Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00364
Entry Name
UniProt Accession
Theoretical PI
6.52
Molecular Weight
134189.83
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Probable phospholipid-transporting ATPase IF
Protein Synonyms/Alias
3.6.3.1; ATPase IR; ATPase class VI type 11B; P4-ATPase flippase complex alpha subunit ATP11B;
Gene Name
ATP11B
Gene Synonyms/Alias
ATPIF; ATPIR; KIAA0956;
Created Date
30-MAY-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
784
Canonical
EKLFMEVCRNCSAVL
[1]
S-Palmitoylation
1083
Canonical
IILMVVTCLFLDIIK
[1]
S-Palmitoylation
1116
Canonical
ETNAGIKCLDSMCCF
[1]
S-Palmitoylation
1121
Canonical
IKCLDSMCCFPEGEA
[1]
S-Palmitoylation
1144
Canonical
LERVIGRCSPTHISR
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Topological domain: 1 55 Cytoplasmic.
Transmembrane: 56 77 Helical.
Topological domain: 78 82 Extracellular.
Transmembrane: 83 104 Helical.
Topological domain: 105 289 Cytoplasmic.
Transmembrane: 290 311 Helical.
Topological domain: 312 341 Extracellular.
Transmembrane: 342 359 Helical.
Topological domain: 360 876 Cytoplasmic.
Transmembrane: 877 898 Helical.
Topological domain: 899 910 Extracellular.
Transmembrane: 911 930 Helical.
Topological domain: 931 960 Cytoplasmic.
Transmembrane: 961 982 Helical.
Topological domain: 983 997 Extracellular.
Transmembrane: 998 1020 Helical.
Topological domain: 1021 1025 Cytoplasmic.
Transmembrane: 1026 1047 Helical.
Topological domain: 1048 1065 Extracellular.
Transmembrane: 1066 1090 Helical.
Topological domain: 1091 1177 Cytoplasmic.
Active site: 407 407 4-aspartylphosphate intermediate.
Metal binding site: 821 821 Magnesium.
Metal binding site: 825 825 Magnesium.
Modified residue: 1154 1154 Phosphoserine.
Protein Length
1177 AA.
Protein Sequence
(Canonical)
MWRWIRQQLG FDPPHQSDTR TIYVANRFPQ NGLYTPQKFI DNRIISSKYT VWNFVPKNLF  60
EQFRRVANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV TAIKQGYEDW LRHNSDNEVN  120
GAPVYVVRSG GLVKTRSKNI RVGDIVRIAK DEIFPADLVL LSSDRLDGSC HVTTASLDGE  180
TNLKTHVAVP ETALLQTVAN LDTLVAVIEC QQPEADLYRF MGRMIITQQM EEIVRPLGPE  240
SLLLRGARLK NTKEIFGVAV YTGMETKMAL NYKSKSQKRS AVEKSMNTFL IIYLVILISE  300
AVISTILKYT WQAEEKWDEP WYNQKTEHQR NSSKILRFIS DFLAFLVLYN FIIPISLYVT  360
VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMQFR  420
ECSINGMKYQ EINGRLVPEG PTPDSSEGNL SYLSSLSHLN NLSHLTTSSS FRTSPENETE  480
LIKEHDLFFK AVSLCHTVQI SNVQTDCTGD GPWQSNLAPS QLEYYASSPD EKALVEAAAR  540
IGIVFIGNSE ETMEVKTLGK LERYKLLHIL EFDSDRRRMS VIVQAPSGEK LLFAKGAESS  600
ILPKCIGGEI EKTRIHVDEF ALKGLRTLCI AYRKFTSKEY EEIDKRIFEA RTALQQREEK  660
LAAVFQFIEK DLILLGATAV EDRLQDKVRE TIEALRMAGI KVWVLTGDKH ETAVSVSLSC  720
GHFHRTMNIL ELINQKSDSE CAEQLRQLAR RITEDHVIQH GLVVDGTSLS LALREHEKLF  780
MEVCRNCSAV LCCRMAPLQK AKVIRLIKIS PEKPITLAVG DGANDVSMIQ EAHVGIGIMG  840
KEGRQAARNS DYAIARFKFL SKLLFVHGHF YYIRIATLVQ YFFYKNVCFI TPQFLYQFYC  900
LFSQQTLYDS VYLTLYNICF TSLPILIYSL LEQHVDPHVL QNKPTLYRDI SKNRLLSIKT  960
FLYWTILGFS HAFIFFFGSY LLIGKDTSLL GNGQMFGNWT FGTLVFTVMV ITVTVKMALE  1020
THFWTWINHL VTWGSIIFYF VFSLFYGGIL WPFLGSQNMY FVFIQLLSSG SAWFAIILMV  1080
VTCLFLDIIK KVFDRHLHPT STEKAQLTET NAGIKCLDSM CCFPEGEAAC ASVGRMLERV  1140
IGRCSPTHIS RSWSASDPFY TNDRSILTLS TMDSSTC                           1177
FASTA
(Canonical)
>LipidDB-9606-00364|Q9Y2G3
MWRWIRQQLGFDPPHQSDTRTIYVANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLF
EQFRRVANFYFLIIFLVQLMIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHNSDNEVN
GAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDGSCHVTTASLDGE
TNLKTHVAVPETALLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPE
SLLLRGARLKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLVILISE
AVISTILKYTWQAEEKWDEPWYNQKTEHQRNSSKILRFISDFLAFLVLYNFIIPISLYVT
VEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDKTGTLTENEMQFR
ECSINGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHLNNLSHLTTSSSFRTSPENETE
LIKEHDLFFKAVSLCHTVQISNVQTDCTGDGPWQSNLAPSQLEYYASSPDEKALVEAAAR
IGIVFIGNSEETMEVKTLGKLERYKLLHILEFDSDRRRMSVIVQAPSGEKLLFAKGAESS
ILPKCIGGEIEKTRIHVDEFALKGLRTLCIAYRKFTSKEYEEIDKRIFEARTALQQREEK
LAAVFQFIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSC
GHFHRTMNILELINQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLF
MEVCRNCSAVLCCRMAPLQKAKVIRLIKISPEKPITLAVGDGANDVSMIQEAHVGIGIMG
KEGRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVCFITPQFLYQFYC
LFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHVDPHVLQNKPTLYRDISKNRLLSIKT
FLYWTILGFSHAFIFFFGSYLLIGKDTSLLGNGQMFGNWTFGTLVFTVMVITVTVKMALE
THFWTWINHLVTWGSIIFYFVFSLFYGGILWPFLGSQNMYFVFIQLLSSGSAWFAIILMV
VTCLFLDIIKKVFDRHLHPTSTEKAQLTETNAGIKCLDSMCCFPEGEAACASVGRMLERV
IGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC
Gene Ontology
GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005637; C:nuclear inner membrane; NAS:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0055037; C:recycling endosome; IDA:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro
GO:0015075; F:ion transmembrane transporter activity; NAS:UniProtKB
GO:0000287; F:magnesium ion binding; IEA:InterPro
GO:0004012; F:phospholipid-translocating ATPase activity; TAS:UniProtKB
GO:0015917; P:aminophospholipid transport; TAS:UniProtKB
GO:0034220; P:ion transmembrane transport; TAS:Reactome
GO:0006811; P:ion transport; NAS:UniProtKB
GO:0045332; P:phospholipid translocation; NAS:UniProtKB
GO:0055085; P:transmembrane transport; TAS:Reactome
Interpro
InterPro; IPR023299; ATPase_P-typ_cyto_domN
InterPro; IPR018303; ATPase_P-typ_P_site
InterPro; IPR006539; ATPase_P-typ_Plipid-transp
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A
InterPro; IPR001757; Cation_transp_P_typ_ATPase
InterPro; IPR023214; HAD-like_dom
Pfam
Pfam; PF00122; E1-E2_ATPase;
Pfam; PF00702; Hydrolase;
SMART
PROSITE
PROSITE; PS00154; ATPASE_E1_E2;
PRINTS
PRINTS; PR00119; CATATPASE;