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Q9Y2G3

- AT11B_HUMAN

UniProt

Q9Y2G3 - AT11B_HUMAN

Protein

Probable phospholipid-transporting ATPase IF

Gene

ATP11B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (30 Apr 2003)
      Previous versions | rss
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    Functioni

    Catalytic 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. Involved in regulation of sensitivity to cisplatin; may contribute to secretory vesicle transport of cisplatin from Golgi to plasma membrane.1 PublicationCurated

    Catalytic activityi

    ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei407 – 40714-aspartylphosphate intermediateBy similarity
    Metal bindingi821 – 8211MagnesiumBy similarity
    Metal bindingi825 – 8251MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cation-transporting ATPase activity Source: InterPro
    3. ion transmembrane transporter activity Source: UniProtKB
    4. magnesium ion binding Source: InterPro
    5. phospholipid-translocating ATPase activity Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. aminophospholipid transport Source: UniProtKB
    2. ion transmembrane transport Source: Reactome
    3. ion transport Source: UniProtKB
    4. phospholipid translocation Source: UniProtKB
    5. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_25149. Ion transport by P-type ATPases.

    Protein family/group databases

    TCDBi3.A.3.8.12. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable phospholipid-transporting ATPase IF (EC:3.6.3.1)
    Alternative name(s):
    ATPase IR
    ATPase class VI type 11B
    P4-ATPase flippase complex alpha subunit ATP11B
    Gene namesi
    Name:ATP11B
    Synonyms:ATPIF, ATPIR, KIAA0956
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:13553. ATP11B.

    Subcellular locationi

    Recycling endosome membrane; Multi-pass membrane protein. Early endosome. Endoplasmic reticulum. Golgi apparatustrans-Golgi network
    Note: Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, mainly located in recycling endosomes.

    GO - Cellular componenti

    1. early endosome Source: UniProtKB-SubCell
    2. endoplasmic reticulum Source: UniProtKB
    3. Golgi apparatus Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: UniProtKB
    6. nuclear inner membrane Source: UniProtKB
    7. plasma membrane Source: Reactome
    8. recycling endosome Source: UniProtKB
    9. recycling endosome membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25102.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11771177Probable phospholipid-transporting ATPase IFPRO_0000046371Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1154 – 11541Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2G3.
    PaxDbiQ9Y2G3.
    PRIDEiQ9Y2G3.

    PTM databases

    PhosphoSiteiQ9Y2G3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y2G3.
    BgeeiQ9Y2G3.
    CleanExiHS_ATP11B.
    GenevestigatoriQ9Y2G3.

    Organism-specific databases

    HPAiHPA036237.
    HPA036238.

    Interactioni

    Subunit structurei

    Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit Probable. Interacts with beta subunit TMEM30A.1 PublicationCurated

    Protein-protein interaction databases

    BioGridi116809. 2 interactions.
    STRINGi9606.ENSP00000321195.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2G3.
    SMRiQ9Y2G3. Positions 396-895.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5555CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini78 – 825ExtracellularSequence Analysis
    Topological domaini105 – 289185CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini312 – 34130ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini360 – 876517CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini899 – 91012ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini931 – 96030CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini983 – 99715ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1021 – 10255CytoplasmicSequence Analysis
    Topological domaini1048 – 106518ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1091 – 117787CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei56 – 7722HelicalSequence AnalysisAdd
    BLAST
    Transmembranei83 – 10422HelicalSequence AnalysisAdd
    BLAST
    Transmembranei290 – 31122HelicalSequence AnalysisAdd
    BLAST
    Transmembranei342 – 35918HelicalSequence AnalysisAdd
    BLAST
    Transmembranei877 – 89822HelicalSequence AnalysisAdd
    BLAST
    Transmembranei911 – 93020HelicalSequence AnalysisAdd
    BLAST
    Transmembranei961 – 98222HelicalSequence AnalysisAdd
    BLAST
    Transmembranei998 – 102023HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1026 – 104722HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1066 – 109025HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOGENOMiHOG000202528.
    HOVERGENiHBG050601.
    InParanoidiQ9Y2G3.
    KOiK01530.
    OMAiPHVLQSK.
    OrthoDBiEOG7HHWRB.
    PhylomeDBiQ9Y2G3.
    TreeFamiTF326897.

    Family and domain databases

    Gene3Di2.70.150.10. 2 hits.
    3.40.1110.10. 2 hits.
    3.40.50.1000. 2 hits.
    InterProiIPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR006539. ATPase_P-typ_Plipid-transp.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view]
    PANTHERiPTHR24092. PTHR24092. 1 hit.
    PfamiPF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SUPFAMiSSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 2 hits.
    TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y2G3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWRWIRQQLG FDPPHQSDTR TIYVANRFPQ NGLYTPQKFI DNRIISSKYT     50
    VWNFVPKNLF EQFRRVANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV 100
    TAIKQGYEDW LRHNSDNEVN GAPVYVVRSG GLVKTRSKNI RVGDIVRIAK 150
    DEIFPADLVL LSSDRLDGSC HVTTASLDGE TNLKTHVAVP ETALLQTVAN 200
    LDTLVAVIEC QQPEADLYRF MGRMIITQQM EEIVRPLGPE SLLLRGARLK 250
    NTKEIFGVAV YTGMETKMAL NYKSKSQKRS AVEKSMNTFL IIYLVILISE 300
    AVISTILKYT WQAEEKWDEP WYNQKTEHQR NSSKILRFIS DFLAFLVLYN 350
    FIIPISLYVT VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ 400
    VEYVFTDKTG TLTENEMQFR ECSINGMKYQ EINGRLVPEG PTPDSSEGNL 450
    SYLSSLSHLN NLSHLTTSSS FRTSPENETE LIKEHDLFFK AVSLCHTVQI 500
    SNVQTDCTGD GPWQSNLAPS QLEYYASSPD EKALVEAAAR IGIVFIGNSE 550
    ETMEVKTLGK LERYKLLHIL EFDSDRRRMS VIVQAPSGEK LLFAKGAESS 600
    ILPKCIGGEI EKTRIHVDEF ALKGLRTLCI AYRKFTSKEY EEIDKRIFEA 650
    RTALQQREEK LAAVFQFIEK DLILLGATAV EDRLQDKVRE TIEALRMAGI 700
    KVWVLTGDKH ETAVSVSLSC GHFHRTMNIL ELINQKSDSE CAEQLRQLAR 750
    RITEDHVIQH GLVVDGTSLS LALREHEKLF MEVCRNCSAV LCCRMAPLQK 800
    AKVIRLIKIS PEKPITLAVG DGANDVSMIQ EAHVGIGIMG KEGRQAARNS 850
    DYAIARFKFL SKLLFVHGHF YYIRIATLVQ YFFYKNVCFI TPQFLYQFYC 900
    LFSQQTLYDS VYLTLYNICF TSLPILIYSL LEQHVDPHVL QNKPTLYRDI 950
    SKNRLLSIKT FLYWTILGFS HAFIFFFGSY LLIGKDTSLL GNGQMFGNWT 1000
    FGTLVFTVMV ITVTVKMALE THFWTWINHL VTWGSIIFYF VFSLFYGGIL 1050
    WPFLGSQNMY FVFIQLLSSG SAWFAIILMV VTCLFLDIIK KVFDRHLHPT 1100
    STEKAQLTET NAGIKCLDSM CCFPEGEAAC ASVGRMLERV IGRCSPTHIS 1150
    RSWSASDPFY TNDRSILTLS TMDSSTC 1177
    Length:1,177
    Mass (Da):134,190
    Last modified:April 30, 2003 - v2
    Checksum:i665110145457B220
    GO

    Sequence cautioni

    The sequence AAH42180.1 differs from that shown. Reason: Intron retention.
    The sequence AAH10630.1 differs from that shown. Reason: Frameshift at position 884.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF156548 mRNA. Translation: AAF09446.1.
    AC069431 Genomic DNA. No translation available.
    BC042180 mRNA. Translation: AAH42180.1. Sequence problems.
    BC010630 mRNA. Translation: AAH10630.1. Frameshift.
    AB023173 mRNA. Translation: BAA76800.1.
    AL133061 mRNA. Translation: CAB61385.1.
    CCDSiCCDS33896.1.
    PIRiT42662.
    RefSeqiNP_055431.1. NM_014616.2.
    UniGeneiHs.478429.

    Genome annotation databases

    EnsembliENST00000323116; ENSP00000321195; ENSG00000058063.
    ENST00000493826; ENSP00000419032; ENSG00000058063.
    GeneIDi23200.
    KEGGihsa:23200.
    UCSCiuc003flb.3. human.

    Polymorphism databases

    DMDMi30316395.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF156548 mRNA. Translation: AAF09446.1 .
    AC069431 Genomic DNA. No translation available.
    BC042180 mRNA. Translation: AAH42180.1 . Sequence problems.
    BC010630 mRNA. Translation: AAH10630.1 . Frameshift.
    AB023173 mRNA. Translation: BAA76800.1 .
    AL133061 mRNA. Translation: CAB61385.1 .
    CCDSi CCDS33896.1.
    PIRi T42662.
    RefSeqi NP_055431.1. NM_014616.2.
    UniGenei Hs.478429.

    3D structure databases

    ProteinModelPortali Q9Y2G3.
    SMRi Q9Y2G3. Positions 396-895.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116809. 2 interactions.
    STRINGi 9606.ENSP00000321195.

    Protein family/group databases

    TCDBi 3.A.3.8.12. the p-type atpase (p-atpase) superfamily.

    PTM databases

    PhosphoSitei Q9Y2G3.

    Polymorphism databases

    DMDMi 30316395.

    Proteomic databases

    MaxQBi Q9Y2G3.
    PaxDbi Q9Y2G3.
    PRIDEi Q9Y2G3.

    Protocols and materials databases

    DNASUi 23200.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323116 ; ENSP00000321195 ; ENSG00000058063 .
    ENST00000493826 ; ENSP00000419032 ; ENSG00000058063 .
    GeneIDi 23200.
    KEGGi hsa:23200.
    UCSCi uc003flb.3. human.

    Organism-specific databases

    CTDi 23200.
    GeneCardsi GC03P182511.
    HGNCi HGNC:13553. ATP11B.
    HPAi HPA036237.
    HPA036238.
    MIMi 605869. gene.
    neXtProti NX_Q9Y2G3.
    PharmGKBi PA25102.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0474.
    HOGENOMi HOG000202528.
    HOVERGENi HBG050601.
    InParanoidi Q9Y2G3.
    KOi K01530.
    OMAi PHVLQSK.
    OrthoDBi EOG7HHWRB.
    PhylomeDBi Q9Y2G3.
    TreeFami TF326897.

    Enzyme and pathway databases

    Reactomei REACT_25149. Ion transport by P-type ATPases.

    Miscellaneous databases

    ChiTaRSi ATP11B. human.
    GeneWikii ATP11B.
    GenomeRNAii 23200.
    NextBioi 44715.
    PROi Q9Y2G3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2G3.
    Bgeei Q9Y2G3.
    CleanExi HS_ATP11B.
    Genevestigatori Q9Y2G3.

    Family and domain databases

    Gene3Di 2.70.150.10. 2 hits.
    3.40.1110.10. 2 hits.
    3.40.50.1000. 2 hits.
    InterProi IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR006539. ATPase_P-typ_Plipid-transp.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view ]
    PANTHERi PTHR24092. PTHR24092. 1 hit.
    Pfami PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SUPFAMi SSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 2 hits.
    TIGRFAMsi TIGR01652. ATPase-Plipid. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential expression of putative transbilayer amphipath transporters."
      Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P., Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D., Williamson P.L., Schlegel R.A.
      Physiol. Genomics 1:139-150(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-248.
      Tissue: Colon.
    2. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-195 AND 540-1177.
      Tissue: Colon and Mammary gland.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-450.
    5. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-1111.
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 688-1111.
      Tissue: Testis.
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent manner."
      Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K., Shin H.W.
      J. Biol. Chem. 286:38159-38167(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMEM30A, SUBCELLULAR LOCATION.
    9. Cited for: FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiAT11B_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2G3
    Secondary accession number(s): Q96FN1, Q9UKK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Depletion of ATP11B by RNAi restores sensitivity of ovarian cancer cells to cisplatin.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3