Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Bile salt export pump (ATP-binding cassette sub-family B member 11)

 ABCBB_HUMAN             Reviewed;        1321 AA.
O95342; Q53TL2; Q9UNB2;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 2.
07-NOV-2018, entry version 175.
RecName: Full=Bile salt export pump;
AltName: Full=ATP-binding cassette sub-family B member 11;
Name=ABCB11; Synonyms=BSEP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PFIC2 GLY-297; GLU-461;
GLY-482; ARG-982; CYS-1153 AND GLN-1268.
PubMed=9806540; DOI=10.1038/3034;
Strautnieks S.S., Bull L.N., Knisely A.S., Kocoshis S.A., Dahl N.,
Arnell H., Sokal E.M., Dahan K., Childs S., Ling V., Tanner M.S.,
Kagalwalla A.F., Nemeth A., Pawlowska J., Baker A., Mieli-Vergani G.,
Freimer N.B., Gardiner R.M., Thompson R.J.;
"A gene encoding a liver-specific ABC transporter is mutated in
progressive familial intrahepatic cholestasis.";
Nat. Genet. 20:233-238(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-444.
Mol O., Hooiveld G.J.E.J., Jansen P.L.M., Muller M.;
"Cellular localization and functional characterization of the human
bile salt export pump (BSEP).";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
GLYCOSYLATION AT ASN-109; ASN-116; ASN-122 AND ASN-125.
PubMed=17082223; DOI=10.1152/ajpgi.00415.2006;
Mochizuki K., Kagawa T., Numari A., Harris M.J., Itoh J., Watanabe N.,
Mine T., Arias I.M.;
"Two N-linked glycans are required to maintain the transport activity
of the bile salt export pump (ABCB11) in MDCK II cells.";
Am. J. Physiol. 292:G818-G828(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-586; SER-587; SER-704
AND SER-1214, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[6]
VARIANTS PFIC2 VAL-238 AND SER-336.
PubMed=10579978; DOI=10.1016/S0016-5085(99)70287-8;
Jansen P.L.M., Strautnieks S.S., Jacquemin E., Hadchouel M.,
Sokal E.M., Hooiveld G.J.E.J., Koning J.H., De Jager-Krikken A.,
Kuipers F., Stellaard F., Bijleveld C.M., Gouw A., Van Goor H.,
Thompson R.J., Muller M.;
"Hepatocanalicular bile salt export pump deficiency in patients with
progressive familial intrahepatic cholestasis.";
Gastroenterology 117:1370-1379(1999).
[7]
VARIANT ALA-444.
PubMed=11829140; DOI=10.1007/s10038-002-8653-6;
Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S.,
Higuchi S., Nakamura Y.;
"Three hundred twenty-six genetic variations in genes encoding nine
members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the
Japanese population.";
J. Hum. Genet. 47:38-50(2002).
[8]
VARIANTS PFIC2 LEU-284 AND ASP-1004.
PubMed=11815775; DOI=10.1067/mpd.2002.119993;
Chen H.-L., Chang P.-S., Hsu H.-C., Ni Y.-H., Hsu H.-Y., Lee J.-H.,
Jeng Y.-M., Shau W.-Y., Chang M.-H.;
"FIC1 and BSEP defects in Taiwanese patients with chronic intrahepatic
cholestasis with low gamma-glutamyltranspeptidase levels.";
J. Pediatr. 140:119-124(2002).
[9]
VARIANTS BRIC2 GLY-186; GLY-297; THR-570; PRO-923; PRO-926; CYS-1050
AND HIS-1128.
PubMed=15300568; DOI=10.1053/j.gastro.2004.04.065;
van Mil S.W.C., van der Woerd W.L., van der Brugge G., Sturm E.,
Jansen P.L.M., Bull L.N., van den Berg I.E.T., Berger R.,
Houwen R.H.J., Klomp L.W.J.;
"Benign recurrent intrahepatic cholestasis type 2 is caused by
mutations in ABCB11.";
Gastroenterology 127:379-384(2004).
[10]
VARIANTS GLN-415; ALA-444; SER-591 AND VAL-677.
PubMed=15077010; DOI=10.1097/00008571-200402000-00003;
Pauli-Magnus C., Lang T., Meier Y., Zodan-Marin T., Jung D.,
Breymann C., Zimmermann R., Kenngott S., Beuers U., Reichel C.,
Kerb R., Penger A., Meier P.J., Kullak-Ublick G.A.;
"Sequence analysis of bile salt export pump (ABCB11) and multidrug
resistance p-glycoprotein 3 (ABCB4, MDR3) in patients with
intrahepatic cholestasis of pregnancy.";
Pharmacogenetics 14:91-102(2004).
[11]
VARIANTS BRIC2 GLY-297 AND THR-432, AND CHARACTERIZATION OF VARIANTS
BRIC2 GLY-297 AND THR-432.
PubMed=16039748; DOI=10.1016/j.jhep.2005.05.020;
Noe J., Kullak-Ublick G.A., Jochum W., Stieger B., Kerb R., Haberl M.,
Muellhaupt B., Meier P.J., Pauli-Magnus C.;
"Impaired expression and function of the bile salt export pump due to
three novel ABCB11 mutations in intrahepatic cholestasis.";
J. Hepatol. 43:536-543(2005).
[12]
VARIANTS VAL-206; ALA-284; LYS-299; ALA-444; GLY-616; ALA-619;
VAL-677; HIS-698; VAL-865 AND GLN-958.
PubMed=16763017; DOI=10.1124/dmd.105.008854;
Lang T., Haberl M., Jung D., Drescher A., Schlagenhaufer R., Keil A.,
Mornhinweg E., Stieger B., Kullak-Ublick G.A., Kerb R.;
"Genetic variability, haplotype structures, and ethnic diversity of
hepatic transporters MDR3 (ABCB4) and bile salt export pump
(ABCB11).";
Drug Metab. Dispos. 34:1582-1599(2006).
[13]
VARIANTS ALA-444 AND VAL-677.
PubMed=16799996; DOI=10.1002/hep.21214;
Meier Y., Pauli-Magnus C., Zanger U.M., Klein K., Schaeffeler E.,
Nussler A.K., Nussler N., Eichelbaum M., Meier P.J., Stieger B.;
"Interindividual variability of canalicular ATP-binding-cassette
(ABC)-transporter expression in human liver.";
Hepatology 44:62-74(2006).
[14]
VARIANTS ALA-284; ALA-444; TYR-676; VAL-677; HIS-698 AND ARG-855,
BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION OF VARIANTS
ALA-444; TYR-676; VAL-677 AND ARG-855.
PubMed=17264802; DOI=10.1097/01.fpc.0000230418.28091.76;
Lang C., Meier Y., Stieger B., Beuers U., Lang T., Kerb R.,
Kullak-Ublick G.A., Meier P.J., Pauli-Magnus C.;
"Mutations and polymorphisms in the bile salt export pump and the
multidrug resistance protein 3 associated with drug-induced liver
injury.";
Pharmacogenet. Genomics 17:47-60(2007).
[15]
VARIANTS PFIC2 HIS-337; CYS-472; TRP-696; PRO-931; VAL-1131 AND
ARG-1198, AND VARIANTS ALA-444 AND VAL-865.
PubMed=24969679; DOI=10.3892/mmr.2014.2349;
Hu G., He P., Liu Z., Chen Q., Zheng B., Zhang Q.;
"Diagnosis of ABCB11 gene mutations in children with intrahepatic
cholestasis using high resolution melting analysis and direct
sequencing.";
Mol. Med. Report. 10:1264-1274(2014).
-!- FUNCTION: Involved in the ATP-dependent secretion of bile salts
into the canaliculus of hepatocytes.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=30.4 uM for taurocholate {ECO:0000269|PubMed:17264802};
Vmax=232 pmol/min/mg enzyme for taurocholate transport
{ECO:0000269|PubMed:17264802};
-!- SUBUNIT: Interacts with HAX1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Expressed predominantly, if not exclusively in
the liver, where it was further localized to the canalicular
microvilli and to subcanalicular vesicles of the hepatocytes by in
situ.
-!- DOMAIN: Multifunctional polypeptide with two homologous halves,
each containing a hydrophobic membrane-anchoring domain and an ATP
binding cassette (ABC) domain.
-!- DISEASE: Cholestasis, progressive familial intrahepatic, 2 (PFIC2)
[MIM:601847]: A disorder characterized by early onset of
cholestasis that progresses to hepatic fibrosis, cirrhosis, and
end-stage liver disease before adulthood.
{ECO:0000269|PubMed:10579978, ECO:0000269|PubMed:11815775,
ECO:0000269|PubMed:24969679, ECO:0000269|PubMed:9806540}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Cholestasis, benign recurrent intrahepatic, 2 (BRIC2)
[MIM:605479]: A disorder characterized by intermittent episodes of
cholestasis without progression to liver failure. There is initial
elevation of serum bile acids, followed by cholestatic jaundice
which generally spontaneously resolves after periods of weeks to
months. The cholestatic attacks vary in severity and duration.
Patients are asymptomatic between episodes, both clinically and
biochemically. {ECO:0000269|PubMed:15300568,
ECO:0000269|PubMed:16039748}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=O95342";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF091582; AAC77455.1; -; mRNA.
EMBL; AF136523; AAD28285.1; -; mRNA.
EMBL; AC008177; AAY24305.1; -; Genomic_DNA.
EMBL; AC093723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC069137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS46444.1; -.
RefSeq; NP_003733.2; NM_003742.2.
UniGene; Hs.158316; -.
UniGene; Hs.658439; -.
ProteinModelPortal; O95342; -.
SMR; O95342; -.
BioGrid; 114199; 5.
IntAct; O95342; 3.
STRING; 9606.ENSP00000263817; -.
BindingDB; O95342; -.
ChEMBL; CHEMBL6020; -.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB00559; Bosentan.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB00501; Cimetidine.
DrugBank; DB00845; Clofazimine.
DrugBank; DB00091; Cyclosporine.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB03619; Deoxycholic Acid.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB00390; Digoxin.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB00977; Ethinyl Estradiol.
DrugBank; DB00693; Fluorescein.
DrugBank; DB02703; Fusidic Acid.
DrugBank; DB01016; Glyburide.
DrugBank; DB02123; Glycochenodeoxycholic Acid.
DrugBank; DB01026; Ketoconazole.
DrugBank; DB01051; Novobiocin.
DrugBank; DB01229; Paclitaxel.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB08901; Ponatinib.
DrugBank; DB00175; Pravastatin.
DrugBank; DB00396; Progesterone.
DrugBank; DB00908; Quinidine.
DrugBank; DB00206; Reserpine.
DrugBank; DB01045; Rifampicin.
DrugBank; DB01098; Rosuvastatin.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB04348; Taurocholic Acid.
DrugBank; DB00197; Troglitazone.
DrugBank; DB01586; Ursodeoxycholic acid.
DrugBank; DB00661; Verapamil.
DrugBank; DB00570; Vinblastine.
DrugBank; DB00541; Vincristine.
GuidetoPHARMACOLOGY; 778; -.
SwissLipids; SLP:000001597; -.
TCDB; 3.A.1.201.2; the atp-binding cassette (abc) superfamily.
iPTMnet; O95342; -.
PhosphoSitePlus; O95342; -.
BioMuta; ABCB11; -.
EPD; O95342; -.
MaxQB; O95342; -.
PaxDb; O95342; -.
PeptideAtlas; O95342; -.
PRIDE; O95342; -.
ProteomicsDB; 50810; -.
Ensembl; ENST00000263817; ENSP00000263817; ENSG00000073734.
GeneID; 8647; -.
KEGG; hsa:8647; -.
UCSC; uc002ueo.2; human.
CTD; 8647; -.
DisGeNET; 8647; -.
EuPathDB; HostDB:ENSG00000073734.8; -.
GeneCards; ABCB11; -.
GeneReviews; ABCB11; -.
H-InvDB; HIX0029772; -.
HGNC; HGNC:42; ABCB11.
HPA; HPA019035; -.
MalaCards; ABCB11; -.
MIM; 601847; phenotype.
MIM; 603201; gene.
MIM; 605479; phenotype.
neXtProt; NX_O95342; -.
OpenTargets; ENSG00000073734; -.
Orphanet; 99961; Benign recurrent intrahepatic cholestasis type 2.
Orphanet; 69665; Intrahepatic cholestasis of pregnancy.
Orphanet; 79304; Progressive familial intrahepatic cholestasis type 2.
PharmGKB; PA374; -.
eggNOG; KOG0055; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00530000062896; -.
HOVERGEN; HBG080809; -.
InParanoid; O95342; -.
KO; K05664; -.
OMA; FIQRMTT; -.
OrthoDB; EOG091G0HVA; -.
PhylomeDB; O95342; -.
TreeFam; TF105193; -.
Reactome; R-HSA-159418; Recycling of bile acids and salts.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-5678520; Defective ABCB11 causes progressive familial intrahepatic cholestasis 2 and benign recurrent intrahepatic cholestasis 2.
ChiTaRS; ABCB11; human.
GeneWiki; ABCB11; -.
GenomeRNAi; 8647; -.
PRO; PR:O95342; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000073734; Expressed in 39 organ(s), highest expression level in liver.
CleanEx; HS_ABCB11; -.
ExpressionAtlas; O95342; baseline and differential.
Genevisible; O95342; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0015432; F:bile acid-exporting ATPase activity; TAS:Reactome.
GO; GO:0015126; F:canalicular bile acid transmembrane transporter activity; IBA:GO_Central.
GO; GO:0008554; F:sodium-exporting ATPase activity, phosphorylative mechanism; TAS:ProtInc.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
GO; GO:0015722; P:canalicular bile acid transport; IBA:GO_Central.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR030278; BSEP.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR039421; Type_I_exporter.
PANTHER; PTHR24221; PTHR24221; 1.
PANTHER; PTHR24221:SF165; PTHR24221:SF165; 1.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Complete proteome; Disease mutation; Glycoprotein;
Intrahepatic cholestasis; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1321 Bile salt export pump.
/FTId=PRO_0000093296.
TOPO_DOM 1 62 Cytoplasmic. {ECO:0000255}.
TRANSMEM 63 83 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 84 147 Extracellular. {ECO:0000255}.
TRANSMEM 148 168 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 169 215 Cytoplasmic. {ECO:0000255}.
TRANSMEM 216 236 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 237 240 Extracellular. {ECO:0000255}.
TRANSMEM 241 261 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 262 319 Cytoplasmic. {ECO:0000255}.
TRANSMEM 320 340 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 341 353 Extracellular. {ECO:0000255}.
TRANSMEM 354 374 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 375 755 Cytoplasmic. {ECO:0000255}.
TRANSMEM 756 776 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 777 794 Extracellular. {ECO:0000255}.
TRANSMEM 795 815 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 816 869 Cytoplasmic. {ECO:0000255}.
TRANSMEM 870 890 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 891 911 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 912 979 Cytoplasmic. {ECO:0000255}.
TRANSMEM 980 1000 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1001 1011 Extracellular. {ECO:0000255}.
TRANSMEM 1012 1032 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1033 1321 Cytoplasmic. {ECO:0000255}.
DOMAIN 62 385 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 420 656 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 755 1043 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1078 1316 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 455 462 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1113 1120 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 651 672 Interaction with HAX1. {ECO:0000250}.
MOD_RES 586 586 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 587 587 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 690 690 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QY30}.
MOD_RES 701 701 Phosphoserine.
{ECO:0000250|UniProtKB:O70127}.
MOD_RES 704 704 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1214 1214 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1321 1321 Phosphoserine.
{ECO:0000250|UniProtKB:O70127}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17082223}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17082223}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17082223}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17082223}.
VARIANT 56 56 S -> L (in dbSNP:rs11568361).
/FTId=VAR_055472.
VARIANT 186 186 E -> G (in BRIC2; dbSNP:rs72551307).
{ECO:0000269|PubMed:15300568}.
/FTId=VAR_030386.
VARIANT 206 206 I -> V (in dbSNP:rs11568357).
{ECO:0000269|PubMed:16763017}.
/FTId=VAR_030387.
VARIANT 238 238 G -> V (in PFIC2; dbSNP:rs72551306).
{ECO:0000269|PubMed:10579978}.
/FTId=VAR_030388.
VARIANT 284 284 V -> A (in dbSNP:rs200739891).
{ECO:0000269|PubMed:16763017,
ECO:0000269|PubMed:17264802}.
/FTId=VAR_035349.
VARIANT 284 284 V -> L (in PFIC2).
{ECO:0000269|PubMed:11815775}.
/FTId=VAR_013332.
VARIANT 297 297 E -> G (in PFIC2 and BRIC2; reduced
transport capacity for taurocholate;
dbSNP:rs11568372).
{ECO:0000269|PubMed:15300568,
ECO:0000269|PubMed:16039748,
ECO:0000269|PubMed:9806540}.
/FTId=VAR_010271.
VARIANT 299 299 R -> K (in dbSNP:rs2287617).
{ECO:0000269|PubMed:16763017}.
/FTId=VAR_030389.
VARIANT 336 336 C -> S (in PFIC2; dbSNP:rs72551305).
{ECO:0000269|PubMed:10579978}.
/FTId=VAR_030390.
VARIANT 337 337 Y -> H (in PFIC2; unknown pathological
significance).
{ECO:0000269|PubMed:24969679}.
/FTId=VAR_073967.
VARIANT 415 415 R -> Q (in dbSNP:rs371656014).
{ECO:0000269|PubMed:15077010}.
/FTId=VAR_043074.
VARIANT 432 432 R -> T (in BRIC2; reduced transport
capacity for taurocholate;
dbSNP:rs121908935).
{ECO:0000269|PubMed:16039748}.
/FTId=VAR_030391.
VARIANT 444 444 V -> A (common polymorphism; more
frequent in patients with drug-induced
cholestasis than healthy controls;
associated with lower hepatic expression;
does not affect transport capacity for
taurocholate; dbSNP:rs2287622).
{ECO:0000269|PubMed:11829140,
ECO:0000269|PubMed:15077010,
ECO:0000269|PubMed:16763017,
ECO:0000269|PubMed:16799996,
ECO:0000269|PubMed:17264802,
ECO:0000269|PubMed:24969679,
ECO:0000269|Ref.2}.
/FTId=VAR_013333.
VARIANT 444 444 V -> D (in dbSNP:rs2287622).
/FTId=VAR_059106.
VARIANT 444 444 V -> G (in dbSNP:rs2287622).
/FTId=VAR_059107.
VARIANT 461 461 K -> E (in PFIC2).
{ECO:0000269|PubMed:9806540}.
/FTId=VAR_013334.
VARIANT 472 472 Y -> C (in PFIC2; compound heterozygous
with V-1131; dbSNP:rs369860506).
{ECO:0000269|PubMed:24969679}.
/FTId=VAR_073968.
VARIANT 482 482 D -> G (in PFIC2; dbSNP:rs72549402).
{ECO:0000269|PubMed:9806540}.
/FTId=VAR_013335.
VARIANT 570 570 A -> T (in BRIC2; dbSNP:rs886043807).
{ECO:0000269|PubMed:15300568}.
/FTId=VAR_030392.
VARIANT 591 591 N -> S (in a patient with intrahepatic
cholestasis of pregnancy;
dbSNP:rs11568367).
{ECO:0000269|PubMed:15077010}.
/FTId=VAR_043075.
VARIANT 616 616 R -> G. {ECO:0000269|PubMed:16763017}.
/FTId=VAR_035350.
VARIANT 619 619 T -> A (in dbSNP:rs912519986).
{ECO:0000269|PubMed:16763017}.
/FTId=VAR_035351.
VARIANT 676 676 D -> Y (in fluvastatin-induced
cholestasis; does not affect transport
capacity for taurocholate).
{ECO:0000269|PubMed:17264802}.
/FTId=VAR_043076.
VARIANT 677 677 M -> V (does not affect transport
capacity for taurocholate;
dbSNP:rs11568364).
{ECO:0000269|PubMed:15077010,
ECO:0000269|PubMed:16763017,
ECO:0000269|PubMed:16799996,
ECO:0000269|PubMed:17264802}.
/FTId=VAR_030393.
VARIANT 696 696 R -> W (in PFIC2; unknown pathological
significance; dbSNP:rs376216286).
{ECO:0000269|PubMed:24969679}.
/FTId=VAR_073969.
VARIANT 698 698 R -> H (in dbSNP:rs138642043).
{ECO:0000269|PubMed:16763017,
ECO:0000269|PubMed:17264802}.
/FTId=VAR_035352.
VARIANT 855 855 G -> R (in ethinylestradiol/gestodene-
induced cholestasis; loss of transport
capacity for taurocholate).
{ECO:0000269|PubMed:17264802}.
/FTId=VAR_043077.
VARIANT 865 865 A -> V (polymorphism; dbSNP:rs118109635).
{ECO:0000269|PubMed:16763017,
ECO:0000269|PubMed:24969679}.
/FTId=VAR_035353.
VARIANT 923 923 T -> P (in BRIC2; dbSNP:rs777469571).
{ECO:0000269|PubMed:15300568}.
/FTId=VAR_030394.
VARIANT 926 926 A -> P (in BRIC2; dbSNP:rs72549400).
{ECO:0000269|PubMed:15300568}.
/FTId=VAR_030395.
VARIANT 931 931 Q -> P (in PFIC2; unknown pathological
significance).
{ECO:0000269|PubMed:24969679}.
/FTId=VAR_073970.
VARIANT 958 958 R -> Q (in dbSNP:rs761363245).
{ECO:0000269|PubMed:16763017}.
/FTId=VAR_035354.
VARIANT 982 982 G -> R (in PFIC2; dbSNP:rs72549399).
{ECO:0000269|PubMed:9806540}.
/FTId=VAR_013336.
VARIANT 1004 1004 G -> D (in PFIC2).
{ECO:0000269|PubMed:11815775}.
/FTId=VAR_013337.
VARIANT 1050 1050 R -> C (in BRIC2; dbSNP:rs72549398).
{ECO:0000269|PubMed:15300568}.
/FTId=VAR_030396.
VARIANT 1128 1128 R -> H (in BRIC2; dbSNP:rs756220860).
{ECO:0000269|PubMed:15300568}.
/FTId=VAR_030397.
VARIANT 1131 1131 D -> V (in PFIC2; compound heterozygous
with C-472).
{ECO:0000269|PubMed:24969679}.
/FTId=VAR_073971.
VARIANT 1153 1153 R -> C (in PFIC2; dbSNP:rs72549395).
{ECO:0000269|PubMed:9806540}.
/FTId=VAR_013338.
VARIANT 1186 1186 E -> K (in dbSNP:rs1521808).
/FTId=VAR_030398.
VARIANT 1198 1198 H -> R (in PFIC2; unknown pathological
significance).
{ECO:0000269|PubMed:24969679}.
/FTId=VAR_073972.
VARIANT 1268 1268 R -> Q (in PFIC2; dbSNP:rs72549394).
{ECO:0000269|PubMed:9806540}.
/FTId=VAR_013339.
CONFLICT 339 339 L -> V (in Ref. 1; AAC77455).
{ECO:0000305}.
SEQUENCE 1321 AA; 146407 MW; 61EE2173E2351D80 CRC64;
MSDSVILRSI KKFGEENDGF ESDKSYNNDK KSRLQDEKKG DGVRVGFFQL FRFSSSTDIW
LMFVGSLCAF LHGIAQPGVL LIFGTMTDVF IDYDVELQEL QIPGKACVNN TIVWTNSSLN
QNMTNGTRCG LLNIESEMIK FASYYAGIAV AVLITGYIQI CFWVIAAARQ IQKMRKFYFR
RIMRMEIGWF DCNSVGELNT RFSDDINKIN DAIADQMALF IQRMTSTICG FLLGFFRGWK
LTLVIISVSP LIGIGAATIG LSVSKFTDYE LKAYAKAGVV ADEVISSMRT VAAFGGEKRE
VERYEKNLVF AQRWGIRKGI VMGFFTGFVW CLIFLCYALA FWYGSTLVLD EGEYTPGTLV
QIFLSVIVGA LNLGNASPCL EAFATGRAAA TSIFETIDRK PIIDCMSEDG YKLDRIKGEI
EFHNVTFHYP SRPEVKILND LNMVIKPGEM TALVGPSGAG KSTALQLIQR FYDPCEGMVT
VDGHDIRSLN IQWLRDQIGI VEQEPVLFST TIAENIRYGR EDATMEDIVQ AAKEANAYNF
IMDLPQQFDT LVGEGGGQMS GGQKQRVAIA RALIRNPKIL LLDMATSALD NESEAMVQEV
LSKIQHGHTI ISVAHRLSTV RAADTIIGFE HGTAVERGTH EELLERKGVY FTLVTLQSQG
NQALNEEDIK DATEDDMLAR TFSRGSYQDS LRASIRQRSK SQLSYLVHEP PLAVVDHKST
YEEDRKDKDI PVQEEVEPAP VRRILKFSAP EWPYMLVGSV GAAVNGTVTP LYAFLFSQIL
GTFSIPDKEE QRSQINGVCL LFVAMGCVSL FTQFLQGYAF AKSGELLTKR LRKFGFRAML
GQDIAWFDDL RNSPGALTTR LATDASQVQG AAGSQIGMIV NSFTNVTVAM IIAFSFSWKL
SLVILCFFPF LALSGATQTR MLTGFASRDK QALEMVGQIT NEALSNIRTV AGIGKERRFI
EALETELEKP FKTAIQKANI YGFCFAFAQC IMFIANSASY RYGGYLISNE GLHFSYVFRV
ISAVVLSATA LGRAFSYTPS YAKAKISAAR FFQLLDRQPP ISVYNTAGEK WDNFQGKIDF
VDCKFTYPSR PDSQVLNGLS VSISPGQTLA FVGSSGCGKS TSIQLLERFY DPDQGKVMID
GHDSKKVNVQ FLRSNIGIVS QEPVLFACSI MDNIKYGDNT KEIPMERVIA AAKQAQLHDF
VMSLPEKYET NVGSQGSQLS RGEKQRIAIA RAIVRDPKIL LLDEATSALD TESEKTVQVA
LDKAREGRTC IVIAHRLSTI QNADIIAVMA QGVVIEKGTH EELMAQKGAY YKLVTTGSPI
S


Related products :

Catalog number Product name Quantity
EM501 Bile salt export pump Elisa Kit 96T
PC064 Bile salt export pump _ BSEP 0.2 ml
MC333 Bile salt export pump _ BSEP 0.1 mg
ARP43644_P050 Bile salt export pump _ BSEP 50 µg
GTX102608 Bile salt export pump _ BSEP 100 µl
NBP1-31824 Bile salt export pump _ BSEP 0.1 ml
AP13073PU-N Bile salt export pump _ BSEP (C_term) 0.1 mg
CSB-EL001049RA Rat Bile salt export pump(ABCB11) ELISA kit 96T
CSB-EL001049RA Rat Bile salt export pump(ABCB11) ELISA kit SpeciesRat 96T
CSB-EL001049MO Mouse Bile salt export pump(ABCB11) ELISA kit 96T
CSB-EL001049HU Human Bile salt export pump(ABCB11) ELISA kit 96T
AP13073CP-N Bile salt export pump _ BSEP Control Peptide 0.1 mg
10-P1393 Polyclonal antibody Anti-Bile Salt Export Pump, BSEP 100μg
'GTX102608 Bile salt export pump BSEP antibody Host rabbit 0.1 ml
'ARP43644_P050 Bile salt export pump BSEP antibody Host rabbit 50
'BB-PA1393 Bile salt export pump BSEP IgG antibody Ab host: Rabbit 0.1 mg
'AP13073CP-N Bile salt export pump _ BSEP Control Peptide antibody _CP 0.1 mg
'AP13073CP-N Bile salt export pump BSEP Control Peptide antibody CP 0.1 mg
CSB-EL001049MO Mouse Bile salt export pump(ABCB11) ELISA kit SpeciesMouse 96T
'AP13073CP-N Bile salt export pump BSEP Control Peptide antibody Ab CP 0.1 mg
GTX102608 Bile salt export pump _ BSEP Rabbit antibody Ab Aff - Purified 0.1 ml
CSB-EL001049RB Rabbit Bile salt export pump(ABCB11) ELISA kit SpeciesRabbit 96T
'ARP43644_P050 Bile salt export pump _ BSEP antibody Host rabbit 50
'GTX102608 Bile salt export pump _ BSEP antibody Host rabbit 0.1 ml
CSB-EL001049HU Human Bile salt export pump(ABCB11) ELISA kit SpeciesHuman 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur