UniProt ID | LAIR1_HUMAN | |
---|---|---|
UniProt AC | Q6GTX8 | |
Protein Name | Leukocyte-associated immunoglobulin-like receptor 1 | |
Gene Name | LAIR1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 287 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . |
|
Protein Description | Functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. May also play its inhibitory role independently of SH2-containing phosphatases. Modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG production while inducing secretion of transforming growth factor beta. Down-regulates also IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits the differentiation of peripheral blood precursors towards dendritic cells.. | |
Protein Sequence | MSPHPTALLGLVLCLAQTIHTQEEDLPRPSISAEPGTVIPLGSHVTFVCRGPVGVQTFRLERESRSTYNDTEDVSQASPSESEARFRIDSVSEGNAGPYRCIYYKPPKWSEQSDYLELLVKETSGGPDSPDTEPGSSAGPTQRPSDNSHNEHAPASQGLKAEHLYILIGVSVVFLFCLLLLVLFCLHRQNQIKQGPPRSKDEEQKPQQRPDLAVDVLERTADKATVNGLPEKDRETDTSALAAGSSQEVTYAQLDHWALTQRTARAVSPQSTKPMAESITYAAVARH | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSPHPTALL ------CCCCHHHHH | 31.73 | 24043423 | |
6 | Phosphorylation | --MSPHPTALLGLVL --CCCCHHHHHHHHH | 27.23 | 24043423 | |
18 | Phosphorylation | LVLCLAQTIHTQEED HHHHHHHHHHCCCCC | 14.76 | 24043423 | |
21 | Phosphorylation | CLAQTIHTQEEDLPR HHHHHHHCCCCCCCC | 33.55 | 24043423 | |
32 | Phosphorylation | DLPRPSISAEPGTVI CCCCCCCCCCCCCEE | 30.80 | 22210691 | |
67 | Phosphorylation | LERESRSTYNDTEDV EEECCCCCCCCCCCH | 25.82 | 30576142 | |
68 | Phosphorylation | ERESRSTYNDTEDVS EECCCCCCCCCCCHH | 16.58 | 30576142 | |
69 | N-linked_Glycosylation | RESRSTYNDTEDVSQ ECCCCCCCCCCCHHH | 50.22 | 19349973 | |
69 | N-linked_Glycosylation | RESRSTYNDTEDVSQ ECCCCCCCCCCCHHH | 50.22 | 19349973 | |
80 | Phosphorylation | DVSQASPSESEARFR CHHHCCCCHHHHCEE | 51.78 | 30576142 | |
141 | O-linked_Glycosylation | PGSSAGPTQRPSDNS CCCCCCCCCCCCCCC | 35.97 | OGP | |
200 | Ubiquitination | KQGPPRSKDEEQKPQ HCCCCCCCCCCCCCC | 71.13 | - | |
205 | Ubiquitination | RSKDEEQKPQQRPDL CCCCCCCCCCCCCCH | 48.34 | - | |
245 | Phosphorylation | TSALAAGSSQEVTYA HHHHHCCCCCEEEHH | 24.91 | 27080861 | |
246 | Phosphorylation | SALAAGSSQEVTYAQ HHHHCCCCCEEEHHH | 29.46 | 27080861 | |
250 | Phosphorylation | AGSSQEVTYAQLDHW CCCCCEEEHHHHHHH | 16.64 | - | |
251 | Phosphorylation | GSSQEVTYAQLDHWA CCCCEEEHHHHHHHH | 9.49 | 22817900 | |
260 | Phosphorylation | QLDHWALTQRTARAV HHHHHHHHHHHHHCC | 14.30 | 26074081 | |
263 | Phosphorylation | HWALTQRTARAVSPQ HHHHHHHHHHCCCCC | 15.63 | 26074081 | |
268 | Phosphorylation | QRTARAVSPQSTKPM HHHHHCCCCCCCCCH | 19.08 | 22115753 | |
271 | Phosphorylation | ARAVSPQSTKPMAES HHCCCCCCCCCHHHH | 41.61 | 28464451 | |
272 | Phosphorylation | RAVSPQSTKPMAESI HCCCCCCCCCHHHHH | 33.64 | 28464451 | |
273 | Ubiquitination | AVSPQSTKPMAESIT CCCCCCCCCHHHHHH | 37.73 | - | |
278 | Phosphorylation | STKPMAESITYAAVA CCCCHHHHHHHHHHH | 15.64 | 28796482 | |
280 | Phosphorylation | KPMAESITYAAVARH CCHHHHHHHHHHHCC | 19.18 | 25072903 | |
281 | Phosphorylation | PMAESITYAAVARH- CHHHHHHHHHHHCC- | 7.29 | 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 LAIR1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LAIR1_HUMAN !! |
* 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 LAIR1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PTN11_HUMAN | PTPN11 | physical | 10903717 | |
PTN6_HUMAN | PTPN6 | physical | 10903717 | |
PTN6_HUMAN | PTPN6 | physical | 9285412 | |
PTN11_HUMAN | PTPN11 | physical | 9285412 | |
PTN6_HUMAN | PTPN6 | physical | 10764762 | |
A4_HUMAN | APP | physical | 21832049 | |
LAIR1_HUMAN | LAIR1 | physical | 21982860 | |
PTN6_HUMAN | PTPN6 | physical | 15703304 |
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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N-linked Glycosylation | |
Reference | PubMed |
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Identification and characterization of leukocyte-associated Ig-likereceptor-1 as a major anchor protein of tyrosine phosphatase SHP-1 inhematopoietic cells."; Xu M.-J., Zhao R., Zhao Z.J.; J. Biol. Chem. 275:17440-17446(2000). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION,PHOSPHORYLATION AT TYR-251 AND TYR-281, MUTAGENESIS OF TYR-251 ANDTYR-281, AND INTERACTION WITH PTPN6. |