Q8TF62 · AT8B4_HUMAN

  • Protein
    Probable phospholipid-transporting ATPase IM
  • Gene
    ATP8B4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable).

Catalytic activity

  • ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
    EC:7.6.2.1 (UniProtKB | ENZYME | Rhea)

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site, binding site.

111921002003004005006007008009001,0001,100
TypeIDPosition(s)Description
Active site3924-aspartylphosphate intermediate
Binding site392ATP (UniProtKB | ChEBI)
Binding site392Mg2+ (UniProtKB | ChEBI)
Binding site393ATP (UniProtKB | ChEBI)
Binding site394ATP (UniProtKB | ChEBI)
Binding site394Mg2+ (UniProtKB | ChEBI)
Binding site496ATP (UniProtKB | ChEBI)
Binding site537ATP (UniProtKB | ChEBI)
Binding site560ATP (UniProtKB | ChEBI)
Binding site594ATP (UniProtKB | ChEBI)
Binding site674ATP (UniProtKB | ChEBI)
Binding site675ATP (UniProtKB | ChEBI)
Binding site676ATP (UniProtKB | ChEBI)
Binding site789ATP (UniProtKB | ChEBI)
Binding site795ATP (UniProtKB | ChEBI)
Binding site815Mg2+ (UniProtKB | ChEBI)
Binding site818ATP (UniProtKB | ChEBI)
Binding site819ATP (UniProtKB | ChEBI)
Binding site819Mg2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentGolgi apparatus
Cellular Componentphospholipid-translocating ATPase complex
Cellular Componentplasma membrane
Cellular Componentspecific granule membrane
Cellular Componenttertiary granule membrane
Cellular Componenttrans-Golgi network
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATPase-coupled intramembrane lipid transporter activity
Molecular Functionmagnesium ion binding
Biological ProcessGolgi organization
Biological Processphospholipid translocation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable phospholipid-transporting ATPase IM
  • EC number
  • Alternative names
    • ATPase class I type 8B member 4
    • P4-ATPase flippase complex alpha subunit ATP8B4

Gene names

    • Name
      ATP8B4
    • Synonyms
      KIAA1939

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q8TF62
  • Secondary accessions
    • Q9H727

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-44Cytoplasmic
Transmembrane45-66Helical
Topological domain67-72Exoplasmic loop
Transmembrane73-92Helical
Topological domain93-276Cytoplasmic
Transmembrane277-298Helical
Topological domain299-327Exoplasmic loop
Transmembrane328-349Helical
Topological domain350-871Cytoplasmic
Transmembrane872-892Helical
Topological domain893-904Exoplasmic loop
Transmembrane905-924Helical
Topological domain925-954Cytoplasmic
Transmembrane955-976Helical
Topological domain977-990Exoplasmic loop
Transmembrane991-1013Helical
Topological domain1014-1019Cytoplasmic
Transmembrane1020-1040Helical
Topological domain1041-1060Exoplasmic loop
Transmembrane1061-1085Helical
Topological domain1086-1192Cytoplasmic

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_046962225in dbSNP:rs16963151
Natural variantVAR_046963452in dbSNP:rs2452524
Natural variantVAR_0469641165in dbSNP:rs16962989
Natural variantVAR_0469651190in dbSNP:rs16962987

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,680 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00000463681-1192UniProtProbable phospholipid-transporting ATPase IM
Modified residue (large scale data)728PRIDEPhosphoserine
Modified residue (large scale data)1166PRIDEPhosphoserine
Modified residue (large scale data)1168PRIDEPhosphoserine

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitously expressed at moderate levels.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit (Probable). Interacts with beta subunits TMEM30A and TMEM30B.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q8TF62TMEM30A Q9NV964EBI-9527207, EBI-2836942
View interactors in UniProtKB
View CPX-6305 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1104-1130Disordered
Compositional bias1106-1124Basic residues
Region1143-1163Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,192
  • Mass (Da)
    135,868
  • Last updated
    2008-10-14 v3
  • Checksum
    FFE8D935B7544D73
MFCSEKKLREVERIVKANDREYNEKFQYADNRIHTSKYNILTFLPINLFEQFQRVANAYFLCLLILQLIPEISSLTWFTTIVPLVLVITMTAVKDATDDYFRHKSDNQVNNRQSEVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRHALSVTSELGADISRLAGFDGIVVCEVPNNKLDKFMGILSWKDSKHSLNNEKIILRGCILRNTSWCFGMVIFAGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLICLGIILAIGNSIWESQTGDQFRTFLFWNEGEKSSVFSGFLTFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWDRKMYYSRKAIPAVARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKRCSINGRIYGEVHDDLDQKTEITQEKEPVDFSVKSQADREFQFFDHHLMESIKMGDPKVHEFLRLLALCHTVMSEENSAGELIYQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTLVTYQLLAFLDFNNTRKRMSVIVRNPEGQIKLYSKGADTILFEKLHPSNEVLLSLTSDHLSEFAGEGLRTLAIAYRDLDDKYFKEWHKMLEDANAATEERDERIAGLYEEIERDLMLLGATAVEDKLQEGVIETVTSLSLANIKIWVLTGDKQETAINIGYACNMLTDDMNDVFVIAGNNAVEVREELRKAKQNLFGQNRNFSNGHVVCEKKQQLELDSIVEETITGDYALIINGHSLAHALESDVKNDLLELACMCKTVICCRVTPLQKAQVVELVKKYRNAVTLAIGDGANDVSMIKSAHIGVGISGQEGLQAVLASDYSFAQFRYLQRLLLVHGRWSYFRMCKFLCYFFYKNFAFTLVHFWFGFFCGFSAQTVYDQWFITLFNIVYTSLPVLAMGIFDQDVSDQNSVDCPQLYKPGQLNLLFNKRKFFICVLHGIYTSLVLFFIPYGAFYNVAGEDGQHIADYQSFAVTMATSLVIVVSVQIALDTSYWTFINHVFIWGSIAIYFSILFTMHSNGIFGIFPNQFPFVGNARHSLTQKCIWLVILLTTVASVMPVVAFRFLKVDLYPTLSDQIRRWQKAQKKARPPSSRRPRTRRSSSRRSGYAFAHQEGYGELITSGKNMRAKNPPPTSGLEKTHYNSTSWIENLCKKTTDTVSSFSQDKTVKL

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0YMP8H0YMP8_HUMANATP8B4717
H0YM66H0YM66_HUMANATP8B484
H0YLJ1H0YLJ1_HUMANATP8B4122
H0YMB5H0YMB5_HUMANATP8B453
H0YLC1H0YLC1_HUMANATP8B495
A0A6I8PRR9A0A6I8PRR9_HUMANATP8B4345
A0A6I8PS08A0A6I8PS08_HUMANATP8B4237

Sequence caution

The sequence BAB15072.1 differs from that shown. Reason: Frameshift
The sequence BAB85525.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Sequence of unknown origin inserted in the coding sequence.

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict631in Ref. 1; BAB85525
Compositional bias1106-1124Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB075819
EMBL· GenBank· DDBJ
BAB85525.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AC009753
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC016045
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC025040
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AK025125
EMBL· GenBank· DDBJ
BAB15072.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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