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Literature summary extracted from
- Assembly and function of the major histocompatibility complex (MHC) I peptide-loading complex are conserved across higher vertebrates (2014), J. Biol. Chem., 289, 33109-33117 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin | Coturnix japonica |
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin | Meleagris gallopavo |
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin. Anas platyrhynchos TAP1 lacking its correct 3'-region does not express. TAP2 from Anas platyrhynchos is coexpressed with Gallus gallus TAP1 | Anas platyrhynchos |
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin. from Anas platyrhynchos is coexpressed with Gallus gallus TAP1 | Gallus gallus |
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin. TAP1-deficient BRE169 and TAP2-deficient STF169 cells are transfected with mammalian TAP1 or TAP2, respectively, which does not lead either to an upregulation of MHC I surface expression. Transfection of TAP1-negative BRE169 cells with TAP1 genes of various mammalian species leads to an upregulation of MHC I complexes at the cell surface by more than one order of magnitude | Bos taurus |
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin. TAP1-deficient BRE169 and TAP2-deficient STF169 cells are transfected with mammalian TAP1 or TAP2, respectively. Transfection of TAP1-negative BRE169 cells with TAP1 genes of various mammalian species leads to a slight upregulation of MHC I complexes at the cell surface | Sus scrofa |
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin. TAP1-deficient BRE169 and TAP2-deficient STF169 cells are transfected with mammalian TAP1 or TAP2, respectively. Transfection of TAP1-negative BRE169 cells with TAP1 genes of various mammalian species leads to an upregulation of MHC I complexes at the cell surface by more than one order of magnitude | Mus musculus |
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin. TAP1-deficient BRE169 and TAP2-deficient STF169 cells are transfected with mammalian TAP1 or TAP2, respectively. Transfection of TAP1-negative BRE169 cells with TAP1 genes of various mammalian species leads to an upregulation of MHC I complexes at the cell surface by more than one order of magnitude | Rattus norvegicus |
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin. TAP1-deficient BRE169 and TAP2-deficient STF169 cells are transfected with mammalian TAP1 or TAP2, respectively. Transfection of TAP1-negative BRE169 cells with TAP1 genes of various mammalian species leads to an upregulation of MHC I complexes at the cell surface by more than one order of magnitude | Canis lupus familiaris |
| 7.4.2.14 | genes TAP1 and TAP2, DNA and amino acid sequence determination and analysis, recombinant expression from expression vectors pcDXc3YCH (TAP1) or pcDXc3CMS (TAP2) in HEK-293 cells. The plasmid pcDXc3YCH is generated by replacing eGFP and the streptavidin-binding peptide (SBP) with mVenus followed by a C8-tag (PRGPDRPEGIEE) and a His10-tag. In pcDXc3CMS, the region coding for eGFP is exchanged by mCerulean. The fluorescent proteins can be cleaved by human rhinovirus 3C protease. Coexpression of TAP1, TAP2, and tapasin. TAP1-deficient BRE169 and TAP2-deficient STF169 cells are transfected with mammalian TAP1 or TAP2, respectively. Transfection of TAP1-negative BRE169 cells with TAP1 genes of various mammalian species leads to an upregulation of MHC I complexes at the cell surface by more than one order of magnitude. Avian TAP complexes are functional but not across taxa | Homo sapiens |
| 7.4.2.14 | genes TAP1 and TAP2, recombinant expression of His-tagged wild-type and mutant TAP1 and TAP2 in Spodoptera frugiperda Sf21 insect cell microsomes via baculovirus transfection method | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 7.4.2.14 | K509M | site-directed mutagenesis of TAP2 conserved lysine residue in the Walker A motif of the nucleotide binding domain (NBD), the mutant TAP2 subunit is not significantly impaired for nucleotide binding compared to wild-type TAP2 | Homo sapiens |
| 7.4.2.14 | K544M | site-directed mutagenesis of TAP1 conserved lysine residue in the Walker A motif of the nucleotide binding domain (NBD), the mutant TAP1 subunit is significantly impaired for nucleotide binding relative to wild-type TAP1 | Homo sapiens |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK-293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. All combinations of avian TAP1 and TAP2 lead to an identical increase of peptide-loaded MHC I surface expression of TAP-deficient cells | Anas platyrhynchos |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK-293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. All combinations of avian TAP1 and TAP2 lead to an identical increase of peptide-loaded MHC I surface expression of TAP-deficient cells | Gallus gallus |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK-293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. All combinations of avian TAP1 and TAP2 lead to an identical increase of peptide-loaded MHC I surface expression of TAP-deficient cells | Meleagris gallopavo |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK-293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. All mammalian TAP1 and TAP2 restore MHC I surface expression in TAP-deficient cells. But expression of avian TAP2 and TAP1 in TAP1- and TAP2-deficient cells does not lead to up-regulation of MHC I surface expression | Homo sapiens |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK-293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. All mammalian TAP1 and TAP2 restore MHC I surface expression in TAP-deficient cells. But expression of avian TAP2 and TAP1 in TAP1- and TAP2-deficient cells does not lead to upregulation of MHC I surface expression | Mus musculus |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK-293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. All mammalian TAP1 and TAP2 restore MHC I surface expression in TAP-deficient cells. But expression of avian TAP2 and TAP1 in TAP1- and TAP2-deficient cells does not lead to upregulation of MHC I surface expression | Rattus norvegicus |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK-293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. All mammalian TAP1 and TAP2 restore MHC I surface expression in TAP-deficient cells. But expression of avian TAP2 and TAP1 in TAP1- and TAP2-deficient cells does not lead to upregulation of MHC I surface expression | Bos taurus |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK-293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. All mammalian TAP1 and TAP2 restore MHC I surface expression in TAP-deficient cells. But expression of avian TAP2 and TAP1 in TAP1- and TAP2-deficient cells does not lead to upregulation of MHC I surface expression | Sus scrofa |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK-293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. Chicken TAP1 is only functional in combination with avian TAP2 and not with endogenous or overexpressed human TAP2. All combinations of avian TAP1 and TAP2 lead to an identical increase of peptide-loaded MHC I surface expression of TAP-deficient cells | Coturnix japonica |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex, achieved by transfecting HEK293T cells with either mammalian or avian TAP1/TAP2 in various combinations with human tapasin. TAP complexes are subsequently tandem-affinity purified. All mammalian TAP1 and TAP2 restore MHC I surface expression in TAP-deficient cells. But expression of avian TAP2 and TAP1 in TAP1- and TAP2-deficient cells does not lead to upregulation of MHC I surface expression | Canis lupus familiaris |
| 7.4.2.14 | additional information | the mutant TAP1 subunit is significantly impaired for nucleotide binding relative to wild-type TAP1. The identical mutation in TAP2 does not significantly impair nucleotide binding relative to wild-type TAP2. Both mutants, in combination with their wild-type partners, can bind peptides. Since the mutant TAP1 is significantly impaired for nucleotide binding, these results indicate that nucleotide binding to TAP1 is not a requirement for peptide binding to TAP complexes. Peptide translocation is undetectable for TAP1-TAP2(K509M) complexes, but low levels of translocation are detectable with TAP1(K544M)-TAP2 complexes. These results suggest an impairment in nucleotide hydrolysis by TAP complexes containing either mutant TAP subunit and indicate that the presence of one intact TAP nucleotide binding domain (NBD) is insufficient for efficient catalysis of peptide translocation | Homo sapiens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.4.2.14 | additional information | - |
additional information | peptide binding and translocation kinetics of recombinant wild-type and mutant TAP1 and TAP2 with fluorescence-labeled substrate peptides | Homo sapiens |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Mus musculus | 5789 | - |
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Homo sapiens | 5789 | - |
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Rattus norvegicus | 5789 | - |
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Bos taurus | 5789 | - |
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Sus scrofa | 5789 | - |
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Canis lupus familiaris | 5789 | - |
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Anas platyrhynchos | 5789 | - |
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Coturnix japonica | 5789 | - |
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Gallus gallus | 5789 | - |
| 7.4.2.14 | endoplasmic reticulum membrane | - |
Meleagris gallopavo | 5789 | - |
| 7.4.2.14 | microsome | - |
Homo sapiens | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.4.2.14 | Mg2+ | required | Mus musculus |  |
| 7.4.2.14 | Mg2+ | required | Homo sapiens | |
| 7.4.2.14 | Mg2+ | required | Rattus norvegicus | |
| 7.4.2.14 | Mg2+ | required | Bos taurus | |
| 7.4.2.14 | Mg2+ | required | Sus scrofa | |
| 7.4.2.14 | Mg2+ | required | Canis lupus familiaris | |
| 7.4.2.14 | Mg2+ | required | Anas platyrhynchos | |
| 7.4.2.14 | Mg2+ | required | Coturnix japonica | |
| 7.4.2.14 | Mg2+ | required | Gallus gallus | |
| 7.4.2.14 | Mg2+ | required | Meleagris gallopavo | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Mus musculus | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Homo sapiens | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Rattus norvegicus | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Bos taurus | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Sus scrofa | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Canis lupus familiaris | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Anas platyrhynchos | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Coturnix japonica | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Gallus gallus | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | Meleagris gallopavo | - |
ADP + phosphate + antigen peptide[side 2] | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.4.2.14 | Anas platyrhynchos | Q2VQZ1 AND Q6JWQ3 | TAP1 and TAP2 subunits | - |
| 7.4.2.14 | Bos taurus | F1MVY8 AND Q32S33 | TAP1 and TAP2 subunits | - |
| 7.4.2.14 | Canis lupus familiaris | Q5W414 AND Q5W417 | TAP1 and TAP2 subunits | - |
| 7.4.2.14 | Coturnix japonica | Q76LI9 AND Q9PWI8 | TAP1 and TAP2 subunits; Coturnix coturnix japonica | - |
| 7.4.2.14 | Gallus gallus | B5BSK4 AND B5BSD5 | TAP1 and TAP2 subunits | - |
| 7.4.2.14 | Homo sapiens | Q03518 AND Q03519 | TAP1 and TAP2 subunits | - |
| 7.4.2.14 | Meleagris gallopavo | B1N1D9 AND B1N1E0 | TAP1 and TAP2 subunits | - |
| 7.4.2.14 | Mus musculus | P21958 AND P36371 | subunits TAP1 and TAP2 | - |
| 7.4.2.14 | Rattus norvegicus | P36370 AND P36372 | TAP1 and TAP2 subunits | - |
| 7.4.2.14 | Sus scrofa | A5D9J3 AND A5D9J7 | TAP1 and TAP2 subunits | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.4.2.14 | recombinant TAP1, TAP2, and tapasin are copurified by tandem affinity chromatography, firstly via the streptavidin-binding tag of TAP2 and specific elution with biotin, and secondly via the C8-tag fused to TAP1 | Homo sapiens |
| 7.4.2.14 | recombinant wild-type and mutant TAP1 and TAP2 from Spodoptera frugiperda Sf21 insect cells by microsome preparation and isolation | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 7.4.2.14 | T-lymphocyte | - |
Mus musculus | - |
| 7.4.2.14 | T-lymphocyte | - |
Homo sapiens | - |
| 7.4.2.14 | T-lymphocyte | - |
Rattus norvegicus | - |
| 7.4.2.14 | T-lymphocyte | - |
Bos taurus | - |
| 7.4.2.14 | T-lymphocyte | - |
Sus scrofa | - |
| 7.4.2.14 | T-lymphocyte | - |
Canis lupus familiaris | - |
| 7.4.2.14 | T-lymphocyte | - |
Anas platyrhynchos | - |
| 7.4.2.14 | T-lymphocyte | - |
Coturnix japonica | - |
| 7.4.2.14 | T-lymphocyte | - |
Gallus gallus | - |
| 7.4.2.14 | T-lymphocyte | - |
Meleagris gallopavo | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Mus musculus | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Homo sapiens | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Rattus norvegicus | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Bos taurus | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Sus scrofa | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Canis lupus familiaris | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Anas platyrhynchos | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Coturnix japonica | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Gallus gallus | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + antigen peptide[side 1] | - |
Meleagris gallopavo | ADP + phosphate + antigen peptide[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + RRYNASTEL[side 1] | synthetic peptide RRYNASTEL, fluorescence-labeled using 5-iodoacetamidofluorescein | Homo sapiens | ADP + phosphate + RRYNASTEL[side 2] | - |
? | |
| 7.4.2.14 | ATP + H2O + RRYQKCTEL[side 1] | synthetic peptide RRYQKCTEL, fluorescence-labeled using 5-iodoacetamidofluorescein | Homo sapiens | ADP + phosphate + RRYQKCTEL[side 2] | - |
? | |
| 7.4.2.14 | additional information | addition of exogenous ATP is required for peptide translocation by TAP, and translocation is not supported by nonhydrolyzable ATP analogues or ADP | Homo sapiens | ? | - |
- |
|
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.4.2.14 | heterodimer | - |
Mus musculus |
| 7.4.2.14 | heterodimer | - |
Homo sapiens |
| 7.4.2.14 | heterodimer | - |
Rattus norvegicus |
| 7.4.2.14 | heterodimer | - |
Bos taurus |
| 7.4.2.14 | heterodimer | - |
Sus scrofa |
| 7.4.2.14 | heterodimer | - |
Canis lupus familiaris |
| 7.4.2.14 | heterodimer | - |
Anas platyrhynchos |
| 7.4.2.14 | heterodimer | - |
Coturnix japonica |
| 7.4.2.14 | heterodimer | - |
Gallus gallus |
| 7.4.2.14 | heterodimer | - |
Meleagris gallopavo |
| 7.4.2.14 | More | TAP1 and TAP2 each comprise one membrane-spanning region with several membrane-spanning segments and one cytosolic nucleotide binding domain (NBD) | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.4.2.14 | TAP | - |
Mus musculus |
| 7.4.2.14 | TAP | - |
Homo sapiens |
| 7.4.2.14 | TAP | - |
Rattus norvegicus |
| 7.4.2.14 | TAP | - |
Bos taurus |
| 7.4.2.14 | TAP | - |
Sus scrofa |
| 7.4.2.14 | TAP | - |
Canis lupus familiaris |
| 7.4.2.14 | TAP | - |
Anas platyrhynchos |
| 7.4.2.14 | TAP | - |
Coturnix japonica |
| 7.4.2.14 | TAP | - |
Gallus gallus |
| 7.4.2.14 | TAP | - |
Meleagris gallopavo |
| 7.4.2.14 | TAP1 | - |
Mus musculus |
| 7.4.2.14 | TAP1 | - |
Homo sapiens |
| 7.4.2.14 | TAP1 | - |
Rattus norvegicus |
| 7.4.2.14 | TAP1 | - |
Bos taurus |
| 7.4.2.14 | TAP1 | - |
Sus scrofa |
| 7.4.2.14 | TAP1 | - |
Canis lupus familiaris |
| 7.4.2.14 | TAP1 | - |
Anas platyrhynchos |
| 7.4.2.14 | TAP1 | - |
Coturnix japonica |
| 7.4.2.14 | TAP1 | - |
Gallus gallus |
| 7.4.2.14 | TAP1 | - |
Meleagris gallopavo |
| 7.4.2.14 | TAP2 | - |
Mus musculus |
| 7.4.2.14 | TAP2 | - |
Homo sapiens |
| 7.4.2.14 | TAP2 | - |
Rattus norvegicus |
| 7.4.2.14 | TAP2 | - |
Bos taurus |
| 7.4.2.14 | TAP2 | - |
Sus scrofa |
| 7.4.2.14 | TAP2 | - |
Canis lupus familiaris |
| 7.4.2.14 | TAP2 | - |
Anas platyrhynchos |
| 7.4.2.14 | TAP2 | - |
Coturnix japonica |
| 7.4.2.14 | TAP2 | - |
Gallus gallus |
| 7.4.2.14 | TAP2 | - |
Meleagris gallopavo |
| 7.4.2.14 | transporter associated with antigen processing | - |
Mus musculus |
| 7.4.2.14 | transporter associated with antigen processing | - |
Homo sapiens |
| 7.4.2.14 | transporter associated with antigen processing | - |
Rattus norvegicus |
| 7.4.2.14 | transporter associated with antigen processing | - |
Bos taurus |
| 7.4.2.14 | transporter associated with antigen processing | - |
Sus scrofa |
| 7.4.2.14 | transporter associated with antigen processing | - |
Canis lupus familiaris |
| 7.4.2.14 | transporter associated with antigen processing | - |
Anas platyrhynchos |
| 7.4.2.14 | transporter associated with antigen processing | - |
Coturnix japonica |
| 7.4.2.14 | transporter associated with antigen processing | - |
Gallus gallus |
| 7.4.2.14 | transporter associated with antigen processing | - |
Meleagris gallopavo |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.4.2.14 | 37 | - |
assay at | Homo sapiens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.4.2.14 | 7.3 | 7.4 | assay at | Homo sapiens |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.4.2.14 | ATP | - |
Mus musculus | |
| 7.4.2.14 | ATP | - |
Homo sapiens | |
| 7.4.2.14 | ATP | - |
Rattus norvegicus | |
| 7.4.2.14 | ATP | - |
Bos taurus | |
| 7.4.2.14 | ATP | - |
Sus scrofa | |
| 7.4.2.14 | ATP | - |
Canis lupus familiaris | |
| 7.4.2.14 | ATP | - |
Anas platyrhynchos | |
| 7.4.2.14 | ATP | - |
Coturnix japonica | |
| 7.4.2.14 | ATP | - |
Gallus gallus | |
| 7.4.2.14 | ATP | - |
Meleagris gallopavo | |
| 7.4.2.14 | ATP | addition of exogenous ATP is required for peptide translocation by TAP | Homo sapiens | |
| 7.4.2.14 | additional information | translocation is not supported by nonhydrolyzable ATP analogues or ADP | Homo sapiens |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 7.4.2.14 | Homo sapiens | tapasin has been shown to enhance the expression level of TAP1 and increase peptide transport by TAP complexes. But tapasin is not required for peptide binding by TAP1-TAP2 complexes or for translocation per se, since TAP1-TAP2 complexes expressed heterologously in insect cells can bind and transport peptides | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 7.4.2.14 | evolution | TAP is a member of the ATP-binding cassette (ABC) family of transmembrane transport proteins | Homo sapiens |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa. The transmembrane domain (TMD)0 of avian TAP2 is essential and sufficient for mediating the interaction with human tapasin, because all avian TAP1 subunits sequenced so far lack a TMD0, in analogy to human core-TAP1. The dimerization interface between avian and human TAP1 and TAP2 is complementary over a long distance in evolution. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates. Avian TAP complexes are functional but not across taxa | Anas platyrhynchos |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa. The transmembrane domain (TMD)0 of avian TAP2 is essential and sufficient for mediating the interaction with human tapasin, because all avian TAP1 subunits sequenced so far lack a TMD0, in analogy to human core-TAP1. The dimerization interface between avian and human TAP1 and TAP2 is complementary over a long distance in evolution. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates. Avian TAP complexes are functional but not across taxa | Gallus gallus |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa. The transmembrane domain (TMD)0 of avian TAP2 is essential and sufficient for mediating the interaction with human tapasin, because all avian TAP1 subunits sequenced so far lack a TMD0, in analogy to human core-TAP1. The dimerization interface between avian and human TAP1 and TAP2 is complementary over a long distance in evolution. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates. Avian TAP complexes are functional but not across taxa | Meleagris gallopavo |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa. The transmembrane domain (TMD)0 of avian TAP2 is essential and sufficient for mediating the interaction with human tapasin, because all avian TAP1 subunits sequenced so far lack a TMD0, in analogy to human core-TAP1. The dimerization interface between avian and human TAP1 and TAP2 is complementary over a long distance in evolution. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates. Avian TAP complexes are functional but not across taxa. Chicken TAP1 is only functional in combination with avian TAP2 and not with endogenous or overexpressed human TAP2 | Coturnix japonica |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates | Mus musculus |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates | Rattus norvegicus |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates | Bos taurus |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates | Sus scrofa |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates | Canis lupus familiaris |
| 7.4.2.14 | evolution | the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. The dimerization interface between avian and human TAP1 and TAP2 is complementary over a long distance in evolution. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates | Homo sapiens |
| 7.4.2.14 | malfunction | the mutant TAP1 subunit is significantly impaired for nucleotide binding relative to wild-type TAP1. The identical mutation in TAP2 does not significantly impair nucleotide binding relative to wild-type TAP2. Both mutants, in combination with their wild-type partners, can bind peptides. Since the mutant TAP1 is significantly impaired for nucleotide binding, these results indicate that nucleotide binding to TAP1 is not a requirement for peptide binding to TAP complexes. Peptide translocation is undetectable for TAP1-TAP2(K509M) complexes, but low levels of translocation are detectable with TAP1(K544M)-TAP2 complexes. These results suggest an impairment in nucleotide hydrolysis by TAP complexes containing either mutant TAP subunit and indicate that the presence of one intact TAP nucleotide binding domain (NBD) is insufficient for efficient catalysis of peptide translocation | Homo sapiens |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex | Mus musculus |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex | Homo sapiens |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex | Rattus norvegicus |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex | Bos taurus |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex | Sus scrofa |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex | Canis lupus familiaris |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa | Anas platyrhynchos |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa | Gallus gallus |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa | Meleagris gallopavo |
| 7.4.2.14 | additional information | recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa, but chicken TAP1 is only functional in combination with avian TAP2 and not with endogenous or overexpressed human TAP2 | Coturnix japonica |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Mus musculus |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Homo sapiens |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Rattus norvegicus |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Bos taurus |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Sus scrofa |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Canis lupus familiaris |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Anas platyrhynchos |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Coturnix japonica |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Gallus gallus |
| 7.4.2.14 | physiological function | antigen presentation to cytotoxic T-lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHCI molecules in the endoplasmic reticulum, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin | Meleagris gallopavo |
| 7.4.2.14 | physiological function | the transporter associated with antigen processing (TAP) is a critical component of the major histocompatibility complex (MHC) class I antigen presentation. TAP functions to translocate peptides from the cytosol to the ER. Binding of peptides to newly synthesized MHC class I molecules in the endoplasmic reticulum (ER) stabilizes the MHC class I heterodimer and allows transit of MHC class I-peptide complexes to the cell surface for immune surveillance by T cells. Two structurally related subunits of the TAP transporter, TAP1 and TAP2, form a complex on the ER membrane that is necessary and sufficient for peptide translocation from the cytosol into the ER. The cytosolic face of TAP1zTAP2 complexes contains a binding site for peptides | Homo sapiens |
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