Protein detail
PHLB2
Pleckstrin homology-like domain family B member 2 (Protein LL5-beta)
Entry name PHLB2 | UniProt ID | EVMP confidence score 0.50 |
Supporting publications (n) 6 | Transmembrane count | Protein classification Predicted intracellular proteinsPredicted membrane proteins |
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.70High >= 0.60Medium >= 0.40Low >= 0.30Basic Information
Protein Names
Pleckstrin homology-like domain family B member 2 (Protein LL5-beta)
Protein Class (2)
Predicted intracellular proteinsPredicted membrane proteins
Protein Function
Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym (3)
FLJ21791LL5bLL5beta
Gene Description
Pleckstrin homology like domain family B member 2
Chromosome
3
Position
111732497-111976517
Supporting publications (n)
6
EVMP confidence score
0.50
Fluorescence & Localization
Tissue SpecificbrainCell SpecificBergmann gliaBlood Cell SpecificneutrophilBlood Lineage Specificgranulocytes
Function & Pathway
Protein Function
Predicted intracellular proteins
Cellular Component (9)
Molecular Function (2)
Biological Process (3)
Mediation Categories (2)
Adhesion and uptake mediationFusion and delivery mediation
Relations & Evidence8
Enzyme-Mediated Modification (1)
1 record.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| PHLDB2 | CSNK2A2 | P19784 | S | 489 | phosphorylation | KEA | KEA:17570479 |
Ligand-Receptor Signaling (4)
4 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | |||||
| intracellular | intracellular | GO_Intercell | |||||
| intracellular | intracellular | UniProt_location | |||||
| intracellular | intracellular | OmniPath |
Protein Complex Composition (2)
Isolation & Detection Technology (1)
Sequence, Structure & Domains
Sequences
Length
1,253
Mass
142,158
Sequence
MEEHSYIQKELDLQNGSLEEDSVVHSVENDSQNMMESLSPKKYSSSLRFKANGDYSGSYLTLSQPVPAKRSPSPLGTSVRSSPSLAKIQGSKQFSYDGTDKNIPMKPPTPLLNTTSSLSGYPLGRADFDHYTGRDSERALRLSEKPPYSKYSSRHKSHDNVYSLGGLEGRKASGSLLAMWNGSSLSDAGPPPISRSGAASMPSSPKQARKMSIQDSLALQPKLTRHKELASENINLRTRKYSSSSLSHMGAYSRSLPRLYRATENQLTPLSLPPRNSLGNSKRTKLGEKDLPHSVIDNDNYLNFSSLSSGALPYKTSASEGNPYVSSTLSVPASPRVARKMLLASTSSCASDDFDQASYVGTNPSHSLLAGESDRVFATRRNFSCGSVEFDEADLESLRQASGTPQPALRERKSSISSISGRDDLMDYHRRQREERLREQEMERLERQRLETILSLCAEYTKPDSRLSTGTTVEDVQKINKELEKLQLSDEESVFEEALMSPDTRYRCHRKDSLPDADLASCGSLSQSSASFFTPRSTRNDELLSDLTRTPPPPSSTFPKASSESSYLSILPKTPEGISEEQRSQELAAMEETRIVILNNLEELKQKIKDINDQMDESFRELDMECALLDGEQKSETTELMKEKEILDHLNRKIAELEKNIVGEKTKEKVKLDAEREKLERLQELYSEQKTQLDNCPESMREQLQQQLKRDADLLDVESKHFEDLEFQQLEHESRLDEEKENLTQQLLREVAEYQRNIVSRKEKISALKKQANHIVQQAQREQDHFVKEKNNLIMMLQREKENLCNLEKKYSSLSGGKGFPVNPNTLKEGYISVNEINEPCGNSTNLSPSTQFPADADAVATEPATAVLASQPQSKEHFRSLEERKKQHKEGLYLSDTLPRKKTTSSISPHFSSATMGRSITPKAHLPLGQSNSCGSVLPPSLAAMAKDSESRRMLRGYNHQQMSEGHRQKSEFYNRTASESNVYLNSFHYPDHSYKDQAFDTLSLDSSDSMETSISACSPDNISSASTSNIARIEEMERLLKQAHAEKTRLLESREREMEAKKRALEEEKRRREILEKRLQEETSQRQKLIEKEVKIRERQRAQARPLTRYLPVRKEDFDLRSHVETAGHNIDTCYHVSITEKTCRGFLIKMGGKIKTWKKRWFVFDRNKRTFSYYADKHETKLKGVIYFQAIEEVYYDHLKNANKSPNPLLTFSVKTHDRIYYMVAPSPEAMRIWMDVIVTGAEGYTHFLL
Alternative Products
Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q86SQ0-1; Sequence=Displayed; Name=2; IsoId=Q86SQ0-2; Sequence=VSP_016745; Name=3; IsoId=Q86SQ0-3; Sequence=VSP_016744, VSP_016745
Alternative Sequence
1; M -> MEEEDTKREVPKEDGVGDVQHFDSSKIM (in isoform 3); 668..710; Missing (in isoform 2 and isoform 3)
3D Structural Models
3D Structure
X-ray crystallography (3)
Domain & Motif Annotations
Compositional Bias
1..12; Basic and acidic residues; 29..43; Polar residues; 74..96; Polar residues; 126..144; Basic and acidic residues
Coiled Coil
584..696; 722..807; 1032..1098
Domain (CC)
The PH domain mediates the binding to phosphoinositides.
Domain (FT)
1143..1246; PH
Region
1..43; Disordered; 60..159; Disordered; 187..212; Disordered; 265..286; Disordered; 525..567; Disordered
Clinical Relevance
Supporting Publications6
| PMID | Title | Related sentences |
|---|---|---|
| 33613873 | Proteomic profile of melanoma cell-derived small extracellular vesicles in patients' plasma: a potential correlate of melanoma progression. | No related sentences available |
| 34265469 | Proteomic 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. |
| 35741093 | Proteomic and Metabolomic Profiles of T Cell-Derived Exosomes Isolated from Human Plasma. | No related sentences available |
| 36573687 | Proteomic and phosphoproteomic landscape of salivary extracellular vesicles to assess OSCC therapeutical outcomes. | No related sentences available |
| 39408670 | Proteomic Characterization of Corneal Epithelial and Stromal Cell-Derived Extracellular Vesicles. | No related sentences available |
| 39948040 | Quantitative proteomics identifies possible flow of metastatic cues between progressive stages of colorectal cancer via transfer of ceramide-dependent exosomal cargoes. | No related sentences available |