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O43520 (AT8B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipid-transporting ATPase IC

EC=3.6.3.1
Alternative name(s):
ATPase class I type 8B member 1
Familial intrahepatic cholestasis type 1
P4-ATPase flippase complex alpha subunit ATP8B1
Gene names
Name:ATP8B1
Synonyms:ATPIC, FIC1, PFIC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1251 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. May play a role in asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both. In cooperation with ABCB4 may be involved in establishing integrity of the canalicular membrane thus protecting hepatocytes from bile salts. Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine. Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity. Required for the preservation of cochlear hair cells in the inner ear. May act as cardiolipin transporter during inflammatory injury. Ref.5 Ref.6 Ref.7

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. The probable flippase ATP8B1:TMEM30A complex can form an intermediate phosphoenzyme in vitro. Also interacts with beta subunit TMEM30B. Ref.5 Ref.8 Ref.9 Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein. Apical cell membrane. Cell projectionstereocilium By similarity. Endoplasmic reticulum. Golgi apparatus. Note: Exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B. Localizes to apical membranes in epithelial cells. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10

Tissue specificity

Found in most tissues except brain and skeletal muscle. Most abundant in pancreas and small intestine.

Involvement in disease

Cholestasis, progressive familial intrahepatic, 1 (PFIC1) [MIM:211600]: 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.12 Ref.13 Ref.17 Ref.18 Ref.19

Cholestasis, benign recurrent intrahepatic, 1 (BRIC1) [MIM:243300]: 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.1 Ref.11 Ref.13 Ref.17

Cholestasis of pregnancy, intrahepatic 1 (ICP1) [MIM:147480]: A liver disorder of pregnancy. It presents during the second or, more commonly, the third trimester of pregnancy with intense pruritus which becomes more severe with advancing gestation and cholestasis. Cholestasis results from abnormal biliary transport from the liver into the small intestine. ICP1 causes fetal distress, spontaneous premature delivery and intrauterine death. ICP1 patients have spontaneous and progressive disappearance of cholestasis after delivery.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.17

Sequence similarities

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

Ontologies

Keywords
   Biological processHearing
Lipid transport
Transport
   Cellular componentCell membrane
Cell projection
Endoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Intrahepatic cholestasis
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid and bile salt transport

Non-traceable author statement PubMed 12880872. Source: UniProtKB

bile acid metabolic process

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 16628629. Source: UniProtKB

phospholipid translocation

Non-traceable author statement. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 11682026Ref.7. Source: UniProtKB

brush border membrane

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay Ref.10. Source: UniProtKB

integral component of plasma membrane

Non-traceable author statement PubMed 12880872. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cation-transporting ATPase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipid-translocating ATPase activity

Traceable author statement PubMed 12880872. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12511251Phospholipid-transporting ATPase IC
PRO_0000046364

Regions

Topological domain1 – 108108Cytoplasmic Potential
Transmembrane109 – 13022Helical; Potential
Topological domain131 – 1366Exoplasmic loop Potential
Transmembrane137 – 15620Helical; Potential
Topological domain157 – 340184Cytoplasmic Potential
Transmembrane341 – 36222Helical; Potential
Topological domain363 – 38927Exoplasmic loop Potential
Transmembrane390 – 41122Helical; Potential
Topological domain412 – 949538Cytoplasmic Potential
Transmembrane950 – 97021Helical; Potential
Topological domain971 – 98212Exoplasmic loop Potential
Transmembrane983 – 100220Helical; Potential
Topological domain1003 – 103230Cytoplasmic Potential
Transmembrane1033 – 105422Helical; Potential
Topological domain1055 – 106814Exoplasmic loop Potential
Transmembrane1069 – 109123Helical; Potential
Topological domain1092 – 10976Cytoplasmic Potential
Transmembrane1098 – 111821Helical; Potential
Topological domain1119 – 113820Exoplasmic loop Potential
Transmembrane1139 – 116325Helical; Potential
Topological domain1164 – 125188Cytoplasmic Potential

Sites

Active site45414-aspartylphosphate intermediate By similarity
Metal binding8931Magnesium By similarity
Metal binding8971Magnesium By similarity

Amino acid modifications

Modified residue12231Phosphoserine By similarity

Natural variations

Natural variant451N → T in ICP1. Ref.14
Corresponds to variant rs146599962 [ dbSNP | Ensembl ].
VAR_043044
Natural variant701D → N in BRIC1; compound heterozygote with Q-600; uncertain pathological significance; may be associated with ICP; reduces interaction with TMEM30A. Ref.13 Ref.15 Ref.17
Corresponds to variant rs34719006 [ dbSNP | Ensembl ].
VAR_043045
Natural variant781H → Q.
Corresponds to variant rs3745079 [ dbSNP | Ensembl ].
VAR_029271
Natural variant1271L → P in PFIC1. Ref.13
VAR_043046
Natural variant2031K → E in ICP1. Ref.14
Corresponds to variant rs56355310 [ dbSNP | Ensembl ].
VAR_043047
Natural variant2091P → T in PFIC1. Ref.18
VAR_071045
Natural variant2881L → S in PFIC1. Ref.1
VAR_008809
Natural variant3051F → I. Ref.15
Corresponds to variant rs150860808 [ dbSNP | Ensembl ].
VAR_043048
Natural variant3081G → D in BRIC1. Ref.13
Corresponds to variant rs28939685 [ dbSNP | Ensembl ].
VAR_043049
Natural variant3081G → V in PFIC1; greatly reduced expression due to proteosomal degradation; abolishes interaction with TMEM30A. Ref.1 Ref.17
Corresponds to variant rs28939685 [ dbSNP | Ensembl ].
VAR_008810
Natural variant3441I → F in BRIC1. Ref.13
VAR_043050
Natural variant3841R → H.
Corresponds to variant rs2271260 [ dbSNP | Ensembl ].
VAR_043051
Natural variant3931I → V.
Corresponds to variant rs34315917 [ dbSNP | Ensembl ].
VAR_043052
Natural variant4031S → Y in PFIC1. Ref.13
VAR_043053
Natural variant4121R → P in PFIC1. Ref.13
VAR_043054
Natural variant4291E → A. Ref.13
Corresponds to variant rs34018205 [ dbSNP | Ensembl ].
VAR_043055
Natural variant4531S → Y in BRIC1. Ref.13
VAR_043056
Natural variant4541D → G in BRIC1. Ref.13
VAR_043057
Natural variant4561T → M in PFIC1. Ref.13
VAR_043058
Natural variant5001Y → H in PFIC1. Ref.13
VAR_043059
Natural variant5291Missing in PFIC1. Ref.13
VAR_043060
Natural variant5351H → L in PFIC1. Ref.13
VAR_043061
Natural variant5541D → N in PFIC1; greatly reduced expression due to proteosomal degradation; abolishes interaction with TMEM30A. Ref.12 Ref.13 Ref.17
VAR_015423
Natural variant5771I → V.
Corresponds to variant rs3745078 [ dbSNP | Ensembl ].
VAR_029272
Natural variant5801S → N.
Corresponds to variant rs33963153 [ dbSNP | Ensembl ].
VAR_043062
Natural variant6001R → Q in BRIC1; compound heterozygote with N-70. Ref.13
VAR_043063
Natural variant6001R → W in BRIC1. Ref.13
VAR_043064
Natural variant6281R → W in BRIC1. Ref.13
VAR_043065
Natural variant645 – 69955Missing in PFIC1.
VAR_008811
Natural variant6611I → T in BRIC1 and PFIC1; common mutation; reduces interaction with TMEM30A. Ref.1 Ref.11 Ref.13 Ref.17
Corresponds to variant rs28939686 [ dbSNP | Ensembl ].
VAR_008812
Natural variant6741M → T.
Corresponds to variant rs35470719 [ dbSNP | Ensembl ].
VAR_043066
Natural variant6881D → G in PFIC1. Ref.13
VAR_043067
Natural variant6941I → T in BRIC1. Ref.13
VAR_043068
Natural variant7331G → R in PFIC1. Ref.13
VAR_043069
Natural variant795 – 7973Missing in BRIC1.
VAR_008814
Natural variant8141K → N.
Corresponds to variant rs34018300 [ dbSNP | Ensembl ].
VAR_043070
Natural variant8531F → S in PFIC1. Ref.13
VAR_043071
Natural variant8671R → C in ICP1; reduces interaction with TMEM30A. Ref.15 Ref.17
VAR_043072
Natural variant8861A → V in a breast cancer sample; somatic mutation. Ref.16
VAR_036499
Natural variant8921G → R in PFIC1 and BRIC1. Ref.1 Ref.13
VAR_008813
Natural variant9521R → Q. Ref.14 Ref.15
Corresponds to variant rs12968116 [ dbSNP | Ensembl ].
VAR_029273
Natural variant10121S → I in PFIC1. Ref.19
VAR_071046
Natural variant10401G → R in PFIC1; greatly reduces interaction with TMEM30A. Ref.13 Ref.17
VAR_043073
Natural variant11521A → T. Ref.1 Ref.4
Corresponds to variant rs222581 [ dbSNP | Ensembl ].
VAR_055045
Natural variant11781I → M in a breast cancer sample; somatic mutation. Ref.16
VAR_036500

Experimental info

Mutagenesis4541D → A: Greatly reduced expression due to proteosomal degradation; abolishes interaction with TMEM30A. Ref.17
Sequence conflict10161P → L in AAH03534. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O43520 [UniParc].

Last modified May 5, 2009. Version 3.
Checksum: 770FEF3946CB579F

FASTA1,251143,695
        10         20         30         40         50         60 
MSTERDSETT FDEDSQPNDE VVPYSDDETE DELDDQGSAV EPEQNRVNRE AEENREPFRK 

        70         80         90        100        110        120 
ECTWQVKAND RKYHEQPHFM NTKFLCIKES KYANNAIKTY KYNAFTFIPM NLFEQFKRAA 

       130        140        150        160        170        180 
NLYFLALLIL QAVPQISTLA WYTTLVPLLV VLGVTAIKDL VDDVARHKMD KEINNRTCEV 

       190        200        210        220        230        240 
IKDGRFKVAK WKEIQVGDVI RLKKNDFVPA DILLLSSSEP NSLCYVETAE LDGETNLKFK 

       250        260        270        280        290        300 
MSLEITDQYL QREDTLATFD GFIECEEPNN RLDKFTGTLF WRNTSFPLDA DKILLRGCVI 

       310        320        330        340        350        360 
RNTDFCHGLV IFAGADTKIM KNSGKTRFKR TKIDYLMNYM VYTIFVVLIL LSAGLAIGHA 

       370        380        390        400        410        420 
YWEAQVGNSS WYLYDGEDDT PSYRGFLIFW GYIIVLNTMV PISLYVSVEV IRLGQSHFIN 

       430        440        450        460        470        480 
WDLQMYYAEK DTPAKARTTT LNEQLGQIHY IFSDKTGTLT QNIMTFKKCC INGQIYGDHR 

       490        500        510        520        530        540 
DASQHNHNKI EQVDFSWNTY ADGKLAFYDH YLIEQIQSGK EPEVRQFFFL LAVCHTVMVD 

       550        560        570        580        590        600 
RTDGQLNYQA ASPDEGALVN AARNFGFAFL ARTQNTITIS ELGTERTYNV LAILDFNSDR 

       610        620        630        640        650        660 
KRMSIIVRTP EGNIKLYCKG ADTVIYERLH RMNPTKQETQ DALDIFANET LRTLCLCYKE 

       670        680        690        700        710        720 
IEEKEFTEWN KKFMAASVAS TNRDEALDKV YEEIEKDLIL LGATAIEDKL QDGVPETISK 

       730        740        750        760        770        780 
LAKADIKIWV LTGDKKETAE NIGFACELLT EDTTICYGED INSLLHARME NQRNRGGVYA 

       790        800        810        820        830        840 
KFAPPVQESF FPPGGNRALI ITGSWLNEIL LEKKTKRNKI LKLKFPRTEE ERRMRTQSKR 

       850        860        870        880        890        900 
RLEAKKEQRQ KNFVDLACEC SAVICCRVTP KQKAMVVDLV KRYKKAITLA IGDGANDVNM 

       910        920        930        940        950        960 
IKTAHIGVGI SGQEGMQAVM SSDYSFAQFR YLQRLLLVHG RWSYIRMCKF LRYFFYKNFA 

       970        980        990       1000       1010       1020 
FTLVHFWYSF FNGYSAQTAY EDWFITLYNV LYTSLPVLLM GLLDQDVSDK LSLRFPGLYI 

      1030       1040       1050       1060       1070       1080 
VGQRDLLFNY KRFFVSLLHG VLTSMILFFI PLGAYLQTVG QDGEAPSDYQ SFAVTIASAL 

      1090       1100       1110       1120       1130       1140 
VITVNFQIGL DTSYWTFVNA FSIFGSIALY FGIMFDFHSA GIHVLFPSAF QFTGTASNAL 

      1150       1160       1170       1180       1190       1200 
RQPYIWLTII LAVAVCLLPV VAIRFLSMTI WPSESDKIQK HRKRLKAEEQ WQRRQQVFRR 

      1210       1220       1230       1240       1250 
GVSTRRSAYA FSHQRGYADL ISSGRSIRKK RSPLDAIVAD GTAEYRRTGD S 

« Hide

References

« Hide 'large scale' references
[1]"A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis."
Bull L.N., van Eijk M.J.T., Pawlikowska L., DeYoung J.A., Juijn J.A., Liao M., Klomp L.W.J., Lomri N., Berger R., Scharschmidt B.F., Knisely A.S., Houwen R.H.J., Freimer N.B.
Nat. Genet. 18:219-223(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PFIC1 SER-288; VAL-308; 645-ILE--ILE-699 DEL AND ARG-892, VARIANTS BRIC1 THR-661 AND 795-GLY--ARG-797 DEL, VARIANT THR-1152.
Tissue: Intestine and Liver.
[2]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Multiple members of a third subfamily of P-type ATPases identified by genomic sequences and ESTs."
Halleck M.S., Pradhan D., Blackman C.F., Berkes C., Williamson P.L., Schlegel R.A.
Genome Res. 8:354-361(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 388-661.
Tissue: Colon tumor.
[4]"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 359-1251, VARIANT THR-1152.
Tissue: Uterus.
[5]"ATP8B1 requires an accessory protein for endoplasmic reticulum exit and plasma membrane lipid flippase activity."
Paulusma C.C., Folmer D.E., Ho-Mok K.S., de Waart D.R., Hilarius P.M., Verhoeven A.J., Oude Elferink R.P.
Hepatology 47:268-278(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[6]"CDC50A plays a key role in the uptake of the anticancer drug perifosine in human carcinoma cells."
Munoz-Martinez F., Torres C., Castanys S., Gamarro F.
Biochem. Pharmacol. 80:793-800(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"A flippase-independent function of ATP8B1, the protein affected in familial intrahepatic cholestasis type 1, is required for apical protein expression and microvillus formation in polarized epithelial cells."
Verhulst P.M., van der Velden L.M., Oorschot V., van Faassen E.E., Klumperman J., Houwen R.H., Pomorski T.G., Holthuis J.C., Klomp L.W.
Hepatology 51:2049-2060(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases."
van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A., Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.
J. Biol. Chem. 285:40088-40096(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM30A AND TMEM30B, SUBCELLULAR LOCATION.
[9]"CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery."
Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G., Holthuis J.C.
J. Biol. Chem. 285:40562-40572(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM30A AND TMEM30B, SUBCELLULAR LOCATION.
[10]"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 AND TMEM30B, SUBCELLULAR LOCATION.
[11]"Recurrent familial intrahepatic cholestasis in the Faeroe Islands. Phenotypic heterogeneity but genetic homogeneity."
Tygstrup N., Steig B.A., Juijn J.A., Bull L.N., Houwen R.H.J.
Hepatology 29:506-508(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BRIC1 THR-661.
[12]"A missense mutation in FIC1 is associated with Greenland familial cholestasis."
Klomp L.W.J., Bull L.N., Knisely A.S., van Der Doelen M.A., Juijn J.A., Berger R., Forget S., Nielsen I.-M., Eiberg H., Houwen R.H.J.
Hepatology 32:1337-1341(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PFIC1 ASN-554.
[13]"Characterization of mutations in ATP8B1 associated with hereditary cholestasis."
Klomp L.W.J., Vargas J.C., van Mil S.W.C., Pawlikowska L., Strautnieks S.S., van Eijk M.J.T., Juijn J.A., Pabon-Pena C., Smith L.B., DeYoung J.A., Byrne J.A., Gombert J., van der Brugge G., Berger R., Jankowska I., Pawlowska J., Villa E., Knisely A.S. expand/collapse author list , Thompson R.J., Freimer N.B., Houwen R.H.J., Bull L.N.
Hepatology 40:27-38(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PFIC1 PRO-127; TYR-403; PRO-412; MET-456; HIS-500; PHE-529 DEL; LEU-535; ASN-554; THR-661; GLY-688; ARG-733; SER-853; ARG-892 AND ARG-1040, VARIANTS BRIC1 ASN-70; ASP-308; PHE-344; TYR-453; GLY-454; TRP-600; GLN-600; TRP-628; THR-661; THR-694 AND ARG-892, VARIANT ALA-429.
[14]"Sequence variation in the ATP8B1 gene and intrahepatic cholestasis of pregnancy."
Painter J.N., Savander M., Ropponen A., Nupponen N., Riikonen S., Ylikorkala O., Lehesjoki A.E., Aittomaki K.
Eur. J. Hum. Genet. 13:435-439(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ICP1 THR-45 AND GLU-203, VARIANT GLN-952.
[15]"ATP8B1 mutations in British cases with intrahepatic cholestasis of pregnancy."
Muellenbach R., Bennett A., Tetlow N., Patel N., Hamilton G., Cheng F., Chambers J., Howard R., Taylor-Robinson S.D., Williamson C.
Gut 54:829-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ICP1 CYS-867, VARIANTS ASN-70; ILE-305 AND GLN-952.
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-886 AND MET-1178.
[17]"Differential effects of progressive familial intrahepatic cholestasis type 1 and benign recurrent intrahepatic cholestasis type 1 mutations on canalicular localization of ATP8B1."
Folmer D.E., van der Mark V.A., Ho-Mok K.S., Oude Elferink R.P., Paulusma C.C.
Hepatology 50:1597-1605(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS PFIC1 VAL-308; ASN-554; THR-661 AND ARG-1040, CHARACTERIZATION OF VARIANTS BRIC1 ASN-70 AND THR-661, CHARACTERIZATION OF VARIANT ICP1 CYS-867, MUTAGENESIS OF ASP-454.
[18]"Characterization of ATP8B1 gene mutations and a hot-linked mutation found in Chinese children with progressive intrahepatic cholestasis and low GGT."
Liu L.Y., Wang X.H., Wang Z.L., Zhu Q.R., Wang J.S.
J. Pediatr. Gastroenterol. Nutr. 50:179-183(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PFIC1 THR-209.
[19]"Novel ATP8B1 mutation in an adult male with progressive familial intrahepatic cholestasis."
Deng B.C., Lv S., Cui W., Zhao R., Lu X., Wu J., Liu P.
World J. Gastroenterol. 18:6504-6509(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PFIC1 ILE-1012.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF038007 mRNA. Translation: AAC63461.1.
AC027097 Genomic DNA. No translation available.
AF032442 mRNA. Translation: AAC04328.1.
BC003534 mRNA. Translation: AAH03534.1.
CCDSCCDS11965.1.
RefSeqNP_005594.1. NM_005603.4.
XP_006722544.1. XM_006722481.1.
UniGeneHs.216623.

3D structure databases

ProteinModelPortalO43520.
SMRO43520. Positions 434-784, 867-927.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111227. 2 interactions.
STRING9606.ENSP00000283684.

Protein family/group databases

TCDB3.A.3.8.11. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteO43520.

Proteomic databases

MaxQBO43520.
PaxDbO43520.
PRIDEO43520.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283684; ENSP00000283684; ENSG00000081923.
ENST00000536015; ENSP00000445359; ENSG00000081923.
GeneID5205.
KEGGhsa:5205.
UCSCuc002lgw.3. human.

Organism-specific databases

CTD5205.
GeneCardsGC18M055290.
GeneReviewsATP8B1.
HGNCHGNC:3706. ATP8B1.
HPAHPA018673.
HPA018674.
MIM147480. phenotype.
211600. phenotype.
243300. phenotype.
602397. gene.
neXtProtNX_O43520.
Orphanet99960. Benign recurrent intrahepatic cholestasis type 1.
69665. Intrahepatic cholestasis of pregnancy.
79306. Progressive familial intrahepatic cholestasis type 1.
PharmGKBPA265.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000202528.
HOVERGENHBG050601.
InParanoidO43520.
KOK01530.
OMAHSKIEPV.
OrthoDBEOG7RRF68.
PhylomeDBO43520.
TreeFamTF300654.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressO43520.
BgeeO43520.
CleanExHS_ATP8B1.
GenevestigatorO43520.

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.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATP8B1.
GenomeRNAi5205.
NextBio20132.
PROO43520.
SOURCESearch...

Entry information

Entry nameAT8B1_HUMAN
AccessionPrimary (citable) accession number: O43520
Secondary accession number(s): Q9BTP8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 147 of the entry and version 3 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 18

Human chromosome 18: entries, gene names and cross-references to MIM