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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6MPB

Cryo-EM structure of the human neutral amino acid transporter ASCT2

Functional Information from GO Data
ChainGOidnamespacecontents
A0001618molecular_functionvirus receptor activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006865biological_processamino acid transport
A0006868biological_processglutamine transport
A0009925cellular_componentbasal plasma membrane
A0010585biological_processglutamine secretion
A0015171molecular_functionamino acid transmembrane transporter activity
A0015175molecular_functionneutral L-amino acid transmembrane transporter activity
A0015183molecular_functionL-aspartate transmembrane transporter activity
A0015186molecular_functionL-glutamine transmembrane transporter activity
A0015194molecular_functionL-serine transmembrane transporter activity
A0015293molecular_functionsymporter activity
A0015297molecular_functionantiporter activity
A0015804biological_processneutral amino acid transport
A0015825biological_processL-serine transport
A0016020cellular_componentmembrane
A0022834molecular_functionligand-gated channel activity
A0030218biological_processerythrocyte differentiation
A0034451cellular_componentcentriolar satellite
A0036064cellular_componentciliary basal body
A0038023molecular_functionsignaling receptor activity
A0042470cellular_componentmelanosome
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0070207biological_processprotein homotrimerization
A0140009biological_processL-aspartate import across plasma membrane
A0150104biological_processtransport across blood-brain barrier
A1903803biological_processL-glutamine import across plasma membrane
B0001618molecular_functionvirus receptor activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006865biological_processamino acid transport
B0006868biological_processglutamine transport
B0009925cellular_componentbasal plasma membrane
B0010585biological_processglutamine secretion
B0015171molecular_functionamino acid transmembrane transporter activity
B0015175molecular_functionneutral L-amino acid transmembrane transporter activity
B0015183molecular_functionL-aspartate transmembrane transporter activity
B0015186molecular_functionL-glutamine transmembrane transporter activity
B0015194molecular_functionL-serine transmembrane transporter activity
B0015293molecular_functionsymporter activity
B0015297molecular_functionantiporter activity
B0015804biological_processneutral amino acid transport
B0015825biological_processL-serine transport
B0016020cellular_componentmembrane
B0022834molecular_functionligand-gated channel activity
B0030218biological_processerythrocyte differentiation
B0034451cellular_componentcentriolar satellite
B0036064cellular_componentciliary basal body
B0038023molecular_functionsignaling receptor activity
B0042470cellular_componentmelanosome
B0046718biological_processsymbiont entry into host cell
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0070207biological_processprotein homotrimerization
B0140009biological_processL-aspartate import across plasma membrane
B0150104biological_processtransport across blood-brain barrier
B1903803biological_processL-glutamine import across plasma membrane
C0001618molecular_functionvirus receptor activity
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0006865biological_processamino acid transport
C0006868biological_processglutamine transport
C0009925cellular_componentbasal plasma membrane
C0010585biological_processglutamine secretion
C0015171molecular_functionamino acid transmembrane transporter activity
C0015175molecular_functionneutral L-amino acid transmembrane transporter activity
C0015183molecular_functionL-aspartate transmembrane transporter activity
C0015186molecular_functionL-glutamine transmembrane transporter activity
C0015194molecular_functionL-serine transmembrane transporter activity
C0015293molecular_functionsymporter activity
C0015297molecular_functionantiporter activity
C0015804biological_processneutral amino acid transport
C0015825biological_processL-serine transport
C0016020cellular_componentmembrane
C0022834molecular_functionligand-gated channel activity
C0030218biological_processerythrocyte differentiation
C0034451cellular_componentcentriolar satellite
C0036064cellular_componentciliary basal body
C0038023molecular_functionsignaling receptor activity
C0042470cellular_componentmelanosome
C0046718biological_processsymbiont entry into host cell
C0046872molecular_functionmetal ion binding
C0070062cellular_componentextracellular exosome
C0070207biological_processprotein homotrimerization
C0140009biological_processL-aspartate import across plasma membrane
C0150104biological_processtransport across blood-brain barrier
C1903803biological_processL-glutamine import across plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00713
Number of Residues15
DetailsNA_DICARBOXYL_SYMP_1 Sodium:dicarboxylate symporter family signature 1. P.GElLLrLLRMIIlP
ChainResidueDetails
BPRO92-PRO106
site_idPS00714
Number of Residues24
DetailsNA_DICARBOXYL_SYMP_2 Sodium:dicarboxylate symporter family signature 2. PiGaTvNMDGAaLFqcVaaVFIAQ
ChainResidueDetails
BPRO380-GLN403
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues87
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"29872227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues378
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues63
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"29872227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues99
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues66
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"29872227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues69
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"29872227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues81
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"29872227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues63
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"29872227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues189
DetailsIntramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"29872227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues78
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"29872227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues63
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"29872227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O59010","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P43003","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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