UniProt ID | SLAF1_HUMAN | |
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UniProt AC | Q13291 | |
Protein Name | Signaling lymphocytic activation molecule | |
Gene Name | SLAMF1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 335 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein. Present on the surface of B-cells and T-cells. Located at the plasma membrane contacts between neighboring T-cells (PubMed:11806999). Isoform 3: Secreted . Isoform 4: Cell membrane . Overexp |
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Protein Description | Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. SLAMF1-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAMF1 signaling seem to exist: one depending on SH2D1A (and perhaps SH2D1B) and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates. Initially it has been proposed that association with SH2D1A prevents binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2. [PubMed: 11806999 However, signaling is also regulated by SH2D1A which can simultaneously interact with and recruit FYN which subsequently phosphorylates and activates SLAMF1] | |
Protein Sequence | MDPKGLLSLTFVLFLSLAFGASYGTGGRMMNCPKILRQLGSKVLLPLTYERINKSMNKSIHIVVTMAKSLENSVENKIVSLDPSEAGPPRYLGDRYKFYLENLTLGIRESRKEDEGWYLMTLEKNVSVQRFCLQLRLYEQVSTPEIKVLNKTQENGTCTLILGCTVEKGDHVAYSWSEKAGTHPLNPANSSHLLSLTLGPQHADNIYICTVSNPISNNSQTFSPWPGCRTDPSETKPWAVYAGLLGGVIMILIMVVILQLRRRGKTNHYQTTVEKKSLTIYAQVQKPGPLQKKLDSFPAQDPCTTIYVAATEPVPESVQETNSITVYASVTLPES | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
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53 | N-linked_Glycosylation | PLTYERINKSMNKSI ECCHHHHHHHCCCCE | 36.25 | UniProtKB CARBOHYD | |
57 | N-linked_Glycosylation | ERINKSMNKSIHIVV HHHHHHCCCCEEEEE | 41.85 | UniProtKB CARBOHYD | |
73 | Phosphorylation | MAKSLENSVENKIVS CHHHHCHHHHCCEEE | 22.79 | - | |
102 | N-linked_Glycosylation | RYKFYLENLTLGIRE HHHHHHHHEEEEEEE | 35.41 | UniProtKB CARBOHYD | |
118 | Phosphorylation | RKEDEGWYLMTLEKN CCCCCCEEEEEEECC | 9.46 | 28555341 | |
121 | Phosphorylation | DEGWYLMTLEKNVSV CCCEEEEEEECCCCH | 29.21 | 28555341 | |
125 | N-linked_Glycosylation | YLMTLEKNVSVQRFC EEEEEECCCCHHHHH | 23.17 | UniProtKB CARBOHYD | |
147 | Ubiquitination | QVSTPEIKVLNKTQE CCCCCCEEEEEECCC | 38.72 | 25015289 | |
150 | N-linked_Glycosylation | TPEIKVLNKTQENGT CCCEEEEEECCCCCE | 48.60 | UniProtKB CARBOHYD | |
153 | Ubiquitination | IKVLNKTQENGTCTL EEEEEECCCCCEEEE | 43.71 | 25015289 | |
155 | N-linked_Glycosylation | VLNKTQENGTCTLIL EEEECCCCCEEEEEE | 41.05 | UniProtKB CARBOHYD | |
189 | N-linked_Glycosylation | THPLNPANSSHLLSL CCCCCCCCCCCEEEE | 45.35 | UniProtKB CARBOHYD | |
217 | N-linked_Glycosylation | TVSNPISNNSQTFSP EECCCCCCCCCCCCC | 53.55 | UniProtKB CARBOHYD | |
256 | Ubiquitination | IMILIMVVILQLRRR HHHHHHHHHHHHHHC | 1.68 | 25015289 | |
262 | Ubiquitination | VVILQLRRRGKTNHY HHHHHHHHCCCCCCC | 61.36 | 25015289 | |
266 | Phosphorylation | QLRRRGKTNHYQTTV HHHHCCCCCCCEEEE | 30.01 | 29978859 | |
269 | Phosphorylation | RRGKTNHYQTTVEKK HCCCCCCCEEEEEEC | 15.04 | 29978859 | |
271 | Phosphorylation | GKTNHYQTTVEKKSL CCCCCCEEEEEECEE | 26.16 | 30622161 | |
272 | Phosphorylation | KTNHYQTTVEKKSLT CCCCCEEEEEECEEE | 15.90 | 30622161 | |
277 | Phosphorylation | QTTVEKKSLTIYAQV EEEEEECEEEEEEEE | 41.64 | 30108239 | |
279 | Phosphorylation | TVEKKSLTIYAQVQK EEEECEEEEEEEECC | 21.02 | 30108239 | |
281 | Phosphorylation | EKKSLTIYAQVQKPG EECEEEEEEEECCCC | 5.92 | 11806999 | |
286 | Ubiquitination | TIYAQVQKPGPLQKK EEEEEECCCCCHHHH | 53.75 | 25015289 | |
292 | Ubiquitination | QKPGPLQKKLDSFPA CCCCCHHHHHCCCCC | 64.09 | 25015289 | |
307 | Phosphorylation | QDPCTTIYVAATEPV CCCCCEEEEEECCCC | 5.07 | 11806999 | |
327 | Phosphorylation | ETNSITVYASVTLPE CCCCEEEEEEEECCC | 5.63 | 11806999 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
281 | Y | Phosphorylation | Kinase | FYN | P06241 | Uniprot |
307 | Y | Phosphorylation | Kinase | FYN | P06241 | Uniprot |
307 | Y | Phosphorylation | Kinase | LCK | P06239 | PSP |
327 | Y | Phosphorylation | Kinase | FYN | P06241 | Uniprot |
327 | Y | Phosphorylation | Kinase | LYN | P07948 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | MARCHF9 | Q86YJ5 | PMID:19457934 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of SLAF1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of SLAF1_HUMAN !! |
Kegg Disease | ||||||
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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. |
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Phosphorylation | |
Reference | PubMed |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, AND MASSSPECTROMETRY. |