UniProt ID | KI2L1_HUMAN | |
---|---|---|
UniProt AC | P43626 | |
Protein Name | Killer cell immunoglobulin-like receptor 2DL1 | |
Gene Name | KIR2DL1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 348 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein. |
|
Protein Description | Receptor on natural killer (NK) cells for some HLA-C alleles such as w4 and w6. Inhibits the activity of NK cells thus preventing cell lysis.. | |
Protein Sequence | MSLLVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGPLVKSEETVILQCWSDVMFEHFLLHREGMFNDTLRLIGEHHDGVSKANFSISRMTQDLAGTYRCYGSVTHSPYQVSAPSDPLDIVIIGLYEKPSLSAQPGPTVLAGENVTLSCSSRSSYDMYHLSREGEAHERRLPAGPKVNGTFQADFPLGPATHGGTYRCFGSFHDSPYEWSKSSDPLLVSVTGNPSNSWPSPTEPSSKTGNPRHLHILIGTSVVIILFILLFFLLHRWCSNKKNAAVMDQESAGNRTANSEDSDEQDPQEVTYTQLNHCVFTQRKITRPSQRPKTPPTDIIVYTELPNAESRSKVVSCP | |
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 |
---|---|---|---|---|---|
41 | Phosphorylation | HPGPLVKSEETVILQ CCCCCCCCCCEEEEH | 32.93 | - | |
44 | Phosphorylation | PLVKSEETVILQCWS CCCCCCCEEEEHHHH | 14.59 | - | |
51 | Phosphorylation | TVILQCWSDVMFEHF EEEEHHHHHHHHHHH | 28.14 | - | |
67 | N-linked_Glycosylation | LHREGMFNDTLRLIG HHCCCCCHHHHHHHH | 32.25 | UniProtKB CARBOHYD | |
84 | N-linked_Glycosylation | HDGVSKANFSISRMT CCCHHHCCEEHHHCC | 34.63 | UniProtKB CARBOHYD | |
86 | Phosphorylation | GVSKANFSISRMTQD CHHHCCEEHHHCCHH | 21.33 | - | |
97 | Phosphorylation | MTQDLAGTYRCYGSV CCHHCCCCEEEEEEE | 11.37 | - | |
144 | N-linked_Glycosylation | PTVLAGENVTLSCSS CEEECCCCEEEEECC | 31.02 | UniProtKB CARBOHYD | |
178 | N-linked_Glycosylation | LPAGPKVNGTFQADF CCCCCCCCCEEEECC | 50.33 | UniProtKB CARBOHYD | |
180 | Phosphorylation | AGPKVNGTFQADFPL CCCCCCCEEEECCCC | 13.84 | - | |
254 (in isoform 2) | Phosphorylation | - | 1.81 | 22210691 | |
255 (in isoform 2) | Phosphorylation | - | 1.41 | 22210691 | |
256 (in isoform 2) | Phosphorylation | - | 1.18 | 22210691 | |
281 | Phosphorylation | AAVMDQESAGNRTAN CEEECHHHCCCCCCC | 35.52 | - | |
289 | Phosphorylation | AGNRTANSEDSDEQD CCCCCCCCCCCCCCC | 40.07 | - | |
292 | Phosphorylation | RTANSEDSDEQDPQE CCCCCCCCCCCCCCC | 38.71 | - | |
302 | Phosphorylation | QDPQEVTYTQLNHCV CCCCCCHHHHHCCEE | 9.54 | 18083107 | |
311 | Phosphorylation | QLNHCVFTQRKITRP HHCCEEEECCCCCCH | 13.68 | - | |
319 | Phosphorylation | QRKITRPSQRPKTPP CCCCCCHHHCCCCCC | 35.21 | - | |
327 | Phosphorylation | QRPKTPPTDIIVYTE HCCCCCCCCEEEEEE | 40.82 | 22210691 | |
332 | Phosphorylation | PPTDIIVYTELPNAE CCCCEEEEEECCCCH | 5.54 | - | |
340 | Phosphorylation | TELPNAESRSKVVSC EECCCCHHHCCCCCC | 39.17 | 22210691 | |
342 | Phosphorylation | LPNAESRSKVVSCP- CCCCHHHCCCCCCC- | 38.80 | 22210691 |
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 KI2L1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KI2L1_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 KI2L1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
1C07_HUMAN | HLA-C | physical | 12454284 | |
1C07_HUMAN | HLA-C | physical | 11163076 | |
1C07_HUMAN | HLA-C | physical | 11323700 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
D10444 | Lirilumab (USAN/INN) | |||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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