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8-azido-ATP + H2O + antigen peptide[side 1]
8-azido-ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + AARAVFLAL[side 1]
ADP + phosphate + AARAVFLAL[side 2]
-
-
-
?
ATP + H2O + acetyI-FAPGNYPAL[side 1]
ADP + phosphate + acetyI-FAPGNYPAL[side 2]
ATP + H2O + AKAYAAEEF[side 1]
ADP + phosphate + AKAYAAEEF[side 2]
synthesis and use of the photopeptide analogue EEF.1-HSAB (EEF.1 = AKAYAAEEF)
-
-
?
ATP + H2O + ANATKVSAKQALEAKQAVSAKQLEY peptide[side 1]
ADP + phosphate + ANATKVSAKQALEAKQAVSAKQLEY peptide[side 2]
ATP + H2O + ANATKVSKQLEKQVSKQLEY peptide[side 1]
ADP + phosphate + ANATKVSKQLEKQVSKQLEY peptide[side 2]
ATP + H2O + ANATKVSKQLEVSKQLEY peptide[side 1]
ADP + phosphate + ANATKVSKQLEVSKQLEY peptide[side 2]
ATP + H2O + ANATKVSLEKQLEY peptide[side 1]
ADP + phosphate + ANATKVSLEKQLEY peptide[side 2]
ATP + H2O + ANATKVSLEVSKQLEY peptide[side 1]
ADP + phosphate + ANATKVSLEVSKQLEY peptide[side 2]
ATP + H2O + ANATKVSLEVSY peptide[side 1]
ADP + phosphate + ANATKVSLEVSY peptide[side 2]
ATP + H2O + ANATKVSLEY peptide[side 1]
ADP + phosphate + ANATKVSLEY peptide[side 2]
ATP + H2O + ANATKVSY peptide[side 1]
ADP + phosphate + ANATKVSY peptide[side 2]
ATP + H2O + ANATKY peptide[side 1]
ADP + phosphate + ANATKY peptide[side 2]
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
ATP + H2O + APGNYPAL[side 1]
ADP + phosphate + APGNYPAL[side 2]
ATP + H2O + ASN9-6h-Gal2 glycopeptide[side 1]
ADP + phosphate + ASN9-6h-Gal2 glycopeptide[side 2]
ATP + H2O + AYGLDFYIL[side 1]
ADP + phosphate + AYGLDFYIL[side 2]
-
-
-
?
ATP + H2O + EADPTGHSY[side 1]
ADP + phosphate + EADPTGHSY[side 2]
-
-
-
?
ATP + H2O + EVDPIGHLY[side 1]
ADP + phosphate + EVDPIGHLY[side 2]
-
-
-
?
ATP + H2O + FAP9-7h-Gal2 glycopeptide[side 1]
ADP + phosphate + FAP9-7h-Gal2 glycopeptide[side 2]
ATP + H2O + FAPGNYPADamide[side 1]
ADP + phosphate + FAPGNYPADamide[side 2]
ATP + H2O + GNYPAL[side 1]
ADP + phosphate + GNYPAL[side 2]
-
-
-
?
ATP + H2O + IYLGPFSPNVTL[side 1]
ADP + phosphate + IYLGPFSPNVTL[side 2]
-
-
-
?
ATP + H2O + LLDGTATLRL[side 1]
ADP + phosphate + LLDGTATLRL[side 2]
-
-
-
?
ATP + H2O + MLLAVLYCL[side 1]
ADP + phosphate + MLLAVLYCL[side 2]
-
-
-
?
ATP + H2O + peptide ASLSTFQQMWlSKQEYDESGPSI[side 1]
ADP + phosphate + peptide ASLSTFQQMWlSKQEYDESGPSI[side 2]
ATP + H2O + peptide ASLSTFQQM[side 1]
ADP + phosphate + peptide ASLSTFQQM[side 2]
ATP + H2O + peptide ASLSTF[side 1]
ADP + phosphate + peptide ASLSTF[side 2]
ATP + H2O + peptide ASNENMETM[side 1]
ADP + phosphate + peptide ASNENMETM[side 2]
-
-
-
?
ATP + H2O + peptide ESlINFEKL[side 1]
ADP + phosphate + peptide ESlINFEKL[side 2]
-
-
-
?
ATP + H2O + peptide FAPGNYPAL[side 1]
ADP + phosphate + peptide FAPGNYPAL[side 2]
labeled Sendal virus nucleoprotein peptide, FAPGNYPAL 324332
-
-
?
ATP + H2O + peptide FAPGNYPAL[side 1]
ADP + phosphate + peptide LKEFNIISE[side 2]
-
-
-
?
ATP + H2O + peptide KKYQKSTEL[side 1]
ADP + phosphate + peptide KKYQKSTEL[side 2]
-
-
-
?
ATP + H2O + peptide MQQFTSLSA[side 1]
ADP + phosphate + peptide MQQFTSLSA[side 2]
-
-
-
?
ATP + H2O + peptide SIINFEKL[side 1]
ADP + phosphate + peptide SIINFEKL[side 2]
-
-
-
?
ATP + H2O + peptide TYQRTRALV[side 1]
ADP + phosphate + peptide TYQRTRALV[side 2]
-
-
-
?
ATP + H2O + peptide VAITRIEQQLSPFPFDL[side 1]
ADP + phosphate + peptide VAITRIEQQLSPFPFDL[side 2]
-
-
-
?
ATP + H2O + peptide WlSKQEYDESGPSI[side 1]
ADP + phosphate + peptide WlSKQEYDESGPSI[side 2]
-
-
-
?
ATP + H2O + PGNYPAL[side 1]
ADP + phosphate + PGNYPAL[side 2]
-
-
-
?
ATP + H2O + QVPLRPMTYK[side 1]
ADP + phosphate + QVPLRPMTYK[side 2]
ATP + H2O + R9LQK peptide[side 1]
ADP + phosphate + R9LQK peptide[side 2]
radiolabeled peptide substrate
-
-
?
ATP + H2O + RGY8-6h-Gal2 glycopeptide[side 1]
ADP + phosphate + RGY8-6h-Gal2 glycopeptide[side 2]
ATP + H2O + RRYNASTEL[side 1]
ADP + phosphate + RRYNASTEL[side 2]
synthetic peptide RRYNASTEL, fluorescence-labeled using 5-iodoacetamidofluorescein
-
-
?
ATP + H2O + RRYQKCTEL[side 1]
ADP + phosphate + RRYQKCTEL[side 2]
synthetic peptide RRYQKCTEL, fluorescence-labeled using 5-iodoacetamidofluorescein
-
-
?
ATP + H2O + RRYQNSTEL peptide[side 1]
ADP + phosphate + RRYQNSTEL peptide[side 2]
radiolabeled peptide substrate
-
-
?
ATP + H2O + RRYQNSTEL[side 1]
ADP + phosphate + RRYQNSTEL[side 2]
-
-
-
?
ATP + H2O + RYWANATRI peptide[side 1]
ADP + phosphate + RYWANATRI peptide[side 2]
radiolabeled peptide substrate
-
-
?
ATP + H2O + SAYGEPRKL[side 1]
ADP + phosphate + SAYGEPRKL[side 2]
-
-
-
?
ATP + H2O + SGVI 2-Gal2 glycopeptide[side 1]
ADP + phosphate + SGVI 2-Gal2 glycopeptide[side 2]
specificity of glycopeptide binding to MHC I Db
-
-
?
ATP + H2O + TNKRGQIDRFGQY peptide[side 1]
ADP + phosphate + TNKRGQIDRFGQY peptide[side 2]
ATP + H2O + TNKRGQRFIDIDRFGQY peptide[side 1]
ADP + phosphate + TNKRGQRFIDIDRFGQY peptide[side 2]
ATP + H2O + TNKRGQRFIDRFGQY peptide[side 1]
ADP + phosphate + TNKRGQRFIDRFGQY peptide[side 2]
ATP + H2O + TNKRGQY peptide[side 1]
ADP + phosphate + TNKRGQY peptide[side 2]
ATP + H2O + TNKRIDGQY peptide[side 1]
ADP + phosphate + TNKRIDGQY peptide[side 2]
ATP + H2O + TNKRIDRFGQY peptide[side 1]
ADP + phosphate + TNKRIDRFGQY peptide[side 2]
ATP + H2O + TNKRRFAGQARFAIDAIDRFGQY peptide[side 1]
ADP + phosphate + TNKRRFAGQARFAIDAIDRFGQY peptide[side 2]
ATP + H2O + TNKRRFGQRFIDIDRFGQY peptide[side 1]
ADP + phosphate + TNKRRFGQRFIDIDRFGQY peptide[side 2]
ATP + H2O + TNKRRFSAGQASRFSAIDASlDSARFGQY peptide[side 1]
ADP + phosphate + TNKRRFSAGQASRFSAIDASlDSARFGQY peptide[side 2]
ATP + H2O + TNKRY peptide[side 1]
ADP + phosphate + TNKRY peptide[side 2]
ATP + H2O + TNKTRIDGQY peptide[side 1]
ADP + phosphate + TNKTRIDGQY peptide[side 2]
radiolabeled peptide substrate
-
-
?
ATP + H2O + TNKTRRFGQRFIDIDRFGQY peptide[side 1]
ADP + phosphate + TNKTRRFGQRFIDIDRFGQY peptide[side 2]
ATP + H2O + TVDNKTRYE[side 1]
ADP + phosphate + TVDNKTRYE[side 2]
-
-
-
?
ATP + H2O + TYQIkTRALV[side 1]
ADP + phosphate + TYQIkTRALV[side 2]
-
-
-
?
ATP + H2O + TYQRTRALV[side 1]
ADP + phosphate + TYQRTRALV[side 2]
a synthetic peptide
-
-
?
ATP + H2O + YLEPGPVTA[side 1]
ADP + phosphate + YLEPGPVTA[side 2]
-
-
-
?
ATP + H2O + YMDGTMSQV[side 1]
ADP + phosphate + YMDGTMSQV[side 2]
-
-
-
?
ATP + H2O + YMNGTMSQV[side 1]
ADP + phosphate + YMNGTMSQV[side 2]
-
-
-
?
GTP + H2O + antigen peptide[side 1]
GDP + phosphate + antigen peptide[side 2]
less than 40% activity compared to ATP
-
-
?
additional information
?
-
ATP + H2O + acetyI-FAPGNYPAL[side 1]
ADP + phosphate + acetyI-FAPGNYPAL[side 2]
-
-
-
?
ATP + H2O + acetyI-FAPGNYPAL[side 1]
ADP + phosphate + acetyI-FAPGNYPAL[side 2]
-
-
-
?
ATP + H2O + ANATKVSAKQALEAKQAVSAKQLEY peptide[side 1]
ADP + phosphate + ANATKVSAKQALEAKQAVSAKQLEY peptide[side 2]
-
-
-
?
ATP + H2O + ANATKVSAKQALEAKQAVSAKQLEY peptide[side 1]
ADP + phosphate + ANATKVSAKQALEAKQAVSAKQLEY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + ANATKVSKQLEKQVSKQLEY peptide[side 1]
ADP + phosphate + ANATKVSKQLEKQVSKQLEY peptide[side 2]
-
-
-
?
ATP + H2O + ANATKVSKQLEKQVSKQLEY peptide[side 1]
ADP + phosphate + ANATKVSKQLEKQVSKQLEY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + ANATKVSKQLEVSKQLEY peptide[side 1]
ADP + phosphate + ANATKVSKQLEVSKQLEY peptide[side 2]
-
-
-
?
ATP + H2O + ANATKVSKQLEVSKQLEY peptide[side 1]
ADP + phosphate + ANATKVSKQLEVSKQLEY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + ANATKVSLEKQLEY peptide[side 1]
ADP + phosphate + ANATKVSLEKQLEY peptide[side 2]
-
-
-
?
ATP + H2O + ANATKVSLEKQLEY peptide[side 1]
ADP + phosphate + ANATKVSLEKQLEY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + ANATKVSLEVSKQLEY peptide[side 1]
ADP + phosphate + ANATKVSLEVSKQLEY peptide[side 2]
-
-
-
?
ATP + H2O + ANATKVSLEVSKQLEY peptide[side 1]
ADP + phosphate + ANATKVSLEVSKQLEY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + ANATKVSLEVSY peptide[side 1]
ADP + phosphate + ANATKVSLEVSY peptide[side 2]
-
-
-
?
ATP + H2O + ANATKVSLEVSY peptide[side 1]
ADP + phosphate + ANATKVSLEVSY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + ANATKVSLEY peptide[side 1]
ADP + phosphate + ANATKVSLEY peptide[side 2]
-
-
-
?
ATP + H2O + ANATKVSLEY peptide[side 1]
ADP + phosphate + ANATKVSLEY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + ANATKVSY peptide[side 1]
ADP + phosphate + ANATKVSY peptide[side 2]
-
-
-
?
ATP + H2O + ANATKVSY peptide[side 1]
ADP + phosphate + ANATKVSY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + ANATKY peptide[side 1]
ADP + phosphate + ANATKY peptide[side 2]
-
-
-
?
ATP + H2O + ANATKY peptide[side 1]
ADP + phosphate + ANATKY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
Q2VQZ1; Q6JWQ3
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
F1MVY8; Q32S33
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
Q5W414; Q5W417
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
Q76LI9; Q9PWI8
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
B5BSK4; B5BSD5
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
the peptide series RYWANATRSX (R..X) and TVDNKTRXY (T..XY), are used, where X is one of the 20 amino acids indicated
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
B1N1D9; B1N1E0
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
the peptide series RYWANATRSX (R..X) and TVDNKTRXY (T..XY), are used, where X is one of the 20 amino acids indicated
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
the peptide series RYWANATRSX (R..X) and TVDNKTRXY (T..XY), are used, where X is one of the 20 amino acids indicated
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
P36370; P36372
the peptide series RYWANATRSX (R..X) and TVDNKTRXY (T..XY), are used, where X is one of the 20 amino acids indicated
-
-
?
ATP + H2O + antigen peptide[side 1]
ADP + phosphate + antigen peptide[side 2]
A5D9J3; A5D9J7
-
-
-
?
ATP + H2O + APGNYPAL[side 1]
ADP + phosphate + APGNYPAL[side 2]
-
-
-
?
ATP + H2O + APGNYPAL[side 1]
ADP + phosphate + APGNYPAL[side 2]
-
-
-
?
ATP + H2O + ASN9-6h-Gal2 glycopeptide[side 1]
ADP + phosphate + ASN9-6h-Gal2 glycopeptide[side 2]
specificity of glycopeptide binding to MHC I Db
-
-
?
ATP + H2O + ASN9-6h-Gal2 glycopeptide[side 1]
ADP + phosphate + ASN9-6h-Gal2 glycopeptide[side 2]
specificity of glycopeptide binding to MHC I Db
-
-
?
ATP + H2O + FAP9-7h-Gal2 glycopeptide[side 1]
ADP + phosphate + FAP9-7h-Gal2 glycopeptide[side 2]
specificity of glycopeptide binding to MHC I Kb
-
-
?
ATP + H2O + FAP9-7h-Gal2 glycopeptide[side 1]
ADP + phosphate + FAP9-7h-Gal2 glycopeptide[side 2]
specificity of glycopeptide binding to MHC I Kb
-
-
?
ATP + H2O + FAPGNYPADamide[side 1]
ADP + phosphate + FAPGNYPADamide[side 2]
-
-
-
?
ATP + H2O + FAPGNYPADamide[side 1]
ADP + phosphate + FAPGNYPADamide[side 2]
-
-
-
?
ATP + H2O + peptide ASLSTFQQMWlSKQEYDESGPSI[side 1]
ADP + phosphate + peptide ASLSTFQQMWlSKQEYDESGPSI[side 2]
-
-
-
?
ATP + H2O + peptide ASLSTFQQMWlSKQEYDESGPSI[side 1]
ADP + phosphate + peptide ASLSTFQQMWlSKQEYDESGPSI[side 2]
-
-
-
?
ATP + H2O + peptide ASLSTFQQM[side 1]
ADP + phosphate + peptide ASLSTFQQM[side 2]
-
-
-
?
ATP + H2O + peptide ASLSTFQQM[side 1]
ADP + phosphate + peptide ASLSTFQQM[side 2]
-
-
-
?
ATP + H2O + peptide ASLSTF[side 1]
ADP + phosphate + peptide ASLSTF[side 2]
-
-
-
?
ATP + H2O + peptide ASLSTF[side 1]
ADP + phosphate + peptide ASLSTF[side 2]
-
-
-
?
ATP + H2O + QVPLRPMTYK[side 1]
ADP + phosphate + QVPLRPMTYK[side 2]
-
-
-
?
ATP + H2O + QVPLRPMTYK[side 1]
ADP + phosphate + QVPLRPMTYK[side 2]
synthesis and use of the photopeptide nef7B-N-hydroxysuccinimidyl-4-azidobenzoate (HSAB) (nef7B = QVPLRPMTYK)
-
-
?
ATP + H2O + RGY8-6h-Gal2 glycopeptide[side 1]
ADP + phosphate + RGY8-6h-Gal2 glycopeptide[side 2]
specificity of glycopeptide binding to MHC I Kb
-
-
?
ATP + H2O + RGY8-6h-Gal2 glycopeptide[side 1]
ADP + phosphate + RGY8-6h-Gal2 glycopeptide[side 2]
specificity of glycopeptide binding to MHC I Kb
-
-
?
ATP + H2O + TNKRGQIDRFGQY peptide[side 1]
ADP + phosphate + TNKRGQIDRFGQY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRGQIDRFGQY peptide[side 1]
ADP + phosphate + TNKRGQIDRFGQY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKRGQRFIDIDRFGQY peptide[side 1]
ADP + phosphate + TNKRGQRFIDIDRFGQY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRGQRFIDIDRFGQY peptide[side 1]
ADP + phosphate + TNKRGQRFIDIDRFGQY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKRGQRFIDRFGQY peptide[side 1]
ADP + phosphate + TNKRGQRFIDRFGQY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRGQRFIDRFGQY peptide[side 1]
ADP + phosphate + TNKRGQRFIDRFGQY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKRGQY peptide[side 1]
ADP + phosphate + TNKRGQY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRGQY peptide[side 1]
ADP + phosphate + TNKRGQY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKRIDGQY peptide[side 1]
ADP + phosphate + TNKRIDGQY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRIDGQY peptide[side 1]
ADP + phosphate + TNKRIDGQY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKRIDRFGQY peptide[side 1]
ADP + phosphate + TNKRIDRFGQY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRIDRFGQY peptide[side 1]
ADP + phosphate + TNKRIDRFGQY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKRRFAGQARFAIDAIDRFGQY peptide[side 1]
ADP + phosphate + TNKRRFAGQARFAIDAIDRFGQY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRRFAGQARFAIDAIDRFGQY peptide[side 1]
ADP + phosphate + TNKRRFAGQARFAIDAIDRFGQY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKRRFGQRFIDIDRFGQY peptide[side 1]
ADP + phosphate + TNKRRFGQRFIDIDRFGQY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRRFGQRFIDIDRFGQY peptide[side 1]
ADP + phosphate + TNKRRFGQRFIDIDRFGQY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKRRFSAGQASRFSAIDASlDSARFGQY peptide[side 1]
ADP + phosphate + TNKRRFSAGQASRFSAIDASlDSARFGQY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRRFSAGQASRFSAIDASlDSARFGQY peptide[side 1]
ADP + phosphate + TNKRRFSAGQASRFSAIDASlDSARFGQY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKRY peptide[side 1]
ADP + phosphate + TNKRY peptide[side 2]
-
-
-
?
ATP + H2O + TNKRY peptide[side 1]
ADP + phosphate + TNKRY peptide[side 2]
P36370; P36372
-
-
-
?
ATP + H2O + TNKTRRFGQRFIDIDRFGQY peptide[side 1]
ADP + phosphate + TNKTRRFGQRFIDIDRFGQY peptide[side 2]
-
-
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?
ATP + H2O + TNKTRRFGQRFIDIDRFGQY peptide[side 1]
ADP + phosphate + TNKTRRFGQRFIDIDRFGQY peptide[side 2]
P36370; P36372
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additional information
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no activity with CTP and UTP
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additional information
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no activity with CTP and UTP
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additional information
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some melanoma-specific epitopes are good substrates for TAP, while others are poor substrates for TAP. One of the epitopes derived from tyrosinase is transported into the endoplasmic reticulum (ER) in spite of being a poor competitor for reporter peptide transport and for peptide binding. Transport of melanoma epitopes which posess N-linked glycosylation sites, substrate specificity, overview
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additional information
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TAP transports proteasomal degradation products into the ER lumen for loading onto MHC class I molecules. Analysis of the translocation machinery is the peptide-binding event and its allosteric coupling with ATP hydrolysis, overview
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additional information
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addition of exogenous ATP is required for peptide translocation by TAP, and translocation is not supported by nonhydrolyzable ATP analogues or ADP
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additional information
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ATP hydrolysis is coupled to peptide binding and transport. Photolabeling preferentially occurred at TAP2. Peptide-induced BeFx trapping of TAP1 and TAP2, and the peptide-induced BeFx trapping directly reflects ATP hydrolysis during the catalytic cycle of TAP. Peptide transport and nucleotide binding, but not peptide binding, is inhibited in the BeFx-trapped state of TAP
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additional information
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cross-linkable peptides are designed as derivatives of peptides known to be efficiently transported by TAP synthesized by F-moc chemistry using an AMS multiple synthesizer, cross-linking assays with Sf9 cells infected with baculoviruses encoding human TAP1 and TAP2 and peptide binding epitope sequence determination, detailed overview
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additional information
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for human transporter TAP, the most efficient ATP-dependent transport is observed for peptides with 8-12 amino acid length. Hexamers and longer peptides of up to 40 amino acids are also translocated, albeit less efficiently. TAP is selective for the primary sequence of peptide substrates with particular importance of the C-terminal residue of the peptide. TAP contains specific interaction sites for peptides. Peptide specificity, overview. No activity with 25-mer peptide TNKRRFAGQARFAIDAIDRFGQY and 30mer peptide TNKRRFSAGQASRFSAIDASlDSARFGQY. Elongation of peptide chain lengths above 6-8 amino acids significantly improves the rates of oligosaccharide transfer in vitro
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additional information
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importance of the three N-terminal and the last C-terminal residues in substrate recognition. The remaining residues do not significantly contribute to peptide binding, thus maximizing the pool of protein fragments presented on MHC I molecules
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additional information
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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
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additional information
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TAP1-dependent peptide translocation in vitro is ATP dependent and peptide selective. Peptide binding can be assayed using a photoreactive radioiodinated peptide, [125I]-labeled KB11-HSAB peptide
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additional information
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the EEF.1 photopeptide labels TAP to a 20fold higher degree than the nef7B photopeptide
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additional information
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the TAP2 and TAP2iso alternative splicing forms show large and opposite preferences with regard to peptide IYLGPFSPNVTL and peptide TVDNKTRYE
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additional information
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TAP transports proteasomal degradation products into the ER lumen for loading onto MHC class I molecules. Analysis of the translocation machinery is the peptide-binding event and its allosteric coupling with ATP hydrolysis, overview
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additional information
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Db and Kb binding peptides are coupled with the carbohydrate galabiose (Galcr4Gal), either to an internal cysteine, or to a substituted homocysteine. Usage of a Db binding glycopeptide to measure empty MHC class-I molecules on activated T cells from TAP transporters, beta2-M and TAP/beta2-M gene targeted mice
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additional information
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peptide accumulation in mouse microsomes is influenced by the presence of MHC class I products. Accumulation of FAPGNYPAL in microsomal vesicles requires an intact/32m gene, and therefore binding to class I molecules affects the outcome of such translocation assays. Alternatively, the presence of a glycosylation site in the translocation substrate renders the assay independent of class I binding sites. The TAP transporter prefers peptides with free peptide termini and of a minimum length of 9 amino acid, substrate specificity, overview
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additional information
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peptide accumulation in mouse microsomes is influenced by the presence of MHC class I products. Accumulation of FAPGNYPAL in microsomal vesicles requires an intact/32m gene, and therefore binding to class I molecules affects the outcome of such translocation assays. Alternatively, the presence of a glycosylation site in the translocation substrate renders the assay independent of class I binding sites. The TAP transporter prefers peptides with free peptide termini and of a minimum length of 9 amino acid, substrate specificity, overview
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additional information
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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
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additional information
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TAP-independent presentation of endogenously synthesized peptides is enhanced by endoplasmic reticulum insertion sequences located at the N- but not C-terminus of the peptide, overview. Peptides can be presented in a TAP-independent manner in association with HLA A2.1 or H-2 Kd if they are expressed C-terminally to an endoplasmic reticulum insertion/signal sequence derived from the adenovirus E3/19K glycoprotein. (1) The E3/19K signal sequence greatly enhances the presentation of each of four additional peptides tested in association with H-2 Kb or Kk, (2) the E3/19K signal sequence can be substituted by a signal sequence derived from P-IFN, and (3) the E3/19K signal sequence does not function when located at the C-terminus of antigenic peptides. Many peptides require TAP for efficient presentation to T cells. Expression of peptides C-terminally to signal sequences is a generally applicable method of bypassing the TAP-dependence of peptide presentation, and the leader sequence does not act to bypass TAP simply by increasing the hydrophobic nature of peptides. Recombinant expression of peptides in L929 cells via transfection with recombinant Vaccinia virus (rVV) for immunopresentation
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additional information
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TAP1-dependent peptide translocation in vitro is ATP dependent and peptide selective. Measurement of translocation of a radiolabeled peptide FAPGNYPAL into the lumen of crude microsomes purified from TAP1-/- and TAP1+/+ mice. ATP is not required for supply of peptide or assembly of H-2Kb with peptide in TAP1+/+ microsomes. TAP1+/+ microsomes accumulate peptide at a higher rate than TAP1-/- microsomes. Competition between peptides for transport by TAP1, overview
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additional information
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peptide accumulation in mouse microsomes is influenced by the presence of MHC class I products. Accumulation of FAPGNYPAL in microsomal vesicles requires an intact/32m gene, and therefore binding to class I molecules affects the outcome of such translocation assays. Alternatively, the presence of a glycosylation site in the translocation substrate renders the assay independent of class I binding sites. The TAP transporter prefers peptides with free peptide termini and of a minimum length of 9 amino acid, substrate specificity, overview
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additional information
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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
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additional information
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TAP1-dependent peptide translocation in vitro is ATP dependent and peptide selective. Measurement of translocation of a radiolabeled peptide FAPGNYPAL into the lumen of crude microsomes purified from TAP1-/- and TAP1+/+ mice. ATP is not required for supply of peptide or assembly of H-2Kb with peptide in TAP1+/+ microsomes. TAP1+/+ microsomes accumulate peptide at a higher rate than TAP1-/- microsomes. Competition between peptides for transport by TAP1, overview
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additional information
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Db and Kb binding peptides are coupled with the carbohydrate galabiose (Galcr4Gal), either to an internal cysteine, or to a substituted homocysteine. Usage of a Db binding glycopeptide to measure empty MHC class-I molecules on activated T cells from TAP transporters, beta2-M and TAP/beta2-M gene targeted mice
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additional information
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P36370; P36372
TAP transports proteasomal degradation products into the ER lumen for loading onto MHC class I molecules. Analysis of the translocation machinery is the peptide-binding event and its allosteric coupling with ATP hydrolysis, overview
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additional information
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P36370; P36372
for rat transporters TAPl/2a and TAP1/2u, the most efficient ATP-dependent transport is observed for peptides with 8-12 amino acid length. Hexamers and longer peptides of up to 40 amino acids are also translocated, albeit less efficiently. TAP is selective for the primary sequence of peptide substrates with particular importance of the C-terminal residue of the peptide. TAP contains specific interaction sites for peptides. Peptide specificity, overview. Elongation of peptide chain lengths above 6-8 amino acids significantly improves the rates of oligosaccharide transfer in vitro
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additional information
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P36370; P36372
residues in TAP2 peptide transporters control the substrate specificity, overview. Iodinated peptides of the RYWANATRSX and TVDNKTRYX with X = different amino acids are used for peptide transport assays, overview
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additional information
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P36370; P36372
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
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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
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
evolution
P36370; P36372
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
evolution
TAP is a member of the ATP-binding cassette (ABC) family of transmembrane transport proteins
evolution
TAP1 and TAP2 are members of the ABC transporter family
evolution
TAP1 and TAP2 are members of the ATP-binding cassette family of membrane transIocators
evolution
TAP1 and TAP2 belong to the ATP-binding cassette (ABC) transporter family
evolution
Q2VQZ1; Q6JWQ3
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
evolution
B5BSK4; B5BSD5
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
evolution
B1N1D9; B1N1E0
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
evolution
Q76LI9; Q9PWI8
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
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
evolution
P36370; P36372
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
evolution
F1MVY8; Q32S33
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
evolution
A5D9J3; A5D9J7
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
evolution
Q5W414; Q5W417
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
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
evolution
the enzyme belongs to the ABC transporters, which have a conserved architecture of two transmembrane domains (TMDs) and two cytosolic nucleotide-binding domains (NBD). These domains can be expressed individually or can be arranged on a single polypeptide chain. While the TMDs of ABC import and export systems show diversity in their structural organization, the NBDs are highly conserved. The species-dependent differences in substrate specificity correlate with the epitope repertoire presented by MHC class I molecules, reflecting a co-evolution of TAP, MHC, and the T-cell receptor
evolution
the enzyme belongs to the ABC transporters, which have a conserved architecture of two transmembrane domains (TMDs) and two cytosolic nucleotide-binding domains (NBD). These domains can be expressed individually or can be arranged on a single polypeptide chain. While the TMDs of ABC import and export systems show diversity in their structural organization, the NBDs are highly conserved. The species-dependent differences in substrate specificity correlate with the epitope repertoire presented by MHC class I molecules, reflecting a co-evolution of TAP, MHC, and the T-cell receptor
evolution
P36370; P36372
the enzyme belongs to the ABC transporters, which have a conserved architecture of two transmembrane domains (TMDs) and two cytosolic nucleotide-binding domains (NBD). These domains can be expressed individually or can be arranged on a single polypeptide chain. While the TMDs of ABC import and export systems show diversity in their structural organization, the NBDs are highly conserved. The species-dependent differences in substrate specificity correlate with the epitope repertoire presented by MHC class I molecules, reflecting a co-evolution of TAP, MHC, and the T-cell receptor
evolution
the peptide supply factors, PSF1 and PSF2, are members of the multidrug-resistance family of transporters. They share 25% homology in a hydrophobic domain with a tentative number of eight membrane-spanning segments. The C-terminal 25 amino acids are entirely unrelated. close evolutionary relationship between PSF1 and PSF2 (TAP1 and TAP2)
evolution
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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
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evolution
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TAP1 and TAP2 are members of the ATP-binding cassette family of membrane transIocators
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malfunction
class I polymorphism influences the HC-Tpn-TAP interaction
malfunction
class I polymorphism influences the HC-Tpn-TAP interaction
malfunction
defects in the genes encoding TAPI or TAP2 account for impaired class I assembly and antigen presentation in several human cell lines
malfunction
defects in the genes encoding TAPI or TAP2 account for impaired class I assembly and antigen presentation in several rodent cell lines
malfunction
P36370; P36372
defects in the genes encoding TAPI or TAP2 account for impaired class I assembly and antigen presentation in several rodent cell lines
malfunction
expression of TAP1 and TAP2 in a mutant cell line result in the delivery of an 11-amino acid oligomer model peptide to the endoplasmic reticulum (ER). Peptide translocation is inhibited in a concentration-dependent manner
malfunction
in tapasin-deficient (Tpn-/-) mice the absence of tapasin has a dramatic effect on the stability of the TAP1/TAP2 heterodimeric peptide transporter. Steady-state expression of TAP protein is reduced more than 100fold from about 3×104 TAP molecules per wild-type splenocyte to about 1×102 TAP per Tpn-/- splenocyte. The low amount of TAP molecules in Tpn-/- lymphocytes is likely to contribute to the severe impairment of MHC class I expression. Activation of Tpn-/- lymphocytes yields strongly enhanced class I expression comparable to wild-type levels, although TAP expression remains low and in the magnitude of several hundred molecules per cell. The high level of class I on activates Tpn-/- cells depends on peptides generated by the proteasome as indicated by blockade with the proteasome-specific inhibitor lactacystin. In contrast to Tpn-/- cells, Con A activation of TAP1-/- splenocytes does not induce high class I expression
malfunction
microsomal preparations from beta2m-mice fail to significantly accumulate the [3H]FAPGNYPAL substrate in an ATP-dependent fashion
malfunction
mutations in the signature motif affect neither ATP nor peptide binding, but abolish peptide translocation, and result in decreased cell surface MHC class I expression. Despite a comparable expression level of TAP1 and TAP2 at the cell surface, expression of HLA-B is significantly reduced in T2 cells expressing the TAP signature-motif mutant, and is comparable to expression levels seen in the untransfected T2 cells. Therefore, the introduction of mutations into the signature motifs of either TAP1 or TAP2 severely compromises TAP function
malfunction
N-terminally truncated TAP variants lacking the additional N-terminal sequences retain the ability to bind peptide and nucleotide substrates at a level comparable to that of wild-type TAP. The truncated constructs are also capable of peptide translocation in vitro although with reduced efficiency. Loss of tapasin reduces surface class I expression or leads to suboptimal class I-peptide complexes, depending on the experimental system. ATP-dependent transport activity is preserved in 7TM- and 6TM-TAP, albeit at a lower rate. Deletion of the TAP N-termini reduces co-precipitation with MHC class I and tapasin
malfunction
some allelic variants of PSFI and/or PSF2 can restrict antigen presentation and are related to several autoimmune diseases that are associated with genes in the MHC class II region
malfunction
P36370; P36372
TAP variants lacking the N domain in TAP2, but not in TAP1, build PLCs that fail to generate stable MHC I-peptide complexes. This correlates with a substantially reduced recruitment of accessory chaperones into the PLC demonstrating their important role in the quality control of MHC I loading. stable surface expression of MHC I can be rescued in post-endoplasmic reticulum compartments by a proprotein convertase-dependent mechanism. TAP mutant variants 1-2DELTAN and 2-1DELTAN show different effects on the quality control of Ag presentation
malfunction
TAP1 or TAP2 expressed alone possess no capability or very limited capability to bind peptide
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
malfunction
the TAP1-TAP2iso transporter splicing variant facilitates the maturation of MHC class I molecules in the ER and restored surface expression of class I. TAP1-TAP2iso transporters expressed in T2 cells exhibit distinct and opposing influences on peptide selectivities, at times exceeding 30fold differences in competition experiments and attributable to diversity in the 3'-COOH tail. The common coexpression of an alternative splice product of the Tap2 gene may contribute to broaden immune diversity, a mechanism previously described to occur predominantly at the level of the TCR and MHC class I gene products
malfunction
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microsomal preparations from beta2m-mice fail to significantly accumulate the [3H]FAPGNYPAL substrate in an ATP-dependent fashion
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malfunction
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defects in the genes encoding TAPI or TAP2 account for impaired class I assembly and antigen presentation in several rodent cell lines
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metabolism
P36370; P36372
critical role for the tapasin-docking site of TAP2 in the functional integrity of the MHC class I-peptide-loading complex. The translocation pathway of TAP opens out into a large endoplasmic reticulum lumenal cavity, confined by the membrane entry points of tapasin and MHC-I. Two lateral windows channel the antigenic peptides to MHC-I. Structures of PLC captured at distinct assembly states provide mechanistic insight into the recruitment and release of MHC-I. Molecular symbiosis of an ABC transporter and an endoplasmic reticulum chaperone network in MHC-I assembly, insight into the onset of the adaptive immune response. Assembled and nonassembled TAP1 uses different TMD subregions for tapasin binding
metabolism
involvement of the MHC-encoded peptide transporter subunits associated with antigen processing (TAP1 and TAP2) in class I MHC-restricted antigen presentation
metabolism
molecular complexes of the endoplasmic reticlum (ER) involved in the maturation and peptide loading of class I molecules. After biosynthesis into the ER membrane class I HC assembles with Cnx. ERp57 may facilitate disulfide bond oxidation in early HC. HC releases Cnx and assembles with beta2m and chaperone calreticulin (Crt), and subsequently (or simultaneously) binds to TAP1/TAP2 heterodimers through the assistance of tapasin (Tpn). ERp57 recruited by Tpn may isomerize HC disulfide bonds in the loading complex. Mouse class I molecules can remain associated with Cnx throughout their stay in the ER. In the absence of TAP, HC/beta2m-Crt-Tpn-(ERp57) complexes can assemble, albeit less efficiently. Upon binding of a suitable peptide, the trimeric HC/beta2m/peptide complex is released from ER chaperones and migrates to the cell surface. Intermediate TAP-associated complexes contain Tpn, ERp57, and Cnx. Cnx is released from maturing human TAP complexes. Tpn-dependent/HC-independent association of beta2m and Crt with TAP has also been described, but the precursor relationship to the mature loading complex is not established. Tpn stabilizes steady-state levels of TAP1/TAP2 and, thereby, increases TAP-dependent peptide supply. In TAP-deficient cells, the assembly of HC/beta2m with Crt and Tpn and also the assembly of ERp57 with beta2m or Crt is less productive than in the presence of TAP. Roles of TAP-associated and TAP-independent loading complexes, overview
metabolism
molecular complexes of the endoplasmic reticlum (ER) involved in the maturation and peptide loading of class I molecules. After biosynthesis into the ER membrane class I HC assembles with Cnx. ERp57 may facilitate disulfide bond oxidation in early HC. HC releases Cnx and assembles with beta2m and chaperone calreticulin (Crt), and subsequently (or simultaneously) binds to TAP1/TAP2 heterodimers through the assistance of tapasin (Tpn). ERp57 recruited by Tpn may isomerize HC disulfide bonds in the loading complex. Mouse class I molecules can remain associated with Cnx throughout their stay in the ER. In the absence of TAP, HC/beta2m-Crt-Tpn-(ERp57) complexes can assemble, albeit less efficiently. Upon binding of a suitable peptide, the trimeric HC/beta2m/peptide complex is released from ER chaperones and migrates to the cell surface. Intermediate TAP-associated complexes contain Tpn, ERp57, and Cnx. Cnx is released from maturing human TAP complexes. Tpn-dependent/HC-independent association of beta2m and Crt with TAP has also been described, but the precursor relationship to the mature loading complex is not established. Tpn stabilizes steady-state levels of TAP1/TAP2 and, thereby, increases TAP-dependent peptide supply. In TAP-deficient cells, the assembly of HC/beta2m with Crt and Tpn and also the assembly of ERp57 with beta2m or Crt is less productive than in the presence of TAP. Roles of TAP-associated and TAP-independent loading complexes, overview
metabolism
p53 induces TAP1 and enhances the transport of MHC class I peptides. Since more than 50% of tumors have a dysfunctional p53, evasion of tumor surveillance by tumor cells may be linked to loss of p53 function. TAP1 is strongly induced by p53 and DNA-damaging agents through a p53-responsive element. p73, which is homologous to p53, is capable of inducing TAP1 and cooperates with p53 to activate TAP1. By inducing TAP1, p53 enhances the transport of MHC class I peptides and expression of surface MHC-peptide complexes, and cooperates with interferon gamma to activate the MHC class I pathway. Tumor surveillance may be a mechanism by which p53 and/or p73 function as tumor suppressors. The tumor-derived p53 mutant p53(R249S) is defective in transactivation. TAP1, but no other components in the MHC class I pathway, is induced by p53
metabolism
tapasin is a member of the MHC class I loading complex where it bridges the TAP peptide transporter to class I molecules. The main role of tapasin is assumed to be the facilitation of peptide loading and optimization of the peptide cargo. It plays a major role as a stabilizer of the TAP peptide transporter. In the presence of a large peptide pool in the cytosol, a small number of TAP transporters is sufficient to translocate enough peptides for high class I expression. Analysis shows that tapasin is not only required for stabilization of TAP but also for optimization of the spectrum of bound peptides. TAP is part of a multimeric structure termed the peptide loading complex. Fully assembled loading complexes are fundamental for optimal peptide binding to class I molecules and consist of class I heavy chain, beta2-microglobulin, endoplasmic reticulum (ER) chaperones calreticulin and ER-60, TAP1/TAP2 and tapasin. Tapasin is an ER-resident accessory glycoprotein specific for the MHC class I antigen presentation pathway. Class I molecules on activated tapasin-deficient cells, Tpn-/- cells, are loaded with peptides generated by the proteasome and transported by TAP
metabolism
the enzyme complex is part of the antigen processing pathway via major histocompatibility complex I, MHC I, overview. Peptides, derived by proteasomal degradation are translocated by TAP into the ER lumen and afterwards loaded onto MHC class I molecules. The process is chaperoned by interaction of the peptide-loading complex (PLC). Assembly of high-affinity peptide-MHC complexes is catalyzed by the macromolecular peptide-loading complex (PLC), consisting of TAP1, TAP2, the chaperones tapasin (TSN), and calreticulin (CRT), the ER-resident disulfide isomerase ERp57, the MHC class I heavy chain and beta2-microglobulin
metabolism
the enzyme complex is part of the antigen processing pathway via major histocompatibility complex I, MHC I, overview. Peptides, derived by proteasomal degradation are translocated by TAP into the ER lumen and afterwards loaded onto MHC class I molecules. The process is chaperoned by interaction of the peptide-loading complex (PLC). Assembly of high-affinity peptide-MHC complexes is catalyzed by the macromolecular peptide-loading complex (PLC), consisting of TAP1, TAP2, the chaperones tapasin (TSN), and calreticulin (CRT), the ER-resident disulfide isomerase ERp57, the MHC class I heavy chain and beta2-microglobulin
metabolism
P36370; P36372
the enzyme complex is part of the antigen processing pathway via major histocompatibility complex I, MHC I, overview. Peptides, derived by proteasomal degradation are translocated by TAP into the ER lumen and afterwards loaded onto MHC class I molecules. The process is chaperoned by interaction of the peptide-loading complex (PLC). Assembly of high-affinity peptide-MHC complexes is catalyzed by the macromolecular peptide-loading complex (PLC), consisting of TAP1, TAP2, the chaperones tapasin (TSN), and calreticulin (CRT), the ER-resident disulfide isomerase ERp57, the MHC class I heavy chain and beta2-microglobulin
metabolism
the peptide-loading complex (PLC) is a transient, multisubunit membrane complex in the endoplasmic reticulum that is essential for establishing a hierarchical immune response. The PLC coordinates peptide translocation into the endoplasmic reticulum with loading and editing of major histocompatibility complex class I (MHC-I) molecules. After final proofreading in the PLC, stable peptide-MHC-I complexes are released to the cell surface to evoke a T-cell response against infected or malignant cells. Sampling of different MHC-I allomorphs requires the precise coordination of seven different subunits in a single macromolecular assembly, including the transporter associated with antigen processing (TAP1 and TAP2, jointly referred to as TAP), the oxidoreductase ERp57, the MHC-I heterodimer, and the chaperones tapasin and calreticulin. Molecular organization of and mechanistic events taking place in the PLC. Two endoplasmic reticulum-resident editing modules composed of tapasin, calreticulin, ERp57, and MHC-I are centred around TAP in a pseudo-symmetric orientation. A multivalent chaperone network within and across the editing modules establishes the proofreading function at two lateral binding platforms for MHC-I molecules
metabolism
-
involvement of the MHC-encoded peptide transporter subunits associated with antigen processing (TAP1 and TAP2) in class I MHC-restricted antigen presentation
-
physiological function
a large and dynamic membrane-associated machinery orchestrates the translocation of antigenic peptides into the endoplasmic reticulum (ER) lumen for subsequent loading onto major histocompatibility complex (MHC) class I molecules. The peptide-loading complex, and ABC transporter, ensures that only high-affinity peptides, which guarantee longterm stability of MHC I complexes, are presented to T-lymphocytes. Adaptive immunity is dependent on surface display of the cellular proteome in the form of protein fragments, thus allowing efficient recognition of infected or malignant transformed cells. Mechanism of antigen translocation by the transporter associated with antigen processing and loading of MHC class I molecules in the ER, overview. The TAP complex is composed of two half-transporters, TAP1 (ABCB2) and TAP2 (ABCB3). Both subunits are essential and sufficient for ATP-dependent peptide translocation into the ER lumen. The ATP-binding cassette (ABC) transporter TAP represents a key checkpoint within the antigen-processing pathway. Affinity, specificity, and diversity are optimally combined in one translocation machinery. Thus, human, mouse, and rat TAP have different substrate specificities
physiological function
a large and dynamic membrane-associated machinery orchestrates the translocation of antigenic peptides into the endoplasmic reticulum (ER) lumen for subsequent loading onto major histocompatibility complex (MHC) class I molecules. The peptide-loading complex, and ABC transporter, ensures that only high-affinity peptides, which guarantee longterm stability of MHC I complexes, are presented to T-lymphocytes. Adaptive immunity is dependent on surface display of the cellular proteome in the form of protein fragments, thus allowing efficient recognition of infected or malignant transformed cells. Mechanism of antigen translocation by the transporter associated with antigen processing and loading of MHC class I molecules in the ER, overview. The TAP complex is composed of two half-transporters, TAP1 (ABCB2) and TAP2 (ABCB3). Both subunits are essential and sufficient for ATP-dependent peptide translocation into the ER lumen. The ATP-binding cassette (ABC) transporter TAP represents a key checkpoint within the antigen-processing pathway. Affinity, specificity, and diversity are optimally combined in one translocation machinery. Thus, human, mouse, and rat TAP have different substrate specificities. A functional polymorphism has been identified for rodent TAPs only. The rat TAPu isoform, similar to mouse TAP, prefers hydrophobic residues at the C-terminus of the peptide, while the rat TAPa isoform, which is comparable to human TAP, accepts hydrophobic and basic residues at this position. Mouse TAPs display not only slight differences in the C-terminal but also in the N-terminal positions
physiological function
P36370; P36372
a large and dynamic membrane-associated machinery orchestrates the translocation of antigenic peptides into the endoplasmic reticulum (ER) lumen for subsequent loading onto major histocompatibility complex (MHC) class I molecules. The peptide-loading complex, and ABC transporter, ensures that only high-affinity peptides, which guarantee longterm stability of MHC I complexes, are presented to T-lymphocytes. Adaptive immunity is dependent on surface display of the cellular proteome in the form of protein fragments, thus allowing efficient recognition of infected or malignant transformed cells. Mechanism of antigen translocation by the transporter associated with antigen processing and loading of MHC class I molecules in the ER, overview. The TAP complex is composed of two half-transporters, TAP1 (ABCB2) and TAP2 (ABCB3). Both subunits are essential and sufficient for ATP-dependent peptide translocation into the ER lumen. The ATP-binding cassette (ABC) transporter TAP represents a key checkpoint within the antigen-processing pathway. Affinity, specificity, and diversity are optimally combined in one translocation machinery. Thus, human, mouse, and rat TAP have different substrate specificities. A functional polymorphism has been identified for rodent TAPs only. The rat TAPu isoform, similar to mouse TAP, prefers hydrophobic residues at the C-terminus of the peptide, while the rat TAPa isoform, which is comparable to human TAP, accepts hydrophobic and basic residues at this position. Mouse TAPs display not only slight differences in the C-terminal but also in the N-terminal positions
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
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
physiological function
P36370; P36372
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
physiological function
F1MVY8; Q32S33
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
physiological function
A5D9J3; A5D9J7
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
physiological function
Q5W414; Q5W417
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
physiological function
Q2VQZ1; Q6JWQ3
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
physiological function
Q76LI9; Q9PWI8
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
physiological function
B5BSK4; B5BSD5
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
physiological function
B1N1D9; B1N1E0
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
physiological function
binding and transport of melanoma-specific antigenic peptides by the transporter associated with antigen processing. The melanoma epitopes exhibit differential capacities to be transported by TAP in streptolysin O-permeabilized cells, as well as differential competition for peptide binding to TAP. The melanoma antigens follow distinct pathways for presentation, along the MHC class I pathway. The epitopes YMNGTMSQV and YMDGTMSQV are two forms of the same epitope derived from tyrosinase. The D form of the epitope is thought to arise from the conversion of asparagine to aspartic acid during enzymatic deglycosylation of the epitope. The competition by melanoma epitopes observed in permeabilized cells also occurs at the level of peptide binding to TAP, overview
physiological function
major histocompatibility complex (MHC) class I molecules present peptides derived from nuclear and cytosolic proteins to CD8+ T cells. These peptides are translocated into the lumen of the endoplasmic reticulum (ER) to associate with class I molecules. Two MHC-encoded putative transporter proteins, TAP1 and TAP2, are required for efficient assembly of class I molecules and presentation of endogenous peptides. Peptide translocation depends on the sequence of the peptide, is adenosine triphosphate (ATP)-dependent, and requires ATP hydrolysis
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
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
physiological function
P36370; P36372
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
physiological function
MHC class I molecules are loaded with peptides that mostly originate from the degradation of cytosolic protein antigens and are translocated across the endoplasmic reticulum (ER) membrane by the transporter associated with antigen processing (TAP). The ER-resident molecule tapasin (Tpn) is uniquely dedicated to tether class I molecules jointly with the chaperone calreticulin (Crt) and the oxidoreductase ERp57 to TAP. The transient association of class I molecules with Tpn and TAP is critically important for the stabilization of class I molecules and the optimization of the peptide cargo presented to cytotoxic T cells. The different functions of molecular domains of Tpn and the highly coordinated formation of the TAP-associated peptide loading complex. In the presence of TAP, the assembly machinery appears to be skewed towards the TAP-associated complex. This is indicated by elegant pulse-chase experiments with HeLa cells, where no HC/beta2m-Crt complexes are detected outside of assemblages with Tpn-ERp57-TAP. TAP strongly supports the assembly of the other components of the peptide loading complex
physiological function
MHC class I molecules are loaded with peptides that mostly originate from the degradation of cytosolic protein antigens and are translocated across the endoplasmic reticulum (ER) membrane by the transporter associated with antigen processing (TAP). The ER-resident molecule tapasin (Tpn) is uniquely dedicated to tether class I molecules jointly with the chaperone calreticulin (Crt) and the oxidoreductase ERp57 to TAP. The transient association of class I molecules with Tpn and TAP is critically important for the stabilization of class I molecules and the optimization of the peptide cargo presented to cytotoxic T cells. The different functions of molecular domains of Tpn and the highly coordinated formation of the TAP-associated peptide loading complex. In the presence of TAP, the assembly machinery appears to be skewed towards the TAP-associated complex. This is indicated by elegant pulse-chase experiments with HeLa cells, where no HC/beta2m-Crt complexes are detected outside of assemblages with Tpn-ERp57-TAP. TAP strongly supports the assembly of the other components of the peptide loading complex
physiological function
MHC class I molecules bind peptides derived from proteins in the cytosol and transport them to the cell surface for recognition by cytotoxic T cells. The molecule responsible for translocation of the antigenic peptides from the cytosol, where they are generated, to the endoplasmic reticulum, where they associate with MHC class I molecules, is the transporter associated with Ag processing (TAP). TAPis an MHC-encoded member of the ATP binding cassette (ABC) transporter family that localizes to the endoplasmic reticulum (ER) membrane. It is composed of two subunits, TAPl and TAP2, each containing an N-terminal transmembrane (TM) domain predicted to span the membrane 6 to 10 times and a C-terminal cytoplasmic domain with an ATP binding site. TAPl and TAP2 form stable complexes in vivo, and the expression of both subunits is required for TAP function. MHC class I molecules transiently associate with TAP via the TAPl chain, a process that has been shown to facilitate peptide loading. The transporter associated with Ag processing (TAP) translocates cytosolic peptides into the endoplasmic reticulum, where they can bind to MHC class I molecules. TAP does not translocate all peptides with equal efficiency, but selects peptides with regard to both their length and their sequence and, in this manner, affects the pool of peptides available for binding to MHC class I molecules. Peptide selection by TAP predominantly occurs during the first step in the translocation process, namely the association of the peptide with a binding site present on the TAP molecule. Involvement of both TAPl and TAP2 in determining translocation specificity and in peptide binding
physiological function
peptides and major histocompatibility complex class I/beta2-microglobulin bind to the transporters associated with antigen processing, TAP1 and TAP2. TAP possesses a peptide-recognition site with broad specificity and that MHC class I/beta2m dimers physically associate with TAP, interaction analysis, overview. Elements of both TAPN and TAP2 compose the peptide-recognition site. The TAP proteins transport antigenic peptides across the endoplasmic reticulum membrane where they can assemble with newly synthesized major histocompatibility complex (MHC) class I/beta2-microglobulin (beta2m) dimers. TAP functions as a heterodimer. MHC class I/beta2m dimers associate with individual TAP1 chains but are not detectable with individual TAP2 chains, suggesting that the site of interaction for MHC class I/beta2m dimers with TAP locates on TAP1. Although peptide translocation across the ER membrane requires ATP, peptide binding to TAP occurs in the absence of ATP, suggesting that peptide recognition and translocation are separate events. Peptide binding and translocation occur only in the presence of both TAP1 and TAP2
physiological function
presentation of intracellularly derived antigenic peptides to T cells requires their assembly together with MHC class I molecules in the endoplasmic reticulum (ER). Such peptides are delivered to the ER by an MHC-encoded transporter composed of TAP1 and TAP2 protein delivery. The TAP1-TAP2iso transporter splicing variant facilitates the maturation of MHC class I molecules in the ER and restored surface expression of class I. TAP1-TAP2iso transporters expressed in T2 cells exhibit distinct and opposing influences on peptide selectivities, at times exceeding 30fold differences in competition experiments and attributable to diversity in the 3'-COOH tail. The common coexpression of an alternative splice product of the Tap2 gene may contribute to broaden immune diversity, a mechanism previously described to occur predominantly at the level of the TCR and MHC class I gene products. Influence of TAP1-TAP2iso transporter on the maturation of MHC class I molecules in the ER, overview
physiological function
T cells detect infection of cells by recognizing peptide fragments of foreign proteins bound to class I molecules of the major histocompatibility complex (MHC) on the surface of the infected cell. MHC class I molecules bind peptide in the endoplasmic reticulum, and an adequate supply of peptides requires the presence of two genes in the MHC class II locus that encode proteins called transporters associated with antigen processing (TAP) 1 and 2. TAP1 and TAP2 are members of the ATP-binding cassette family of membrane trans-Iocators. TAP1 is part of an ATP-dependent, sequence-specific, peptide translocator
physiological function
T cells detect infection of cells by recognizing peptide fragments of foreign proteins bound to class I molecules of the major histocompatibility complex (MHC) on the surface of the infected cell. MHC class I molecules bind peptide in the endoplasmic reticulum, and an adequate supply of peptides requires the presence of two genes in the MHC class II locus that encode proteins called transporters associated with antigen processing (TAP) 1 and 2. TAP1 and TAP2 are members of the ATP-binding cassette family of membrane trans-Iocators. TAP1 is part of an ATP-dependent, sequence-specific, peptide translocator. TAP1 protein is required for ATP-dependent peptide trans location into the lumen of the microsomes. The translocated peptides bind to class I H-2K b molecules within the microsomes
physiological function
TAP1 and TAP2 are necessary and sufficient for peptide translocation across the endoplasmic reticulum (ER) membrane during loading of MHC class I molecules. In addition to TAP, MHC class I loading also requires ER-resident chaperones, including the class I-specific chaperone tapasin. Tapasin comprises an N-terminal ER lumenal domain that associates with MHC molecules, followed by a C-terminal transmembrane (TM) and cytosolic stalk that bind TAP. Domain boundaries within the N-termini of TAP1 and TAP2 are important in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I. Tapasin has also been shown to increase TAP stability, and by linking TAP to MHC class I it may act to increase the local peptide concentration for efficient loading
physiological function
the heterodimeric peptide transporter associated with antigen processing (TAP) consisting of the subunits TAP1 and TAP2 mediates the transport of cytosolic peptides into the lumen of the endoplasic reticulum (ER). Specific regions of the TAP1 subunit are crucial for the proper processing and presentation of cytosolic antigens to MHC class I-restricted T cells, whereas others may play a minor in this process. TAP is involved in numerous interactions inside the ER and the cytosol
physiological function
the major histocompatibility complex (MHC)-encoded transporters associated with antigen processing (TAP) translocate peptides from the cytosol into the lumen of the endoplasmic reticulum (ER) where they associate with MHC class I molecules. TAP molecules are composed of two noncovalently associated subunits, TAPl and TAP2, both of which contain a multimembrane-spanning domain and a hydrophilic cytosol domain with a binding cassette for ATP. Consistent with this structure, translocation of peptides into the ER is ATP-dependent and requires expression of both TAPl and TAP2
physiological function
P36370; P36372
the major histocompatibility complex (MHC)-encoded transporters associated with antigen processing (TAP) translocate peptides from the cytosol into the lumen of the endoplasmic reticulum (ER) where they associate with MHC class I molecules. TAP molecules are composed of two noncovalently associated subunits, TAPl and TAP2, both of which contain a multimembrane-spanning domain and a hydrophilic cytosol domain with a binding cassette for ATP. Consistent with this structure, translocation of peptides into the ER is ATP-dependent and requires expression of both TAPl and TAP2
physiological function
the peptide supply factors, PSF1 and PSF2, are members of the multidrug-resistance family of transporters and may pump cytosolic peptides into the membrane-bound compartment where class I molecules assemble. Coregulation of PSFI and PSF2 by gamma interferon. They have a common role in peptide-loading of class I molecules
physiological function
P36370; P36372
the transporter associated with Ag processing (TAP) translocates antigenic peptides into the endoplasmic reticulum for binding onto MHC class I (MHC I) molecules. Tapasin organizes a peptide-loading complex (PLC) by recruiting MHC I and accessory chaperones to the N-terminal regions (N domains) of the TAP subunits TAP1 and TAP2. Tapasin, a type I transmembrane glycoprotein, is believed to play a key role in the formation of the PLC because it binds to MHC I molecules as well as to the transmembrane domains (TMDs) of the TAP subunits, TAP1 and TAP2. In the absence of tapasin, the stability of MHC I-peptide complexes is drastically reduced and the repertoire of surface-presented peptide Ags is altered, suggesting that tapasin acts as an editor that selects peptides for stable binding onto MHC I. TAP1 and TAP2 differ in the structural requirements for stable recruitment of accessory chaperones and the tapasin-docking site of TAP2 plays a pivotal role in the functional integrity of the PLC
physiological function
P36370; P36372
the transporter associated with Ag processing (TAP) translocates peptides from the cytosol into the endoplasmic reticulum lumen where they associate with MHC class I molecules
physiological function
the transporter associated with antigen processing (TAP) 1 is required for the major histocompatibility complex (MHC) class I antigen presentation pathway, which plays a key role in host tumor surveillance. Since more than 50% of tumors have a dysfunctional p53, evasion of tumor surveillance by tumor cells may be linked to loss of p53 function. TAP1 is strongly induced by p53 and DNA-damaging agents through a p53-responsive element. p73, which is homologous to p53, is capable of inducing TAP1 and cooperates with p53 to activate TAP1. By inducing TAP1, p53 enhances the transport of MHC class I peptides and expression of surface MHC-peptide complexes, and cooperates with interferon gamma to activate the MHC class I pathway
physiological function
the transporter associated with antigen processing (TAP) delivers peptides to the lumen of the endoplasmic reticuhm in an adenosine triphosphate (ATP) dependent fashion for presentation by major histocompatibility complex class I molecules. The mouse TAP translocator (H-2 b haplotype) selects peptides based on a minimal size of nine residues, and on the presence of a hydrophobic COOH-terminal amino add. The preponderance of COOH-terminal hydrophobic amino acids in peptides capable of binding to mouse class I molecules thus fits remarkably wellwith the specificity of the TAP translocator. In addition to transport in the lumenal direction, either of peptide in the cytosolic direction is observed in an ATP- and temperature-dependent manner. By maintaining a low peptide concentration at the site of class I assembly, this feflux mechanism may ensure that class I molecules are loaded preferentially with high affinity peptides
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
physiological function
the transporter associated with antigen processing (TAP) transports short peptides from the cytosol to the endoplasmic reticulum, where peptides assemble with class I molecules of the major histocompatibility complex. TAP is comprised of two subunits, termed TAP1 and TAP2
physiological function
transporter associated with antigen processing (TAP) is part of a multimeric structure termed the peptide loading complex. TAP expression is a requirement for normal class I antigen presentation. The function of TAP is to translocate peptides from the cytosol into the endoplasmic reticulum (ER)
physiological function
-
the transporter associated with antigen processing (TAP) delivers peptides to the lumen of the endoplasmic reticuhm in an adenosine triphosphate (ATP) dependent fashion for presentation by major histocompatibility complex class I molecules. The mouse TAP translocator (H-2 b haplotype) selects peptides based on a minimal size of nine residues, and on the presence of a hydrophobic COOH-terminal amino add. The preponderance of COOH-terminal hydrophobic amino acids in peptides capable of binding to mouse class I molecules thus fits remarkably wellwith the specificity of the TAP translocator. In addition to transport in the lumenal direction, either of peptide in the cytosolic direction is observed in an ATP- and temperature-dependent manner. By maintaining a low peptide concentration at the site of class I assembly, this feflux mechanism may ensure that class I molecules are loaded preferentially with high affinity peptides
-
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
-
physiological function
-
T cells detect infection of cells by recognizing peptide fragments of foreign proteins bound to class I molecules of the major histocompatibility complex (MHC) on the surface of the infected cell. MHC class I molecules bind peptide in the endoplasmic reticulum, and an adequate supply of peptides requires the presence of two genes in the MHC class II locus that encode proteins called transporters associated with antigen processing (TAP) 1 and 2. TAP1 and TAP2 are members of the ATP-binding cassette family of membrane trans-Iocators. TAP1 is part of an ATP-dependent, sequence-specific, peptide translocator. TAP1 protein is required for ATP-dependent peptide trans location into the lumen of the microsomes. The translocated peptides bind to class I H-2K b molecules within the microsomes
-
additional information
identification of sequences in the human peptide transporter subunit TAP1 required for transporter associated with antigen processing (TAP) function, structure-function analysis, overview
additional information
-
identification of sequences in the human peptide transporter subunit TAP1 required for transporter associated with antigen processing (TAP) function, structure-function analysis, overview
additional information
isolation of human PLC from Burkitt's lymphoma cells using an engineered viral inhibitor as bait and determination of the structure of native PLC by electron cryo-microscopy, overview
additional information
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isolation of human PLC from Burkitt's lymphoma cells using an engineered viral inhibitor as bait and determination of the structure of native PLC by electron cryo-microscopy, overview
additional information
P36370; P36372
mapping of two short stretches in rat TAP2, with two polymorphic residues each, that essentially control the differential peptide transport observed for the rat alleles by constructing several hybrids between rat TAP2a and TAP2u and coexpressing them wmith rat TAPl in TAP-deficient T2 cells
additional information
monomeric as well as dimeric NBDs reveal an L-shaped molecule with two subdomains, a RecA-like domain (arm I) and an a-helical domain (arm II). The NBD harbors a P-loop Walker A motif, GXXGXGK(S/T)x, interacting with the alpha- and beta-phosphate of the bound ATP, a signature motif (C-Loop, LSGGQ), positioning the gamma-phosphate, and a conserved glutamate adjacent to the Walker B motif (PhiPhiPhiPhiD, with Phi being a hydrophobic residue), catalyzing the nucleophilic attack of the beta/gamma phosphoanhydride bond by a water molecule. In addition, the NBDs display a conserved histidine (H-loop, switch region) involved in ATP hydrolysis, a Q-Loop, which is suggested to sense the gamma-phosphate and to communicate with the TMDs, as well as the conserved D-Loop, displaying a contact-site within the NBD dimer interface. Walker A and Walker B as well as the H-loop and the Q-loop are arranged in arm I, while the signature motif is located in arm II. The ATP molecule is positioned by residues of the Walker A and Walker B motif and the C-loop of the opposite NBD. ATP binding results in a rigid body movement of arm I towards arm II, causing the largest conformational changes within the Q- and D-loop. The TAP complex is composed of two half-transporters, TAP1 (ABCB2) and TAP2 (ABCB3). Both subunits are essential and sufficient for ATP-dependent peptide translocation into the endoplasmic reticulum (ER) lumen. Biogenesis of the heterodimer requires the assembly of preexisting TAP1 with newly synthesized TAP2. Three-dimensional modeling of the core TAP complex, overview
additional information
monomeric as well as dimeric NBDs reveal an L-shaped molecule with two subdomains, a RecA-like domain (arm I) and an a-helical domain (arm II). The NBD harbors a P-loop wWalker A motif, GXXGXGK(S/T)x, interacting with the alpha- and beta-phosphate of the bound ATP, a signature motif (C-Loop, LSGGQ), positioning the gamma-phosphate, and a conserved glutamate adjacent to the Walker B motif (PhiPhiPhiPhiD, with Phi being a hydrophobic residue), catalyzing the nucleophilic attack of the beta/gamma-phosphoanhydride bond by a water molecule. In addition, the NBDs display a conserved histidine (H-loop, switch region) involved in ATP hydrolysis, a Q-Loop, which is suggested to sense the gamma-phosphate and to communicate with the TMDs, as well as the conserved D-Loop, displaying a contact-site within the NBD dimer interface. Walker A and Walker B as well as the H-loop and the Q-loop are arranged in arm I, while the signature motif is located in arm II. The ATP molecule is positioned by residues of the Walker A and Walker B motif and the C-loop of the opposite NBD. ATP binding results in a rigid body movement of arm I towards arm II, causing the largest conformational changes within the Q- and D-loop. The TAP complex is composed of two half-transporters, TAP1 (ABCB2) and TAP2 (ABCB3). Both subunits are essential and sufficient for ATP-dependent peptide translocation into the endoplasmic reticulum (ER) lumen. Biogenesis of the heterodimer requires the assembly of preexisting TAP1 with newly synthesized TAP2. Three-dimensional modeling of the core TAP complex, overview
additional information
P36370; P36372
monomeric as well as dimeric NBDs reveal an L-shaped molecule with two subdomains, a RecA-like domain (arm I) and an alpha-helical domain (arm II). The NBD harbors a P-loop wWalker A motif, GXXGXGK(S/T)x, interacting with the alpha- and beta-phosphate of the bound ATP, a signature motif (C-Loop, LSGGQ), positioning the gamma-phosphate, and a conserved glutamate adjacent to the Walker B motif (PhiPhiPhiPhiD, with Phi being a hydrophobic residue), catalyzing the nucleophilic attack of the b/gphosphoanhydride bond by a water molecule. In addition, the NBDs display a conserved histidine (H-loop, switch region) involved in ATP hydrolysis, a Q-Loop, which is suggested to sense the gamma-phosphate and to communicate with the TMDs, as well as the conserved D-Loop, displaying a contact-site within the NBD dimer interface. Walker A and Walker B as well as the H-loop and the Q-loop are arranged in arm I, while the signature motif is located in arm II. The ATP molecule is positioned by residues of the Walker A and Walker B motif and the C-loop of the opposite NBD. ATP binding results in a rigid body movement of arm I towards arm II, causing the largest conformational changes within the Q- and D-loop. The TAP complex is composed of two half-transporters, TAP1 (ABCB2) and TAP2 (ABCB3). Both subunits are essential and sufficient for ATP-dependent peptide translocation into the endoplasmic reticulum (ER) lumen. Biogenesis of the heterodimer requires the assembly of preexisting TAP1 with newly synthesized TAP2. Three-dimensional modeling of the core TAP complex, overview
additional information
most ABC transporters comprise a transmembrane region with six membrane-spanning helices. TAP1 and TAP2 also contain additional N-terminal sequences whose functions may be linked to interactions with tapasin and MHC class I molecules
additional information
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most ABC transporters comprise a transmembrane region with six membrane-spanning helices. TAP1 and TAP2 also contain additional N-terminal sequences whose functions may be linked to interactions with tapasin and MHC class I molecules
additional information
P36370; P36372
neither the N domain of TAP1 nor the N domain of TAP2 is required for ER-export and surface expression of MHC I
additional information
peptide selection by TAP predominantly occurs during the first step in the translocation process, namely the association of the peptide with a binding site present on the TAP molecule. Four regions, two on the TAPl and two on the TAP2 subunit, are identified that make major contributions to this binding site. For TAP1, one surrounding the Ip3 and one surrounding the lp4 epitope. Both TAPl and TAP2, the identified regions overlap with the cytosol-membrane boundaries of the two transmembrane segments closest to the ATP binding site. The data is consistent with a model in which the transmembrane segments of TAP form a pore in the membrane, with the peptide binding site being formed by the cytosolic mouth of this pore
additional information
recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex
additional information
recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex
additional information
P36370; P36372
recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex
additional information
F1MVY8; Q32S33
recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex
additional information
A5D9J3; A5D9J7
recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex
additional information
Q5W414; Q5W417
recruitment of tapasin by TAP is essential for the assembly of the peptide-loading complex
additional information
Q2VQZ1; Q6JWQ3
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
additional information
B5BSK4; B5BSD5
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
additional information
B1N1D9; B1N1E0
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
additional information
Q76LI9; Q9PWI8
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
additional information
stabilization of TAP by the transmembrane domain of tapasin (Tpn)
additional information
stabilization of TAP by the transmembrane domain of tapasin (Tpn)
additional information
TAP is a mammalian ABC transporter that is a heterodimer made up of TAP1 and TAP2 polypeptides, which each have an N-terminal polytopic membrane domain and a C-terminal cytoplasmic nucleotide-binding domain (NBD). The peptide-binding site is shared between the two TAP subunits and both are required for peptide transport. Cooperative interaction between the two TAP NBD occurs, but the NBDs of TAP1 and 2 are not functionally equivalent. Absolute requirement for the signature motif in both TAP1 and 2
additional information
the two subunits of the assembled complex present in detergent extracts photolabeled equally with 8-azido-[alpha-32P]ATP. Photolabeling of the two subunits is inhibited in parallel by various di- and trinucleotides, suggesting that their nucleotide binding sites function in a highly similar manner
additional information
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the two subunits of the assembled complex present in detergent extracts photolabeled equally with 8-azido-[alpha-32P]ATP. Photolabeling of the two subunits is inhibited in parallel by various di- and trinucleotides, suggesting that their nucleotide binding sites function in a highly similar manner
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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
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
additional information
Q2VQZ1; Q6JWQ3
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
additional information
F1MVY8; Q32S33
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
additional information
Q5W414; Q5W417
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
additional information
Q76LI9; Q9PWI8
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
additional information
B5BSK4; B5BSD5
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
additional information
construction and analysis of a Tpn-deficient cell line 220.B8, phenotype, overview. Because peptide depletion by lactacystin induces a time-dependent decay of preexisting surface Kb/Db molecules on Tpn-/- cells, it can be concluded that Tpn deficiency does not override the need of peptide ligands for ER exit and surface expression of class I
additional information
construction of N-terminally truncated TAP variants lacking the additional N-terminal sequences. In an insect cell-based assay that reconstituted the class I loading pathway, the truncated TAP variants promote HLA-B*2705 processing to similar levels as wild-type TAP. The two deletion constructs are designed as 7TM-TAP (TAP1 [125-746]/TAP2 [87-686]) and 6TMTAP (TAP1 [174-746]/TAP2 [138-686]). Mutants 7TM- and 6TM-TAP bind nucleotides and peptide. ATP-dependent transport activity is preserved in 7TM- and 6TM-TAP, albeit at a lower rate. Deletion of the TAP N-termini reduces co-precipitation with MHC class I and tapasin
additional information
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construction of N-terminally truncated TAP variants lacking the additional N-terminal sequences. In an insect cell-based assay that reconstituted the class I loading pathway, the truncated TAP variants promote HLA-B*2705 processing to similar levels as wild-type TAP. The two deletion constructs are designed as 7TM-TAP (TAP1 [125-746]/TAP2 [87-686]) and 6TMTAP (TAP1 [174-746]/TAP2 [138-686]). Mutants 7TM- and 6TM-TAP bind nucleotides and peptide. ATP-dependent transport activity is preserved in 7TM- and 6TM-TAP, albeit at a lower rate. Deletion of the TAP N-termini reduces co-precipitation with MHC class I and tapasin
additional information
generation of TAP deletion mutant del1 (aa345-365), del2 (aa 366-385), del3 (aa 386-405), del3a, del3b, del4 (aa 465-487), and del1-3 for determination of the sequences or residues of human TAP1 responsible for TAP function. The peptide transport activity of the deletion mutants is highly reduced or completely abolished. Distinct MHC I surface expression profiles in TAP1 deletion mutants, some mutants show altered LCMV-specific lysis
additional information
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generation of TAP deletion mutant del1 (aa345-365), del2 (aa 366-385), del3 (aa 386-405), del3a, del3b, del4 (aa 465-487), and del1-3 for determination of the sequences or residues of human TAP1 responsible for TAP function. The peptide transport activity of the deletion mutants is highly reduced or completely abolished. Distinct MHC I surface expression profiles in TAP1 deletion mutants, some mutants show altered LCMV-specific lysis
additional information
production of recombinant vaccinia viruses that direct synthesis of the TAP subunits, either individually or together. Virus-encoded TAP is rapidly and efficiently assembles (t1/2 of 5 min or less) by cells and does not spontaneously assemble in detergent extracts. Metabolic labeling with [2-3H]mannose demonstrates that TAP1 (but not TAP2) possesses Asn-linked oligosaccharides, but the lack of binding of [35S]methionine-labeled TAP to concanavalin A-agarose suggests that the glycosylated form represents a minor population of TAP1. The two subunits of the assembled complex present in detergent extracts photolabeled equally with 8-azido-[alpha-32P]ATP. Photolabeling of the two subunits is inhibited in parallel by various di- and trinucleotides, suggesting that their nucleotide binding sites function in a highly similar manner
additional information
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production of recombinant vaccinia viruses that direct synthesis of the TAP subunits, either individually or together. Virus-encoded TAP is rapidly and efficiently assembles (t1/2 of 5 min or less) by cells and does not spontaneously assemble in detergent extracts. Metabolic labeling with [2-3H]mannose demonstrates that TAP1 (but not TAP2) possesses Asn-linked oligosaccharides, but the lack of binding of [35S]methionine-labeled TAP to concanavalin A-agarose suggests that the glycosylated form represents a minor population of TAP1. The two subunits of the assembled complex present in detergent extracts photolabeled equally with 8-azido-[alpha-32P]ATP. Photolabeling of the two subunits is inhibited in parallel by various di- and trinucleotides, suggesting that their nucleotide binding sites function in a highly similar manner
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
additional information
TAP1 and TAP2 signature-motif-mutations are made by site-directed mutagenesis. Functional consequences of the signature-motif mutations on cell surface MHC class I expression are examined by flow cytometry. Despite a comparable expression level of TAP1 and TAP2 at the cell surface, expression of HLA-B is significantly reduced in T2 cells expressing the TAP signature-motif mutant, and is comparable to expression levels seen in the untransfected T2 cells. Mutation of the signature motifs in TAP1, TAP2 or both subunits does not prevent ATP binding by TAP. Cell surface expression of MHC class I is reduced in cells expressing signature-motif-mutant TAP molecules
additional information
TAP1-Fluc is cotransfected into H-1299 cells with pcDNA3 or a vector that expresses wild-type p73alpha or p73beta. The fold increase in relative luciferase activity is calculated. TAP1-Fluc is co-transfected into H1299 cells with 5 mg of pcDNA3 or a vector that expresses p53(V143A), p53(R175H), p53(R249S), or p53(R273H). p53 mutants are unable to increase the luciferase activity for TAP1-Fluc
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
additional information
B1N1D9; B1N1E0
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
additional information
construction and analysis of mice harboring a disrupted tapasin (Tpn) gene, phenotype, overview. Tpn-/- mice demonstrate the importance of Tpn for the maturation of CD8+ T cells and their response to select class I-restricted antigens. Depending on the nature and the abundance of the antigen, antigen presentation can strongly be impaired in the absence of Tpn as a consequence of defective assembly of stable class I-peptide complexes and presumably also of the reduced TAP-mediated peptide transport
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
additional information
the absence of tapasin (Tpn) has a much more dramatic effect on TAP expression in cells from Tpn-/- mice than in human cells. In Tpn-/- splenocytes TAP is reduced about 300fold under steady-state conditions as compared to wild-type splenocytes. Despite low TAP levels, activation of Tpn-/- splenocytes results in high MHC class I surface expression. Strongly decreased TAP expression in bone marrow-derived cells (BMDC) from Tpn-/- mice. MHC class I molecules on activated Tpn-/- cells are peptide-occupied but exhibit reduced half-life. In contrast to Tpn-/- cells, ConA activation of TAP1-/- splenocytes does not induce high class I expression
additional information
P36370; P36372
generation of N-terminally truncated variants of TAP1 and TAP2 in combination with wild-type chains, as fusion proteins or as single subunits (TAP1-2DELTAN, and 2-1DELTAN. In the case of TD1/2DELTAN and TD1DELTAN/2DELTAN). TAP variants lacking the N domain in TAP2, but not in TAP1, form PLCs that are disturbed in the physical interaction with calreticulin (Crt), calnexin (Cnx), and ER60 and the quality control of MHC I loading. Head-to-tail-fusion of TAP chains allows stable expression of transporters lacking both N domains
additional information
P36370; P36372
mapping of two short stretches in rat TAP2, with two polymorphic residues each, that essentially control the differential peptide transport observed for the rat alleles by constructing several hybrids between rat TAP2a and TAP2u and co-expressing them wmith rat TAPl in TAP-deficient T2 cells. The critical residues are located in putative cytoplasmic loops close to the membrane. Relation of diverse polymorphic residues TAP2 controlling substrate specificity to the membrane topology, overview
additional information
P36370; P36372
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
additional information
A5D9J3; A5D9J7
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
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gene Abcb2 and Abcb3 or Tap1 and Tap2, recombinant expression of TAP1 and TAP2 in lymphoblastoid cell line T2
gene tap2, sequence analysis of exon junctions of two distinct Tap2 cDNAs isolated from the same human spleen cDNA library, sequence determination and analysis, an alternative splicing of Tap2 is identified, the human splice variant, termed Tap2iso, lacks exon 11 and original 3' untranslated region and contains a distinct identified exon 12 and 3' untranslated region. The full-length Tap2iso cDNA (2496 bp) predicts a protein of 653 amino acids. Tap2iso mRNA is normally coexpressed with Tap2 mRNA in all human lymphocyte cell lines examined. Function of TAP2iso is evaluated at multilevel in TAP1/2iso and TAP1/2 cotransfected T2 (TAP-deficient) cells, a mutant cell line deplete of endogenous Tap gene products. The TAP1-TAP2iso transporter facilitated the maturation of MHC class I molecules in the ER and restored surface expression of class I. RT-PCR analysis and sequencing of the RT-PCR products reveals the presence of both Tap2 and Tap2iso mRNAs in all human fresh peripheral blood lymphocytes, EBV-immortalized B cell lines, MOLT4, acute lymphoblastic leukemia cells, THP-1 monocytic cells, U-937 histocytic lymphoma cells, HeLa epithelioid carcinoma cells, and PACA (pancreatic carcinoma cells)
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
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
Q2VQZ1; Q6JWQ3
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
B5BSK4; B5BSD5
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
F1MVY8; Q32S33
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
A5D9J3; A5D9J7
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
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
genes TAP1 and TAP2, or PSF1 and PSF2, DNA and amino acid sequence determination and analysis, PSF2 is identified 10 kb from PSFI, near the class I DOB gene, sequence comparisons
genes TAP1 and TAP2, recombinant coexpression of His-tagged subunits in Spodoptera frugiperda Sf9 insect cells via baculovirus transfection method
genes tap1 and tap2, recombinant coexpression of wild-type and mutant TAP1 and TAP2 subunits in human TAP-deficient T2 cells
P36370; P36372
genes TAP1 and TAP2, recombinant expression of chimeric rTAP2 molecules together with rTAPl in human TAP-deficient T2 cells. All hybrids are functional, the surface expression of HLA-B51 molecules on T2 cells is induced to comparable extents, indicating TAP-dependent peptide transport and class I loading. Peptide transport by T2 cells expressing wild-type rTAP2a, rTAP2u, or rTAP2 hybrids is analyzed
P36370; P36372
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
human TAP1 (a allotype) and TAP2 (b allotype) genes, recombinant expression using Vaccinia virus (VV) constructs (rVVs encoding A/Puerto Rico/8/34 influenza virus HA and NP under the control of the VV p7.5 promoter) and human T2 an B6 cells, which are deficient for antigen processing, or murine L929 fibroblasts. VV-expressed TAP1 and TAP2 are functional, but only when expressed together
mouse Ft1+ fibroblasts or TK143 human fibroblasts are infected with a recombinant Vaccinia virus expressing human TAP1/2
recombinant expression of C-terminally His6-tagged wild-type TAP1/TAP2 and C-terminally His6-tagged mutants 7TM- and 6TM-TAP in Spodoptera fugiperda Sf21 cells using the baculovirus transfection method, mutants 7TM-TAP or 6TM-TAP coexpression with HLA-B27/beta2-microglobulin, a TAP construct, and tapasin
recombinant expression of His6-tagged TAP1/TAP2 in Spodoptera fugiperda cells using the baculovirus transfection method
recombinant expression of murine TAP1/2 in RMA-S cells, TlDb cells, and T2Db cells
recombinant expression of rat TAP1, TAP2a, and TAP2u in human TAP1-TAP2-deficient mutant cell line T2
P36370; P36372
recombinant expression of TAP1 and TAP2 in the processing mutant 721.174, which is deficient of both TAP1 and TAP2, functional recombinant coexpression in Swei cells, TAP1 or TAP2 expressed alone possess no capability or very limited capability to bind peptide
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
Q76LI9; Q9PWI8
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
B1N1D9; B1N1E0
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
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
P36370; P36372
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
Q5W414; Q5W417
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Schoelz, C.; Tampe, R.
The peptide-loading complex - antigen translocation and MHC class I loading
Biol. Chem.
390
783-794
2009
Mus musculus (P21958 AND P36371), Rattus norvegicus (P36370 AND P36372), Homo sapiens (Q03518 AND Q03519)
brenda
Shepherd, J.; Schumacher, T.; Ashton-Rickardt, P.; Imaeda, S.; Ploegh, H.; Janeway Jr., C.; Tonegawa, S.
TAP1-dependent peptide translocation in vitro is ATP dependent and peptide selective
Cell
74
577-584
1993
Mus musculus (P21958), Mus musculus C57BL/6 (P21958)
brenda
Koopmann, J.; Post, M.; Neefjes, J.; Haemmerling, G.; Momburg, F.
Translocation of long peptides by transporters associated with antigen processing (TAP)
Eur. J. Immunol.
26
1720-1728
1996
Rattus norvegicus (P36370 AND P36372), Homo sapiens (Q03518 AND Q03519)
brenda
Garbi, N.; Tiwari, N.; Momburg, F.; Haemmerling, G.
A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression
Eur. J. Immunol.
33
264-273
2003
Mus musculus (P21958 AND P36371)
brenda
Hewitt, E.; Lehner, P.
The ABC-transporter signature motif is required for peptide translocation but not peptide binding by TAP
Eur. J. Immunol.
33
422-427
2003
Homo sapiens (Q03518 AND Q03519)
brenda
Procko, E.; Raghuraman, G.; Wiley, D.; Raghavan, M.; Gaudet, R.
Identification of domain boundaries within the N-termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I
Immunol. Cell Biol.
83
475-482
2005
Homo sapiens (Q03518 AND Q03519), Homo sapiens
brenda
Abdel-Motal, U.; Dahmen, J.; Tianmin, L.; Ljunggren, H.; Jondal, M.
External glycopeptide binding to MHC class-I in relation to expression of TAP transporters, beta2-microglobulin and to pH
Immunol. Lett.
54
31-35
1996
Mus musculus (P21958 AND P36371), Mus musculus C57BL/6 (P21958 AND P36371)
brenda
Ritz, U.; Momburg, F.; Pircher, H.; Strand, D.; Huber, C.; Seliger, B.
Identification of sequences in the human peptide transporter subunit TAP1 required for transporter associated with antigen processing (TAP) function
Int. Immunol.
13
31-41
2001
Homo sapiens (Q03518 AND Q03519), Homo sapiens
brenda
Russ, G.; Esquivel, F.; Yewdell, J.; Cresswell, P.; Spies, T.; Bennink, J.
Assembly, intracellular localization, and nucleotide binding properties of the human peptide transporters TAP1 and TAP2 expressed by recombinant vaccinia viruses
J. Biol. Chem.
270
21312-21318
1995
Homo sapiens (Q03518 AND Q03519), Homo sapiens
brenda
Chen, M.; Abele, R.; Tampe, R.
Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
J. Biol. Chem.
278
29686-29692
2003
Homo sapiens (Q03518 AND Q03519)
brenda
Hinz, A.; Jedamzick, J.; Herbring, V.; Fischbach, H.; Hartmann, J.; Parcej, D.; Koch, J.; Tampe, R.
Assembly and function of the major histocompatibility complex (MHC) I peptide-loading complex are conserved across higher vertebrates
J. Biol. Chem.
289
33109-33117
2014
Sus scrofa (A5D9J3 AND A5D9J7), Meleagris gallopavo (B1N1D9 AND B1N1E0), Gallus gallus (B5BSK4 AND B5BSD5), Bos taurus (F1MVY8 AND Q32S33), Mus musculus (P21958 AND P36371), Rattus norvegicus (P36370 AND P36372), Homo sapiens (Q03518 AND Q03519), Anas platyrhynchos (Q2VQZ1 AND Q6JWQ3), Canis lupus familiaris (Q5W414 AND Q5W417), Coturnix japonica (Q76LI9 AND Q9PWI8)
brenda
Schumacher, T.; Kantesaria, D.; Heemels, M.; Ashton-Rickardt, P.; Shepherd, J.; Fruh, K.; Yang, Y.; Peterson, P.; Tonegawa, S.; Ploegh, H.
Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator
J. Exp. Med.
179
533-540
1994
Mus musculus (P21958 AND P36371), Mus musculus, Mus musculus C57B1/6 (P21958 AND P36371)
brenda
Galocha, B.; Hill, A.; Barnett, B.; Dolan, A.; Raimondi, A.; Cook, R.; Brunner, J.; McGeoch, D.; Ploegh, H.
The active site of ICP47, a Herpes simplex virus-encoded inhibitor of the major histocompatibility complex (MHC)-encoded peptide transporter associated with antigen processing (TAP), maps to the NH2-terminal 35 residues
J. Exp. Med.
185
1565-1572
1997
Homo sapiens (Q03518 AND Q03519), Homo sapiens
brenda
Bacik, I.; Cox, J.; Anderson, R.; Yewdell, J.; Bennink, J.
TAP (transporter associated with antigen processing)-independent presentation of endogenously synthesized peptides is enhanced by endoplasmic reticulum insertion sequences located at the amino- but not carboxyl-terminus of the peptide
J. Immunol.
152
381-387
1994
Mus musculus (P21958 AND P36371)
brenda
Momburg, F.; Armandola, E.; Post, M.; Hammerling, G.
Residues in TAP2 peptide transporters controlling substrate specificity
J. Immunol.
156
1756-1763
1996
Rattus norvegicus (P36370 AND P36372)
brenda
Nijenhuis, M.; Hammerling, G.
Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site
J. Immunol.
157
5467-5477
1996
Homo sapiens (Q03518 AND Q03519)
brenda
Yan, G.; Shi, L.; Faustman, D.
Novel splicing of the human MHC-encoded peptide transporter confers unique properties
J. Immunol.
162
852-859
1999
Homo sapiens (Q03518 AND Q03519)
brenda
Leonhardt, R.; Keusekotten, K.; Bekpen, C.; Knittler, M.
Critical role for the tapasin-docking site of TAP2 in the functional integrity of the MHC class I-peptide-loading complex
J. Immunol.
175
5104-5114
2005
Rattus norvegicus (P36370 AND P36372)
brenda
Chang, S.; Lacaille, V.; Guttoh, D.; Androlewicz, M.
Binding and transport of melanoma-specific antigenic peptides by the transporter associated with antigen processing
Mol. Immunol.
33
1165-1169
1996
Homo sapiens (Q03518 AND Q03519)
brenda
Momburg, F.; Tan, P.
Tapasin - The keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum
Mol. Immunol.
39
217-233
2002
Mus musculus (P21958 AND P36371), Homo sapiens (Q03518 AND Q03519)
brenda
Momburg, F.; Roelse, J.; Howard, J.; Butcher, G.; Haemmerling, G.; Neefjes, J.
Selectivity of MHC-encoded peptide transporters from human, mouse and rat
Nature
367
648-651
1994
Mus musculus (P21958 AND P36371), Rattus norvegicus (P36370 AND P36372), Homo sapiens (Q03518 AND Q03519), Mus musculus C57B1/6 (P21958 AND P36371)
brenda
Blees, A.; Januliene, D.; Hofmann, T.; Koller, N.; Schmidt, C.; Trowitzsch, S.; Moeller, A.; Tampe, R.
Structure of the human MHC-I peptide-loading complex
Nature
551
525-528
2017
Homo sapiens (Q03518 AND Q03519), Homo sapiens
brenda
Zhu, K.; Wang, J.; Zhu, J.; Jiang, J.; Shou, J.; Chen, X.
p53 induces TAP1 and enhances the transport of MHC class I peptides
Oncogene
18
7740-7747
1999
Homo sapiens (Q03518)
brenda
Bahram, S.; Arnold, D.; Bresnahan, M.; Strominger, J.; Spies, T.
Two putative subunits of a peptide pump encoded in the human major histocompatibility complex class II region
Proc. Natl. Acad. Sci. USA
88
10094-10098
1991
Homo sapiens (Q03518 AND Q03519), Homo sapiens
brenda
Androlewicz, M.; Ortmann, B.; Van Endert, P.; Spies, T.; Cresswell, P.
Characteristics of peptide and major histocompatibility complex class I/beta2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2)
Proc. Natl. Acad. Sci. USA
91
12716-12720
1994
Homo sapiens (Q03518 AND Q03519)
brenda
Neefjes, J.; Momburg, F.; Haemmerling, G.
Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
Science
261
769-771
1993
Homo sapiens (Q03518 AND Q03519)
brenda