UniProt ID | SLAP2_MOUSE | |
---|---|---|
UniProt AC | Q8R4L0 | |
Protein Name | Src-like-adapter 2 | |
Gene Name | Sla2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 259 | |
Subcellular Localization | Cytoplasm. Cell membrane. Cytoplasmic vesicle. Late endosome. Localized to the plasma membrane and intracellular vesicles, including late endosomal vesicles. | |
Protein Description | Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins.. | |
Protein Sequence | MGSLSSRGKTSSPSPSSSGPDQEPVSMQPERHKVTAVALGSFPAGEQARLSLRLGEPLTIISEDGDWWTVQSEVSGREYHMPSVYVAKVAHGWLYEGLSREKAEELLLLPGNPGGAFLIRESQTRRGCYSLSVRLSRPASWDRIRHYRIQRLDNGWLYISPRLTFPSLHALVEHYSELADGICCPLREPCVLQKLGPLPGKDTPPPVTVPTSSLNWKKLDRSLLFLEAPASGEASLLSEGLRESLSSYISLAEDPLDDA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | N-myristoyl glycine | ------MGSLSSRGK ------CCCCCCCCC | 36.98 | - | |
2 | Myristoylation | ------MGSLSSRGK ------CCCCCCCCC | 36.98 | 11891219 | |
12 | Phosphorylation | SSRGKTSSPSPSSSG CCCCCCCCCCCCCCC | 34.33 | 30482847 | |
16 | Phosphorylation | KTSSPSPSSSGPDQE CCCCCCCCCCCCCCC | 41.28 | 30482847 | |
51 | Phosphorylation | AGEQARLSLRLGEPL HHHHHHHEEECCCCE | 13.09 | 24704852 | |
136 | Phosphorylation | YSLSVRLSRPASWDR EEEEEECCCCCCHHH | 26.17 | 23140645 | |
201 | Acetylation | KLGPLPGKDTPPPVT CCCCCCCCCCCCCCC | 57.39 | 19861615 | |
201 | Ubiquitination | KLGPLPGKDTPPPVT CCCCCCCCCCCCCCC | 57.39 | - | |
203 | Phosphorylation | GPLPGKDTPPPVTVP CCCCCCCCCCCCCCC | 40.98 | 25266776 | |
208 | Phosphorylation | KDTPPPVTVPTSSLN CCCCCCCCCCCCCCC | 26.92 | 26745281 | |
211 | Phosphorylation | PPPVTVPTSSLNWKK CCCCCCCCCCCCCEE | 26.98 | 26745281 | |
212 | Phosphorylation | PPVTVPTSSLNWKKL CCCCCCCCCCCCEEC | 27.10 | 26745281 | |
213 | Phosphorylation | PVTVPTSSLNWKKLD CCCCCCCCCCCEECC | 28.35 | 21082442 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of SLAP2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SLAP2_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of SLAP2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ZAP70_MOUSE | Zap70 | physical | 12024036 | |
CBL_MOUSE | Cbl | physical | 12024036 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Myristoylation | |
Reference | PubMed |
"A novel Src homology 2 domain-containing molecule, Src-like adapterprotein-2 (SLAP-2), which negatively regulates T cell receptorsignaling."; Pandey A., Ibarrola N., Kratchmarova I., Fernandez M.M.,Constantinescu S.N., Ohara O., Sawasdikosol S., Lodish H.F., Mann M.; J. Biol. Chem. 277:19131-19138(2002). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION,MYRISTOYLATION AT GLY-2, INTERACTION WITH CBL; ZAP70 AND CD3Z, ANDMUTAGENESIS OF GLY-2; PRO-82 AND ARG-120. | |
"Functional cooperation between c-Cbl and Src-like adaptor protein 2in the negative regulation of T-cell receptor signaling."; Loreto M.P., Berry D.M., McGlade C.J.; Mol. Cell. Biol. 22:4241-4255(2002). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE INITIATION,CHARACTERIZATION, FUNCTION, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION,INTERACTION WITH ZAP70 AND CBL, AND MUTAGENESIS OF GLY-2; MET-27 ANDARG-120. |