TAP2
entrez
6891
canonical
uniprot
Q03519
canonical
ensembl
ENSG00000204267
resolver
ensembl
ENSG00000206235
resolver
ensembl
ENSG00000206299
resolver
ensembl
ENSG00000223481
resolver
ensembl
ENSG00000225967
resolver
ensembl
ENSG00000228582
resolver
ensembl
ENSG00000232326
resolver
ensembl
ENSG00000237599
resolver
ensp
ENSP00000364032
resolver
ensp
ENSP00000390013
resolver
ensp
ENSP00000393580
resolver
ensp
ENSP00000406540
resolver
ensp
ENSP00000416471
resolver
ensp
ENSP00000498827
resolver
enst
ENST00000419142
resolver
enst
ENST00000452371
resolver
enst
ENST00000455842
resolver
enst
ENST00000457634
resolver
genesymbol
TAP2
resolver
genesymbol_syn
ABCB3
resolver
genesymbol_syn
PSF2
resolver
genesymbol_syn
RING11
resolver
genesymbol_syn
Y1
resolver
hgnc
HGNC:44
resolver
uniprot
B0V2J8
resolver
uniprot
O95410
resolver
uniprot
Q53FI6
resolver
uniprot
Q5HY71
resolver
uniprot
Q5JNW1
resolver
uniprot
Q96PT8
resolver
uniprot
Q9UP03
resolver
uniprot
Q9UQ83
resolver
uniprot
X5CMH5
resolver
uniprot_entry
Q5JNW1_HUMAN
resolver
uniprot_entry
Q9UP03_HUMAN
resolver
uniprot_entry
TAP2_HUMAN
resolver
uniprot_entry
X5CMH5_HUMAN
resolver
uniprot_sec
B0V2J8
resolver
uniprot_sec
O95410
resolver
uniprot_sec
Q53FI6
resolver
uniprot_sec
Q5HY71
resolver
uniprot_sec
Q96PT8
resolver
uniprot_sec
Q9UQ83
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
MRLPDLRPWTSLLLVDAALLWLLQGPLGTLLPQGLPGLWLEGTLRLGGLWGLLKLRGLLGFVGTLLLPLCLATPLTVSLRALVAGASRAPPARVASAPWSWLLVGYGAAGLSWSLWAVLSPPGAQEKEQDQVNNKVLMWRLLKLSRPDLPLLVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDRQPNLPSPGTLAPTTLQGVVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQALQDWNSRGDRTVLVIAHRLQTVQRAHQILVLQEGKLQKLAQL
uniprot
proteins
disease_involvement
DISEASE: MHC class I deficiency 2 (MHC1D2) [MIM:620813]: An autosomal recessive, progressive disorder characterized by chronic bacterial infections of the upper and lower respiratory tract apparent in the first or second decades of life, nasal polyps, and ulcers with granulomatous inflammation affecting the nasal cavity, upper respiratory tract, or skin. Patients may develop bronchiectasis and respiratory failure. {ECO:0000269|PubMed:7517574}. 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 TAP1 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
75664
uniprot
proteins
mutagenesis
MUTAGEN 16; /note="D->K: Complete loss of interaction with TAPBP, resulting in impaired PLC assembly and antigen presentation."; /evidence="ECO:0000269|PubMed:26611325"; MUTAGEN 638; /note="D->A: Inactive in peptide transport when associated with 'A-734' of TAP1."; /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
10227971
uniprot
proteins
pubmed
10605026
uniprot
proteins
pubmed
11157746
uniprot
proteins
pubmed
11274390
uniprot
proteins
pubmed
11294565
uniprot
proteins
pubmed
1453454
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
1538751
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1570316
uniprot
proteins
pubmed
1589036
uniprot
proteins
pubmed
1741401
uniprot
proteins
pubmed
19201886
uniprot
proteins
pubmed
1946428
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22638925
uniprot
proteins
pubmed
25377891
uniprot
proteins
pubmed
25656091
uniprot
proteins
pubmed
26611325
uniprot
proteins
pubmed
7500034
uniprot
proteins
pubmed
7517574
uniprot
proteins
pubmed
7760936
uniprot
proteins
pubmed
7792761
uniprot
proteins
pubmed
8162639
uniprot
proteins
pubmed
8428770
uniprot
proteins
pubmed
8568858
uniprot
proteins
pubmed
8630735
uniprot
proteins
pubmed
8670825
uniprot
proteins
pubmed
8805302
uniprot
proteins
pubmed
8955196
uniprot
proteins
pubmed
9175839
uniprot
proteins
pubmed
9256420
uniprot
proteins
pubmed
9324024
uniprot
proteins
pubmed
9427624
uniprot
proteins
pubmed
9672156
uniprot
proteins
pubmed
9916708
uniprot
proteins
sequence_length
686
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 7..27; /note="Helical; Name=1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 57..77; /note="Helical; Name=2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 99..119; /note="Helical; Name=3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 149..169; /note="Helical; Name=4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 188..208; /note="Helical; Name=5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 267..287; /note="Helical; Name=6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 294..314; /note="Helical; Name=7"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 375..395; /note="Helical; Name=8"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 409..429; /note="Helical; Name=9"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441
uniprot
proteins