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8WVG

Human VMAT2 in complex with tetrabenazine

Functional Information from GO Data
ChainGOidnamespacecontents
A0001975biological_processresponse to amphetamine
A0002552biological_processserotonin secretion by mast cell
A0002553biological_processhistamine secretion by mast cell
A0005335molecular_functionserotonin:sodium:chloride symporter activity
A0005515molecular_functionprotein binding
A0005813cellular_componentcentrosome
A0005886cellular_componentplasma membrane
A0006836biological_processneurotransmitter transport
A0006837biological_processserotonin transport
A0007268biological_processchemical synaptic transmission
A0007626biological_processlocomotory behavior
A0008021cellular_componentsynaptic vesicle
A0008504molecular_functionmonoamine transmembrane transporter activity
A0009636biological_processresponse to toxic substance
A0009791biological_processpost-embryonic development
A0015311molecular_functionmonoamine:proton antiporter activity
A0015842biological_processaminergic neurotransmitter loading into synaptic vesicle
A0015844biological_processmonoamine transport
A0015872biological_processdopamine transport
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0030658cellular_componenttransport vesicle membrane
A0030667cellular_componentsecretory granule membrane
A0030672cellular_componentsynaptic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0042995cellular_componentcell projection
A0043195cellular_componentterminal bouton
A0045202cellular_componentsynapse
A0051610biological_processserotonin uptake
A0051615biological_processhistamine uptake
A0051649biological_processestablishment of localization in cell
A0055085biological_processtransmembrane transport
A0070083cellular_componentclathrin-sculpted monoamine transport vesicle membrane
A0098691cellular_componentdopaminergic synapse
A0098700biological_processneurotransmitter loading into synaptic vesicle
A0099123biological_processsomato-dendritic dopamine secretion
A1902600biological_processproton transmembrane transport
A1903427biological_processnegative regulation of reactive oxygen species biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR192-HIS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues112
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
AMET1-LYS20
ALEU151-PRO159
ATYR211-ASN219
APRO272-ASP291
AHIS353-ARG357
AASP411-HIS414
APHE463-ASP514

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
ALEU21-VAL41

site_idSWS_FT_FI3
Number of Residues130
DetailsTOPO_DOM: Lumenal, vesicle => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
APRO42-VAL129
ASER181-ARG189
ATYR243-LYS248
AGLU312-TRP328
ALYS379-PHE389
AGLY436-GLY440

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
AGLN130-GLY150

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
AILE160-SER180

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
ASER190-VAL210

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
AVAL220-LEU242

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
ATHR249-GLN271

site_idSWS_FT_FI9
Number of Residues19
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
APRO292-LEU311

site_idSWS_FT_FI10
Number of Residues23
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
AGLN329-ALA352

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
ATRP358-ALA378

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
AGLY390-VAL410

site_idSWS_FT_FI13
Number of Residues20
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
AVAL415-ILE435

site_idSWS_FT_FI14
Number of Residues21
DetailsTRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0000269|PubMed:38517752, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8JT9, ECO:0007744|PDB:8JTA, ECO:0007744|PDB:8JTC, ECO:0007744|PDB:8T69, ECO:0007744|PDB:8T6A, ECO:0007744|PDB:8T6B, ECO:0007744|PDB:8THR
ChainResidueDetails
AGLY441-LEU462

site_idSWS_FT_FI15
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:38081299
ChainResidueDetails
ALEU228
ATYR341
AASP399

site_idSWS_FT_FI16
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299
ChainResidueDetails
AVAL232
AILE308

site_idSWS_FT_FI17
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:38081299, ECO:0007744|PDB:8JSW
ChainResidueDetails
AASN305

site_idSWS_FT_FI18
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0007744|PDB:8JSW, ECO:0007744|PDB:8T6B
ChainResidueDetails
AGLU312

site_idSWS_FT_FI19
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:37914936, ECO:0000269|PubMed:38081299, ECO:0007744|PDB:8T6B
ChainResidueDetails
APHE334
ATYR433

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q01827
ChainResidueDetails
ASER511
ASER513

site_idSWS_FT_FI21
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN84
AASN91

236963

PDB entries from 2025-06-04

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