Q8TF62 · AT8B4_HUMAN
- ProteinProbable phospholipid-transporting ATPase IM
- GeneATP8B4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1192 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Cofactor
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 392 | 4-aspartylphosphate intermediate | ||||
Sequence: D | ||||||
Binding site | 392 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 392 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 393 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 394 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 394 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 496 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 537 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 560 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 594 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 674 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 675 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 676 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 789 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 795 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 815 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 818 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 819 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 819 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | phospholipid-translocating ATPase complex | |
Cellular Component | plasma membrane | |
Cellular Component | specific granule membrane | |
Cellular Component | tertiary granule membrane | |
Cellular Component | trans-Golgi network | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATPase-coupled intramembrane lipid transporter activity | |
Molecular Function | magnesium ion binding | |
Biological Process | Golgi organization | |
Biological Process | phospholipid translocation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable phospholipid-transporting ATPase IM
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TF62
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-44 | Cytoplasmic | ||||
Sequence: MFCSEKKLREVERIVKANDREYNEKFQYADNRIHTSKYNILTFL | ||||||
Transmembrane | 45-66 | Helical | ||||
Sequence: PINLFEQFQRVANAYFLCLLIL | ||||||
Topological domain | 67-72 | Exoplasmic loop | ||||
Sequence: QLIPEI | ||||||
Transmembrane | 73-92 | Helical | ||||
Sequence: SSLTWFTTIVPLVLVITMTA | ||||||
Topological domain | 93-276 | Cytoplasmic | ||||
Sequence: VKDATDDYFRHKSDNQVNNRQSEVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRHALSVTSELGADISRLAGFDGIVVCEVPNNKLDKFMGILSWKDSKHSLNNEKIILRGCILRNTSWCFGMVIFAGPDTKLMQNSGKTKFKRTSIDRLMNTL | ||||||
Transmembrane | 277-298 | Helical | ||||
Sequence: VLWIFGFLICLGIILAIGNSIW | ||||||
Topological domain | 299-327 | Exoplasmic loop | ||||
Sequence: ESQTGDQFRTFLFWNEGEKSSVFSGFLTF | ||||||
Transmembrane | 328-349 | Helical | ||||
Sequence: WSYIIILNTVVPISLYVSVEVI | ||||||
Topological domain | 350-871 | Cytoplasmic | ||||
Sequence: RLGHSYFINWDRKMYYSRKAIPAVARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKRCSINGRIYGEVHDDLDQKTEITQEKEPVDFSVKSQADREFQFFDHHLMESIKMGDPKVHEFLRLLALCHTVMSEENSAGELIYQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTLVTYQLLAFLDFNNTRKRMSVIVRNPEGQIKLYSKGADTILFEKLHPSNEVLLSLTSDHLSEFAGEGLRTLAIAYRDLDDKYFKEWHKMLEDANAATEERDERIAGLYEEIERDLMLLGATAVEDKLQEGVIETVTSLSLANIKIWVLTGDKQETAINIGYACNMLTDDMNDVFVIAGNNAVEVREELRKAKQNLFGQNRNFSNGHVVCEKKQQLELDSIVEETITGDYALIINGHSLAHALESDVKNDLLELACMCKTVICCRVTPLQKAQVVELVKKYRNAVTLAIGDGANDVSMIKSAHIGVGISGQEGLQAVLASDYSFAQFRYLQRLLLVHGRWSYFRMCK | ||||||
Transmembrane | 872-892 | Helical | ||||
Sequence: FLCYFFYKNFAFTLVHFWFGF | ||||||
Topological domain | 893-904 | Exoplasmic loop | ||||
Sequence: FCGFSAQTVYDQ | ||||||
Transmembrane | 905-924 | Helical | ||||
Sequence: WFITLFNIVYTSLPVLAMGI | ||||||
Topological domain | 925-954 | Cytoplasmic | ||||
Sequence: FDQDVSDQNSVDCPQLYKPGQLNLLFNKRK | ||||||
Transmembrane | 955-976 | Helical | ||||
Sequence: FFICVLHGIYTSLVLFFIPYGA | ||||||
Topological domain | 977-990 | Exoplasmic loop | ||||
Sequence: FYNVAGEDGQHIAD | ||||||
Transmembrane | 991-1013 | Helical | ||||
Sequence: YQSFAVTMATSLVIVVSVQIALD | ||||||
Topological domain | 1014-1019 | Cytoplasmic | ||||
Sequence: TSYWTF | ||||||
Transmembrane | 1020-1040 | Helical | ||||
Sequence: INHVFIWGSIAIYFSILFTMH | ||||||
Topological domain | 1041-1060 | Exoplasmic loop | ||||
Sequence: SNGIFGIFPNQFPFVGNARH | ||||||
Transmembrane | 1061-1085 | Helical | ||||
Sequence: SLTQKCIWLVILLTTVASVMPVVAF | ||||||
Topological domain | 1086-1192 | Cytoplasmic | ||||
Sequence: RFLKVDLYPTLSDQIRRWQKAQKKARPPSSRRPRTRRSSSRRSGYAFAHQEGYGELITSGKNMRAKNPPPTSGLEKTHYNSTSWIENLCKKTTDTVSSFSQDKTVKL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_046962 | 225 | in dbSNP:rs16963151 | |||
Sequence: N → S | ||||||
Natural variant | VAR_046963 | 452 | in dbSNP:rs2452524 | |||
Sequence: H → N | ||||||
Natural variant | VAR_046964 | 1165 | in dbSNP:rs16962989 | |||
Sequence: N → K | ||||||
Natural variant | VAR_046965 | 1190 | in dbSNP:rs16962987 | |||
Sequence: V → G |
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.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000046368 | 1-1192 | UniProt | Probable phospholipid-transporting ATPase IM | |||
Sequence: MFCSEKKLREVERIVKANDREYNEKFQYADNRIHTSKYNILTFLPINLFEQFQRVANAYFLCLLILQLIPEISSLTWFTTIVPLVLVITMTAVKDATDDYFRHKSDNQVNNRQSEVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRHALSVTSELGADISRLAGFDGIVVCEVPNNKLDKFMGILSWKDSKHSLNNEKIILRGCILRNTSWCFGMVIFAGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLICLGIILAIGNSIWESQTGDQFRTFLFWNEGEKSSVFSGFLTFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWDRKMYYSRKAIPAVARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKRCSINGRIYGEVHDDLDQKTEITQEKEPVDFSVKSQADREFQFFDHHLMESIKMGDPKVHEFLRLLALCHTVMSEENSAGELIYQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTLVTYQLLAFLDFNNTRKRMSVIVRNPEGQIKLYSKGADTILFEKLHPSNEVLLSLTSDHLSEFAGEGLRTLAIAYRDLDDKYFKEWHKMLEDANAATEERDERIAGLYEEIERDLMLLGATAVEDKLQEGVIETVTSLSLANIKIWVLTGDKQETAINIGYACNMLTDDMNDVFVIAGNNAVEVREELRKAKQNLFGQNRNFSNGHVVCEKKQQLELDSIVEETITGDYALIINGHSLAHALESDVKNDLLELACMCKTVICCRVTPLQKAQVVELVKKYRNAVTLAIGDGANDVSMIKSAHIGVGISGQEGLQAVLASDYSFAQFRYLQRLLLVHGRWSYFRMCKFLCYFFYKNFAFTLVHFWFGFFCGFSAQTVYDQWFITLFNIVYTSLPVLAMGIFDQDVSDQNSVDCPQLYKPGQLNLLFNKRKFFICVLHGIYTSLVLFFIPYGAFYNVAGEDGQHIADYQSFAVTMATSLVIVVSVQIALDTSYWTFINHVFIWGSIAIYFSILFTMHSNGIFGIFPNQFPFVGNARHSLTQKCIWLVILLTTVASVMPVVAFRFLKVDLYPTLSDQIRRWQKAQKKARPPSSRRPRTRRSSSRRSGYAFAHQEGYGELITSGKNMRAKNPPPTSGLEKTHYNSTSWIENLCKKTTDTVSSFSQDKTVKL | |||||||
Modified residue (large scale data) | 728 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1166 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1168 | PRIDE | Phosphoserine | ||||
Sequence: S |
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TF62 | TMEM30A Q9NV96 | 4 | EBI-9527207, EBI-2836942 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1104-1130 | Disordered | ||||
Sequence: QKAQKKARPPSSRRPRTRRSSSRRSGY | ||||||
Compositional bias | 1106-1124 | Basic residues | ||||
Sequence: AQKKARPPSSRRPRTRRSS | ||||||
Region | 1143-1163 | Disordered | ||||
Sequence: TSGKNMRAKNPPPTSGLEKTH |
Sequence similarities
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,192
- Mass (Da)135,868
- Last updated2008-10-14 v3
- ChecksumFFE8D935B7544D73
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YMP8 | H0YMP8_HUMAN | ATP8B4 | 717 | ||
H0YM66 | H0YM66_HUMAN | ATP8B4 | 84 | ||
H0YLJ1 | H0YLJ1_HUMAN | ATP8B4 | 122 | ||
H0YMB5 | H0YMB5_HUMAN | ATP8B4 | 53 | ||
H0YLC1 | H0YLC1_HUMAN | ATP8B4 | 95 | ||
A0A6I8PRR9 | A0A6I8PRR9_HUMAN | ATP8B4 | 345 | ||
A0A6I8PS08 | A0A6I8PS08_HUMAN | ATP8B4 | 237 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 631 | in Ref. 1; BAB85525 | ||||
Sequence: G → E | ||||||
Compositional bias | 1106-1124 | Basic residues | ||||
Sequence: AQKKARPPSSRRPRTRRSS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |