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5U1D

Cryo-EM structure of the human TAP ATP-Binding Cassette Transporter

Functional Information from GO Data
ChainGOidnamespacecontents
A0002250biological_processadaptive immune response
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006952biological_processdefense response
A0015031biological_processprotein transport
A0015433molecular_functionABC-type peptide antigen transporter activity
A0015833biological_processpeptide transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
A0023029molecular_functionMHC class Ib protein binding
A0030670cellular_componentphagocytic vesicle membrane
A0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
A0034451cellular_componentcentriolar satellite
A0042288molecular_functionMHC class I protein binding
A0042605molecular_functionpeptide antigen binding
A0042803molecular_functionprotein homodimerization activity
A0042824cellular_componentMHC class I peptide loading complex
A0042825cellular_componentTAP complex
A0043531molecular_functionADP binding
A0046872molecular_functionmetal ion binding
A0046967biological_processcytosol to endoplasmic reticulum transport
A0046978molecular_functionTAP1 binding
A0046979molecular_functionTAP2 binding
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
A1904680molecular_functionpeptide transmembrane transporter activity
B0001913biological_processT cell mediated cytotoxicity
B0001916biological_processpositive regulation of T cell mediated cytotoxicity
B0002237biological_processresponse to molecule of bacterial origin
B0002250biological_processadaptive immune response
B0002481biological_processantigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent
B0002485biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent
B0002489biological_processantigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0015031biological_processprotein transport
B0015433molecular_functionABC-type peptide antigen transporter activity
B0015440molecular_functionABC-type peptide transporter activity
B0015833biological_processpeptide transport
B0016020cellular_componentmembrane
B0016607cellular_componentnuclear speck
B0016887molecular_functionATP hydrolysis activity
B0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
B0023029molecular_functionMHC class Ib protein binding
B0030670cellular_componentphagocytic vesicle membrane
B0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
B0042287molecular_functionMHC protein binding
B0042605molecular_functionpeptide antigen binding
B0042824cellular_componentMHC class I peptide loading complex
B0042825cellular_componentTAP complex
B0046872molecular_functionmetal ion binding
B0046967biological_processcytosol to endoplasmic reticulum transport
B0046968biological_processpeptide antigen transport
B0046978molecular_functionTAP1 binding
B0046980molecular_functiontapasin binding
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
B1904680molecular_functionpeptide transmembrane transporter activity
X0005737cellular_componentcytoplasm
X0019049biological_processvirus-mediated perturbation of host defense response
X0030430cellular_componenthost cell cytoplasm
X0039588biological_processsymbiont-mediated suppression of host antigen processing and presentation
X0042025cellular_componenthost cell nucleus
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LAAGQKQRLAIARAL
ChainResidueDetails
BLEU607-LEU621
ALEU643-LEU657

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues59
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
BMET1-LEU6
BSER78-PRO98
BPRO170-HIS187
BILE288-THR293
BLEU396-SER408

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BARG7-LEU27

site_idSWS_FT_FI3
Number of Residues428
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BGLY28-ARG56
BSER120-ASP148
BCYS209-LEU266
BGLN315-ALA374
BTYR430-LEU686

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BGLY57-VAL77

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BTRP99-LEU119

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BLEU149-ILE169

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BALA188-GLY208

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BASN267-SER287

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BLEU294-HIS314

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=8 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BLEU375-GLY395

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=9 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BLEU409-ILE429

site_idSWS_FT_FI12
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
BGLY503

site_idSWS_FT_FI13
Number of Residues1
DetailsSITE: Inter-subunit salt bridge with TAPBP => ECO:0000269|PubMed:26611325
ChainResidueDetails
BASP16
ASER641

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PDB entries from 2024-07-24

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