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Q9Y2G3

- AT11B_HUMAN

UniProt

Q9Y2G3 - AT11B_HUMAN

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Protein

Probable phospholipid-transporting ATPase IF

Gene
ATP11B, ATPIF, ATPIR, KIAA0956
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei407 – 40714-aspartylphosphate intermediate By similarity
Metal bindingi821 – 8211Magnesium By similarity
Metal bindingi825 – 8251Magnesium By 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
Complete GO annotation...

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.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5555Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei56 – 7722Helical; Reviewed predictionAdd
BLAST
Topological domaini78 – 825Extracellular Reviewed prediction
Transmembranei83 – 10422Helical; Reviewed predictionAdd
BLAST
Topological domaini105 – 289185Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei290 – 31122Helical; Reviewed predictionAdd
BLAST
Topological domaini312 – 34130Extracellular Reviewed predictionAdd
BLAST
Transmembranei342 – 35918Helical; Reviewed predictionAdd
BLAST
Topological domaini360 – 876517Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei877 – 89822Helical; Reviewed predictionAdd
BLAST
Topological domaini899 – 91012Extracellular Reviewed predictionAdd
BLAST
Transmembranei911 – 93020Helical; Reviewed predictionAdd
BLAST
Topological domaini931 – 96030Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei961 – 98222Helical; Reviewed predictionAdd
BLAST
Topological domaini983 – 99715Extracellular Reviewed predictionAdd
BLAST
Transmembranei998 – 102023Helical; Reviewed predictionAdd
BLAST
Topological domaini1021 – 10255Cytoplasmic Reviewed prediction
Transmembranei1026 – 104722Helical; Reviewed predictionAdd
BLAST
Topological domaini1048 – 106518Extracellular Reviewed predictionAdd
BLAST
Transmembranei1066 – 109025Helical; Reviewed predictionAdd
BLAST
Topological domaini1091 – 117787Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. early endosome Source: UniProtKB-SubCell
  2. endoplasmic reticulum Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. nuclear inner membrane Source: UniProtKB
  5. plasma membrane Source: Reactome
  6. recycling endosome Source: UniProtKB
  7. recycling endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

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 Inferred. Interacts with beta subunit TMEM30A.1 Publication

Protein-protein interaction databases

BioGridi116809. 2 interactions.
STRINGi9606.ENSP00000321195.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2G3.
SMRiQ9Y2G3. Positions 396-895.

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

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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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 129 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

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