Protein detail

PRSR2

Proline and serine-rich protein 2

Entry name
PRSR2
UniProt ID
EVMP confidence score
0.38
Supporting publications (n)
1
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
Proline and serine-rich protein 2
Protein Class
Predicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym (2)
C10orf47MGC35403
Gene Description
Proline and serine rich 2
Chromosome
10
Position
11823339-11872277
Supporting publications (n)
1
EVMP confidence score
0.38
Fluorescence & Localization2
Cell SpecificColonocytesBlood Cell Specificneutrophil
Function & Pathway5
Protein Function
Predicted intracellular proteins
Canonical Pathways
M266 Pid ncadherin pathway
Mediation Categories
Other mediation
Relations & Evidence6

Enzyme-Mediated Modification (1)

1 record.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
PROSER2CHEK1O14757S43phosphorylationphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper

Ligand-Receptor Signaling (2)

2 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Protein Complex Composition (2)

2 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
PHF1PROSER2RDH13SLC25A43O43189Q86WR7Q8NBN7Q8WUT90:0:0:0hu.MAP2
PROSER2RDH13SLC25A43Q86WR7Q8NBN7Q8WUT90:0:0hu.MAP2

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry127605433
Sequence, Structure & Domains7

Sequences

Length
435
Mass
45,802
Sequence
MPVTHRKSDASDMNSDTSPSCRLRAFSRGGSLESRSSSSRSRSFTLDDESLKYLTHEEKDVLLFFEETIDSLDEDFEEPVLCDGGVCCLCSPSLEESTSSPSEPEDVIDLVQPAPGAGEAEGLPEGTQAAGPAPAGKEHRKQDAETPPPPDPPAPETLLAPPPLPSTPDPPRRELRAPSPPVEHPRLLRSVPTPLVMAQKISERMAGNEALSPTSPFREGRPGEWRTPAARGPRSGDPGPGPSHPAQPKAPRFPSNIIVTNGAAREPRRTLSRAAVSVQERRAQVLATIHGHAGAFPAAGDAGEGAPGGGSSPERVARGRGLPGPAESLRAGGQAPRGPALANGFPSAHEALKSAPSSFAPAGKSLCFRPGPALPSTRARQSFPGPRQPNGAQDWRRADSLPRPQGITVQFAGRGSSEEARREALRKLGLLRESS
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q86WR7-1; Sequence=Displayed; Name=2; IsoId=Q86WR7-2; Sequence=VSP_014955
Alternative Sequence
245..338; Missing (in isoform 2)

Domain & Motif Annotations

Compositional Bias
1..10; Basic and acidic residues; 11..20; Polar residues; 92..102; Low complexity; 113..126; Low complexity; 146..169; Pro residues; 228..237; Low complexity; 302..311; Gly residues
Region
1..22; Disordered; 92..276; Disordered; 295..420; Disordered
Clinical Relevance1
Antibody
Supporting Publications1
PMIDTitleAbstract
34265469Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer.Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes.