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O95342 (ABCBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bile salt export pump
Alternative name(s):
ATP-binding cassette sub-family B member 11
Gene names
Name:ABCB11
Synonyms:BSEP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1321 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the ATP-dependent secretion of bile salts into the canaliculus of hepatocytes.

Subunit structure

Interacts with HAX1 By similarity.

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.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.5 Ref.7

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.10

Sequence similarities

Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. [View classification]

Contains 2 ABC transmembrane type-1 domains.

Contains 2 ABC transporter domains.

Biophysicochemical properties

Kinetic parameters:

KM=30.4 µM for taurocholate Ref.13

Vmax=232 pmol/min/mg enzyme for taurocholate transport

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Intrahepatic cholestasis
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid and bile salt transport

Traceable author statement. Source: Reactome

bile acid biosynthetic process

Traceable author statement. Source: Reactome

bile acid metabolic process

Traceable author statement. Source: Reactome

canalicular bile acid transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

small molecule metabolic process

Traceable author statement. Source: Reactome

sodium ion transmembrane transport

Traceable author statement Ref.1. Source: GOC

transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

apical plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

intercellular canaliculus

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Traceable author statement Ref.1. Source: ProtInc

ATPase activity, coupled to transmembrane movement of substances

Inferred from Biological aspect of Ancestor. Source: RefGenome

bile acid-exporting ATPase activity

Traceable author statement Ref.1. Source: ProtInc

canalicular bile acid transmembrane transporter activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

sodium-exporting ATPase activity, phosphorylative mechanism

Traceable author statement Ref.1. Source: ProtInc

transporter activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13211321Bile salt export pump
PRO_0000093296

Regions

Topological domain1 – 6262Cytoplasmic Potential
Transmembrane63 – 8321Helical; Potential
Topological domain84 – 14764Extracellular Potential
Transmembrane148 – 16821Helical; Potential
Topological domain169 – 21547Cytoplasmic Potential
Transmembrane216 – 23621Helical; Potential
Topological domain237 – 2404Extracellular Potential
Transmembrane241 – 26121Helical; Potential
Topological domain262 – 31958Cytoplasmic Potential
Transmembrane320 – 34021Helical; Potential
Topological domain341 – 35313Extracellular Potential
Transmembrane354 – 37421Helical; Potential
Topological domain375 – 755381Cytoplasmic Potential
Transmembrane756 – 77621Helical; Potential
Topological domain777 – 79418Extracellular Potential
Transmembrane795 – 81521Helical; Potential
Topological domain816 – 86954Cytoplasmic Potential
Transmembrane870 – 89021Helical; Potential
Transmembrane891 – 91121Helical; Potential
Topological domain912 – 97968Cytoplasmic Potential
Transmembrane980 – 100021Helical; Potential
Topological domain1001 – 101111Extracellular Potential
Transmembrane1012 – 103221Helical; Potential
Topological domain1033 – 1321289Cytoplasmic Potential
Domain62 – 385324ABC transmembrane type-1 1
Domain420 – 656237ABC transporter 1
Domain755 – 1043289ABC transmembrane type-1 2
Domain1078 – 1316239ABC transporter 2
Nucleotide binding455 – 4628ATP 1 Potential
Nucleotide binding1113 – 11208ATP 2 Potential
Region651 – 67222Interaction with HAX1 By similarity

Amino acid modifications

Modified residue6901Phosphoserine By similarity
Glycosylation1091N-linked (GlcNAc...) Ref.4
Glycosylation1161N-linked (GlcNAc...) Ref.4
Glycosylation1221N-linked (GlcNAc...) Ref.4
Glycosylation1251N-linked (GlcNAc...) Ref.4

Natural variations

Natural variant561S → L.
Corresponds to variant rs11568361 [ dbSNP | Ensembl ].
VAR_055472
Natural variant1861E → G in BRIC2. Ref.8
VAR_030386
Natural variant2061I → V. Ref.11
Corresponds to variant rs11568357 [ dbSNP | Ensembl ].
VAR_030387
Natural variant2381G → V in PFIC2. Ref.5
VAR_030388
Natural variant2841V → A. Ref.11 Ref.13
VAR_035349
Natural variant2841V → L in PFIC2. Ref.7
VAR_013332
Natural variant2971E → G in PFIC2 and BRIC2; reduced transport capacity for taurocholate. Ref.1 Ref.8 Ref.10
VAR_010271
Natural variant2991R → K. Ref.11
Corresponds to variant rs2287617 [ dbSNP | Ensembl ].
VAR_030389
Natural variant3361C → S in PFIC2. Ref.5
VAR_030390
Natural variant4151R → Q. Ref.9
VAR_043074
Natural variant4321R → T in BRIC2; reduced transport capacity for taurocholate. Ref.10
VAR_030391
Natural variant4441V → A More frequent in patients with drug-induced cholestasis than healthy controls; associated with lower hepatic expression; does not affect transport capacity for taurocholate. Ref.2 Ref.6 Ref.9 Ref.11 Ref.12 Ref.13
Corresponds to variant rs2287622 [ dbSNP | Ensembl ].
VAR_013333
Natural variant4441V → D.
Corresponds to variant rs2287622 [ dbSNP | Ensembl ].
VAR_059106
Natural variant4441V → G.
Corresponds to variant rs2287622 [ dbSNP | Ensembl ].
VAR_059107
Natural variant4611K → E in PFIC2. Ref.1
VAR_013334
Natural variant4821D → G in PFIC2. Ref.1
VAR_013335
Natural variant5701A → T in BRIC2. Ref.8
VAR_030392
Natural variant5911N → S in a patient with intrahepatic cholestasis of pregnancy. Ref.9
Corresponds to variant rs11568367 [ dbSNP | Ensembl ].
VAR_043075
Natural variant6161R → G. Ref.11
VAR_035350
Natural variant6191T → A. Ref.11
VAR_035351
Natural variant6761D → Y in fluvastatin-induced cholestasis; does not affect transport capacity for taurocholate. Ref.13
VAR_043076
Natural variant6771M → V Does not affect transport capacity for taurocholate. Ref.9 Ref.11 Ref.12 Ref.13
Corresponds to variant rs11568364 [ dbSNP | Ensembl ].
VAR_030393
Natural variant6981R → H. Ref.11 Ref.13
Corresponds to variant rs138642043 [ dbSNP | Ensembl ].
VAR_035352
Natural variant8551G → R in ethinylestradiol/gestodene-induced cholestasis; loss of transport capacity for taurocholate. Ref.13
VAR_043077
Natural variant8651A → V. Ref.11
Corresponds to variant rs118109635 [ dbSNP | Ensembl ].
VAR_035353
Natural variant9231T → P in BRIC2. Ref.8
VAR_030394
Natural variant9261A → P in BRIC2. Ref.8
VAR_030395
Natural variant9581R → Q. Ref.11
VAR_035354
Natural variant9821G → R in PFIC2. Ref.1
VAR_013336
Natural variant10041G → D in PFIC2. Ref.7
VAR_013337
Natural variant10501R → C in BRIC2. Ref.8
VAR_030396
Natural variant11281R → H in BRIC2. Ref.8
VAR_030397
Natural variant11531R → C in PFIC2. Ref.1
VAR_013338
Natural variant11861E → K.
Corresponds to variant rs1521808 [ dbSNP | Ensembl ].
VAR_030398
Natural variant12681R → Q in PFIC2. Ref.1
VAR_013339

Experimental info

Sequence conflict3391L → V in AAC77455. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O95342 [UniParc].

Last modified November 3, 2009. Version 2.
Checksum: 61EE2173E2351D80

FASTA1,321146,407
        10         20         30         40         50         60 
MSDSVILRSI KKFGEENDGF ESDKSYNNDK KSRLQDEKKG DGVRVGFFQL FRFSSSTDIW 

        70         80         90        100        110        120 
LMFVGSLCAF LHGIAQPGVL LIFGTMTDVF IDYDVELQEL QIPGKACVNN TIVWTNSSLN 

       130        140        150        160        170        180 
QNMTNGTRCG LLNIESEMIK FASYYAGIAV AVLITGYIQI CFWVIAAARQ IQKMRKFYFR 

       190        200        210        220        230        240 
RIMRMEIGWF DCNSVGELNT RFSDDINKIN DAIADQMALF IQRMTSTICG FLLGFFRGWK 

       250        260        270        280        290        300 
LTLVIISVSP LIGIGAATIG LSVSKFTDYE LKAYAKAGVV ADEVISSMRT VAAFGGEKRE 

       310        320        330        340        350        360 
VERYEKNLVF AQRWGIRKGI VMGFFTGFVW CLIFLCYALA FWYGSTLVLD EGEYTPGTLV 

       370        380        390        400        410        420 
QIFLSVIVGA LNLGNASPCL EAFATGRAAA TSIFETIDRK PIIDCMSEDG YKLDRIKGEI 

       430        440        450        460        470        480 
EFHNVTFHYP SRPEVKILND LNMVIKPGEM TALVGPSGAG KSTALQLIQR FYDPCEGMVT 

       490        500        510        520        530        540 
VDGHDIRSLN IQWLRDQIGI VEQEPVLFST TIAENIRYGR EDATMEDIVQ AAKEANAYNF 

       550        560        570        580        590        600 
IMDLPQQFDT LVGEGGGQMS GGQKQRVAIA RALIRNPKIL LLDMATSALD NESEAMVQEV 

       610        620        630        640        650        660 
LSKIQHGHTI ISVAHRLSTV RAADTIIGFE HGTAVERGTH EELLERKGVY FTLVTLQSQG 

       670        680        690        700        710        720 
NQALNEEDIK DATEDDMLAR TFSRGSYQDS LRASIRQRSK SQLSYLVHEP PLAVVDHKST 

       730        740        750        760        770        780 
YEEDRKDKDI PVQEEVEPAP VRRILKFSAP EWPYMLVGSV GAAVNGTVTP LYAFLFSQIL 

       790        800        810        820        830        840 
GTFSIPDKEE QRSQINGVCL LFVAMGCVSL FTQFLQGYAF AKSGELLTKR LRKFGFRAML 

       850        860        870        880        890        900 
GQDIAWFDDL RNSPGALTTR LATDASQVQG AAGSQIGMIV NSFTNVTVAM IIAFSFSWKL 

       910        920        930        940        950        960 
SLVILCFFPF LALSGATQTR MLTGFASRDK QALEMVGQIT NEALSNIRTV AGIGKERRFI 

       970        980        990       1000       1010       1020 
EALETELEKP FKTAIQKANI YGFCFAFAQC IMFIANSASY RYGGYLISNE GLHFSYVFRV 

      1030       1040       1050       1060       1070       1080 
ISAVVLSATA LGRAFSYTPS YAKAKISAAR FFQLLDRQPP ISVYNTAGEK WDNFQGKIDF 

      1090       1100       1110       1120       1130       1140 
VDCKFTYPSR PDSQVLNGLS VSISPGQTLA FVGSSGCGKS TSIQLLERFY DPDQGKVMID 

      1150       1160       1170       1180       1190       1200 
GHDSKKVNVQ FLRSNIGIVS QEPVLFACSI MDNIKYGDNT KEIPMERVIA AAKQAQLHDF 

      1210       1220       1230       1240       1250       1260 
VMSLPEKYET NVGSQGSQLS RGEKQRIAIA RAIVRDPKIL LLDEATSALD TESEKTVQVA 

      1270       1280       1290       1300       1310       1320 
LDKAREGRTC IVIAHRLSTI QNADIIAVMA QGVVIEKGTH EELMAQKGAY YKLVTTGSPI 


S 

« Hide

References

« Hide 'large scale' references
[1]"A gene encoding a liver-specific ABC transporter is mutated in progressive familial intrahepatic cholestasis."
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.
Nat. Genet. 20:233-238(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PFIC2 GLY-297; GLU-461; GLY-482; ARG-982; CYS-1153 AND GLN-1268.
[2]"Cellular localization and functional characterization of the human bile salt export pump (BSEP)."
Mol O., Hooiveld G.J.E.J., Jansen P.L.M., Muller M.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-444.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells."
Mochizuki K., Kagawa T., Numari A., Harris M.J., Itoh J., Watanabe N., Mine T., Arias I.M.
Am. J. Physiol. 292:G818-G828(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-109; ASN-116; ASN-122 AND ASN-125.
[5]"Hepatocanalicular bile salt export pump deficiency in patients with progressive familial intrahepatic cholestasis."
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.
Gastroenterology 117:1370-1379(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PFIC2 VAL-238 AND SER-336.
[6]"Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population."
Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., Higuchi S., Nakamura Y.
J. Hum. Genet. 47:38-50(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-444.
[7]"FIC1 and BSEP defects in Taiwanese patients with chronic intrahepatic cholestasis with low gamma-glutamyltranspeptidase levels."
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.
J. Pediatr. 140:119-124(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PFIC2 LEU-284 AND ASP-1004.
[8]"Benign recurrent intrahepatic cholestasis type 2 is caused by mutations in ABCB11."
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.
Gastroenterology 127:379-384(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BRIC2 GLY-186; GLY-297; THR-570; PRO-923; PRO-926; CYS-1050 AND HIS-1128.
[9]"Sequence analysis of bile salt export pump (ABCB11) and multidrug resistance p-glycoprotein 3 (ABCB4, MDR3) in patients with intrahepatic cholestasis of pregnancy."
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.
Pharmacogenetics 14:91-102(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLN-415; ALA-444; SER-591 AND VAL-677.
[10]"Impaired expression and function of the bile salt export pump due to three novel ABCB11 mutations in intrahepatic cholestasis."
Noe J., Kullak-Ublick G.A., Jochum W., Stieger B., Kerb R., Haberl M., Muellhaupt B., Meier P.J., Pauli-Magnus C.
J. Hepatol. 43:536-543(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BRIC2 GLY-297 AND THR-432, CHARACTERIZATION OF VARIANTS BRIC2 GLY-297 AND THR-432.
[11]"Genetic variability, haplotype structures, and ethnic diversity of hepatic transporters MDR3 (ABCB4) and bile salt export pump (ABCB11)."
Lang T., Haberl M., Jung D., Drescher A., Schlagenhaufer R., Keil A., Mornhinweg E., Stieger B., Kullak-Ublick G.A., Kerb R.
Drug Metab. Dispos. 34:1582-1599(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-206; ALA-284; LYS-299; ALA-444; GLY-616; ALA-619; VAL-677; HIS-698; VAL-865 AND GLN-958.
[12]"Interindividual variability of canalicular ATP-binding-cassette (ABC)-transporter expression in human liver."
Meier Y., Pauli-Magnus C., Zanger U.M., Klein K., Schaeffeler E., Nussler A.K., Nussler N., Eichelbaum M., Meier P.J., Stieger B.
Hepatology 44:62-74(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALA-444 AND VAL-677.
[13]"Mutations and polymorphisms in the bile salt export pump and the multidrug resistance protein 3 associated with drug-induced liver injury."
Lang C., Meier Y., Stieger B., Beuers U., Lang T., Kerb R., Kullak-Ublick G.A., Meier P.J., Pauli-Magnus C.
Pharmacogenet. Genomics 17:47-60(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALA-284; ALA-444; TYR-676; VAL-677; HIS-698 AND ARG-855, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ALA-444; TYR-676; VAL-677 AND ARG-855.
+Additional computationally mapped references.

Web resources

GeneReviews
ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF091582 mRNA. Translation: AAC77455.1.
AF136523 mRNA. Translation: AAD28285.1.
AC008177 Genomic DNA. Translation: AAY24305.1.
AC093723 Genomic DNA. No translation available.
AC069137 Genomic DNA. No translation available.
RefSeqNP_003733.2. NM_003742.2.
UniGeneHs.658439.

3D structure databases

ProteinModelPortalO95342.
SMRO95342. Positions 18-1316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114199. 3 interactions.
IntActO95342. 2 interactions.
MINTMINT-5003953.
STRING9606.ENSP00000263817.

Chemistry

BindingDBO95342.
ChEMBLCHEMBL6020.
DrugBankDB00171. Adenosine triphosphate.
DB00559. Bosentan.
DB01016. Glibenclamide.

Protein family/group databases

TCDB3.A.1.201.2. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteO95342.

Proteomic databases

PaxDbO95342.
PRIDEO95342.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263817; ENSP00000263817; ENSG00000073734.
ENST00000576612; ENSP00000459250; ENSG00000263298.
GeneID8647.
KEGGhsa:8647.
UCSCuc002ueo.1. human.

Organism-specific databases

CTD8647.
GeneCardsGC02M169743.
H-InvDBHIX0029772.
HGNCHGNC:42. ABCB11.
HPAHPA019035.
MIM601847. phenotype.
603201. gene.
605479. phenotype.
neXtProtNX_O95342.
Orphanet99961. Benign recurrent intrahepatic cholestasis type 2.
69665. Intrahepatic cholestasis of pregnancy.
79304. Progressive familial intrahepatic cholestasis type 2.
PharmGKBPA374.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1132.
HOVERGENHBG080809.
InParanoidO95342.
KOK05664.
OMATIVWTNS.
PhylomeDBO95342.
TreeFamTF105193.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO95342.
BgeeO95342.
CleanExHS_ABCB11.
GenevestigatorO95342.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 3 hits.
PROSITEPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABCB11. human.
GeneWikiABCB11.
GenomeRNAi8647.
NextBio32419.
PROO95342.
SOURCESearch...

Entry information

Entry nameABCBB_HUMAN
AccessionPrimary (citable) accession number: O95342
Secondary accession number(s): Q53TL2, Q9UNB2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 3, 2009
Last modified: April 16, 2014
This is version 134 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM