SLAP2_MOUSE - dbPTM
SLAP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2N-myristoyl glycine------MGSLSSRGK
------CCCCCCCCC
36.98-
2Myristoylation------MGSLSSRGK
------CCCCCCCCC
36.9811891219
12PhosphorylationSSRGKTSSPSPSSSG
CCCCCCCCCCCCCCC
34.3330482847
16PhosphorylationKTSSPSPSSSGPDQE
CCCCCCCCCCCCCCC
41.2830482847
51PhosphorylationAGEQARLSLRLGEPL
HHHHHHHEEECCCCE
13.0924704852
136PhosphorylationYSLSVRLSRPASWDR
EEEEEECCCCCCHHH
26.1723140645
201AcetylationKLGPLPGKDTPPPVT
CCCCCCCCCCCCCCC
57.3919861615
201UbiquitinationKLGPLPGKDTPPPVT
CCCCCCCCCCCCCCC
57.39-
203PhosphorylationGPLPGKDTPPPVTVP
CCCCCCCCCCCCCCC
40.9825266776
208PhosphorylationKDTPPPVTVPTSSLN
CCCCCCCCCCCCCCC
26.9226745281
211PhosphorylationPPPVTVPTSSLNWKK
CCCCCCCCCCCCCEE
26.9826745281
212PhosphorylationPPVTVPTSSLNWKKL
CCCCCCCCCCCCEEC
27.1026745281
213PhosphorylationPVTVPTSSLNWKKLD
CCCCCCCCCCCEECC
28.3521082442

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLAP2_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZAP70_MOUSEZap70physical
12024036
CBL_MOUSECblphysical
12024036

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLAP2_MOUSE

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"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.

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