TAP1
entrez
6890
canonical
uniprot
Q03518
canonical
ensembl
ENSG00000168394
resolver
ensembl
ENSG00000206297
resolver
ensembl
ENSG00000224212
resolver
ensembl
ENSG00000226173
resolver
ensembl
ENSG00000227816
resolver
ensembl
ENSG00000230705
resolver
ensembl
ENSG00000232367
resolver
ensp
ENSP00000346206
resolver
genesymbol
TAP1
resolver
genesymbol_syn
ABCB2
resolver
genesymbol_syn
PSF1
resolver
genesymbol_syn
RING4
resolver
genesymbol_syn
Y3
resolver
hgnc
HGNC:43
resolver
uniprot
A0A0S2Z5A6
resolver
uniprot
B7Z7P4
resolver
uniprot
Q16149
resolver
uniprot
Q96CP4
resolver
uniprot_entry
A0A0S2Z5A6_HUMAN
resolver
uniprot_entry
B7Z7P4_HUMAN
resolver
uniprot_entry
TAP1_HUMAN
resolver
uniprot_sec
Q16149
resolver
uniprot_sec
Q96CP4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited at high ER lumenal peptide concentrations. {ECO:0000269|PubMed:25377891}.; ACTIVITY REGULATION: (Microbial infection) Inhibited by herpes simplex virus US12/ICP47 protein, which blocks the peptide-binding site of TAP1-TAP2. {ECO:0000269|PubMed:25656091, ECO:0000269|PubMed:8670825}.; ACTIVITY REGULATION: (Microbial infection) Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of TAP1-TAP2 complex and inhibits peptide translocation by specifically blocking ATP-binding and preventing TAP1-TAP2 conformational rearrangement induced by peptide binding. {ECO:0000269|PubMed:11157746, ECO:0000269|PubMed:25656091, ECO:0000269|PubMed:9175839}.
uniprot
proteins
amino_acid_sequence
MASSRCPAPRGCRCLPGASLAWLGTVLLLLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGSKSENAGAQGWLAALKPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGSHPTAFVVSYAAALPAAALWHKLGSLWVPGGQGGSGNPVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQAPADAPE
uniprot
proteins
disease_involvement
DISEASE: MHC class I deficiency 1 (MHC1D1) [MIM:604571]: An autosomal recessive immunologic disorder characterized by chronic bacterial infections of the respiratory tract, beginning in the first or second decade of life and usually progressing to bronchiectasis. Patients have nasal polyps and may develop chronic necrotizing granulomatous lesions affecting the nasal cavity, upper respiratory tract, and skin. {ECO:0000269|PubMed:10074494}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
7.4.2.14
uniprot
proteins
function
FUNCTION: ABC transporter associated with antigen processing. In complex with TAP2 mediates unidirectional translocation of peptide antigens from cytosol to endoplasmic reticulum (ER) for loading onto MHC class I (MHCI) molecules (PubMed:25377891, PubMed:25656091). Uses the chemical energy of ATP to export peptides against the concentration gradient (PubMed:25377891). During the transport cycle alternates between 'inward-facing' state with peptide binding site facing the cytosol to 'outward-facing' state with peptide binding site facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a switch to hydrolysis-competent 'outward-facing' conformation ready for peptide loading onto nascent MHCI molecules. Subsequently ATP hydrolysis resets the transporter to the 'inward facing' state for a new cycle (PubMed:11274390, PubMed:25377891, PubMed:25656091). Typically transports intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome. Binds peptides with free N- and C-termini, the first three and the C-terminal residues being critical. Preferentially selects peptides having a highly hydrophobic residue at position 3 and hydrophobic or charged residues at the C-terminal anchor. Proline at position 2 has the most destabilizing effect (PubMed:11274390, PubMed:7500034, PubMed:9256420). As a component of the peptide loading complex (PLC), acts as a molecular scaffold essential for peptide-MHCI assembly and antigen presentation (PubMed:1538751, PubMed:25377891, PubMed:26611325). {ECO:0000269|PubMed:11274390, ECO:0000269|PubMed:1538751, ECO:0000269|PubMed:25377891, ECO:0000269|PubMed:25656091, ECO:0000269|PubMed:26611325, ECO:0000269|PubMed:7500034, ECO:0000269|PubMed:9256420}.
uniprot
proteins
mass_dalton
80965
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="D->K: Complete loss of interaction with TAPBP, resulting in impaired PLC assembly and antigen presentation."; /evidence="ECO:0000269|PubMed:26611325"; MUTAGEN 674; /note="D->A: Impairs allosteric coupling of peptide transport to ATP hydrolysis, converting the unidirectional active pump into a passive bidirectional nucleotide-gated facilitator. Inactive in peptide transport when associated with 'A-638' of TAP2."; /evidence="ECO:0000269|PubMed:25377891
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCB family
uniprot
proteins
protein_family
MHC peptide exporter (TC 3.A.1.209) subfamily
uniprot
proteins
pubmed
10074494
uniprot
proteins
pubmed
10227971
uniprot
proteins
pubmed
10605026
uniprot
proteins
pubmed
11157746
uniprot
proteins
pubmed
11250043
uniprot
proteins
pubmed
11274390
uniprot
proteins
pubmed
11532960
uniprot
proteins
pubmed
12878362
uniprot
proteins
pubmed
1453454
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
1538751
uniprot
proteins
pubmed
15488952
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1570316
uniprot
proteins
pubmed
1589036
uniprot
proteins
pubmed
19201886
uniprot
proteins
pubmed
1946428
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2259383
uniprot
proteins
pubmed
2259384
uniprot
proteins
pubmed
22638925
uniprot
proteins
pubmed
25377891
uniprot
proteins
pubmed
25656091
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26611325
uniprot
proteins
pubmed
7500034
uniprot
proteins
pubmed
7760936
uniprot
proteins
pubmed
8168860
uniprot
proteins
pubmed
8248212
uniprot
proteins
pubmed
8568858
uniprot
proteins
pubmed
8630735
uniprot
proteins
pubmed
8640228
uniprot
proteins
pubmed
8670825
uniprot
proteins
pubmed
8805302
uniprot
proteins
pubmed
8955196
uniprot
proteins
pubmed
9175839
uniprot
proteins
pubmed
9256420
uniprot
proteins
pubmed
9310490
uniprot
proteins
pubmed
9427624
uniprot
proteins
sequence_length
748
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1589036, ECO:0000269|PubMed:22638925}; Multi-pass membrane protein {ECO:0000255}. Note=The transmembrane segments seem to form a pore in the membrane.
uniprot
proteins
transmembrane_region
TRANSMEM 16..36; /note="Helical; Name=1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 54..76; /note="Helical; Name=2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 93..113; /note="Helical; Name=3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 134..154; /note="Helical; Name=4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 187..207; /note="Helical; Name=5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 228..248; /note="Helical; Name=6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 299..319; /note="Helical; Name=7"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 329..349; /note="Helical; Name=8"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 419..439; /note="Helical; Name=9"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 444..464; /note="Helical; Name=10"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441
uniprot
proteins