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7VGH

Cryo-EM structure of the human P4-type flippase ATP8B1-CDC50B in the auto-inhibited E2P state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0015247molecular_functionaminophospholipid flippase activity
A0015917biological_processaminophospholipid transport
A0016020cellular_componentmembrane
A0045332biological_processphospholipid translocation
A0070863biological_processpositive regulation of protein exit from endoplasmic reticulum
A0140331biological_processaminophospholipid translocation
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005215molecular_functiontransporter activity
B0005319molecular_functionlipid transporter activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005548molecular_functionphospholipid transporter activity
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005802cellular_componenttrans-Golgi network
B0005886cellular_componentplasma membrane
B0006855biological_processxenobiotic transmembrane transport
B0006869biological_processlipid transport
B0007030biological_processGolgi organization
B0007605biological_processsensory perception of sound
B0012505cellular_componentendomembrane system
B0015247molecular_functionaminophospholipid flippase activity
B0015711biological_processorganic anion transport
B0015721biological_processbile acid and bile salt transport
B0015914biological_processphospholipid transport
B0015917biological_processaminophospholipid transport
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0016887molecular_functionATP hydrolysis activity
B0021650biological_processvestibulocochlear nerve formation
B0032420cellular_componentstereocilium
B0032534biological_processregulation of microvillus assembly
B0034220biological_processmonoatomic ion transmembrane transport
B0045176biological_processapical protein localization
B0045332biological_processphospholipid translocation
B0045892biological_processnegative regulation of DNA-templated transcription
B0046872molecular_functionmetal ion binding
B0060119biological_processinner ear receptor cell development
B0090554molecular_functionphosphatidylcholine floppase activity
B0090556molecular_functionphosphatidylserine floppase activity
B0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
B0140327molecular_functionflippase activity
B0140331biological_processaminophospholipid translocation
B0140345molecular_functionphosphatidylcholine flippase activity
B0140346molecular_functionphosphatidylserine flippase activity
B1901612molecular_functioncardiolipin binding
B1903729biological_processregulation of plasma membrane organization
B1990531cellular_componentphospholipid-translocating ATPase complex
B2001225biological_processregulation of chloride transport
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
BPHD454-THR460

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues248
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues334
DetailsTopological domain: {"description":"Exoplasmic loop","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues217
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"Q9HD20","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8NB49","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q148W0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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