Protein detail
BI2L1
BAR/IMD domain-containing adapter protein 2-like 1 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1) (BAI1-associated protein 2-like protein 1) (Insulin receptor tyrosine kinase substrate)
Protein symbol BI2L1 | UniProt ID | EVMP score 0.38 |
Frequency 1 | Transmembrane count | Protein classification Predicted intracellular proteins |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
BAR/IMD domain-containing adapter protein 2-like 1 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1) (BAI1-associated protein 2-like protein 1) (Insulin receptor tyrosine kinase substrate)
Protein Class
Predicted intracellular proteins
Protein Function
Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym
IRTKS
Gene Description
BAR/IMD domain containing adaptor protein 2 like 1
Chromosome
7
Position
98291650-98401090
Frequency
1
EVMP Score
0.38
Fluorescence & Localization
Tissue SpecificintestineCell SpecificEnterocytesSingle-Nuclei Brain Specificendothelial cellBlood Cell Specificmemory B-cellSecretome LocationSecreted to bloodSecretome FunctionEnzyme
Function & Pathway
Protein Function
Predicted intracellular proteins
Cellular Component
Molecular Function
Biological Process
Reactome
Mediation Categories
Fusion and delivery mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
7 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| BAIAP2L1 | SRC | P12931 | Y | 439 | phosphorylation | PhosphoSiteSIGNOR | SIGNOR:21840312 |
| BAIAP2L1 | SRC | P12931 | Y | 156 | phosphorylation | PhosphoSiteSIGNOR | SIGNOR:21840312 |
| BAIAP2L1 | SRC | P12931 | Y | 163 | phosphorylation | RLIMS-P_ProtMapperPhosphoSiteSIGNORProtMapper | ProtMapper:21840312SIGNOR:21840312 |
| BAIAP2L1 | SRC | P12931 | Y | 274 | phosphorylation | PhosphoSiteSIGNOR | SIGNOR:21840312 |
| BAIAP2L1 | SRC | P12931 | Y | 293 | phosphorylation | PhosphoSiteSIGNOR | SIGNOR:21840312 |
| BAIAP2L1 | SRC | P12931 | Y | 37 | phosphorylation | PhosphoSiteSIGNOR | SIGNOR:21840312 |
| BAIAP2L1 | CHEK2 | O96017 | S | 331 | phosphorylation | Sparser_ProtMapperProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:28647685 |
Ligand-Receptor Signaling
4 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
Regulatory Interaction Network
2 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| SRC | P12931 | BI2L1 | Q9UHR4 | Yes | Yes | No | PhosphoSite_norefSIGNORiPTMnetProtMapperRLIMS-P_ProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | PhosphoSite:21840312ProtMapper:21840312SIGNOR:21840312 |
| CHK2 | O96017 | BI2L1 | Q9UHR4 | Yes | No | No | Sparser_ProtMapperProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:28647685PhosphoSite:28647685 |
Protein Complex Composition
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential Ultracentrifugation | Flow Cytometry | 1 | 38039414 |
Sequence, Structure & Domains
Sequences
Length
511
Mass
56,883
Sequence
MSRGPEEVNRLTESTYRNVMEQFNPGLRNLINLGKNYEKAVNAMILAGKAYYDGVAKIGEIATGSPVSTELGHVLIEISSTHKKLNESLDENFKKFHKEIIHELEKKIELDVKYMNATLKRYQTEHKNKLESLEKSQAELKKIRRKSQGSRNALKYEHKEIEYVETVTSRQSEIQKFIADGCKEALLEEKRRFCFLVDKHCGFANHIHYYHLQSAELLNSKLPRWQETCVDAIKVPEKIMNMIEEIKTPASTPVSGTPQASPMIERSNVVRKDYDTLSKCSPKMPPAPSGRAYTSPLIDMFNNPATAAPNSQRVNNSTGTSEDPSLQRSVSVATGLNMMKKQKVKTIFPHTAGSNKTLLSFAQGDVITLLIPEEKDGWLYGEHDVSKARGWFPSSYTKLLEENETEAVTVPTPSPTPVRSISTVNLSENSSVVIPPPDYLECLSMGAAADRRADSARTTSTFKAPASKPETAAPNDANGTAKPPFLSGENPFATVKLRPTVTNDRSAPIIR
3D Structural Models
Helix
394..396
Beta Strand
343..348; 356..358; 366..373; 378..386; 389..393; 397..400
3D Structure
NMR spectroscopy (2)
Domain & Motif Annotations
Compositional Bias
303..328; Polar residues
Coiled Coil
115..154
Domain (CC)
The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation (By similarity).
Domain (FT)
1..249; IMD; 339..402; SH3
Region
302..328; Disordered; 451..511; Disordered; 483..511; Binds F-actin