SLAP2_HUMAN - dbPTM
SLAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLAP2_HUMAN
UniProt AC Q9H6Q3
Protein Name Src-like-adapter 2
Gene Name SLA2
Organism Homo sapiens (Human).
Sequence Length 261
Subcellular Localization Cytoplasm.
Isoform 1: Cell membrane. Cytoplasmic vesicle. Localized to the plasma membrane and intracellular vesicles, including late endosomal vesicles.
Isoform 2: Cytoplasm . May be cytoplasmic and is not localized to membranes.
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 MGSLPSRRKSLPSPSLSSSVQGQGPVTMEAERSKATAVALGSFPAGGPAELSLRLGEPLTIVSEDGDWWTVLSEVSGREYNIPSVHVAKVSHGWLYEGLSREKAEELLLLPGNPGGAFLIRESQTRRGSYSLSVRLSRPASWDRIRHYRIHCLDNGWLYISPRLTFPSLQALVDHYSELADDICCLLKEPCVLQRAGPLPGKDIPLPVTVQRTPLNWKELDSSLLFSEAATGEESLLSEGLRESLSFYISLNDEAVSLDDA
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------MGSLPSRRK
------CCCCCCCCC
37.58-
2Myristoylation------MGSLPSRRK
------CCCCCCCCC
37.5811696592
6Phosphorylation--MGSLPSRRKSLPS
--CCCCCCCCCCCCC
50.4323532336
10PhosphorylationSLPSRRKSLPSPSLS
CCCCCCCCCCCCCCC
43.6423401153
13PhosphorylationSRRKSLPSPSLSSSV
CCCCCCCCCCCCCCC
32.2029978859
15PhosphorylationRKSLPSPSLSSSVQG
CCCCCCCCCCCCCCC
45.2629978859
17PhosphorylationSLPSPSLSSSVQGQG
CCCCCCCCCCCCCCC
25.5529978859
18PhosphorylationLPSPSLSSSVQGQGP
CCCCCCCCCCCCCCC
39.5629978859
19PhosphorylationPSPSLSSSVQGQGPV
CCCCCCCCCCCCCCC
18.3229978859
27PhosphorylationVQGQGPVTMEAERSK
CCCCCCCCCEEEHHC
16.6626074081
33PhosphorylationVTMEAERSKATAVAL
CCCEEEHHCCEEEEE
20.3926074081
34UbiquitinationTMEAERSKATAVALG
CCEEEHHCCEEEEEC
56.8529967540
52PhosphorylationAGGPAELSLRLGEPL
CCCCCEEEEECCCCE
11.7124719451
103UbiquitinationYEGLSREKAEELLLL
HCCCCHHHHHHHEEC
61.05-
129PhosphorylationESQTRRGSYSLSVRL
ECCCCCCEEEEEEEE
15.1030108239
130PhosphorylationSQTRRGSYSLSVRLS
CCCCCCEEEEEEEEC
19.2230108239
131PhosphorylationQTRRGSYSLSVRLSR
CCCCCEEEEEEEECC
18.8330108239
133PhosphorylationRRGSYSLSVRLSRPA
CCCEEEEEEEECCCC
10.1524719451
159PhosphorylationCLDNGWLYISPRLTF
ECCCCEEEECCCCCC
7.8926074081
161PhosphorylationDNGWLYISPRLTFPS
CCCEEEECCCCCCHH
7.1526074081
202UbiquitinationRAGPLPGKDIPLPVT
ECCCCCCCCCCCCEE
51.0122505724

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLAP2_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD3Z_HUMANCD247physical
11891219
ZAP70_HUMANZAP70physical
11891219
CBL_HUMANCBLphysical
11891219
CBL_HUMANCBLphysical
17353186
CSF1_HUMANCSF1physical
17353186
CBL_HUMANCBLphysical
11696592
CBL_HUMANCBLphysical
16623714
CBL_HUMANCBLphysical
12527895

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLAP2_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Functional cloning of Src-like adapter protein-2 (SLAP-2), a novelinhibitor of antigen receptor signaling.";
Holland S.J., Liao X.C., Mendenhall M.K., Zhou X., Pardo J., Chu P.,Spencer C., Fu A.C., Sheng N., Yu P., Pali E., Nagin A., Shen M.,Yu S., Chan E., Wu X., Li C., Woisetschlager M., Aversa G.,Kolbinger F., Bennett M.K., Molineaux S., Luo Y., Payan D.G.,Mancebo H.S.Y., Wu J.;
J. Exp. Med. 194:1263-1276(2001).
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), CHARACTERIZATION, FUNCTION,MYRISTOYLATION AT GLY-2, INTERACTION WITH CBL, AND MUTAGENESIS OFGLY-2.

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