Literature summary for 7.4.2.14 extracted from

Momburg, F.; Roelse, J.; Howard, J.; Butcher, G.; Haemmerling, G.; Neefjes, J.
Selectivity of MHC-encoded peptide transporters from human, mouse and rat (1994), Nature, 367, 648-651 .

Search for more literature for 7.4.2.14

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of rat TAP1, TAP2a, and TAP2u in human TAP1-TAP2-deficient mutant cell line T2	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum membrane	-	Mus musculus	5789	-
endoplasmic reticulum membrane	-	Homo sapiens	5789	-
endoplasmic reticulum membrane	-	Rattus norvegicus	5789	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Mus musculus
Mg2+	required	Homo sapiens
Mg2+	required	Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + antigen peptide[side 1]	Mus musculus	-	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	Homo sapiens	-	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	Rattus norvegicus	-	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	Mus musculus C57B1/6	-	ADP + phosphate + antigen peptide[side 2]	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q03518 AND Q03519	TAP1 and TAP2 subunits	-
Mus musculus	P21958 AND P36371	subunits TAP1 and TAP2	-
Mus musculus C57B1/6	P21958 AND P36371	subunits TAP1 and TAP2	-
Rattus norvegicus	P36370 AND P36372	TAP1 and TAP2 subunits	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
B-lymphoblastoid cell	-	Homo sapiens	-
LCL-721 cell	-	Homo sapiens	-
RMA cell	-	Mus musculus	-
T-lymphocyte	-	Mus musculus	-
T1 cell	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + antigen peptide[side 1]	-	Mus musculus	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	-	Homo sapiens	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	-	Rattus norvegicus	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	the peptide series RYWANATRSX (R..X) and TVDNKTRXY (T..XY), are used, where X is one of the 20 amino acids indicated	Mus musculus	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	the peptide series RYWANATRSX (R..X) and TVDNKTRXY (T..XY), are used, where X is one of the 20 amino acids indicated	Homo sapiens	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	the peptide series RYWANATRSX (R..X) and TVDNKTRXY (T..XY), are used, where X is one of the 20 amino acids indicated	Rattus norvegicus	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	-	Mus musculus C57B1/6	ADP + phosphate + antigen peptide[side 2]	-	?
ATP + H2O + antigen peptide[side 1]	the peptide series RYWANATRSX (R..X) and TVDNKTRXY (T..XY), are used, where X is one of the 20 amino acids indicated	Mus musculus C57B1/6	ADP + phosphate + antigen peptide[side 2]	-	?
additional information	substitution of the N- and C-terminal and the penultimate amino-acid residues of model peptides to show that these residues influence the efficiency of transport. Human TAP translocates peptides with hydrophobic and basic C termini. The C-terminal amino acid of peptides is crucial for the binding to various MHC class I molecules. Substrate specificity, overview	Homo sapiens	?	-	-
additional information	substitution of the N- and C-terminal and the penultimate amino-acid residues of model peptides to show that these residues influence the efficiency of transport. Mouse TAP prefers peptides with hydrophobic C-termini. The C-terminal amino acid of peptides is crucial for the binding to various MHC class I molecules. Substrate specificity, overview	Mus musculus	?	-	-
additional information	substitution of the N- and C-terminal and the penultimate amino-acid residues of model peptides to show that these residues influence the efficiency of transport. The rat MHC class I molecule, RTI A, suggests a specific conveyance of peptides by rat TAPI-TAP2. Rat TAPa translocate peptides with hydrophobic and basic C termini, whereas rat TAPu prefers peptides with hydrophobic C-termini. The C-terminal amino acid of peptides is crucial for the binding to various MHC class I molecules. Substrate specificity, overview	Rattus norvegicus	?	-	-
additional information	substitution of the N- and C-terminal and the penultimate amino-acid residues of model peptides to show that these residues influence the efficiency of transport. Mouse TAP prefers peptides with hydrophobic C-termini. The C-terminal amino acid of peptides is crucial for the binding to various MHC class I molecules. Substrate specificity, overview	Mus musculus C57B1/6	?	-	-

Synonyms

Synonyms	Comment	Organism
TAP	-	Mus musculus
TAP	-	Homo sapiens
TAP	-	Rattus norvegicus
TAP1	-	Mus musculus
TAP1	-	Homo sapiens
TAP1	-	Rattus norvegicus
TAP2	-	Mus musculus
TAP2	-	Homo sapiens
TAP2	-	Rattus norvegicus
TAPI-TAP2	-	Mus musculus
TAPI-TAP2	-	Homo sapiens
TAPI-TAP2	-	Rattus norvegicus
TAPI-TAP2 transporter	-	Mus musculus
TAPI-TAP2 transporter	-	Homo sapiens
TAPI-TAP2 transporter	-	Rattus norvegicus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Mus musculus
ATP	-	Homo sapiens
ATP	-	Rattus norvegicus

General Information

General Information	Comment	Organism
evolution	human TAP and rat TAPa translocate peptides with hydrophobic and basic C termini, whereas mouse TAP and rat TAPu prefer peptides with hydrophobic C-termini. This pattern correlates with the predominant peptide binding profiles of mouse and human class I molecules	Mus musculus
evolution	human TAP and rat TAPa translocate peptides with hydrophobic and basic C termini, whereas mouse TAP and rat TAPu prefer peptides with hydrophobic C-termini. This pattern correlates with the predominant peptide binding profiles of mouse and human class I molecules	Homo sapiens
evolution	human TAP and rat TAPa translocate peptides with hydrophobic and basic C termini, whereas mouse TAP and rat TAPu prefer peptides with hydrophobic C-termini. This pattern correlates with the predominant peptide binding profiles of mouse and human class I molecules	Rattus norvegicus
malfunction	defects in the genes encoding TAPI or TAP2 account for impaired class I assembly and antigen presentation in several human cell lines	Homo sapiens
malfunction	defects in the genes encoding TAPI or TAP2 account for impaired class I assembly and antigen presentation in several rodent cell lines	Mus musculus
malfunction	defects in the genes encoding TAPI or TAP2 account for impaired class I assembly and antigen presentation in several rodent cell lines	Rattus norvegicus
physiological function	major histocompatibility complex (MHC) class I molecules present peptides from degraded intracellular antigens to CDS+ T-cells. These peptides are translocated in an ATP-dependent fashion into the lumen of the endoplasmic reticulum (ER) for binding to class I molecules by means of the MHC-encoded transporters associated with antigen processing (TAP). Subunits TAPI and TAP2 are members of a family of proteins containing an ATP-binding cassette and form heterodimers (TAP) in the ER membrane. Not only do MHC class I molecules select peptides according to their binding motifs, but also there is some pre-selection by the transporters	Mus musculus
physiological function	major histocompatibility complex (MHC) class I molecules present peptides from degraded intracellular antigens to CDS+ T-cells. These peptides are translocated in an ATP-dependent fashion into the lumen of the endoplasmic reticulum (ER) for binding to class I molecules by means of the MHC-encoded transporters associated with antigen processing (TAP). Subunits TAPI and TAP2 are members of a family of proteins containing an ATP-binding cassette and form heterodimers (TAP) in the ER membrane. Not only do MHC class I molecules select peptides according to their binding motifs, but also there is some pre-selection by the transporters	Homo sapiens
physiological function	major histocompatibility complex (MHC) class I molecules present peptides from degraded intracellular antigens to CDS+ T-cells. These peptides are translocated in an ATP-dependent fashion into the lumen of the endoplasmic reticulum (ER) for binding to class I molecules by means of the MHC-encoded transporters associated with antigen processing (TAP). Subunits TAPI and TAP2 are members of a family of proteins containing an ATP-binding cassette and form heterodimers (TAP) in the ER membrane. Not only do MHC class I molecules select peptides according to their binding motifs, but also there is some pre-selection by the transporters	Rattus norvegicus

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Release 2023.1 (January 2023)