Search results for HLA-DQA1

Showing 22 results out of 281

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Protein (4 results from a total of 160)

Identifier: R-HSA-197585
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: HLA-DQA1: P01909
Identifier: R-HSA-2130686
Species: Homo sapiens
Compartment: lysosomal membrane
Primary external reference: UniProt: HLA-DQA1: P01909
Identifier: R-HSA-2130529
Species: Homo sapiens
Compartment: endocytic vesicle membrane
Primary external reference: UniProt: HLA-DQA1: P01909
Identifier: R-HSA-2130595
Species: Homo sapiens
Compartment: clathrin-coated endocytic vesicle membrane
Primary external reference: UniProt: HLA-DQA1: P01909

DNA Sequence (4 results from a total of 18)

Identifier: R-HSA-9034233
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSEMBL:ENSG00000196735
Identifier: R-HSA-9034152
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSEMBL:ENSG00000206341
Identifier: R-HSA-8963114
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSEMBL:ENSG00000204632
Identifier: R-HSA-8963024
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSEMBL:ENSG00000234745

Complex (4 results from a total of 27)

Identifier: R-HSA-198912
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-199581
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-199567
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-199571
Species: Homo sapiens
Compartment: plasma membrane

Set (4 results from a total of 24)

Identifier: R-HSA-2213230
Species: Homo sapiens
Compartment: lysosomal membrane
Identifier: R-HSA-2272698
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-8943116
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Identifier: R-HSA-8943141
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane

Reaction (4 results from a total of 50)

Identifier: R-HSA-199579
Species: Homo sapiens
Compartment: plasma membrane
A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

Identifier: R-HSA-199576
Species: Homo sapiens
Compartment: plasma membrane
A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

Identifier: R-HSA-199566
Species: Homo sapiens
Compartment: plasma membrane
A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

Identifier: R-HSA-199558
Species: Homo sapiens
Compartment: plasma membrane
A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

Chemical Compound (1 results from a total of 1)

Identifier: R-ALL-1614594
Compartment: cytosol
Primary external reference: ChEBI: L-homolanthionine: 62856

Pathway (1 results from a total of 1)

Identifier: R-HSA-5619063
Species: Homo sapiens
The human gene SLC29A3 encodes the equilibrative nucleoside transporter 3 (ENT3). It is abundant in many tissues, especially the placenta and is localized intracellularly on the lysosomal membrane. SLC29A3 mediates the reversible transport of nucleosides as well as anticancer and antiviral agents such as cladribine, cordycepin, tubercidin and AZT. Defects in SLC29A3 can cause histiocytosis-lymphadenopathy plus syndrome (HLAS; MIM:602782), an autosomal recessive disorder characterised by combined features from 2 or more of four histiocytic disorders (Morgan et al. 2010, Colmenero et al. 2012, Young et al. 2013).
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