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Q9Y2G3 (AT11B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ATP11B
Synonyms:ATPIF, ATPIR, KIAA0956
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Catalytic activity

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

Subunit structure

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. Ref.8

Subcellular location

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. Ref.8 Ref.9

Miscellaneous

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

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Sequence caution

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

The sequence AAH42180.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentEndoplasmic reticulum
Endosome
Golgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaminophospholipid transport

Traceable author statement Ref.1. Source: UniProtKB

ion transmembrane transport

Traceable author statement. Source: Reactome

ion transport

Non-traceable author statement Ref.4. Source: UniProtKB

phospholipid translocation

Non-traceable author statement Ref.8. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentearly endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from direct assay Ref.8. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear inner membrane

Non-traceable author statement Ref.4. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

recycling endosome

Inferred from direct assay Ref.8. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cation-transporting ATPase activity

Inferred from electronic annotation. Source: InterPro

ion transmembrane transporter activity

Non-traceable author statement Ref.4. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipid-translocating ATPase activity

Traceable author statement Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11771177Probable phospholipid-transporting ATPase IF
PRO_0000046371

Regions

Topological domain1 – 5555Cytoplasmic Potential
Transmembrane56 – 7722Helical; Potential
Topological domain78 – 825Extracellular Potential
Transmembrane83 – 10422Helical; Potential
Topological domain105 – 289185Cytoplasmic Potential
Transmembrane290 – 31122Helical; Potential
Topological domain312 – 34130Extracellular Potential
Transmembrane342 – 35918Helical; Potential
Topological domain360 – 876517Cytoplasmic Potential
Transmembrane877 – 89822Helical; Potential
Topological domain899 – 91012Extracellular Potential
Transmembrane911 – 93020Helical; Potential
Topological domain931 – 96030Cytoplasmic Potential
Transmembrane961 – 98222Helical; Potential
Topological domain983 – 99715Extracellular Potential
Transmembrane998 – 102023Helical; Potential
Topological domain1021 – 10255Cytoplasmic Potential
Transmembrane1026 – 104722Helical; Potential
Topological domain1048 – 106518Extracellular Potential
Transmembrane1066 – 109025Helical; Potential
Topological domain1091 – 117787Cytoplasmic Potential

Sites

Active site40714-aspartylphosphate intermediate By similarity
Metal binding8211Magnesium By similarity
Metal binding8251Magnesium By similarity

Amino acid modifications

Modified residue11541Phosphoserine Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q9Y2G3 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 665110145457B220

FASTA1,177134,190
        10         20         30         40         50         60 
MWRWIRQQLG FDPPHQSDTR TIYVANRFPQ NGLYTPQKFI DNRIISSKYT VWNFVPKNLF 

        70         80         90        100        110        120 
EQFRRVANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV TAIKQGYEDW LRHNSDNEVN 

       130        140        150        160        170        180 
GAPVYVVRSG GLVKTRSKNI RVGDIVRIAK DEIFPADLVL LSSDRLDGSC HVTTASLDGE 

       190        200        210        220        230        240 
TNLKTHVAVP ETALLQTVAN LDTLVAVIEC QQPEADLYRF MGRMIITQQM EEIVRPLGPE 

       250        260        270        280        290        300 
SLLLRGARLK NTKEIFGVAV YTGMETKMAL NYKSKSQKRS AVEKSMNTFL IIYLVILISE 

       310        320        330        340        350        360 
AVISTILKYT WQAEEKWDEP WYNQKTEHQR NSSKILRFIS DFLAFLVLYN FIIPISLYVT 

       370        380        390        400        410        420 
VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMQFR 

       430        440        450        460        470        480 
ECSINGMKYQ EINGRLVPEG PTPDSSEGNL SYLSSLSHLN NLSHLTTSSS FRTSPENETE 

       490        500        510        520        530        540 
LIKEHDLFFK AVSLCHTVQI SNVQTDCTGD GPWQSNLAPS QLEYYASSPD EKALVEAAAR 

       550        560        570        580        590        600 
IGIVFIGNSE ETMEVKTLGK LERYKLLHIL EFDSDRRRMS VIVQAPSGEK LLFAKGAESS 

       610        620        630        640        650        660 
ILPKCIGGEI EKTRIHVDEF ALKGLRTLCI AYRKFTSKEY EEIDKRIFEA RTALQQREEK 

       670        680        690        700        710        720 
LAAVFQFIEK DLILLGATAV EDRLQDKVRE TIEALRMAGI KVWVLTGDKH ETAVSVSLSC 

       730        740        750        760        770        780 
GHFHRTMNIL ELINQKSDSE CAEQLRQLAR RITEDHVIQH GLVVDGTSLS LALREHEKLF 

       790        800        810        820        830        840 
MEVCRNCSAV LCCRMAPLQK AKVIRLIKIS PEKPITLAVG DGANDVSMIQ EAHVGIGIMG 

       850        860        870        880        890        900 
KEGRQAARNS DYAIARFKFL SKLLFVHGHF YYIRIATLVQ YFFYKNVCFI TPQFLYQFYC 

       910        920        930        940        950        960 
LFSQQTLYDS VYLTLYNICF TSLPILIYSL LEQHVDPHVL QNKPTLYRDI SKNRLLSIKT 

       970        980        990       1000       1010       1020 
FLYWTILGFS HAFIFFFGSY LLIGKDTSLL GNGQMFGNWT FGTLVFTVMV ITVTVKMALE 

      1030       1040       1050       1060       1070       1080 
THFWTWINHL VTWGSIIFYF VFSLFYGGIL WPFLGSQNMY FVFIQLLSSG SAWFAIILMV 

      1090       1100       1110       1120       1130       1140 
VTCLFLDIIK KVFDRHLHPT STEKAQLTET NAGIKCLDSM CCFPEGEAAC ASVGRMLERV 

      1150       1160       1170 
IGRCSPTHIS RSWSASDPFY TNDRSILTLS TMDSSTC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Reanalysis of ATP11B, a Type IV P-type ATPase."
Halleck M.S., Schlegel R.A., Williamson P.L.
J. Biol. Chem. 277:9736-9740(2002) [PubMed] [Europe PMC] [Abstract]
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"ATP11B mediates platinum resistance in ovarian cancer."
Moreno-Smith M., Halder J.B., Meltzer P.S., Gonda T.A., Mangala L.S., Rupaimoole R., Lu C., Nagaraja A.S., Gharpure K.M., Kang Y., Rodriguez-Aguayo C., Vivas-Mejia P.E., Zand B., Schmandt R., Wang H., Langley R.R., Jennings N.B., Ivan C. expand/collapse author list , Coffin J.E., Armaiz G.N., Bottsford-Miller J., Kim S.B., Halleck M.S., Hendrix M.J., Bornman W., Bar-Eli M., Lee J.S., Siddik Z.H., Lopez-Berestein G., Sood A.K.
J. Clin. Invest. 123:2119-2130(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33896.1.
PIRT42662.
RefSeqNP_055431.1. NM_014616.2.
UniGeneHs.478429.

3D structure databases

ProteinModelPortalQ9Y2G3.
SMRQ9Y2G3. Positions 396-895.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116809. 2 interactions.
STRING9606.ENSP00000321195.

Protein family/group databases

TCDB3.A.3.8.12. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteQ9Y2G3.

Polymorphism databases

DMDM30316395.

Proteomic databases

MaxQBQ9Y2G3.
PaxDbQ9Y2G3.
PRIDEQ9Y2G3.

Protocols and materials databases

DNASU23200.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323116; ENSP00000321195; ENSG00000058063.
ENST00000493826; ENSP00000419032; ENSG00000058063.
GeneID23200.
KEGGhsa:23200.
UCSCuc003flb.3. human.

Organism-specific databases

CTD23200.
GeneCardsGC03P182511.
HGNCHGNC:13553. ATP11B.
HPAHPA036237.
HPA036238.
MIM605869. gene.
neXtProtNX_Q9Y2G3.
PharmGKBPA25102.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000202528.
HOVERGENHBG050601.
InParanoidQ9Y2G3.
KOK01530.
OMAPHVLQSK.
OrthoDBEOG7HHWRB.
PhylomeDBQ9Y2G3.
TreeFamTF326897.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9Y2G3.
BgeeQ9Y2G3.
CleanExHS_ATP11B.
GenevestigatorQ9Y2G3.

Family and domain databases

Gene3D2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProIPR023299. 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]
PANTHERPTHR24092. PTHR24092. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP11B. human.
GeneWikiATP11B.
GenomeRNAi23200.
NextBio44715.
PROQ9Y2G3.
SOURCESearch...

Entry information

Entry nameAT11B_HUMAN
AccessionPrimary (citable) accession number: Q9Y2G3
Secondary accession number(s): Q96FN1, Q9UKK7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 30, 2003
Last modified: July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM