320591 | Exosomes regulate neurogenesis and circuit assembly. | No related sentences available |
| 31508500 | Proteomic profiling of extracellular vesicles allows for human breast cancer subtyping. | No related sentences available |
| 32795414 | Extracellular 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. |
| 33709510 | Unbiased proteomic profiling of host cell extracellular vesicle composition and dynamics upon HIV-1 infection. | No related sentences available |
| 38225453 | Deep proteomic analysis of obstetric antiphospholipid syndrome by DIA-MS of extracellular vesicle enriched fractions. | No related sentences available |
| 38490958 | Proteomic analysis of ascitic extracellular vesicles describes tumour microenvironment and predicts patient survival in ovarian cancer. | No related sentences available |
| 38731868 | The Deep Proteomics Approach Identified Extracellular Vesicular Proteins Correlated to Extracellular Matrix in Type One and Two Endometrial Cancer. | No related sentences available |
| 39290459 | Urinary extracellular vesicles as a monitoring tool for renal damage in patients not meeting criteria for chronic kidney disease. | No related sentences available |
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