ATP11B
Phospholipid-transporting ATPase IF
Also known as: AT11B_HUMAN, ATPIF, ATPIR, KIAA0956
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9Y2G3
- Gene
- ATP11B
- Ensembl
- ENSG00000058063
- Chromosome
- 3
- Canonical length
- 1177 aa
- Protein class
- Enzymes, Predicted membrane proteins, Transporters
- Subcellular location
- Centriolar satellite,Cytosol
OverviewNCBI Gene
P-type ATPases, such as ATP11B, are phosphorylated in their intermediate state and drive uphill transport of ions across membranes. Several subfamilies of P-type ATPases have been identified. One subfamily transports heavy metal ions, such as Cu(2+) or Cd(2+). Another subfamily transports non-heavy metal ions, such as H(+), Na(+), K(+), or Ca(+). A third subfamily transports amphipaths, such as phosphatidylserine.[supplied by OMIM, Feb 2005]
Canonical amino-acid sequenceUniProt
1177 residues, UniProt reviewed canonical sequence.
>Q9Y2G3|ATP11B
1 MWRWIRQQLG FDPPHQSDTR TIYVANRFPQ NGLYTPQKFI DNRIISSKYT VWNFVPKNLF
61 EQFRRVANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV TAIKQGYEDW LRHNSDNEVN
121 GAPVYVVRSG GLVKTRSKNI RVGDIVRIAK DEIFPADLVL LSSDRLDGSC HVTTASLDGE
181 TNLKTHVAVP ETALLQTVAN LDTLVAVIEC QQPEADLYRF MGRMIITQQM EEIVRPLGPE
241 SLLLRGARLK NTKEIFGVAV YTGMETKMAL NYKSKSQKRS AVEKSMNTFL IIYLVILISE
301 AVISTILKYT WQAEEKWDEP WYNQKTEHQR NSSKILRFIS DFLAFLVLYN FIIPISLYVT
361 VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMQFR
421 ECSINGMKYQ EINGRLVPEG PTPDSSEGNL SYLSSLSHLN NLSHLTTSSS FRTSPENETE
481 LIKEHDLFFK AVSLCHTVQI SNVQTDCTGD GPWQSNLAPS QLEYYASSPD EKALVEAAAR
541 IGIVFIGNSE ETMEVKTLGK LERYKLLHIL EFDSDRRRMS VIVQAPSGEK LLFAKGAESS
601 ILPKCIGGEI EKTRIHVDEF ALKGLRTLCI AYRKFTSKEY EEIDKRIFEA RTALQQREEK
661 LAAVFQFIEK DLILLGATAV EDRLQDKVRE TIEALRMAGI KVWVLTGDKH ETAVSVSLSC
721 GHFHRTMNIL ELINQKSDSE CAEQLRQLAR RITEDHVIQH GLVVDGTSLS LALREHEKLF
781 MEVCRNCSAV LCCRMAPLQK AKVIRLIKIS PEKPITLAVG DGANDVSMIQ EAHVGIGIMG
841 KEGRQAARNS DYAIARFKFL SKLLFVHGHF YYIRIATLVQ YFFYKNVCFI TPQFLYQFYC
901 LFSQQTLYDS VYLTLYNICF TSLPILIYSL LEQHVDPHVL QNKPTLYRDI SKNRLLSIKT
961 FLYWTILGFS HAFIFFFGSY LLIGKDTSLL GNGQMFGNWT FGTLVFTVMV ITVTVKMALE
1021 THFWTWINHL VTWGSIIFYF VFSLFYGGIL WPFLGSQNMY FVFIQLLSSG SAWFAIILMV
1081 VTCLFLDIIK KVFDRHLHPT STEKAQLTET NAGIKCLDSM CCFPEGEAAC ASVGRMLERV
1141 IGRCSPTHIS RSWSASDPFY TNDRSILTLS TMDSSTCLocalizationUniProt · AlphaFold · HPA
Whether an antibody against ATP11B can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Other membrane
- Secreted
- No
- Transmembrane segments
- 10
- Mean surface accessibility (rSASA)
- 0.27
- Highest tissue expression
- 67 nTPM
Expression across tissuesHPA
Tissue
- bone marrow: 67 nTPM
- stomach: 48 nTPM
- esophagus: 43 nTPM
- thymus: 42 nTPM
- testis: 30 nTPM
- retina: 29 nTPM
Single-cell type
- neutrophils: 2,239 nCPM
- neutrophil progenitors: 1,086 nCPM
- esophageal apical cells: 689 nCPM
- rod photoreceptor cells: 326 nCPM
- urothelial cells: 322 nCPM
- foveolar cells: 302 nCPM
Immune cell
- basophil: 5.5 nTPM
- eosinophil: 4.3 nTPM
- neutrophil: 3.8 nTPM
- plasmacytoid DC: 2.4 nTPM
- memory B-cell: 2.1 nTPM
- naive CD8 T-cell: 1.8 nTPM
Brain region
- cerebellum: 51 nTPM
- white matter: 50 nTPM
- choroid plexus: 48 nTPM
- cerebral cortex: 35 nTPM
- medulla oblongata: 35 nTPM
- pons: 34 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.41
- gnomAD pLI
- 0
- gnomAD missense Z
- 1.85
- DepMap mean gene effect
- -0.14
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 11% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- aminophospholipid transport
- monoatomic ion transmembrane transport
- monoatomic ion transport
- phospholipid translocation
Molecular functions
- ATP binding
- ATP hydrolysis activity
- ATPase-coupled intramembrane lipid transporter activity
- magnesium ion binding
- monoatomic ion transmembrane transporter activity
- phosphatidylserine floppase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- P-type ATPase
- P-type ATPase, subfamily IV
- P-type ATPase, A domain superfamily
- P-type ATPase, phosphorylation site
- HAD superfamily
- P-type ATPase, transmembrane domain superfamily
- P-type ATPase, cytoplasmic domain N
- P-type ATPase, C-terminal
- P-type ATPase, N-terminal
- HAD-like superfamily
- P-type ATPase, haloacid dehalogenase domain
- P-type ATPase, A domain
- P-type ATPase actuator domain
- P-type ATPase, cytoplasmic domain N
- Phospholipid-translocating ATPase N-terminal
- Phospholipid-translocating P-type ATPase C-terminal
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of ATP11B in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads ATP11B as an antibody target. Whether an autoantibody or antibody against ATP11B could matter depends on whether native ATP11B is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
ATP11B is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label ATP11B as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...