ATP7B_HUMAN
ID ATP7B_HUMAN Reviewed; 1465 AA.
AC P35670; Q16318; Q16319; Q4U3V3; Q59FJ9; Q5T7X7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Copper-transporting ATPase 2;
DE EC=7.2.2.8 {ECO:0000269|PubMed:22240481};
DE AltName: Full=Copper pump 2;
DE AltName: Full=Wilson disease-associated protein;
DE Contains:
DE RecName: Full=WND/140 kDa {ECO:0000303|PubMed:9600907};
GN Name=ATP7B; Synonyms=PWD, WC1, WND;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ASP-96; ARG-875 AND
RP LYS-952.
RX PubMed=7833924; DOI=10.1093/hmg/3.9.1647;
RA Petrukhin K., Lutsenko S., Chernov I., Ross B.M., Kaplan J.H.,
RA Gilliam T.C.;
RT "Characterization of the Wilson disease gene encoding a P-type copper
RT transporting ATPase: genomic organization, alternative splicing, and
RT structure/function predictions.";
RL Hum. Mol. Genet. 3:1647-1656(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANTS ALA-406; LEU-456;
RP LYS-952 AND ALA-1140.
RA Carlini E.J., Booth-Genthe C.L.;
RT "Molecular cloning of mutant ATP7B.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=10334941; DOI=10.1006/bbrc.1999.0732;
RA Oh W.J., Kim E.K., Park K.D., Hahn S.H., Yoo O.J.;
RT "Cloning and characterization of the promoter region of the Wilson disease
RT gene.";
RL Biochem. Biophys. Res. Commun. 259:206-211(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-1465 (ISOFORM 1), AND VARIANT LYS-952.
RX PubMed=8298639; DOI=10.1038/ng1293-327;
RA Bull P.C., Thomas G.R., Rommens J.M., Forbes J.R., Cox D.W.;
RT "The Wilson disease gene is a putative copper transporting P-type ATPase
RT similar to the Menkes gene.";
RL Nat. Genet. 5:327-337(1993).
RN [6]
RP SEQUENCE REVISION.
RA Cox D.W.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 149-1465 (ISOFORM 2), VARIANTS WD GLN-1069
RP AND SER-1270, AND VARIANT ARG-875.
RX PubMed=8298641; DOI=10.1038/ng1293-344;
RA Tanzi R.E., Petrukhin K., Chernov I., Pellequer J.L., Wasco W., Ross B.,
RA Romano D.M., Parano E., Pavone L., Brzustowicz L.M., Devoto M.,
RA Peppercorn J., Bush A.I., Sternlieb I., Pirastu M., Gusella J.F.,
RA Evgrafov O., Penchaszadeh G.K., Honig B., Edelman I.S., Soares M.B.,
RA Scheinberg I.H., Gilliam T.C.;
RT "The Wilson disease gene is a copper transporting ATPase with homology to
RT the Menkes disease gene.";
RL Nat. Genet. 5:344-350(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 488-837 (ISOFORM 4), AND VARIANT ARG-832.
RC TISSUE=Liver;
RX PubMed=8250934; DOI=10.1006/bbrc.1993.2471;
RA Yamaguchi Y., Heiny M.E., Gitlin J.D.;
RT "Isolation and characterization of a human liver cDNA as a candidate gene
RT for Wilson disease.";
RL Biochem. Biophys. Res. Commun. 197:271-277(1993).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 786-1465, AND VARIANTS ARG-832
RP AND ALA-1140.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS WD, AND VARIANTS.
RX PubMed=7626145; DOI=10.1038/ng0295-210;
RA Thomas G.R., Forbes J.R., Roberts E.A., Walshe J.M., Cox D.W.;
RT "The Wilson disease gene: spectrum of mutations and their consequences.";
RL Nat. Genet. 9:210-216(1995).
RN [11]
RP ERRATUM OF PUBMED:7626145.
RA Thomas G.R., Forbes J.R., Roberts E.A., Walshe J.M., Cox D.W.;
RL Nat. Genet. 9:451-451(1995).
RN [12]
RP ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
RX PubMed=9307043; DOI=10.1042/bj3260897;
RA Yang X.-L., Miura N., Kawarada Y., Terada K., Petrukhin K., Gilliam T.C.,
RA Sugiyama T.;
RT "Two forms of Wilson disease protein produced by alternative splicing are
RT localized in distinct cellular compartments.";
RL Biochem. J. 326:897-902(1997).
RN [13]
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS WD ASN-765; VAL-776;
RP LEU-778 AND SER-943.
RX PubMed=10942420; DOI=10.1093/hmg/9.13.1927;
RA Forbes J.R., Cox D.W.;
RT "Copper-dependent trafficking of Wilson disease mutant ATP7B proteins.";
RL Hum. Mol. Genet. 9:1927-1935(2000).
RN [14]
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS WD GLN-1069 AND
RP SER-1270.
RX PubMed=11231950; DOI=10.1053/gast.2001.22543;
RA Harada M., Sakisaka S., Terada K., Kimura R., Kawaguchi T., Koga H.,
RA Kim M., Taniguchi E., Hanada S., Suganuma T., Furuta K., Sugiyama T.,
RA Sata M.;
RT "A mutation of the Wilson disease protein, ATP7B, is degraded in the
RT proteasomes and forms protein aggregates.";
RL Gastroenterology 120:967-974(2001).
RN [15]
RP MUTAGENESIS OF HIS-1069, AND CHARACTERIZATION OF VARIANT GLN-1069.
RX PubMed=12551905; DOI=10.1074/jbc.m300034200;
RA Tsivkovskii R., Efremov R.G., Lutsenko S.;
RT "The role of the invariant His-1069 in folding and function of the Wilson's
RT disease protein, the human copper-transporting ATPase ATP7B.";
RL J. Biol. Chem. 278:13302-13308(2003).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=15681833; DOI=10.1016/s0002-9440(10)62272-9;
RA Harada M., Kawaguchi T., Kumemura H., Terada K., Ninomiya H., Taniguchi E.,
RA Hanada S., Baba S., Maeyama M., Koga H., Ueno T., Furuta K., Suganuma T.,
RA Sugiyama T., Sata M.;
RT "The Wilson disease protein ATP7B resides in the late endosomes with Rab7
RT and the Niemann-Pick C1 protein.";
RL Am. J. Pathol. 166:499-510(2005).
RN [17]
RP INTERACTION WITH ZBTB16.
RX PubMed=16676348; DOI=10.1002/jcb.20980;
RA Ko J.H., Son W., Bae G.Y., Kang J.H., Oh W., Yoo O.J.;
RT "A new hepatocytic isoform of PLZF lacking the BTB domain interacts with
RT ATP7B, the Wilson disease protein, and positively regulates ERK signal
RT transduction.";
RL J. Cell. Biochem. 99:719-734(2006).
RN [18]
RP SUBCELLULAR LOCATION, INTERACTION WITH COMMD1 AND ATOX1, AND
RP CHARACTERIZATION OF VARIANTS WD SER-41; VAL-85; SER-486; SER-492; HIS-532;
RP LYS-541; ASP-591; PRO-604; GLN-616; TRP-616; ALA-626; SER-641; HIS-642 AND
RP ARG-645.
RX PubMed=17919502; DOI=10.1053/j.gastro.2007.07.020;
RA de Bie P., van de Sluis B., Burstein E., van de Berghe P.V., Muller P.,
RA Berger R., Gitlin J.D., Wijmenga C., Klomp L.W.;
RT "Distinct Wilson's disease mutations in ATP7B are associated with enhanced
RT binding to COMMD1 and reduced stability of ATP7B.";
RL Gastroenterology 133:1316-1326(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-478, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP CHARACTERIZATION OF VARIANTS WD ASN-765; VAL-769; VAL-776; LEU-778;
RP GLN-778; SER-943; MET-977 AND LEU-992, AND CHARACTERIZATION OF VARIANT
RP ALA-995.
RX PubMed=9837819; DOI=10.1086/302163;
RA Forbes J.R., Cox D.W.;
RT "Functional characterization of missense mutations in ATP7B: Wilson disease
RT mutation or normal variant?";
RL Am. J. Hum. Genet. 63:1663-1674(1998).
RN [21]
RP POSSIBLE PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=9600907; DOI=10.1073/pnas.95.11.6004;
RA Lutsenko S., Cooper M.J.;
RT "Localization of the Wilson's disease protein product to mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6004-6009(1998).
RN [22]
RP INTERACTION WITH COMMD1.
RX PubMed=12968035; DOI=10.1074/jbc.c300391200;
RA Tao T.Y., Liu F., Klomp L., Wijmenga C., Gitlin J.D.;
RT "The copper toxicosis gene product Murr1 directly interacts with the Wilson
RT disease protein.";
RL J. Biol. Chem. 278:41593-41596(2003).
RN [23]
RP INTERACTION WITH DCTN4.
RX PubMed=16554302; DOI=10.1074/jbc.m512745200;
RA Lim C.M., Cater M.A., Mercer J.F., La Fontaine S.;
RT "Copper-dependent interaction of dynactin subunit p62 with the N terminus
RT of ATP7B but not ATP7A.";
RL J. Biol. Chem. 281:14006-14014(2006).
RN [24]
RP COPPER-BINDING SITES, AND DOMAINS HMA.
RX PubMed=20032459; DOI=10.1074/jbc.m109.074633;
RA LeShane E.S., Shinde U., Walker J.M., Barry A.N., Blackburn N.J., Ralle M.,
RA Lutsenko S.;
RT "Interactions between copper-binding sites determine the redox status and
RT conformation of the regulatory N-terminal domain of ATP7B.";
RL J. Biol. Chem. 285:6327-6336(2010).
RN [25]
RP VARIANTS VAL-390; ALA-406; LEU-456; GLY-723; ARG-832; ARG-875; VAL-929;
RP LYS-952 AND ALA-1140, AND VARIANTS WD VAL-769; GLN-778; LEU-778; VAL-874;
RP GLY-919; MET-935; ASP-943; PRO-1041; ILE-1106; HIS-1142; LYS-1173 AND
RP SER-1270.
RX PubMed=11405812; DOI=10.1001/archneur.58.6.971;
RA Wu Z.Y., Wang N., Lin M.T., Fang L., Murong S.X., Yu L.;
RT "Mutation analysis and the correlation between genotype and phenotype of
RT Arg778Leu mutation in chinese patients with Wilson disease.";
RL Arch. Neurol. 58:971-976(2001).
RN [26]
RP VARIANTS WD LEU-778; MET-935; LEU-992; ARG-1268 AND SER-1270.
RX PubMed=16649058; DOI=10.1007/s00109-005-0036-y;
RA Wu Z.Y., Zhao G.X., Chen W.J., Wang N., Wan B., Lin M.T., Murong S.X.,
RA Yu L.;
RT "Mutation analysis of 218 Chinese patients with Wilson disease revealed no
RT correlation between the canine copper toxicosis gene MURR1 and Wilson
RT disease.";
RL J. Mol. Med. 84:438-442(2006).
RN [27]
RP VARIANTS LEU-149; LEU-456; LEU-825; ALA-1140 AND ARG-1207, AND VARIANTS WD
RP SER-591; ALA-1031 AND ALA-1178.
RX PubMed=17823867; DOI=10.1007/s10571-007-9192-7;
RA Gupta A., Chattopadhyay I., Dey S., Nasipuri P., Das S.K.,
RA Gangopadhyay P.K., Ray K.;
RT "Molecular pathogenesis of Wilson disease among Indians: a perspective on
RT mutation spectrum in ATP7B gene, prevalent defects, clinical heterogeneity
RT and implication towards diagnosis.";
RL Cell. Mol. Neurobiol. 27:1023-1033(2007).
RN [28]
RP VARIANTS WD ARG-645; VAL-769; GLN-778; TRP-778; PRO-827; ALA-858; VAL-874;
RP PHE-899; TRP-919; MET-935; TRP-969; MET-977; VAL-982; MET-991; ARG-1012;
RP VAL-1012; VAL-1018; LYS-1064; SER-1099; CYS-1151; MET-1220; MET-1288;
RP PRO-1322; LYS-1332; ASP-1341 AND LEU-1369.
RX PubMed=17949296; DOI=10.1089/gte.2007.0015;
RA Lepori M.B., Lovicu M., Dessi V., Zappu A., Incollu S., Zancan L.,
RA Giacchino R., Iorio R., Vajro P., Maggiore G., Marcellini M., Barbera C.,
RA Pellecchia M.T., Simonetti R., Kostic V., Farci A.M., Solinas A.,
RA De Virgiliis S., Cao A., Loudianos G.;
RT "Twenty-four novel mutations in Wilson disease patients of predominantly
RT Italian origin.";
RL Genet. Test. 11:328-332(2007).
RN [29]
RP CHARACTERIZATION OF VARIANT WD SER-41, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ALA-32; PHE-37; PHE-39; ASP-40; ASN-41; VAL-42; GLY-43;
RP TYR-44 AND GLU-45.
RX PubMed=19033537; DOI=10.1152/ajpgi.90489.2008;
RA Braiterman L., Nyasae L., Guo Y., Bustos R., Lutsenko S., Hubbard A.;
RT "Apical targeting and Golgi retention signals reside within a 9-amino acid
RT sequence in the copper-ATPase, ATP7B.";
RL Am. J. Physiol. 296:G433-G444(2009).
RN [30]
RP CHARACTERIZATION OF VARIANTS WD ARG-1373; PRO-1373; SER-1375; SER-1379 AND
RP MET-1434.
RX PubMed=21454443; DOI=10.1152/ajpgi.00038.2011;
RA Braiterman L., Nyasae L., Leves F., Hubbard A.L.;
RT "Critical roles for the COOH terminus of the Cu-ATPase ATP7B in protein
RT stability, trans-Golgi network retention, copper sensing, and retrograde
RT trafficking.";
RL Am. J. Physiol. 301:G69-G81(2011).
RN [31]
RP CHARACTERIZATION OF VARIANTS WD ALA-1064 AND GLN-1069.
RX PubMed=21398519; DOI=10.1074/jbc.m110.198101;
RA Dmitriev O.Y., Bhattacharjee A., Nokhrin S., Uhlemann E.M., Lutsenko S.;
RT "Difference in stability of the N-domain underlies distinct intracellular
RT properties of the E1064A and H1069Q mutants of copper-transporting ATPase
RT ATP7B.";
RL J. Biol. Chem. 286:16355-16362(2011).
RN [32]
RP VARIANTS WD ARG-108; VAL-729; GLN-778; LEU-778; TRP-827; VAL-874; ASP-891;
RP 899-ILE--GLN-907 DEL; GLY-919; ASP-943; SER-943; GLN-969; MET-977; LEU-992;
RP THR-1010; ALA-1024; ILE-1029; ALA-1031; VAL-1035; PHE-1083; TYR-1091;
RP ILE-1106; THR-1148; CYS-1151; SER-1168; SER-1186; MET-1216; ALA-1267;
RP SER-1270; LEU-1273 AND ASP-1295, AND CHARACTERIZATION OF VARIANTS WD
RP TRP-827; THR-1010; CYS-1151 AND ASP-1295.
RX PubMed=21645214; DOI=10.1111/j.1478-3231.2011.02503.x;
RA Lee B.H., Kim J.H., Lee S.Y., Jin H.Y., Kim K.J., Lee J.J., Park J.Y.,
RA Kim G.H., Choi J.H., Kim K.M., Yoo H.W.;
RT "Distinct clinical courses according to presenting phenotypes and their
RT correlations to ATP7B mutations in a large Wilson's disease cohort.";
RL Liver Int. 31:831-839(2011).
RN [33]
RP CHARACTERIZATION OF VARIANT ARG-875.
RX PubMed=21406592; DOI=10.1073/pnas.1014959108;
RA Gupta A., Bhattacharjee A., Dmitriev O.Y., Nokhrin S., Braiterman L.,
RA Hubbard A.L., Lutsenko S.;
RT "Cellular copper levels determine the phenotype of the Arg875 variant of
RT ATP7B/Wilson disease protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5390-5395(2011).
RN [34]
RP CHARACTERIZATION OF VARIANTS WD VAL-85; SER-492; TRP-616; ALA-626; ARG-645;
RP SER-710; LEU-760; ASN-765; VAL-769; LEU-840; THR-857; VAL-874; GLN-969;
RP LEU-992; LEU-1052; LYS-1064; GLN-1069; PHE-1083; VAL-1213; VAL-1222;
RP ARG-1266; SER-1270 AND LEU-1273, CHARACTERIZATION OF VARIANTS ALA-406;
RP LEU-456 AND ARG-832, MUTAGENESIS OF ASP-1027 AND THR-1031, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22240481; DOI=10.1053/j.gastro.2011.12.048;
RA Huster D., Kuehne A., Bhattacharjee A., Raines L., Jantsch V., Noe J.,
RA Schirrmeister W., Sommerer I., Sabri O., Berr F., Moessner J., Stieger B.,
RA Caca K., Lutsenko S.;
RT "Diverse functional properties of Wilson disease ATP7B variants.";
RL Gastroenterology 142:947-956(2012).
RN [35]
RP VARIANTS WD LEU-539; SER-710; GLY-779; SER-816; GLN-1069 AND MET-1220.
RX PubMed=22763723; DOI=10.1038/jhg.2012.65;
RA Hofer H., Willheim-Polli C., Knoflach P., Gabriel C., Vogel W., Trauner M.,
RA Mueller T., Ferenci P.;
RT "Identification of a novel Wilson disease gene mutation frequent in Upper
RT Austria: a genetic and clinical study.";
RL J. Hum. Genet. 57:564-567(2012).
RN [36]
RP VARIANT WD 899-ILE--GLN-907 DEL.
RX PubMed=22075048; DOI=10.1016/j.jns.2011.09.007;
RA Lee J.Y., Kim Y.H., Kim T.W., Oh S.Y., Kim D.S., Shin B.S.;
RT "New novel mutation of the ATP7B gene in a family with Wilson disease.";
RL J. Neurol. Sci. 313:129-131(2012).
RN [37]
RP VARIANTS WD VAL-170; HIS-765; GLU-836; CYS-939; ASP-1281 AND LYS-1293.
RX PubMed=22484412; DOI=10.1016/j.mcp.2012.03.007;
RA Lepori M.B., Zappu A., Incollu S., Dessi V., Mameli E., Demelia L.,
RA Nurchi A.M., Gheorghe L., Maggiore G., Sciveres M., Leuzzi V., Indolfi G.,
RA Bonafe L., Casali C., Angeli P., Barone P., Cao A., Loudianos G.;
RT "Mutation analysis of the ATP7B gene in a new group of Wilson's disease
RT patients: contribution to diagnosis.";
RL Mol. Cell. Probes 26:147-150(2012).
RN [38]
RP VARIANTS WD TRP-136; TRP-148; CYS-382; ALA-536; LYS-541; ILE-597; CYS-614;
RP SER-641; ARG-645; ILE-665; ALA-731; PRO-745; VAL-769; TRP-778; ARG-869;
RP TRP-919; VAL-936; MET-977; MET-991; ALA-995; ILE-1017; VAL-1021; TRP-1041;
RP VAL-1058; GLN-1069; SER-1070; VAL-1074; GLY-1250; ARG-1266; SER-1270;
RP ILE-1298; LEU-1298; TYR-1431 AND PHE-1432.
RX PubMed=23518715; DOI=10.1093/brain/awt035;
RA Coffey A.J., Durkie M., Hague S., McLay K., Emmerson J., Lo C., Klaffke S.,
RA Joyce C.J., Dhawan A., Hadzic N., Mieli-Vergani G., Kirk R.,
RA Elizabeth Allen K., Nicholl D., Wong S., Griffiths W., Smithson S.,
RA Giffin N., Taha A., Connolly S., Gillett G.T., Tanner S., Bonham J.,
RA Sharrack B., Palotie A., Rattray M., Dalton A., Bandmann O.;
RT "A genetic study of Wilson's disease in the United Kingdom.";
RL Brain 136:1476-1487(2013).
RN [39]
RP VARIANT WD GLY-779.
RX PubMed=23159873; DOI=10.1016/j.gene.2012.10.085;
RA Dastsooz H., Dehghani S.M., Imanieh M.H., Haghighat M., Moini M.,
RA Fardaei M.;
RT "A new ATP7B gene mutation with severe condition in two unrelated Iranian
RT families with Wilson disease.";
RL Gene 514:48-53(2013).
RN [40]
RP VARIANTS WD ASN-44; PHE-157; GLY-606; HIS-732; PRO-732; GLY-756; GLN-778;
RP LEU-778; PHE-795; PRO-874; VAL-874; MET-890; GLY-919; ARG-921; ASP-943;
RP TYR-975; TYR-980; PRO-987; LEU-992; CYS-1151; ALA-1178; GLU-1266; SER-1270
RP AND LEU-1273, AND VARIANT VAL-929.
RX PubMed=23235335; DOI=10.1038/jhg.2012.134;
RA Li K., Zhang W.M., Lin S., Wen L., Wang Z.F., Xie D., Wei M., Qiu Z.Q.,
RA Dai Y., Lin M.C., Kung H.F., Yao F.X.;
RT "Mutational analysis of ATP7B in north Chinese patients with Wilson
RT disease.";
RL J. Hum. Genet. 58:67-72(2013).
RN [41]
RP VARIANT WD GLY-1202.
RX PubMed=23275100; DOI=10.1007/s12519-012-0388-7;
RA Geng J., Wang J., Yao R.E., Liu X.Q., Fu Q.H.;
RT "Identification of one novel and nine recurrent mutations of the ATP7B gene
RT in 11 children with Wilson disease.";
RL World J. Pediatr. 9:158-162(2013).
RN [42]
RP VARIANT WD SER-1347.
RX PubMed=24555712; DOI=10.1186/1471-2350-15-22;
RA Forbes N., Goodwin S., Woodward K., Morgan D.G., Brady L., Coulthart M.B.,
RA Tarnopolsky M.A.;
RT "Evidence for synergistic effects of PRNP and ATP7B mutations in severe
RT neuropsychiatric deterioration.";
RL BMC Med. Genet. 15:22-22(2014).
RN [43]
RP CHARACTERIZATION OF VARIANTS WD ALA-626; TYR-639; SER-641; HIS-642; ARG-645
RP AND TYR-653, MUTAGENESIS OF SER-653, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24706876; DOI=10.1073/pnas.1314161111;
RA Braiterman L.T., Murthy A., Jayakanthan S., Nyasae L., Tzeng E.,
RA Gromadzka G., Woolf T.B., Lutsenko S., Hubbard A.L.;
RT "Distinct phenotype of a Wilson disease mutation reveals a novel
RT trafficking determinant in the copper transporter ATP7B.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E1364-E1373(2014).
RN [44]
RP STRUCTURE BY NMR OF 238-439, COPPER-BINDING SITES, AND INTERACTION WITH
RP ATOX1.
RX PubMed=18558714; DOI=10.1021/bi8004736;
RA Banci L., Bertini I., Cantini F., Rosenzweig A.C., Yatsunyk L.A.;
RT "Metal binding domains 3 and 4 of the Wilson disease protein: solution
RT structure and interaction with the copper(I) chaperone HAH1.";
RL Biochemistry 47:7423-7429(2008).
RN [45]
RP VARIANTS WD ALA-626; ASN-765; GLY-778; THR-857; GLN-969; LYS-1064 AND
RP SER-1270.
RX PubMed=8533760;
RA Figus A., Angius A., Loudianos G., Bertini C., Dessi V., Loi A., Deiana M.,
RA Lovicu M., Olla N., Sole G., de Virgiliis S., Lilliu F., Farci A.M.G.,
RA Nurchi A., Giacchino R., Barabino A., Marazzi M., Zancan L., Greggio N.A.,
RA Macellini M., Solinas A., Deplano A., Barbera C., Devoto M., Ozsoylu S.,
RA Kocak N., Akar N., Karayalcin S., Mokini V., Cullufi P., Balestrieri A.,
RA Cao A., Pirastu M.;
RT "Molecular pathology and haplotype analysis of Wilson disease in
RT Mediterranean populations.";
RL Am. J. Hum. Genet. 57:1318-1324(1995).
RN [46]
RP VARIANTS WD PHE-967; MET-977; ASP-1106; ARG-1153 AND SER-1355.
RX PubMed=8938442; DOI=10.1006/geno.1996.0564;
RA Waldenstroem E., Lagerkvist A., Dahlman T., Westermark K., Landegren U.;
RT "Efficient detection of mutations in Wilson disease by manifold
RT sequencing.";
RL Genomics 37:303-309(1996).
RN [47]
RP VARIANTS WD.
RX PubMed=8931691; DOI=10.1007/s004390050275;
RA Loudianos G., Dessi V., Angius A., Lovicu M., Loi A., Deiana M., Akar N.,
RA Vajro P., Figus A., Cao A., Pirastu M.;
RT "Wilson disease mutations associated with uncommon haplotypes in
RT Mediterranean patients.";
RL Hum. Genet. 98:640-642(1996).
RN [48]
RP VARIANTS WD GLN-778 AND LEU-778.
RX PubMed=8782057; DOI=10.1136/jmg.33.6.521;
RA Chuang L.-M., Wu H.-P., Jang M.-H., Wang T.-R., Sue W.-C., Lin B.J.,
RA Cox D.W., Tai T.-Y.;
RT "High frequency of two mutations in codon 778 in exon 8 of the ATP7B gene
RT in Taiwanese families with Wilson disease.";
RL J. Med. Genet. 33:521-523(1996).
RN [49]
RP VARIANTS WD.
RX PubMed=9311736; DOI=10.1086/514864;
RA Shah A.B., Chernov I., Zhang H.T., Ross B.M., Das K., Lutsenko S.,
RA Parano E., Pavone L., Evgrafov O., Ivanova-Smolenskaya I.A., Anneren G.,
RA Westermark K., Urrutia F.H., Penchaszadeh G.K., Sternlieb I.,
RA Scheinberg I.H., Gilliam T.C., Petrukhin K.;
RT "Identification and analysis of mutations in the Wilson disease gene
RT (ATP7B): population frequencies, genotype-phenotype correlation, and
RT functional analyses.";
RL Am. J. Hum. Genet. 61:317-328(1997).
RN [50]
RP VARIANT WD CYS-693.
RX PubMed=9772425;
RA Fan Y., Yang R., Yu L., Wu M., Shi S., Ren M., Han Y., Hu J., Zhao S.;
RT "Identification of a novel missense mutation in Wilson's disease gene.";
RL Chin. Med. J. 110:887-890(1997).
RN [51]
RP VARIANTS WD VAL-1278 AND 1285-GLY--ILE-1292 DEL.
RX PubMed=9222767;
RX DOI=10.1002/(sici)1098-1004(1997)10:1<84::aid-humu14>3.0.co;2-w;
RA Orru S., Thomas G., Loizedda A., Cox D.W., Contu L.;
RT "24 bp deletion and Ala1278 to Val mutation of the ATP7B gene in a
RT Sardinian family with Wilson disease.";
RL Hum. Mutat. 10:84-85(1997).
RN [52]
RP VARIANT WD LYS-1038.
RX PubMed=8980283; DOI=10.1111/1523-1747.ep12285622;
RA Kemppainen R., Palatsi R., Kallioinen M., Oikarinen A.;
RT "A homozygous nonsense mutation and a combination of two mutations of the
RT Wilson disease gene in patients with different lysyl oxidase activities in
RT cultured fibroblasts.";
RL J. Invest. Dermatol. 108:35-39(1997).
RN [53]
RP VARIANTS WD ALA-710; CYS-741; ILE-1031; GLN-1069 AND ARG-1176, AND VARIANTS
RP LEU-456; GLY-949 AND ALA-1140.
RX PubMed=9887381; DOI=10.1038/sj.ejhg.5200237;
RA Ha-Hao D., Hefter H., Stremmel W., Castaneda-Guillot C.,
RA Hernandez Hernandez A., Cox D.W., Auburger G.;
RT "His1069Gln and six novel Wilson disease mutations: analysis of relevance
RT for early diagnosis and phenotype.";
RL Eur. J. Hum. Genet. 6:616-623(1998).
RN [54]
RP VARIANTS WD ARG-645; ASN-765; GLN-969; ALA-1064; GLN-1069; VAL-1213 AND
RP 1216-VAL-VAL-1217 DEL, AND VARIANTS SER-565; GLY-723; ARG-832 AND ALA-1140.
RX PubMed=9482578;
RX DOI=10.1002/(sici)1098-1004(1998)11:2<145::aid-humu7>3.0.co;2-i;
RA Kalinsky H., Funes A., Zeldin A., Pel-Or Y., Korostishevsky M.,
RA Gershoni-Baruch R., Farrer L.A., Bonne-Tamir B.;
RT "Novel ATP7B mutations causing Wilson disease in several Israeli ethnic
RT groups.";
RL Hum. Mutat. 11:145-151(1998).
RN [55]
RP VARIANTS WD LEU-778; VAL-874 AND PHE-1083, AND VARIANTS ARG-832; ILE-864;
RP MET-1109 AND ALA-1140.
RX PubMed=9554743;
RX DOI=10.1002/(sici)1098-1004(1998)11:4<275::aid-humu4>3.0.co;2-l;
RA Kim E.K., Yoo O.J., Song K.Y., Yoo H.W., Choi S.Y., Cho S.W., Hahn S.H.;
RT "Identification of three novel mutations and a high frequency of the
RT Arg778Leu mutation in Korean patients with Wilson disease.";
RL Hum. Mutat. 11:275-278(1998).
RN [56]
RP VARIANTS WD LEU-778; VAL-874; GLY-919; SER-1186; ALA-1267 AND SER-1270.
RX PubMed=9452121; DOI=10.1002/humu.13801101100;
RA Yamaguchi A., Matsuura A., Arashima S., Kikuchi Y., Kikuchi K.;
RT "Mutations of ATP7B gene in Wilson disease in Japan: identification of nine
RT mutations and lack of clear founder effect in a Japanese population.";
RL Hum. Mutat. Suppl. 1:S320-S322(1998).
RN [57]
RP VARIANTS WD VAL-85; SER-492; 608-PHE-ASP-609 DELINS TYR; HIS-642; ARG-645;
RP ILE-665; ARG-691; PHE-747; TRP-778; LEU-840; ASN-918; TRP-919; ASN-921;
RP PRO-933; LEU-992; THR-1003; VAL-1018; TRP-1041; VAL-1089; MET-1146;
RP GLY-1183; THR-1183; MET-1216; ASP-1341 AND SER-1358.
RX PubMed=9671269;
RX DOI=10.1002/(sici)1098-1004(1998)12:2<89::aid-humu3>3.0.co;2-g;
RA Loudianos G., Dessi V., Lovicu M., Angius A., Nurchi A., Sturniolo G.C.,
RA Marcellini M., Zancan L., Bragetti P., Akar N., Yagci R., Vegnente A.,
RA Cao A., Pirastu M.;
RT "Further delineation of the molecular pathology of Wilson disease in the
RT Mediterranean population.";
RL Hum. Mutat. 12:89-94(1998).
RN [58]
RP VARIANTS WD.
RX PubMed=9829905;
RX DOI=10.1002/(sici)1098-1004(1998)12:6<370::aid-humu2>3.0.co;2-s;
RA Tsai C.-H., Tsai F.-J., Wu J.-Y., Chang J.-G., Lee C.-C., Lin S.-P.,
RA Yang C.-F., Jong Y.-J., Lo M.-C.;
RT "Mutation analysis of Wilson disease in Taiwan and description of six new
RT mutations.";
RL Hum. Mutat. 12:370-376(1998).
RN [59]
RP VARIANT WD PRO-1041.
RX PubMed=10194254;
RA Wu Z., Wang N., Murong S., Lin M.;
RT "Missense mutations of exons 14 and 18 of Wilson's disease gene in Chinese
RT patients.";
RL Zhonghua Yi Xue Yi Chuan Xue Za Zhi 16:91-93(1999).
RN [60]
RP VARIANTS WD 670-TYR-MET-671 DEL; TYR-985 AND THR-1148.
RX PubMed=10447265;
RX DOI=10.1002/(sici)1098-1004(1999)14:1<88::aid-humu15>3.0.co;2-h;
RA Haas R., Gutierrez-Rivero B., Knoche J., Boeker K., Manns M.P.,
RA Schmidt H.H.-J.;
RT "Mutation analysis in patients with Wilson disease: identification of 4
RT novel mutations.";
RL Hum. Mutat. 14:88-88(1999).
RN [61]
RP VARIANTS WD.
RX PubMed=10502776;
RX DOI=10.1002/(sici)1098-1004(199910)14:4<294::aid-humu4>3.0.co;2-9;
RA Loudianos G., Dessi V., Lovicu M., Angius A., Figus A., Lilliu F.,
RA De Virgiliis S., Nurchi A.M., Deplano A., Moi P., Pirastu M., Cao A.;
RT "Molecular characterization of Wilson disease in the Sardinian population
RT -- evidence of a founder effect.";
RL Hum. Mutat. 14:294-303(1999).
RN [62]
RP VARIANTS WD.
RX PubMed=10502777;
RX DOI=10.1002/(sici)1098-1004(199910)14:4<304::aid-humu5>3.0.co;2-w;
RA Curtis D., Durkie M., Balac P., Sheard D., Goodeve A., Peake I.,
RA Quarrell O., Tanner S.;
RT "A study of Wilson disease mutations in Britain.";
RL Hum. Mutat. 14:304-311(1999).
RN [63]
RP VARIANT WD GLN-1069.
RX PubMed=10051024;
RA Ivanova-Smolenskaya I.A., Ovchinnikov I.V., Karabanov A.V., Deineko N.L.,
RA Poleshchuk V.V., Markova E.D., Illarioshkin S.N.;
RT "The His1069Gln mutation in the ATP7B gene in Russian patients with Wilson
RT disease.";
RL J. Med. Genet. 36:174-174(1999).
RN [64]
RP VARIANTS WD SER-710; ARG-711; LEU-840; VAL-874; GLN-969; VAL-1003;
RP TRP-1041; PRO-1041; GLU-1061; VAL-1063; GLY-1068; GLN-1069; GLU-1089;
RP PHE-1104; HIS-1151; THR-1169; LYS-1173; VAL-1222; PHE-1262; VAL-1327;
RP PHE-1363 AND MET-1434, AND VARIANTS ARG-1207 AND ILE-1297.
RX PubMed=10544227;
RA Loudianos G., Dessi V., Lovicu M., Angius A., Altuntas B., Giacchino R.,
RA Marazzi M., Marcellini M., Sartorelli M.R., Sturniolo G.C., Kocak N.,
RA Yuce A., Akar N., Pirastu M., Cao A.;
RT "Mutation analysis in patients of Mediterranean descent with Wilson
RT disease: identification of 19 novel mutations.";
RL J. Med. Genet. 36:833-836(1999).
RN [65]
RP VARIANTS WD LEU-778; VAL-874; GLY-919; ILE-1029; VAL-1035; SER-1186 AND
RP ASN-1222.
RX PubMed=10453196; DOI=10.1046/j.1442-200x.1999.01092.x;
RA Shimizu N., Nakazono H., Takeshita Y., Ikeda C., Fujii H., Watanabe A.,
RA Yamaguchi Y., Hemmi H., Shimatake H., Aoki T.;
RT "Molecular analysis and diagnosis in Japanese patients with Wilson's
RT disease.";
RL Pediatr. Int. 41:409-413(1999).
RN [66]
RP VARIANTS WD SER-486; GLY-778; MET-890; GLN-969; GLU-1061; GLN-1069;
RP SER-1099 AND THR-1148.
RX PubMed=11216666; DOI=10.1089/109065700750065162;
RA Loudianos G., Lovicu M., Solinas P., Kanavakis E., Tzetis M., Manolaki N.,
RA Panagiotakaki E., Karpathios T., Cao A.;
RT "Delineation of the spectrum of Wilson disease mutations in the Greek
RT population and the identification of six novel mutations.";
RL Genet. Test. 4:399-402(2000).
RN [67]
RP VARIANT WD PRO-708.
RX PubMed=11093740; DOI=10.1053/jhep.2000.20152;
RA Garcia-Villarreal L., Daniels S., Shaw S.H., Cotton D., Galvin M.,
RA Geskes J., Bauer P., Sierra-Hernandez A., Buckler A., Tugores A.;
RT "High prevalence of the very rare Wilson disease gene mutation Leu708Pro in
RT the Island of Gran Canaria (Canary Islands, Spain): a genetic and clinical
RT study.";
RL Hepatology 32:1329-1336(2000).
RN [68]
RP VARIANTS WD ILE-769; LEU-778; TRP-778; VAL-874; GLY-919; THR-1003;
RP PHE-1083; SER-1186; ALA-1267; SER-1270; THR-1336 AND PRO-1373, AND VARIANTS
RP ALA-406; LEU-456 AND ALA-1140.
RX PubMed=10790207;
RX DOI=10.1002/(sici)1098-1004(200005)15:5<454::aid-humu7>3.0.co;2-j;
RA Okada T., Shiono Y., Hayashi H., Satoh H., Sawada T., Suzuki A., Takeda Y.,
RA Yano M., Michitaka K., Onji M., Mabuchi H.;
RT "Mutational analysis of ATP7B and genotype-phenotype correlation in
RT Japanese with Wilson's disease.";
RL Hum. Mutat. 15:454-462(2000).
RN [69]
RP VARIANTS WD LEU-778; VAL-874 AND VAL-1297 DEL, AND VARIANTS LEU-290;
RP ALA-406; LEU-456; ARG-832; ALA-1140 AND GLU-1407.
RX PubMed=10721669; DOI=10.1007/s100380050017;
RA Kusuda Y., Hamaguchi K., Mori T., Shin R., Seike M., Sakata T.;
RT "Novel mutations of the ATP7B gene in Japanese patients with Wilson
RT disease.";
RL J. Hum. Genet. 45:86-91(2000).
RN [70]
RP VARIANT WD GLY-1279.
RX PubMed=11043508; DOI=10.1007/s100380070015;
RA Lee C.C., Wu J.Y., Tsai F.J., Kodama H., Abe T., Yang C.F., Tsai C.H.;
RT "Molecular analysis of Wilson disease in Taiwan: identification of one
RT novel mutation and evidence of haplotype-mutation association.";
RL J. Hum. Genet. 45:275-279(2000).
RN [71]
RP VARIANTS WD LEU-760 AND PRO-1305.
RX PubMed=11180609;
RX DOI=10.1002/1098-1004(200102)17:2<156::aid-humu18>3.0.co;2-0;
RA Genschel J., Czlonkowska A., Sommer G., Buettner C., Bochow B., Lochs H.,
RA Schmidt H.;
RT "Three novel mutations (P760L, L1305P, Q1351Stop) causing Wilson disease.";
RL Hum. Mutat. 17:156-156(2001).
RN [72]
RP VARIANTS WD TRP-616; ALA-710; SER-710; LEU-760; ASN-765; VAL-769; GLN-969;
RP LEU-992; GLN-1069 AND SER-1270, AND VARIANTS ALA-406; LEU-456 AND ARG-832.
RX PubMed=11690702; DOI=10.1016/s0168-8278(01)00219-7;
RA Caca K., Ferenci P., Kuehn H.-J., Polli C., Willgerodt H., Kunath B.,
RA Hermann W., Moessner J., Berr F.;
RT "High prevalence of the H1069Q mutation in East German patients with Wilson
RT disease: rapid detection of mutations by limited sequencing and phenotype-
RT genotype analysis.";
RL J. Hepatol. 35:575-581(2001).
RN [73]
RP VARIANTS WD TRP-778; ARG-898; GLN-1069; THR-1102 AND ARG-1266.
RX PubMed=11243728; DOI=10.1006/mgme.2000.3143;
RA Butler P., McIntyre N., Mistry P.K.;
RT "Molecular diagnosis of Wilson disease.";
RL Mol. Genet. Metab. 72:223-230(2001).
RN [74]
RP VARIANTS WD PHE-1083 AND ASN-1296.
RX PubMed=11954751; DOI=10.1007/s00431-001-0865-9;
RA Ohya K., Abo W., Tamaki H., Sugawara C., Endo T., Nomachi S., Fukushi M.,
RA Kinebuchi M., Matsuura A.;
RT "Presymptomatic diagnosis of Wilson disease associated with a novel
RT mutation of the ATP7B gene.";
RL Eur. J. Pediatr. 161:124-126(2002).
RN [75]
RP VARIANTS WD HIS-768; LEU-778; VAL-874; PHE-1083; SER-1168; ILE-1255;
RP ALA-1267 AND SER-1270.
RX PubMed=12544487; DOI=10.1097/00125817-200211001-00009;
RA Yoo H.-W.;
RT "Identification of novel mutations and the three most common mutations in
RT the human ATP7B gene of Korean patients with Wilson disease.";
RL Genet. Med. 4:43S-48S(2002).
RN [76]
RP VARIANTS WD PRO-721 AND GLY-1183.
RX PubMed=12325021; DOI=10.1002/humu.10121;
RA Loudianos G., Lovicu M., Dessi V., Tzetis M., Kanavakis E., Zancan L.,
RA Zelante L., Galvez-Galvez C., Cao A.;
RT "Abnormal mRNA splicing resulting from consensus sequence splicing
RT mutations of ATP7B.";
RL Hum. Mutat. 20:260-266(2002).
RN [77]
RP VARIANTS WD LEU-778; VAL-874 AND GLY-919.
RX PubMed=12376745; DOI=10.1007/s100380200082;
RA Takeshita Y., Shimizu N., Yamaguchi Y., Nakazono H., Saitou M.,
RA Fujikawa Y., Aoki T.;
RT "Two families with Wilson disease in which siblings showed different
RT phenotypes.";
RL J. Hum. Genet. 47:543-547(2002).
RN [78]
RP VARIANTS WD VAL-85; GLY-765; LEU-778; MET-890; GLY-919; MET-935; TYR-975;
RP LEU-992; ARG-1098; THR-1148; LYS-1173 AND ASN-1248, AND VARIANTS ASP-14;
RP ALA-406; LEU-456; ARG-832; ALA-1140; ASN-1143 AND SER-1245.
RX PubMed=14986826; DOI=10.1046/j.1399-0004.2003.00179.x;
RA Gu Y.-H., Kodama H., Du S.-L., Gu Q.-J., Sun H.-J., Ushijima H.;
RT "Mutation spectrum and polymorphisms in ATP7B identified on direct
RT sequencing of all exons in Chinese Han and Hui ethnic patients with
RT Wilson's disease.";
RL Clin. Genet. 64:479-484(2003).
RN [79]
RP VARIANT WD SER-1341.
RX PubMed=14639035; DOI=10.1159/000075092;
RA Majumdar R., Al Jumah M., Zaidan R.;
RT "A rare homozygous missense mutation in ATP7B exon 19 in a case of Wilson
RT disease.";
RL Eur. Neurol. 51:52-54(2004).
RN [80]
RP VARIANTS WD SER-41; GLY-949; LEU-1094; PRO-1232 AND ARG-1373.
RX PubMed=15024742; DOI=10.1002/humu.9227;
RA Deguti M.M., Genschel J., Cancado E.L.R., Barbosa E.R., Bochow B.,
RA Mucenic M., Porta G., Lochs H., Carrilho F.J., Schmidt H.H.-J.;
RT "Wilson disease: novel mutations in the ATP7B gene and clinical correlation
RT in Brazilian patients.";
RL Hum. Mutat. 23:398-398(2004).
RN [81]
RP VARIANT WD ARG-766.
RX PubMed=15557537; DOI=10.1212/01.wnl.0000144192.30426.38;
RA Pendlebury S.T., Rothwell P.M., Dalton A., Burton E.A.;
RT "Strokelike presentation of Wilson disease with homozygosity for a novel
RT T766R mutation.";
RL Neurology 63:1982-1983(2004).
RN [82]
RP VARIANTS WD LEU-778; ASP-943; ILE-1106 AND MET-1216, AND VARIANT ALA-1140.
RX PubMed=14966923; DOI=10.3748/wjg.v10.i4.590;
RA Liu X.-Q., Zhang Y.-F., Liu T.-T., Hsiao K.-J., Zhang J.-M., Gu X.-F.,
RA Bao K.-R., Yu L.-H., Wang M.-X.;
RT "Correlation of ATP7B genotype with phenotype in Chinese patients with
RT Wilson disease.";
RL World J. Gastroenterol. 10:590-593(2004).
RN [83]
RP VARIANTS WD THR-1148 AND ARG-1176.
RX PubMed=15845031; DOI=10.1046/j.1529-8817.2005.00171.x;
RA Dedoussis G.V.Z., Genschel J., Sialvera T.-E., Bochow B., Manolaki N.,
RA Manios Y., Tsafantakis E., Schmidt H.;
RT "Wilson disease: high prevalence in a mountainous area of Crete.";
RL Ann. Hum. Genet. 69:268-274(2005).
RN [84]
RP VARIANTS WD HIS-992; THR-1003; THR-1102; TYR-1104 AND ARG-1256.
RX PubMed=15811015; DOI=10.1111/j.1399-0004.2005.00440.x;
RA Kumar S., Thapa B.R., Kaur G., Prasad R.;
RT "Identification and molecular characterization of 18 novel mutations in the
RT ATP7B gene from Indian Wilson disease patients: genotype.";
RL Clin. Genet. 67:443-445(2005).
RN [85]
RP VARIANTS WD ARG-645; LEU-690; ARG-869; SER-943; MET-977; GLU-1061;
RP GLN-1069; SER-1099; MET-1216 AND PRO-1232, AND VARIANTS ALA-406; LEU-456;
RP ARG-832 AND ALA-1140.
RX PubMed=15952988; DOI=10.1111/j.1399-0004.2005.00439.x;
RA Margarit E., Bach V., Gomez D., Bruguera M., Jara P., Queralt R.,
RA Ballesta F.;
RT "Mutation analysis of Wilson disease in the Spanish population
RT -identification of a prevalent substitution and eight novel mutations in
RT the ATP7B gene.";
RL Clin. Genet. 68:61-68(2005).
RN [86]
RP VARIANTS WD GLN-616; ALA-626; TRP-778; GLY-778; VAL-874; GLN-969; THR-1003;
RP GLN-1069; 1217-VAL-LEU-1218 DEL; SER-1270; TYR-1279; ASP-1341; SER-1352 AND
RP PRO-1368.
RX PubMed=16207219; DOI=10.1111/j.1399-0004.2005.00516.x;
RA Todorov T., Savov A., Jelev H., Panteleeva E., Konstantinova D.,
RA Krustev Z., Mihaylova V., Tournev I., Tankova L., Tzolova N., Kremensky I.;
RT "Spectrum of mutations in the Wilson disease gene (ATP7B) in the Bulgarian
RT population.";
RL Clin. Genet. 68:474-476(2005).
RN [87]
RP VARIANTS WD GLN-616; TYR-639; TYR-653; PRO-776; GLY-778; MET-977; ARG-988;
RP LEU-992; GLN-1069; PRO-1095; MET-1220; LEU-1273 AND ASP-1341.
RX PubMed=16283883; DOI=10.1111/j.1399-0004.2005.00528.x;
RA Gromadzka G., Schmidt H.H.-J., Genschel J., Bochow B., Rodo M.,
RA Tarnacka B., Litwin T., Chabik G., Czlonkowska A.;
RT "Frameshift and nonsense mutations in the gene for ATPase7B are associated
RT with severe impairment of copper metabolism and with an early clinical
RT manifestation of Wilson's disease.";
RL Clin. Genet. 68:524-532(2005).
RN [88]
RP VARIANTS WD HIS-532; ASP-591; PRO-604; SER-641; TYR-703; VAL-710; GLY-756;
RP MET-766; THR-861; CYS-943; MET-991; THR-996; ARG-1000; GLU-1176; GLU-1221;
RP SER-1287; SER-1331; VAL-1341; SER-1375 AND SER-1379.
RX PubMed=16088907; DOI=10.1002/humu.9358;
RA Cox D.W., Prat L., Walshe J.M., Heathcote J., Gaffney D.;
RT "Twenty-four novel mutations in Wilson disease patients of predominantly
RT European ancestry.";
RL Hum. Mutat. 26:280-280(2005).
RN [89]
RP VARIANTS WD SER-641; SER-710; ARG-737; GLY-778; GLU-918; GLN-969; MET-977;
RP VAL-1018; SER-1033; TRP-1041; VAL-1063; LYS-1064; GLN-1069; THR-1102;
RP ASP-1111; THR-1148; ARG-1176; SER-1186; ASN-1271; LEU-1273; PRO-1305;
RP ASP-1341 AND CYS-1355, AND VARIANTS LEU-456; ARG-832 AND ALA-1140.
RX PubMed=15967699; DOI=10.1016/j.ymgme.2005.05.004;
RA Vrabelova S., Letocha O., Borsky M., Kozak L.;
RT "Mutation analysis of the ATP7B gene and genotype/phenotype correlation in
RT 227 patients with Wilson disease.";
RL Mol. Genet. Metab. 86:277-285(2005).
RN [90]
RP VARIANT WD ARG-691.
RX PubMed=17718866; DOI=10.1111/j.1399-0004.2007.00853.x;
RA Barada K., Nemer G., ElHajj I.I., Touma J., Cortas N., Boustany R.-M.,
RA Usta J.;
RT "Early and severe liver disease associated with homozygosity for an exon 7
RT mutation, G691R, in Wilson's disease.";
RL Clin. Genet. 72:264-267(2007).
RN [91]
RP VARIANTS WD ALA-536; ARG-657; VAL-971; MET-974; PRO-1004; ALA-1149;
RP ASN-1164; GLY-1173; THR-1228; VAL-1230; VAL-1267; THR-1328 AND ILE-1359,
RP AND VARIANTS ALA-406; LEU-456; ARG-832; LYS-952 AND ALA-1140.
RX PubMed=18373411; DOI=10.1089/gte.2007.0072;
RA Davies L.P., Macintyre G., Cox D.W.;
RT "New mutations in the Wilson disease gene, ATP7B: implications for
RT molecular testing.";
RL Genet. Test. 12:139-145(2008).
RN [92]
RP CHARACTERIZATION OF VARIANTS WD HIS-532; ALA-626; HIS-642; TRP-1041;
RP LYS-1064; PHE-1083; ASP-1106; VAL-1169; THR-1183 AND SER-1186,
RP CHARACTERIZATION OF VARIANT ALA-1140, AND FUNCTION.
RX PubMed=18203200; DOI=10.1002/humu.20674;
RA Hsi G., Cullen L.M., Macintyre G., Chen M.M., Glerum D.M., Cox D.W.;
RT "Sequence variation in the ATP-binding domain of the Wilson disease
RT transporter, ATP7B, affects copper transport in a yeast model system.";
RL Hum. Mutat. 29:491-501(2008).
RN [93]
RP VARIANTS WD MET-991; ARG-1000; PRO-1043; ARG-1101; THR-1102; THR-1148;
RP GLY-1173; GLU-1176; THR-1228; GLY-1239; VAL-1267 AND SER-1287, AND
RP CHARACTERIZATION OF VARIANTS WD MET-991; ARG-1000; PRO-1043; ARG-1101;
RP THR-1102; THR-1148; GLY-1173; GLU-1176; THR-1228; GLY-1239; VAL-1267 AND
RP SER-1287.
RX PubMed=20333758; DOI=10.1002/humu.21228;
RA Luoma L.M., Deeb T.M., Macintyre G., Cox D.W.;
RT "Functional analysis of mutations in the ATP loop of the Wilson disease
RT copper transporter, ATP7B.";
RL Hum. Mutat. 31:569-577(2010).
RN [94]
RP VARIANTS WD PRO-549; HIS-642; TYR-703; PRO-744; ASN-765; GLY-778; MET-977;
RP ASP-998; VAL-1063; GLN-1069; ARG-1207; LEU-1273; ASP-1332; ARG-1341 AND
RP ASP-1341.
RX PubMed=21682854; DOI=10.1186/1471-2431-11-56;
RA Abdel Ghaffar T.Y., Elsayed S.M., Elnaghy S., Shadeed A., Elsobky E.S.,
RA Schmidt H.;
RT "Phenotypic and genetic characterization of a cohort of pediatric Wilson
RT disease patients.";
RL BMC Pediatr. 11:56-56(2011).
RN [95]
RP VARIANTS WD SER-710; ASN-765; GLY-778; TRP-778; ILE-788; VAL-874; TRP-919;
RP SER-943; GLN-969; THR-1003; VAL-1003; ILE-1036; TRP-1041; GLN-1069;
RP CYS-1151; THR-1245 AND SER-1270, AND VARIANTS ALA-406; LEU-456; ARG-832;
RP LYS-952; ALA-1140; ARG-1207 AND LEU-1243.
RX PubMed=23333878; DOI=10.1016/j.ejmg.2013.01.003;
RA Simsek Papur O., Akman S.A., Cakmur R., Terzioglu O.;
RT "Mutation analysis of ATP7B gene in Turkish Wilson disease patients:
RT identification of five novel mutations.";
RL Eur. J. Med. Genet. 56:175-179(2013).
RN [96]
RP VARIANT ALA-1140.
RX PubMed=24303094; DOI=10.4254/wjh.v5.i11.649;
RA Nussinson E., Shahbari A., Shibli F., Chervinsky E., Trougouboff P.,
RA Markel A.;
RT "Diagnostic challenges of Wilson's disease presenting as acute
RT pancreatitis, cholangitis, and jaundice.";
RL World J. Hepatol. 5:649-653(2013).
RN [97]
RP VARIANTS WD MET-935 AND THR-982.
RX PubMed=24476933; DOI=10.1016/j.gene.2013.10.044;
RA Chen L., Li X., Zheng Z., Lu X., Lin M., Pan C., Liu J.;
RT "A novel ATP7B gene mutation in a liver failure patient with normal
RT ceruloplasmin and low serum alkaline phosphatase.";
RL Gene 538:204-206(2014).
RN [98]
RP VARIANT WD ARG-645.
RX PubMed=23962630; DOI=10.1016/j.jocn.2013.02.030;
RA Arruda W.O., Munhoz R.P., de Bem R.S., Deguti M.M., Barbosa E.R.,
RA Zavala J.A., Teive H.A.;
RT "Pathogenic compound heterozygous ATP7B mutations with
RT hypoceruloplasminaemia without clinical features of Wilson's disease.";
RL J. Clin. Neurosci. 21:335-336(2014).
RN [99]
RP VARIANTS WD LEU-778; GLY-919; LEU-992; LYS-1136 AND GLU-1149, AND VARIANT
RP LEU-456.
RX PubMed=25704634; DOI=10.1016/j.arcmed.2015.02.001;
RA Liu Y., Zhou H., Guo H., Bai Y.;
RT "Genetic and clinical analysis in a cohort of patients with Wilson's
RT disease in southwestern China.";
RL Arch. Med. Res. 46:164-169(2015).
RN [100]
RP VARIANTS WD PRO-990; VAL-1003; ARG-1010; TRP-1041; PRO-1043; GLU-1061;
RP ARG-1101; SER-1104; MET-1113; SER-1270 AND LYS-1293.
RX PubMed=25982861; DOI=10.1016/j.gene.2015.05.031;
RA Guggilla S.R., Senagari J.R., Rao P.N., Madireddi S.;
RT "Spectrum of mutations in the ATP binding domain of ATP7B gene of Wilson
RT Disease in a regional Indian cohort.";
RL Gene 569:83-87(2015).
RN [101]
RP VARIANTS WD ILE-788 AND ILE-1036, CHARACTERIZATION OF VARIANTS WD ILE-788
RP AND ILE-1036, AND FUNCTION.
RX PubMed=26004889; DOI=10.1016/j.jtemb.2015.02.006;
RA Papur O.S., Terzioglu O., Koc A.;
RT "Functional characterization of new mutations in Wilson disease gene
RT (ATP7B) using the yeast model.";
RL J. Trace Elem. Med. Biol. 31:33-36(2015).
RN [102]
RP POSSIBLE RIBOSOMAL FRAMESHIFT TO TRANSLATE ISOFORM COPZ(A).
RX PubMed=28107647; DOI=10.1016/j.molcel.2016.12.008;
RA Meydan S., Klepacki D., Karthikeyan S., Margus T., Thomas P., Jones J.E.,
RA Khan Y., Briggs J., Dinman J.D., Vazquez-Laslop N., Mankin A.S.;
RT "Programmed ribosomal frameshifting generates a copper transporter and a
RT copper chaperone from the same gene.";
RL Mol. Cell 65:207-219(2017).
RN [103]
RP VARIANTS WD VAL-874; LEU-992; GLU-1010 AND 1331-TYR--ILE-1465 DEL.
RX PubMed=28856630; DOI=10.1007/s12519-017-0055-0;
RA Zhu H.W., Tao Z.B., Su G., Jin Q.Y., Zhao L.T., Zhu J.R., Yan J., Yu T.Y.,
RA Ding J.X., Li Y.M.;
RT "Identification of two novel mutations in the ATP7B gene that cause
RT Wilson's disease.";
RL World J. Pediatr. 13:387-391(2017).
RN [104]
RP CHARACTERIZATION OF VARIANT WD ARG-645.
RX PubMed=32284880; DOI=10.1038/s41525-020-0123-6;
RA Merico D., Spickett C., O'Hara M., Kakaradov B., Deshwar A.G., Fradkin P.,
RA Gandhi S., Gao J., Grant S., Kron K., Schmitges F.W., Shalev Z., Sun M.,
RA Verby M., Cahill M., Dowling J.J., Fransson J., Wienholds E., Frey B.J.;
RT "ATP7B variant c.1934T > G p.Met645Arg causes Wilson disease by promoting
RT exon 6 skipping.";
RL NPJ Genom. Med. 5:16-16(2020).
CC -!- FUNCTION: Copper ion transmembrane transporter involved in the export
CC of copper out of the cells. It is involved in copper homeostasis in the
CC liver, where it ensures the efflux of copper from hepatocytes into the
CC bile in response to copper overload. {ECO:0000269|PubMed:18203200,
CC ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:24706876,
CC ECO:0000269|PubMed:26004889}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000269|PubMed:22240481};
CC -!- SUBUNIT: Monomer. Interacts with COMMD1/MURR1 (PubMed:12968035,
CC PubMed:17919502). Interacts with DCTN4, in a copper-dependent manner
CC (PubMed:16554302). Interacts with ATOX1 (PubMed:18558714,
CC PubMed:17919502). Interacts (via C-terminus) with ZBTB16/PLZF
CC (PubMed:16676348). {ECO:0000269|PubMed:12968035,
CC ECO:0000269|PubMed:16554302, ECO:0000269|PubMed:16676348,
CC ECO:0000269|PubMed:17919502, ECO:0000269|PubMed:18558714}.
CC -!- INTERACTION:
CC P35670; O00244: ATOX1; NbExp=3; IntAct=EBI-11668501, EBI-10179267;
CC P35670; Q8N668: COMMD1; NbExp=10; IntAct=EBI-11668501, EBI-1550112;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:17919502, ECO:0000269|PubMed:19033537,
CC ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:24706876}; Multi-pass
CC membrane protein {ECO:0000255}. Late endosome
CC {ECO:0000269|PubMed:11231950, ECO:0000269|PubMed:15681833}.
CC Note=Predominantly found in the trans-Golgi network (TGN). Localized in
CC the trans-Golgi network under low copper conditions, redistributes to
CC cytoplasmic vesicles when cells are exposed to elevated copper levels,
CC and then recycles back to the trans-Golgi network when copper is
CC removed (PubMed:10942420). {ECO:0000269|PubMed:10942420,
CC ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:24706876,
CC ECO:0000269|PubMed:9307043}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane
CC {ECO:0000269|PubMed:9307043}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9307043}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:9307043}.
CC -!- SUBCELLULAR LOCATION: [WND/140 kDa]: Mitochondrion
CC {ECO:0000269|PubMed:9600907}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Ribosomal frameshifting; Named isoforms=5;
CC Name=1; Synonyms=A;
CC IsoId=P35670-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=P35670-2; Sequence=VSP_000426, VSP_000427;
CC Name=3;
CC IsoId=P35670-3; Sequence=VSP_016559;
CC Name=4;
CC IsoId=P35670-4; Sequence=VSP_016560;
CC Name=5;
CC IsoId=P35670-5; Sequence=VSP_059175;
CC -!- TISSUE SPECIFICITY: Most abundant in liver and kidney and also found in
CC brain. Isoform 2 is expressed in brain but not in liver. The cleaved
CC form WND/140 kDa is found in liver cell lines and other tissues.
CC -!- DOMAIN: Each HMA domain can bind a copper ion, they are tightly packed
CC and closely interact with each other. Wild-type ATP7B can usually be
CC loaded with an average 5.5 copper atoms per molecule.
CC {ECO:0000269|PubMed:20032459}.
CC -!- PTM: Isoform 1 may be proteolytically cleaved at the N-terminus to
CC produce the WND/140 kDa form.
CC -!- DISEASE: Wilson disease (WD) [MIM:277900]: An autosomal recessive
CC disorder of copper metabolism in which copper cannot be incorporated
CC into ceruloplasmin in liver, and cannot be excreted from the liver into
CC the bile. Copper accumulates in the liver and subsequently in the brain
CC and kidney. The disease is characterized by neurologic manifestations
CC and signs of cirrhosis. {ECO:0000269|PubMed:10051024,
CC ECO:0000269|PubMed:10194254, ECO:0000269|PubMed:10447265,
CC ECO:0000269|PubMed:10453196, ECO:0000269|PubMed:10502776,
CC ECO:0000269|PubMed:10502777, ECO:0000269|PubMed:10544227,
CC ECO:0000269|PubMed:10721669, ECO:0000269|PubMed:10790207,
CC ECO:0000269|PubMed:10942420, ECO:0000269|PubMed:11043508,
CC ECO:0000269|PubMed:11093740, ECO:0000269|PubMed:11180609,
CC ECO:0000269|PubMed:11216666, ECO:0000269|PubMed:11231950,
CC ECO:0000269|PubMed:11243728, ECO:0000269|PubMed:11405812,
CC ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:11954751,
CC ECO:0000269|PubMed:12325021, ECO:0000269|PubMed:12376745,
CC ECO:0000269|PubMed:12544487, ECO:0000269|PubMed:14639035,
CC ECO:0000269|PubMed:14966923, ECO:0000269|PubMed:14986826,
CC ECO:0000269|PubMed:15024742, ECO:0000269|PubMed:15557537,
CC ECO:0000269|PubMed:15811015, ECO:0000269|PubMed:15845031,
CC ECO:0000269|PubMed:15952988, ECO:0000269|PubMed:15967699,
CC ECO:0000269|PubMed:16088907, ECO:0000269|PubMed:16207219,
CC ECO:0000269|PubMed:16283883, ECO:0000269|PubMed:16649058,
CC ECO:0000269|PubMed:17718866, ECO:0000269|PubMed:17823867,
CC ECO:0000269|PubMed:17919502, ECO:0000269|PubMed:17949296,
CC ECO:0000269|PubMed:18203200, ECO:0000269|PubMed:18373411,
CC ECO:0000269|PubMed:19033537, ECO:0000269|PubMed:20333758,
CC ECO:0000269|PubMed:21398519, ECO:0000269|PubMed:21454443,
CC ECO:0000269|PubMed:21645214, ECO:0000269|PubMed:21682854,
CC ECO:0000269|PubMed:22075048, ECO:0000269|PubMed:22240481,
CC ECO:0000269|PubMed:22484412, ECO:0000269|PubMed:22763723,
CC ECO:0000269|PubMed:23159873, ECO:0000269|PubMed:23235335,
CC ECO:0000269|PubMed:23275100, ECO:0000269|PubMed:23333878,
CC ECO:0000269|PubMed:23518715, ECO:0000269|PubMed:23962630,
CC ECO:0000269|PubMed:24476933, ECO:0000269|PubMed:24555712,
CC ECO:0000269|PubMed:24706876, ECO:0000269|PubMed:25704634,
CC ECO:0000269|PubMed:25982861, ECO:0000269|PubMed:26004889,
CC ECO:0000269|PubMed:28856630, ECO:0000269|PubMed:32284880,
CC ECO:0000269|PubMed:7626145, ECO:0000269|PubMed:8298641,
CC ECO:0000269|PubMed:8533760, ECO:0000269|PubMed:8782057,
CC ECO:0000269|PubMed:8931691, ECO:0000269|PubMed:8938442,
CC ECO:0000269|PubMed:8980283, ECO:0000269|PubMed:9222767,
CC ECO:0000269|PubMed:9311736, ECO:0000269|PubMed:9452121,
CC ECO:0000269|PubMed:9482578, ECO:0000269|PubMed:9554743,
CC ECO:0000269|PubMed:9671269, ECO:0000269|PubMed:9772425,
CC ECO:0000269|PubMed:9829905, ECO:0000269|PubMed:9837819,
CC ECO:0000269|PubMed:9887381}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 5]: May arise by a -1 programmed ribosomal
CC frameshift at codon 233. A nucleotide 'slippery sequence' followed by
CC an mRNA pseudoknot are found downstream of the frameshift site and
CC direct frameshifting of a gene fragment with about 10% efficiency.
CC {ECO:0000305|PubMed:28107647}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16173.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA79211.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA79212.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wilson Disease Mutation Database;
CC URL="https://www.wilsondisease.med.ualberta.ca/";
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DR EMBL; U11700; AAA92667.1; -; mRNA.
DR EMBL; DQ015922; AAY41166.1; -; mRNA.
DR EMBL; AL138821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF034838; AAD01998.1; -; Genomic_DNA.
DR EMBL; U03464; AAB52902.1; -; mRNA.
DR EMBL; L25591; AAA79211.1; ALT_FRAME; mRNA.
DR EMBL; L25591; AAA79212.1; ALT_FRAME; mRNA.
DR EMBL; L25442; AAA16173.1; ALT_FRAME; mRNA.
DR EMBL; AB209461; BAD92698.1; -; mRNA.
DR EMBL; S77446; AAD14987.1; -; Genomic_DNA.
DR EMBL; S77447; AAB34086.1; -; Genomic_DNA.
DR EMBL; S77450; AAB34087.1; -; Genomic_DNA.
DR CCDS; CCDS41892.1; -. [P35670-1]
DR CCDS; CCDS45049.1; -. [P35670-2]
DR CCDS; CCDS58293.1; -. [P35670-3]
DR PIR; I78536; I78536.
DR PIR; I78537; I78537.
DR PIR; S78555; S78555.
DR RefSeq; NP_000044.2; NM_000053.3. [P35670-1]
DR RefSeq; NP_001230111.1; NM_001243182.1. [P35670-3]
DR RefSeq; NP_001317507.1; NM_001330578.1.
DR RefSeq; NP_001317508.1; NM_001330579.1.
DR RefSeq; XP_005266487.1; XM_005266430.4. [P35670-1]
DR PDB; 2ARF; NMR; -; A=1032-1196.
DR PDB; 2EW9; NMR; -; A=486-633.
DR PDB; 2KOY; NMR; -; A=1036-1196.
DR PDB; 2LQB; NMR; -; A=141-212.
DR PDB; 2N7Y; NMR; -; A=56-127.
DR PDB; 2ROP; NMR; -; A=238-439.
DR PDB; 6A71; X-ray; 1.60 A; A/B=357-428.
DR PDB; 6A72; X-ray; 2.10 A; A/B=357-428.
DR PDBsum; 2ARF; -.
DR PDBsum; 2EW9; -.
DR PDBsum; 2KOY; -.
DR PDBsum; 2LQB; -.
DR PDBsum; 2N7Y; -.
DR PDBsum; 2ROP; -.
DR PDBsum; 6A71; -.
DR PDBsum; 6A72; -.
DR AlphaFoldDB; P35670; -.
DR BMRB; P35670; -.
DR SMR; P35670; -.
DR BioGRID; 107022; 41.
DR IntAct; P35670; 13.
DR STRING; 9606.ENSP00000242839; -.
DR DrugBank; DB00958; Carboplatin.
DR DrugBank; DB00515; Cisplatin.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00526; Oxaliplatin.
DR TCDB; 3.A.3.5.3; the p-type atpase (p-atpase) superfamily.
DR GlyGen; P35670; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35670; -.
DR PhosphoSitePlus; P35670; -.
DR BioMuta; ATP7B; -.
DR DMDM; 239938919; -.
DR EPD; P35670; -.
DR jPOST; P35670; -.
DR MassIVE; P35670; -.
DR MaxQB; P35670; -.
DR PaxDb; P35670; -.
DR PeptideAtlas; P35670; -.
DR PRIDE; P35670; -.
DR ProteomicsDB; 55130; -. [P35670-1]
DR ProteomicsDB; 55131; -. [P35670-2]
DR ProteomicsDB; 55132; -. [P35670-3]
DR ProteomicsDB; 55133; -. [P35670-4]
DR ABCD; P35670; 17 sequenced antibodies.
DR Antibodypedia; 2396; 531 antibodies from 37 providers.
DR DNASU; 540; -.
DR Ensembl; ENST00000242839.10; ENSP00000242839.5; ENSG00000123191.16. [P35670-1]
DR Ensembl; ENST00000344297.9; ENSP00000342559.5; ENSG00000123191.16. [P35670-2]
DR Ensembl; ENST00000400366.6; ENSP00000383217.3; ENSG00000123191.16. [P35670-3]
DR GeneID; 540; -.
DR KEGG; hsa:540; -.
DR MANE-Select; ENST00000242839.10; ENSP00000242839.5; NM_000053.4; NP_000044.2.
DR UCSC; uc001vfw.4; human. [P35670-1]
DR CTD; 540; -.
DR DisGeNET; 540; -.
DR GeneCards; ATP7B; -.
DR GeneReviews; ATP7B; -.
DR HGNC; HGNC:870; ATP7B.
DR HPA; ENSG00000123191; Low tissue specificity.
DR MalaCards; ATP7B; -.
DR MIM; 277900; phenotype.
DR MIM; 606882; gene.
DR neXtProt; NX_P35670; -.
DR OpenTargets; ENSG00000123191; -.
DR Orphanet; 905; Wilson disease.
DR PharmGKB; PA73; -.
DR VEuPathDB; HostDB:ENSG00000123191; -.
DR eggNOG; KOG0207; Eukaryota.
DR GeneTree; ENSGT00940000155749; -.
DR HOGENOM; CLU_001771_0_1_1; -.
DR InParanoid; P35670; -.
DR OMA; NSWISGT; -.
DR PhylomeDB; P35670; -.
DR TreeFam; TF300460; -.
DR BRENDA; 7.2.2.8; 2681.
DR BRENDA; 7.2.2.9; 2681.
DR PathwayCommons; P35670; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; P35670; -.
DR BioGRID-ORCS; 540; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; ATP7B; human.
DR EvolutionaryTrace; P35670; -.
DR GeneWiki; Wilson_disease_protein; -.
DR GenomeRNAi; 540; -.
DR Pharos; P35670; Tbio.
DR PRO; PR:P35670; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P35670; protein.
DR Bgee; ENSG00000123191; Expressed in nasal cavity epithelium and 121 other tissues.
DR ExpressionAtlas; P35670; baseline and differential.
DR Genevisible; P35670; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IMP:UniProtKB.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IEA:Ensembl.
DR GO; GO:0060003; P:copper ion export; IBA:GO_Central.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0015677; P:copper ion import; IDA:UniProtKB.
DR GO; GO:0006825; P:copper ion transport; IDA:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0015680; P:protein maturation by copper ion transfer; IEA:Ensembl.
DR GO; GO:0046688; P:response to copper ion; IDA:UniProtKB.
DR GO; GO:0051208; P:sequestering of calcium ion; IDA:UniProtKB.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IC:GO_Central.
DR CDD; cd00371; HMA; 6.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 6.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 6.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR00003; TIGR00003; 6.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 6.
DR PROSITE; PS50846; HMA_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Copper; Copper transport;
KW Cytoplasm; Disease variant; Endosome; Golgi apparatus; Ion transport;
KW Magnesium; Membrane; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Ribosomal frameshifting;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1465
FT /note="Copper-transporting ATPase 2"
FT /id="PRO_0000046314"
FT CHAIN ?..1465
FT /note="WND/140 kDa"
FT /evidence="ECO:0000305|PubMed:9600907"
FT /id="PRO_0000296199"
FT TOPO_DOM 1..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..697
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..764
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 786..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 920..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..972
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..994
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 995..1322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1323..1340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1341..1351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1352..1371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1372..1465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..124
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 143..209
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 257..323
FT /note="HMA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 359..425
FT /note="HMA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 488..554
FT /note="HMA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 564..630
FT /note="HMA 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1027
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 72
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 154
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 157
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 268
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 271
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 370
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 373
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 499
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 502
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 575
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 578
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459"
FT BINDING 1267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 1271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64535"
FT MOD_RES 1398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64535"
FT VAR_SEQ 234..1465
FT /note="RPLSSANQNFNNSETLGHQGSHVVTLQLRIDGMHCKSCVLNIEENIGQLLGV
FT QSIQVSLENKTAQVKYDPSCTSPVALQRAIEALPPGNFKVSLPDGAEGSGTDHRSSSSH
FT SPGSPPRNQVQGTCSTTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLY
FT NPSVISPEELRAAIEDMGFEASVVSESCSTNPLGNHSAGNSMVQTTDGTPTSVQEVAPH
FT TGRLPANHAPDILAKSPQSTRAVAPQKCFLQIKGMTCASCVSNIERNLQKEAGVLSVLV
FT ALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVMEDYAGSDGNIELTITGMTCASCVH
FT NIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLAQRNPNAH
FT HLDHKMEIKQWKKSFLCSLVFGIPVMALMIYMLIPSNEPHQSMVLDHNIIPGLSILNLI
FT FFILCTFVQLLGGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLVILVVAVAEKAE
FT RSPVTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEDNLIIR
FT EEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAG
FT SINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTL
FT TLVVWIVIGFIDFGVVQRYFPNPNKHISQTEVIIRFAFQTSITVLCIACPCSLGLATPT
FT AVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATLP
FT LRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLGYCTDFQAVPGCGIGCKVSNVEG
FT ILAHSERPLSAPASHLNEAGSLPAEKDAVPQTFSVLIGNREWLRRNGLTISSDVSDAMT
FT DHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARA
FT IATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGT
FT DVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIG
FT IVLQPWMGSAAMAASSVSVVLSSLQLKCYKKPDLERYEAQAHGHMKPLTASQVSVHIGM
FT DDRWRDSPRATPWDQVSYVSQVSLSSLTSDKPSRHSAAADDDGDKWSLLLNGRDEEQYI
FT -> ETFIFC (in isoform 5)"
FT /evidence="ECO:0000305|PubMed:28107647"
FT /id="VSP_059175"
FT VAR_SEQ 269..379
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016559"
FT VAR_SEQ 624..785
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8298641"
FT /id="VSP_000426"
FT VAR_SEQ 911..955
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8298641"
FT /id="VSP_000427"
FT VAR_SEQ 938..955
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8250934"
FT /id="VSP_016560"
FT VARIANT 14
FT /note="A -> D (in dbSNP:rs587783319)"
FT /evidence="ECO:0000269|PubMed:14986826"
FT /id="VAR_023010"
FT VARIANT 41
FT /note="N -> S (in WD; affects copper-induced
FT relocalization; the mutant is constitutively trafficked to
FT the basolateral membrane instead of staying in the TGN
FT under low copper conditions; does not affect interaction
FT with COMMD1; dbSNP:rs201738967)"
FT /evidence="ECO:0000269|PubMed:15024742,
FT ECO:0000269|PubMed:17919502, ECO:0000269|PubMed:19033537"
FT /id="VAR_023011"
FT VARIANT 44
FT /note="Y -> N (in WD; unknown pathological significance;
FT dbSNP:rs1566605396)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076729"
FT VARIANT 85
FT /note="G -> V (in WD; decreased copper transport activity;
FT decreased ATPase activity; increased interaction with
FT COMMD1; decreased localization to trans-Golgi network;
FT increased degradation; dbSNP:rs786204643)"
FT /evidence="ECO:0000269|PubMed:14986826,
FT ECO:0000269|PubMed:17919502, ECO:0000269|PubMed:22240481,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000703"
FT VARIANT 96
FT /note="G -> D (in dbSNP:rs1429553821)"
FT /evidence="ECO:0000269|PubMed:7833924"
FT /id="VAR_000704"
FT VARIANT 108
FT /note="C -> R (in WD; unknown pathological significance;
FT dbSNP:rs1566603189)"
FT /evidence="ECO:0000269|PubMed:21645214"
FT /id="VAR_076730"
FT VARIANT 136
FT /note="R -> W (in WD; unknown pathological significance;
FT dbSNP:rs557577836)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076693"
FT VARIANT 148
FT /note="R -> W (in WD; unknown pathological significance;
FT dbSNP:rs373762572)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076694"
FT VARIANT 149
FT /note="V -> L"
FT /evidence="ECO:0000269|PubMed:17823867"
FT /id="VAR_076793"
FT VARIANT 157
FT /note="C -> F (in WD; unknown pathological significance;
FT dbSNP:rs551275663)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076731"
FT VARIANT 170
FT /note="G -> V (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:22484412"
FT /id="VAR_076810"
FT VARIANT 290
FT /note="V -> L"
FT /evidence="ECO:0000269|PubMed:10721669"
FT /id="VAR_044453"
FT VARIANT 382
FT /note="S -> C (in WD; unknown pathological significance;
FT dbSNP:rs774102085)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076695"
FT VARIANT 390
FT /note="I -> V (in dbSNP:rs770903362)"
FT /evidence="ECO:0000269|PubMed:11405812"
FT /id="VAR_000705"
FT VARIANT 406
FT /note="S -> A (no effect on copper transport activity;
FT dbSNP:rs1801243)"
FT /evidence="ECO:0000269|PubMed:10721669,
FT ECO:0000269|PubMed:10790207, ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:14986826,
FT ECO:0000269|PubMed:15952988, ECO:0000269|PubMed:18373411,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:23333878,
FT ECO:0000269|Ref.2"
FT /id="VAR_000706"
FT VARIANT 446
FT /note="V -> L (in dbSNP:rs587783298)"
FT /id="VAR_000707"
FT VARIANT 456
FT /note="V -> L (decreased copper transport rates; no effect
FT on ATPase activity; dbSNP:rs1801244)"
FT /evidence="ECO:0000269|PubMed:10721669,
FT ECO:0000269|PubMed:10790207, ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:14986826,
FT ECO:0000269|PubMed:15952988, ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:17823867, ECO:0000269|PubMed:18373411,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:25704634, ECO:0000269|PubMed:9887381,
FT ECO:0000269|Ref.2"
FT /id="VAR_000708"
FT VARIANT 466
FT /note="L -> V"
FT /id="VAR_000709"
FT VARIANT 486
FT /note="A -> S (in WD; unknown pathological significance;
FT does not affect interaction with COMMD1;
FT dbSNP:rs1282624946)"
FT /evidence="ECO:0000269|PubMed:11216666,
FT ECO:0000269|PubMed:17919502"
FT /id="VAR_044454"
FT VARIANT 492
FT /note="L -> S (in WD; decreased copper transport activity;
FT decreased ATPase activity; does not affect interaction with
FT COMMD1; dbSNP:rs1566580253)"
FT /evidence="ECO:0000269|PubMed:17919502,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:9671269"
FT /id="VAR_000710"
FT VARIANT 532
FT /note="Y -> H (in WD; unknown pathological significance; no
FT effect on copper transport activity; does not affect
FT interaction with COMMD1)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:17919502, ECO:0000269|PubMed:18203200"
FT /id="VAR_044455"
FT VARIANT 536
FT /note="V -> A (in WD; likely benign variant;
FT dbSNP:rs138427376)"
FT /evidence="ECO:0000269|PubMed:18373411,
FT ECO:0000269|PubMed:23518715"
FT /id="VAR_058925"
FT VARIANT 539
FT /note="P -> L (in WD; dbSNP:rs572122562)"
FT /evidence="ECO:0000269|PubMed:22763723"
FT /id="VAR_076970"
FT VARIANT 541
FT /note="E -> K (in WD; unknown pathological significance;
FT does not affect interaction with COMMD1;
FT dbSNP:rs187046823)"
FT /evidence="ECO:0000269|PubMed:17919502,
FT ECO:0000269|PubMed:23518715"
FT /id="VAR_076696"
FT VARIANT 549
FT /note="L -> P (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:21682854"
FT /id="VAR_067335"
FT VARIANT 565
FT /note="N -> S (in dbSNP:rs778475094)"
FT /evidence="ECO:0000269|PubMed:9482578"
FT /id="VAR_000711"
FT VARIANT 591
FT /note="G -> D (in WD; increased interaction with COMMD1;
FT decreased localization to trans-Glogi network;
FT dbSNP:rs797045402)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:17919502"
FT /id="VAR_044456"
FT VARIANT 591
FT /note="G -> S (in WD; unknown pathological significance;
FT dbSNP:rs1566559224)"
FT /evidence="ECO:0000269|PubMed:17823867"
FT /id="VAR_076794"
FT VARIANT 597
FT /note="V -> I (in WD; unknown pathological significance;
FT dbSNP:rs760501309)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076697"
FT VARIANT 604
FT /note="A -> P (in WD; unknown pathological significance;
FT increased interaction with COMMD1)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:17919502"
FT /id="VAR_044457"
FT VARIANT 606
FT /note="V -> G (in WD; unknown pathological significance;
FT dbSNP:rs1173050016)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076732"
FT VARIANT 608..609
FT /note="FD -> Y (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:9671269"
FT /id="VAR_010009"
FT VARIANT 614
FT /note="G -> C (in WD; unknown pathological significance;
FT dbSNP:rs376565432)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076698"
FT VARIANT 616
FT /note="R -> Q (in WD; unknown pathological significance;
FT does not affect interaction with COMMD1;
FT dbSNP:rs752850609)"
FT /evidence="ECO:0000269|PubMed:16207219,
FT ECO:0000269|PubMed:16283883, ECO:0000269|PubMed:17919502"
FT /id="VAR_009004"
FT VARIANT 616
FT /note="R -> W (in WD; decreased copper transport activity;
FT increased ATPase activity; does not affect interaction with
FT COMMD1; dbSNP:rs374172791)"
FT /evidence="ECO:0000269|PubMed:11690702,
FT ECO:0000269|PubMed:17919502, ECO:0000269|PubMed:22240481"
FT /id="VAR_023012"
FT VARIANT 626
FT /note="G -> A (in WD; unknown pathological significance; no
FT effect on protein abundance; no effect on protein
FT localization; may have an effect on copper transport
FT activity; no effect on ATPase activity; does not affect
FT interaction with COMMD1; dbSNP:rs587783299)"
FT /evidence="ECO:0000269|PubMed:16207219,
FT ECO:0000269|PubMed:17919502, ECO:0000269|PubMed:18203200,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:24706876,
FT ECO:0000269|PubMed:8533760"
FT /id="VAR_000712"
FT VARIANT 639
FT /note="H -> Y (in WD; unknown pathological significance; no
FT effect on protein abundance; no effect on protein
FT localization; no effect on copper transport activity;
FT dbSNP:rs200728096)"
FT /evidence="ECO:0000269|PubMed:16283883,
FT ECO:0000269|PubMed:24706876"
FT /id="VAR_044458"
FT VARIANT 641
FT /note="L -> S (in WD; unknown pathological significance; no
FT effect on protein abundance; no effect on protein
FT localization; no effect on copper transport activity; does
FT not affect interaction with COMMD1; dbSNP:rs186924074)"
FT /evidence="ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:16088907, ECO:0000269|PubMed:17919502,
FT ECO:0000269|PubMed:23518715, ECO:0000269|PubMed:24706876"
FT /id="VAR_023013"
FT VARIANT 642
FT /note="D -> H (in WD; unknown pathological significance; no
FT effect on protein abundance; no effect on protein
FT localization; no effect on copper transport activity; does
FT not affect interaction with COMMD1; dbSNP:rs72552285)"
FT /evidence="ECO:0000269|PubMed:18203200,
FT ECO:0000269|PubMed:21682854, ECO:0000269|PubMed:24706876,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000713"
FT VARIANT 645
FT /note="M -> R (in WD; also found in a patient with
FT hypoceruloplasminemia without clinical manifestations of WD
FT in the central nervous system or liver; a liver biopsy of
FT the patient with hypoceruloplasminemia shows no copper or
FT iron accumulation in Kupffer cells or hepatocytes; due to a
FT nucleotide substitution that also results in out-of-frame
FT partial skipping of exon 6, stop gain and reduced
FT expression of the truncated protein; variant R-645 has no
FT effect on protein localization; no effect on copper
FT transport; does not affect interaction with COMMD1;
FT dbSNP:rs121907998)"
FT /evidence="ECO:0000269|PubMed:15952988,
FT ECO:0000269|PubMed:17919502, ECO:0000269|PubMed:17949296,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:23518715,
FT ECO:0000269|PubMed:23962630, ECO:0000269|PubMed:24706876,
FT ECO:0000269|PubMed:32284880, ECO:0000269|PubMed:9482578,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000714"
FT VARIANT 653
FT /note="S -> Y (in WD; unknown pathological significance; no
FT effect on protein abundance; altered copper-induced
FT relocalization; no effect on copper transport activity)"
FT /evidence="ECO:0000269|PubMed:16283883,
FT ECO:0000269|PubMed:24706876"
FT /id="VAR_044459"
FT VARIANT 657
FT /note="S -> R (in WD; unknown pathological significance;
FT dbSNP:rs372436901)"
FT /evidence="ECO:0000269|PubMed:18373411"
FT /id="VAR_058926"
FT VARIANT 665
FT /note="M -> I (in WD; unknown pathological significance;
FT dbSNP:rs72552259)"
FT /evidence="ECO:0000269|PubMed:23518715,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000715"
FT VARIANT 670..671
FT /note="Missing (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:10447265"
FT /id="VAR_009005"
FT VARIANT 690
FT /note="P -> L (in WD; dbSNP:rs1555291809)"
FT /evidence="ECO:0000269|PubMed:15952988"
FT /id="VAR_023014"
FT VARIANT 691
FT /note="G -> R (in WD; dbSNP:rs121908001)"
FT /evidence="ECO:0000269|PubMed:17718866,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000716"
FT VARIANT 693
FT /note="S -> C (in WD; dbSNP:rs1212479289)"
FT /evidence="ECO:0000269|PubMed:9772425"
FT /id="VAR_023015"
FT VARIANT 703
FT /note="C -> Y (in WD; dbSNP:rs767218895)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:21682854"
FT /id="VAR_044460"
FT VARIANT 708
FT /note="L -> P (in WD; dbSNP:rs121908000)"
FT /evidence="ECO:0000269|PubMed:11093740"
FT /id="VAR_000717"
FT VARIANT 710
FT /note="G -> A (in WD; dbSNP:rs1555291285)"
FT /evidence="ECO:0000269|PubMed:11690702,
FT ECO:0000269|PubMed:9887381"
FT /id="VAR_010010"
FT VARIANT 710
FT /note="G -> R (in WD)"
FT /id="VAR_000718"
FT VARIANT 710
FT /note="G -> S (in WD; decreased copper transport activity;
FT no effect on ATPase activity; dbSNP:rs137853285)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:22763723,
FT ECO:0000269|PubMed:23333878"
FT /id="VAR_000719"
FT VARIANT 710
FT /note="G -> V (in WD)"
FT /evidence="ECO:0000269|PubMed:16088907"
FT /id="VAR_044461"
FT VARIANT 711
FT /note="G -> E (in WD)"
FT /id="VAR_000720"
FT VARIANT 711
FT /note="G -> R (in WD; dbSNP:rs1394999756)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_009006"
FT VARIANT 711
FT /note="G -> W (in WD; dbSNP:rs1394999756)"
FT /id="VAR_009007"
FT VARIANT 713
FT /note="Y -> C (in WD; dbSNP:rs756883878)"
FT /id="VAR_000721"
FT VARIANT 721
FT /note="S -> P (in WD; dbSNP:rs765667658)"
FT /evidence="ECO:0000269|PubMed:12325021"
FT /id="VAR_023016"
FT VARIANT 723
FT /note="R -> G"
FT /evidence="ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:9482578"
FT /id="VAR_000722"
FT VARIANT 729
FT /note="M -> V (in WD; unknown pathological significance;
FT dbSNP:rs773447981)"
FT /evidence="ECO:0000269|PubMed:21645214"
FT /id="VAR_076733"
FT VARIANT 731
FT /note="V -> A (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076699"
FT VARIANT 732
FT /note="L -> H (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076734"
FT VARIANT 732
FT /note="L -> P (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076735"
FT VARIANT 737
FT /note="T -> R (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:15967699"
FT /id="VAR_023017"
FT VARIANT 741
FT /note="Y -> C (in WD; dbSNP:rs770533110)"
FT /evidence="ECO:0000269|PubMed:9887381"
FT /id="VAR_010011"
FT VARIANT 744
FT /note="S -> P (in WD; dbSNP:rs1593726081)"
FT /evidence="ECO:0000269|PubMed:21682854"
FT /id="VAR_009008"
FT VARIANT 745
FT /note="L -> P (in WD; unknown pathological significance;
FT dbSNP:rs1362773192)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076700"
FT VARIANT 747
FT /note="I -> F (in WD)"
FT /evidence="ECO:0000269|PubMed:9671269"
FT /id="VAR_000723"
FT VARIANT 756
FT /note="A -> G (in WD)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:23235335"
FT /id="VAR_044462"
FT VARIANT 760
FT /note="P -> L (in WD; decreased copper transport activity;
FT increased ATPase activity; dbSNP:rs766907687)"
FT /evidence="ECO:0000269|PubMed:11180609,
FT ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:22240481"
FT /id="VAR_023018"
FT VARIANT 765
FT /note="D -> G (in WD; dbSNP:rs1555291147)"
FT /evidence="ECO:0000269|PubMed:14986826"
FT /id="VAR_023019"
FT VARIANT 765
FT /note="D -> H (in WD; unknown pathological significance;
FT dbSNP:rs28942075)"
FT /evidence="ECO:0000269|PubMed:22484412"
FT /id="VAR_076811"
FT VARIANT 765
FT /note="D -> N (in WD; decreased copper transport activity;
FT increased ATPase activity; decreased localization to TGN
FT and reduced capacity to redistribute to cytoplasmic
FT vesicles under high-copper levels; dbSNP:rs28942075)"
FT /evidence="ECO:0000269|PubMed:10942420,
FT ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:21682854,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:8533760, ECO:0000269|PubMed:9482578,
FT ECO:0000269|PubMed:9837819"
FT /id="VAR_000724"
FT VARIANT 766
FT /note="T -> M (in WD; dbSNP:rs121907997)"
FT /evidence="ECO:0000269|PubMed:16088907"
FT /id="VAR_044463"
FT VARIANT 766
FT /note="T -> R (in WD; dbSNP:rs121907997)"
FT /evidence="ECO:0000269|PubMed:15557537"
FT /id="VAR_044464"
FT VARIANT 768
FT /note="P -> H (in WD)"
FT /evidence="ECO:0000269|PubMed:12544487"
FT /id="VAR_023020"
FT VARIANT 769
FT /note="M -> I (in WD)"
FT /evidence="ECO:0000269|PubMed:10790207"
FT /id="VAR_023021"
FT VARIANT 769
FT /note="M -> R (in WD; dbSNP:rs772595172)"
FT /id="VAR_009009"
FT VARIANT 769
FT /note="M -> V (in WD; possible decreased copper transport
FT activity; increased ATPase activity; dbSNP:rs193922103)"
FT /evidence="ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:17949296,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:23518715,
FT ECO:0000269|PubMed:9837819"
FT /id="VAR_000725"
FT VARIANT 776
FT /note="L -> P (in WD)"
FT /evidence="ECO:0000269|PubMed:16283883"
FT /id="VAR_044465"
FT VARIANT 776
FT /note="L -> V (in WD; unknown pathological significance; no
FT effect on copper transport activity; decreased localization
FT to TGN and reduced capacity to redistribute to cytoplasmic
FT vesicles under high-copper levels; dbSNP:rs1217463955)"
FT /evidence="ECO:0000269|PubMed:10942420,
FT ECO:0000269|PubMed:9837819"
FT /id="VAR_000726"
FT VARIANT 778
FT /note="R -> G (in WD; dbSNP:rs137853284)"
FT /evidence="ECO:0000269|PubMed:11216666,
FT ECO:0000269|PubMed:15967699, ECO:0000269|PubMed:16207219,
FT ECO:0000269|PubMed:16283883, ECO:0000269|PubMed:21682854,
FT ECO:0000269|PubMed:23333878, ECO:0000269|PubMed:8533760"
FT /id="VAR_000727"
FT VARIANT 778
FT /note="R -> L (in WD; most common mutation; decreased
FT copper transport activity; extensively localized throughout
FT the cell in the distribution pattern of the endoplasmic
FT reticulum; dbSNP:rs28942074)"
FT /evidence="ECO:0000269|PubMed:10453196,
FT ECO:0000269|PubMed:10721669, ECO:0000269|PubMed:10790207,
FT ECO:0000269|PubMed:10942420, ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:12376745, ECO:0000269|PubMed:12544487,
FT ECO:0000269|PubMed:14966923, ECO:0000269|PubMed:14986826,
FT ECO:0000269|PubMed:16649058, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:23235335, ECO:0000269|PubMed:25704634,
FT ECO:0000269|PubMed:8782057, ECO:0000269|PubMed:9452121,
FT ECO:0000269|PubMed:9554743, ECO:0000269|PubMed:9837819"
FT /id="VAR_000728"
FT VARIANT 778
FT /note="R -> Q (in WD; decreased copper transport activity;
FT dbSNP:rs28942074)"
FT /evidence="ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:23235335, ECO:0000269|PubMed:8782057,
FT ECO:0000269|PubMed:9837819"
FT /id="VAR_000729"
FT VARIANT 778
FT /note="R -> W (in WD; dbSNP:rs137853284)"
FT /evidence="ECO:0000269|PubMed:10790207,
FT ECO:0000269|PubMed:11243728, ECO:0000269|PubMed:16207219,
FT ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:23518715, ECO:0000269|PubMed:9671269"
FT /id="VAR_000730"
FT VARIANT 779
FT /note="W -> G (in WD; dbSNP:rs751798708)"
FT /evidence="ECO:0000269|PubMed:22763723,
FT ECO:0000269|PubMed:23159873"
FT /id="VAR_076971"
FT VARIANT 788
FT /note="T -> I (in WD; decreased copper ion transmembrane
FT transporter activity; dbSNP:rs541408630)"
FT /evidence="ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:26004889"
FT /id="VAR_075336"
FT VARIANT 795
FT /note="L -> F (in WD; unknown pathological significance;
FT dbSNP:rs751710854)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_000731"
FT VARIANT 795
FT /note="L -> R (in WD)"
FT /id="VAR_009010"
FT VARIANT 816
FT /note="R -> S (in WD)"
FT /evidence="ECO:0000269|PubMed:22763723"
FT /id="VAR_076972"
FT VARIANT 825
FT /note="V -> L"
FT /evidence="ECO:0000269|PubMed:17823867"
FT /id="VAR_076795"
FT VARIANT 827
FT /note="R -> P (in WD; unknown pathological significance;
FT dbSNP:rs368589213)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076765"
FT VARIANT 827
FT /note="R -> W (in WD; yeast complementation assays show
FT that the variant does not rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs539585071)"
FT /evidence="ECO:0000269|PubMed:21645214"
FT /id="VAR_076736"
FT VARIANT 832
FT /note="K -> R (decreased copper transport activity; no
FT effect on ATPase activity; dbSNP:rs1061472)"
FT /evidence="ECO:0000269|PubMed:10721669,
FT ECO:0000269|PubMed:11405812, ECO:0000269|PubMed:11690702,
FT ECO:0000269|PubMed:14986826, ECO:0000269|PubMed:15952988,
FT ECO:0000269|PubMed:15967699, ECO:0000269|PubMed:18373411,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:8250934, ECO:0000269|PubMed:9482578,
FT ECO:0000269|PubMed:9554743, ECO:0000269|Ref.9"
FT /id="VAR_000732"
FT VARIANT 836
FT /note="G -> E (in WD; unknown pathological significance;
FT dbSNP:rs773809011)"
FT /evidence="ECO:0000269|PubMed:22484412"
FT /id="VAR_076812"
FT VARIANT 840
FT /note="P -> L (in WD; decreased copper transport activity;
FT increased ATPase activity; dbSNP:rs768671894)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000733"
FT VARIANT 857
FT /note="I -> T (in WD; decreased copper transport activity;
FT increased ATPase activity; dbSNP:rs1057520235)"
FT /evidence="ECO:0000269|PubMed:22240481,
FT ECO:0000269|PubMed:8533760"
FT /id="VAR_000734"
FT VARIANT 858
FT /note="T -> A (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076766"
FT VARIANT 861
FT /note="A -> T (in WD)"
FT /evidence="ECO:0000269|PubMed:16088907"
FT /id="VAR_044466"
FT VARIANT 864
FT /note="V -> I"
FT /evidence="ECO:0000269|PubMed:9554743"
FT /id="VAR_000735"
FT VARIANT 869
FT /note="G -> R (in WD; dbSNP:rs191312027)"
FT /evidence="ECO:0000269|PubMed:15952988,
FT ECO:0000269|PubMed:23518715"
FT /id="VAR_000736"
FT VARIANT 869
FT /note="G -> V (in WD)"
FT /id="VAR_009011"
FT VARIANT 874
FT /note="A -> P (in WD; unknown pathological significance;
FT dbSNP:rs376355660)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076737"
FT VARIANT 874
FT /note="A -> V (in WD; decreased copper transport activity;
FT increased ATPase activity; decreased localization to the
FT TGN; dbSNP:rs121907994)"
FT /evidence="ECO:0000269|PubMed:10453196,
FT ECO:0000269|PubMed:10544227, ECO:0000269|PubMed:10721669,
FT ECO:0000269|PubMed:10790207, ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:12376745, ECO:0000269|PubMed:12544487,
FT ECO:0000269|PubMed:16207219, ECO:0000269|PubMed:17949296,
FT ECO:0000269|PubMed:21645214, ECO:0000269|PubMed:22240481,
FT ECO:0000269|PubMed:23235335, ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:28856630, ECO:0000269|PubMed:9452121,
FT ECO:0000269|PubMed:9554743"
FT /id="VAR_000737"
FT VARIANT 875
FT /note="G -> R (individuals heterozygous for Wilson disease
FT mutations on the R-875 background may manifest the disease
FT phenotype under conditions of copper deficiency; affects
FT protein folding; localized to the ER and absent from TGN
FT under low copper conditions; in response to high copper
FT levels it relocalizes to vesicles and properly cycle back
FT to TGN; dbSNP:rs587783304)"
FT /evidence="ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:21406592, ECO:0000269|PubMed:7833924,
FT ECO:0000269|PubMed:8298641"
FT /id="VAR_023022"
FT VARIANT 875
FT /note="G -> V (in WD; requires 2 nucleotide substitutions)"
FT /id="VAR_044467"
FT VARIANT 890
FT /note="V -> M (in WD; dbSNP:rs786204718)"
FT /evidence="ECO:0000269|PubMed:11216666,
FT ECO:0000269|PubMed:14986826, ECO:0000269|PubMed:23235335"
FT /id="VAR_023023"
FT VARIANT 891
FT /note="G -> D (in WD; unknown pathological significance;
FT dbSNP:rs483352684)"
FT /evidence="ECO:0000269|PubMed:21645214"
FT /id="VAR_076738"
FT VARIANT 891
FT /note="G -> V (in WD)"
FT /id="VAR_010012"
FT VARIANT 898
FT /note="Q -> R (in WD)"
FT /evidence="ECO:0000269|PubMed:11243728"
FT /id="VAR_023024"
FT VARIANT 899..907
FT /note="Missing (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:22075048"
FT /id="VAR_076739"
FT VARIANT 899
FT /note="I -> F (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076767"
FT VARIANT 918
FT /note="D -> E (in WD)"
FT /evidence="ECO:0000269|PubMed:15967699"
FT /id="VAR_023025"
FT VARIANT 918
FT /note="D -> N (in WD; dbSNP:rs540935874)"
FT /evidence="ECO:0000269|PubMed:9671269"
FT /id="VAR_000738"
FT VARIANT 919
FT /note="R -> G (in WD; dbSNP:rs121907993)"
FT /evidence="ECO:0000269|PubMed:10453196,
FT ECO:0000269|PubMed:10790207, ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:12376745, ECO:0000269|PubMed:14986826,
FT ECO:0000269|PubMed:21645214, ECO:0000269|PubMed:23235335,
FT ECO:0000269|PubMed:25704634, ECO:0000269|PubMed:9452121"
FT /id="VAR_000739"
FT VARIANT 919
FT /note="R -> W (in WD; dbSNP:rs121907993)"
FT /evidence="ECO:0000269|PubMed:17949296,
FT ECO:0000269|PubMed:23333878, ECO:0000269|PubMed:23518715,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000740"
FT VARIANT 921
FT /note="S -> N (in WD; dbSNP:rs1230241288)"
FT /evidence="ECO:0000269|PubMed:9671269"
FT /id="VAR_000741"
FT VARIANT 921
FT /note="S -> R (in WD; unknown pathological significance;
FT dbSNP:rs1052485948)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076740"
FT VARIANT 929
FT /note="I -> V (in dbSNP:rs534960245)"
FT /evidence="ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:23235335"
FT /id="VAR_076741"
FT VARIANT 933
FT /note="T -> P (in WD; unknown pathological significance;
FT dbSNP:rs1555288410)"
FT /evidence="ECO:0000269|PubMed:9671269"
FT /id="VAR_000742"
FT VARIANT 935
FT /note="T -> M (in WD; dbSNP:rs750019452)"
FT /evidence="ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:14986826, ECO:0000269|PubMed:16649058,
FT ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:24476933"
FT /id="VAR_000743"
FT VARIANT 936
FT /note="L -> V (in WD; unknown pathological significance;
FT dbSNP:rs367855110)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076701"
FT VARIANT 939
FT /note="W -> C (in WD; dbSNP:rs1057517310)"
FT /evidence="ECO:0000269|PubMed:22484412"
FT /id="VAR_076813"
FT VARIANT 943
FT /note="G -> C (in WD; dbSNP:rs28942076)"
FT /evidence="ECO:0000269|PubMed:16088907"
FT /id="VAR_044468"
FT VARIANT 943
FT /note="G -> D (in WD; dbSNP:rs779323689)"
FT /evidence="ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:14966923, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:23235335"
FT /id="VAR_000744"
FT VARIANT 943
FT /note="G -> S (in WD; no effect on copper transport
FT activity; normally localized to TGN network but unable to
FT redistribute to cytoplasmic vesicles in response to copper;
FT dbSNP:rs28942076)"
FT /evidence="ECO:0000269|PubMed:10942420,
FT ECO:0000269|PubMed:15952988, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:23333878, ECO:0000269|PubMed:9837819"
FT /id="VAR_000745"
FT VARIANT 949
FT /note="V -> G (in WD; dbSNP:rs1169959260)"
FT /evidence="ECO:0000269|PubMed:15024742,
FT ECO:0000269|PubMed:9887381"
FT /id="VAR_023026"
FT VARIANT 952
FT /note="R -> K (in dbSNP:rs732774)"
FT /evidence="ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:18373411, ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:7833924, ECO:0000269|PubMed:8298639,
FT ECO:0000269|Ref.2"
FT /id="VAR_000746"
FT VARIANT 967
FT /note="I -> F (in WD; dbSNP:rs60003608)"
FT /evidence="ECO:0000269|PubMed:8938442"
FT /id="VAR_010013"
FT VARIANT 969
FT /note="R -> Q (in WD; decreased copper transport activity;
FT increased ATPase activity; no effect on localization;
FT dbSNP:rs121907996)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:11216666, ECO:0000269|PubMed:11690702,
FT ECO:0000269|PubMed:15967699, ECO:0000269|PubMed:16207219,
FT ECO:0000269|PubMed:21645214, ECO:0000269|PubMed:22240481,
FT ECO:0000269|PubMed:23333878, ECO:0000269|PubMed:8533760,
FT ECO:0000269|PubMed:9482578"
FT /id="VAR_000747"
FT VARIANT 969
FT /note="R -> W (in WD; unknown pathological significance;
FT dbSNP:rs774028495)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076768"
FT VARIANT 971
FT /note="A -> V (in WD; dbSNP:rs770340441)"
FT /evidence="ECO:0000269|PubMed:18373411"
FT /id="VAR_058927"
FT VARIANT 974
FT /note="T -> M (in WD; dbSNP:rs201061621)"
FT /evidence="ECO:0000269|PubMed:18373411"
FT /id="VAR_058928"
FT VARIANT 975
FT /note="S -> Y (in WD; dbSNP:rs778163447)"
FT /evidence="ECO:0000269|PubMed:14986826,
FT ECO:0000269|PubMed:23235335"
FT /id="VAR_023027"
FT VARIANT 977
FT /note="T -> M (in WD; loss of copper transport activity;
FT dbSNP:rs72552255)"
FT /evidence="ECO:0000269|PubMed:15952988,
FT ECO:0000269|PubMed:15967699, ECO:0000269|PubMed:16283883,
FT ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:21682854, ECO:0000269|PubMed:23518715,
FT ECO:0000269|PubMed:8938442, ECO:0000269|PubMed:9837819"
FT /id="VAR_000748"
FT VARIANT 980
FT /note="C -> Y (in WD; unknown pathological significance;
FT dbSNP:rs1038582488)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076742"
FT VARIANT 982
FT /note="A -> T (in WD; unknown pathological significance;
FT dbSNP:rs750407121)"
FT /evidence="ECO:0000269|PubMed:24476933"
FT /id="VAR_077616"
FT VARIANT 982
FT /note="A -> V (in WD; unknown pathological significance;
FT dbSNP:rs1487547257)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076769"
FT VARIANT 985
FT /note="C -> Y (in WD)"
FT /evidence="ECO:0000269|PubMed:10447265"
FT /id="VAR_009012"
FT VARIANT 987
FT /note="L -> P (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076743"
FT VARIANT 988
FT /note="G -> R (in WD; dbSNP:rs199623434)"
FT /evidence="ECO:0000269|PubMed:16283883"
FT /id="VAR_044469"
FT VARIANT 990
FT /note="A -> P (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25982861"
FT /id="VAR_076814"
FT VARIANT 991
FT /note="T -> M (in WD; yeast complementation assays show
FT that the variant mildly rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs41292782)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:20333758,
FT ECO:0000269|PubMed:23518715"
FT /id="VAR_044470"
FT VARIANT 992
FT /note="P -> H (in WD; dbSNP:rs201038679)"
FT /evidence="ECO:0000269|PubMed:15811015"
FT /id="VAR_044471"
FT VARIANT 992
FT /note="P -> L (in WD; common mutation; decreased copper
FT transport activity; no effect on ATPase activity;
FT dbSNP:rs201038679)"
FT /evidence="ECO:0000269|PubMed:11690702,
FT ECO:0000269|PubMed:14986826, ECO:0000269|PubMed:16283883,
FT ECO:0000269|PubMed:16649058, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:23235335,
FT ECO:0000269|PubMed:25704634, ECO:0000269|PubMed:28856630,
FT ECO:0000269|PubMed:9671269, ECO:0000269|PubMed:9837819"
FT /id="VAR_000749"
FT VARIANT 995
FT /note="V -> A (in WD; unknown pathological significance; no
FT effect on copper transport activity; dbSNP:rs777791532)"
FT /evidence="ECO:0000269|PubMed:23518715,
FT ECO:0000269|PubMed:9837819"
FT /id="VAR_000750"
FT VARIANT 996
FT /note="M -> T (in WD; dbSNP:rs770782111)"
FT /evidence="ECO:0000269|PubMed:16088907"
FT /id="VAR_044472"
FT VARIANT 998
FT /note="G -> D (in WD)"
FT /evidence="ECO:0000269|PubMed:21682854"
FT /id="VAR_067336"
FT VARIANT 1000
FT /note="G -> R (in WD; yeast complementation assays show
FT that the variant does not rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs751078884)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:20333758"
FT /id="VAR_044473"
FT VARIANT 1003
FT /note="A -> T (in WD; dbSNP:rs201497300)"
FT /evidence="ECO:0000269|PubMed:10790207,
FT ECO:0000269|PubMed:15811015, ECO:0000269|PubMed:16207219,
FT ECO:0000269|PubMed:23333878, ECO:0000269|PubMed:9671269"
FT /id="VAR_000751"
FT VARIANT 1003
FT /note="A -> V (in WD; dbSNP:rs775055397)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:23333878, ECO:0000269|PubMed:25982861"
FT /id="VAR_009013"
FT VARIANT 1004
FT /note="Q -> P (in WD; dbSNP:rs587783307)"
FT /evidence="ECO:0000269|PubMed:18373411"
FT /id="VAR_058929"
FT VARIANT 1010
FT /note="K -> E (in WD; unknown pathological significance;
FT dbSNP:rs1414727042)"
FT /evidence="ECO:0000269|PubMed:28856630"
FT /id="VAR_079550"
FT VARIANT 1010
FT /note="K -> R (in WD; unknown pathological significance;
FT dbSNP:rs747584649)"
FT /evidence="ECO:0000269|PubMed:25982861"
FT /id="VAR_076815"
FT VARIANT 1010
FT /note="K -> T (in WD; yeast complementation assays show
FT that the variant does not rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs747584649)"
FT /evidence="ECO:0000269|PubMed:21645214"
FT /id="VAR_076744"
FT VARIANT 1012
FT /note="G -> R (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076770"
FT VARIANT 1012
FT /note="G -> V (in WD; unknown pathological significance;
FT dbSNP:rs772089544)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076771"
FT VARIANT 1017
FT /note="M -> I (in WD; unknown pathological significance;
FT dbSNP:rs755851188)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076702"
FT VARIANT 1018
FT /note="A -> V (in WD; dbSNP:rs371840514)"
FT /evidence="ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:9671269"
FT /id="VAR_000752"
FT VARIANT 1021
FT /note="I -> V (in WD; unknown pathological significance;
FT dbSNP:rs776490710)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076703"
FT VARIANT 1024
FT /note="V -> A (in WD; unknown pathological significance;
FT dbSNP:rs1416453532)"
FT /evidence="ECO:0000269|PubMed:21645214"
FT /id="VAR_076745"
FT VARIANT 1029
FT /note="T -> I (in WD; dbSNP:rs1555286628)"
FT /evidence="ECO:0000269|PubMed:10453196,
FT ECO:0000269|PubMed:21645214"
FT /id="VAR_044474"
FT VARIANT 1031
FT /note="T -> A (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:17823867,
FT ECO:0000269|PubMed:21645214"
FT /id="VAR_076746"
FT VARIANT 1031
FT /note="T -> I (in WD)"
FT /evidence="ECO:0000269|PubMed:9887381"
FT /id="VAR_010014"
FT VARIANT 1033
FT /note="T -> A (in WD; dbSNP:rs1555286620)"
FT /id="VAR_009014"
FT VARIANT 1033
FT /note="T -> S (in WD)"
FT /evidence="ECO:0000269|PubMed:15967699"
FT /id="VAR_023028"
FT VARIANT 1035
FT /note="G -> V (in WD; dbSNP:rs753594031)"
FT /evidence="ECO:0000269|PubMed:10453196,
FT ECO:0000269|PubMed:21645214"
FT /id="VAR_000753"
FT VARIANT 1036
FT /note="V -> I (in WD; copper ion transmembrane transporter
FT activity; dbSNP:rs761147984)"
FT /evidence="ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:26004889"
FT /id="VAR_075337"
FT VARIANT 1038
FT /note="R -> K (in WD; dbSNP:rs59959366)"
FT /evidence="ECO:0000269|PubMed:8980283"
FT /id="VAR_010015"
FT VARIANT 1041
FT /note="R -> P (in WD)"
FT /evidence="ECO:0000269|PubMed:10194254,
FT ECO:0000269|PubMed:10544227, ECO:0000269|PubMed:11405812"
FT /id="VAR_009015"
FT VARIANT 1041
FT /note="R -> W (in WD; unknown pathological significance; no
FT effect on copper transport activity; dbSNP:rs746485916)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:15967699, ECO:0000269|PubMed:18203200,
FT ECO:0000269|PubMed:23333878, ECO:0000269|PubMed:23518715,
FT ECO:0000269|PubMed:25982861, ECO:0000269|PubMed:9671269"
FT /id="VAR_000754"
FT VARIANT 1043
FT /note="L -> P (in WD; yeast complementation assays show
FT that the variant does not rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs1412025509)"
FT /evidence="ECO:0000269|PubMed:20333758,
FT ECO:0000269|PubMed:25982861"
FT /id="VAR_000755"
FT VARIANT 1052
FT /note="P -> L (in WD; loss of copper transport activity; no
FT effect on ATPase activity; dbSNP:rs778543794)"
FT /evidence="ECO:0000269|PubMed:22240481"
FT /id="VAR_009016"
FT VARIANT 1058
FT /note="A -> V (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076704"
FT VARIANT 1061
FT /note="G -> E (in WD; dbSNP:rs764131178)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:11216666, ECO:0000269|PubMed:15952988,
FT ECO:0000269|PubMed:25982861"
FT /id="VAR_009017"
FT VARIANT 1063
FT /note="A -> V (in WD; dbSNP:rs587783309)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:15967699, ECO:0000269|PubMed:21682854"
FT /id="VAR_009018"
FT VARIANT 1064
FT /note="E -> A (in WD; does not bind ATP; the mutant is
FT stable and is properly targeted to the TGN;
FT dbSNP:rs374094065)"
FT /evidence="ECO:0000269|PubMed:21398519,
FT ECO:0000269|PubMed:9482578"
FT /id="VAR_000756"
FT VARIANT 1064
FT /note="E -> K (in WD; loss of copper transport activity;
FT loss of ATPase activity; dbSNP:rs376910645)"
FT /evidence="ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:18203200,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:8533760"
FT /id="VAR_000757"
FT VARIANT 1065
FT /note="A -> P (in WD)"
FT /id="VAR_044475"
FT VARIANT 1068
FT /note="E -> G (in WD; common mutation; dbSNP:rs1555286478)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_009019"
FT VARIANT 1069
FT /note="H -> Q (in WD; common mutation; decreased copper
FT transport activity; loss of ATPase activity; cannot form an
FT acylphosphate intermediate during catalysis; does not alter
FT the folding of the nucleotide-binding domain; decreased
FT stability; does not localizes to late endosomes;
FT dbSNP:rs76151636)"
FT /evidence="ECO:0000269|PubMed:10051024,
FT ECO:0000269|PubMed:10544227, ECO:0000269|PubMed:11216666,
FT ECO:0000269|PubMed:11231950, ECO:0000269|PubMed:11243728,
FT ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:12551905,
FT ECO:0000269|PubMed:15952988, ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:16207219, ECO:0000269|PubMed:16283883,
FT ECO:0000269|PubMed:21398519, ECO:0000269|PubMed:21682854,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:22763723,
FT ECO:0000269|PubMed:23333878, ECO:0000269|PubMed:23518715,
FT ECO:0000269|PubMed:8298641, ECO:0000269|PubMed:9482578,
FT ECO:0000269|PubMed:9887381"
FT /id="VAR_000758"
FT VARIANT 1070
FT /note="P -> S (in WD; unknown pathological significance;
FT dbSNP:rs1423701688)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076705"
FT VARIANT 1074
FT /note="A -> V (in WD; unknown pathological significance;
FT dbSNP:rs1206016866)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076706"
FT VARIANT 1083
FT /note="L -> F (in WD; decreased copper transport activity;
FT no effect on ATPase activity; decreased localization to the
FT TGN; dbSNP:rs1286080173)"
FT /evidence="ECO:0000269|PubMed:10790207,
FT ECO:0000269|PubMed:11954751, ECO:0000269|PubMed:12544487,
FT ECO:0000269|PubMed:18203200, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:9554743"
FT /id="VAR_000759"
FT VARIANT 1089
FT /note="G -> E (in WD; dbSNP:rs1555285911)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_000760"
FT VARIANT 1089
FT /note="G -> V (in WD)"
FT /evidence="ECO:0000269|PubMed:9671269"
FT /id="VAR_000761"
FT VARIANT 1091
FT /note="C -> Y (in WD; unknown pathological significance;
FT dbSNP:rs778825095)"
FT /evidence="ECO:0000269|PubMed:21645214"
FT /id="VAR_076747"
FT VARIANT 1094
FT /note="F -> L (in WD; dbSNP:rs1397083296)"
FT /evidence="ECO:0000269|PubMed:15024742"
FT /id="VAR_023029"
FT VARIANT 1095
FT /note="Q -> P (in WD; dbSNP:rs1555285891)"
FT /evidence="ECO:0000269|PubMed:16283883"
FT /id="VAR_009020"
FT VARIANT 1098
FT /note="P -> R (in WD)"
FT /evidence="ECO:0000269|PubMed:14986826"
FT /id="VAR_023030"
FT VARIANT 1099
FT /note="G -> S (in WD; dbSNP:rs761632029)"
FT /evidence="ECO:0000269|PubMed:11216666,
FT ECO:0000269|PubMed:15952988, ECO:0000269|PubMed:17949296"
FT /id="VAR_023031"
FT VARIANT 1101
FT /note="G -> R (in WD; yeast complementation assays show
FT that the variant does not rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs786204483)"
FT /evidence="ECO:0000269|PubMed:20333758,
FT ECO:0000269|PubMed:25982861"
FT /id="VAR_000762"
FT VARIANT 1102
FT /note="I -> T (in WD; yeast complementation assays show
FT that the variant intermediately rescue iron-uptake
FT deficiency of yeast mutant ccc2; dbSNP:rs560952220)"
FT /evidence="ECO:0000269|PubMed:11243728,
FT ECO:0000269|PubMed:15811015, ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:20333758"
FT /id="VAR_000763"
FT VARIANT 1104
FT /note="C -> F (in WD)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_009021"
FT VARIANT 1104
FT /note="C -> S (in WD)"
FT /evidence="ECO:0000269|PubMed:25982861"
FT /id="VAR_076816"
FT VARIANT 1104
FT /note="C -> Y (in WD; dbSNP:rs764041557)"
FT /evidence="ECO:0000269|PubMed:15811015"
FT /id="VAR_044476"
FT VARIANT 1106
FT /note="V -> D (in WD; marked impairment in copper
FT transport; dbSNP:rs775541743)"
FT /evidence="ECO:0000269|PubMed:18203200,
FT ECO:0000269|PubMed:8938442"
FT /id="VAR_010017"
FT VARIANT 1106
FT /note="V -> I (in WD; unknown pathological significance;
FT dbSNP:rs541208827)"
FT /evidence="ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:14966923, ECO:0000269|PubMed:21645214"
FT /id="VAR_044477"
FT VARIANT 1109
FT /note="V -> M (in dbSNP:rs759109027)"
FT /evidence="ECO:0000269|PubMed:9554743"
FT /id="VAR_000764"
FT VARIANT 1111
FT /note="G -> D (in WD; dbSNP:rs182659444)"
FT /evidence="ECO:0000269|PubMed:15967699"
FT /id="VAR_023032"
FT VARIANT 1113
FT /note="L -> M (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25982861"
FT /id="VAR_076817"
FT VARIANT 1136
FT /note="E -> K (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25704634"
FT /id="VAR_077617"
FT VARIANT 1140
FT /note="V -> A (no effect on copper transport activity;
FT dbSNP:rs1801249)"
FT /evidence="ECO:0000269|PubMed:10721669,
FT ECO:0000269|PubMed:10790207, ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:14966923, ECO:0000269|PubMed:14986826,
FT ECO:0000269|PubMed:15952988, ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:17823867, ECO:0000269|PubMed:18203200,
FT ECO:0000269|PubMed:18373411, ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:24303094, ECO:0000269|PubMed:9482578,
FT ECO:0000269|PubMed:9554743, ECO:0000269|PubMed:9887381,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.9"
FT /id="VAR_000765"
FT VARIANT 1142
FT /note="Q -> H (in WD; dbSNP:rs778749563)"
FT /evidence="ECO:0000269|PubMed:11405812"
FT /id="VAR_000766"
FT VARIANT 1143
FT /note="T -> N (in dbSNP:rs587783313)"
FT /evidence="ECO:0000269|PubMed:14986826"
FT /id="VAR_023033"
FT VARIANT 1146
FT /note="V -> M (in WD; dbSNP:rs1213481140)"
FT /evidence="ECO:0000269|PubMed:9671269"
FT /id="VAR_000767"
FT VARIANT 1148
FT /note="I -> T (in WD; yeast complementation assays show
FT that the variant mildly rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs60431989)"
FT /evidence="ECO:0000269|PubMed:10447265,
FT ECO:0000269|PubMed:11216666, ECO:0000269|PubMed:14986826,
FT ECO:0000269|PubMed:15845031, ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:20333758, ECO:0000269|PubMed:21645214"
FT /id="VAR_000768"
FT VARIANT 1149
FT /note="G -> A (in WD; dbSNP:rs1566462533)"
FT /evidence="ECO:0000269|PubMed:18373411"
FT /id="VAR_058930"
FT VARIANT 1149
FT /note="G -> E (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25704634"
FT /id="VAR_077618"
FT VARIANT 1151
FT /note="R -> C (in WD; yeast complementation assays show
FT that the variant does not rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs755554442)"
FT /evidence="ECO:0000269|PubMed:17949296,
FT ECO:0000269|PubMed:21645214, ECO:0000269|PubMed:23235335,
FT ECO:0000269|PubMed:23333878"
FT /id="VAR_075338"
FT VARIANT 1151
FT /note="R -> H (in WD; dbSNP:rs377297166)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_009022"
FT VARIANT 1153
FT /note="W -> C (in WD; dbSNP:rs1330620114)"
FT /id="VAR_000769"
FT VARIANT 1153
FT /note="W -> R (in WD)"
FT /evidence="ECO:0000269|PubMed:8938442"
FT /id="VAR_010018"
FT VARIANT 1164
FT /note="D -> N (in WD; dbSNP:rs867107727)"
FT /evidence="ECO:0000269|PubMed:18373411"
FT /id="VAR_058931"
FT VARIANT 1168
FT /note="A -> S (in WD; dbSNP:rs777879359)"
FT /evidence="ECO:0000269|PubMed:12544487,
FT ECO:0000269|PubMed:21645214"
FT /id="VAR_023034"
FT VARIANT 1169
FT /note="M -> T (in WD; dbSNP:rs1555285311)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_009023"
FT VARIANT 1169
FT /note="M -> V (in WD; moderate impairment in copper
FT transport; dbSNP:rs749085322)"
FT /evidence="ECO:0000269|PubMed:18203200"
FT /id="VAR_000770"
FT VARIANT 1173
FT /note="E -> G (in WD; yeast complementation assays show
FT that the variant fully rescue iron-uptake deficiency of
FT yeast mutant ccc2)"
FT /evidence="ECO:0000269|PubMed:18373411,
FT ECO:0000269|PubMed:20333758"
FT /id="VAR_058932"
FT VARIANT 1173
FT /note="E -> K (in WD; dbSNP:rs756029120)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:11405812, ECO:0000269|PubMed:14986826"
FT /id="VAR_009024"
FT VARIANT 1176
FT /note="G -> E (in WD; yeast complementation assays show
FT that the variant mildly rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs1318758433)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:20333758"
FT /id="VAR_044478"
FT VARIANT 1176
FT /note="G -> R (in WD; dbSNP:rs137853279)"
FT /evidence="ECO:0000269|PubMed:15845031,
FT ECO:0000269|PubMed:15967699, ECO:0000269|PubMed:9887381"
FT /id="VAR_010019"
FT VARIANT 1178
FT /note="T -> A (in WD; unknown pathological significance;
FT dbSNP:rs1387431334)"
FT /evidence="ECO:0000269|PubMed:17823867,
FT ECO:0000269|PubMed:23235335"
FT /id="VAR_076748"
FT VARIANT 1183
FT /note="A -> G (in WD; dbSNP:rs587783315)"
FT /evidence="ECO:0000269|PubMed:12325021,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000771"
FT VARIANT 1183
FT /note="A -> T (in WD; unknown pathological significance; no
FT effect on copper transport activity)"
FT /evidence="ECO:0000269|PubMed:18203200,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000772"
FT VARIANT 1186
FT /note="G -> C (in WD)"
FT /id="VAR_000773"
FT VARIANT 1186
FT /note="G -> S (in WD; unknown pathological significance; no
FT effect on copper transport activity; dbSNP:rs786204547)"
FT /evidence="ECO:0000269|PubMed:10453196,
FT ECO:0000269|PubMed:10790207, ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:18203200, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:9452121"
FT /id="VAR_000774"
FT VARIANT 1202
FT /note="A -> G (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23275100"
FT /id="VAR_076749"
FT VARIANT 1207
FT /note="H -> R (in dbSNP:rs7334118)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:17823867, ECO:0000269|PubMed:21682854,
FT ECO:0000269|PubMed:23333878"
FT /id="VAR_009025"
FT VARIANT 1213
FT /note="G -> V (in WD; loss of copper transport activity; no
FT effect on ATPase activity; dbSNP:rs1555284582)"
FT /evidence="ECO:0000269|PubMed:22240481,
FT ECO:0000269|PubMed:9482578"
FT /id="VAR_000775"
FT VARIANT 1216..1217
FT /note="Missing (in WD)"
FT /evidence="ECO:0000269|PubMed:9482578"
FT /id="VAR_000777"
FT VARIANT 1216
FT /note="V -> M (in WD; dbSNP:rs776280797)"
FT /evidence="ECO:0000269|PubMed:14966923,
FT ECO:0000269|PubMed:15952988, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000776"
FT VARIANT 1217..1218
FT /note="Missing (in WD)"
FT /evidence="ECO:0000269|PubMed:16207219"
FT /id="VAR_044479"
FT VARIANT 1220
FT /note="T -> M (in WD; dbSNP:rs193922107)"
FT /evidence="ECO:0000269|PubMed:16283883,
FT ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:22763723"
FT /id="VAR_000778"
FT VARIANT 1221
FT /note="G -> E (in WD; dbSNP:rs1486594906)"
FT /evidence="ECO:0000269|PubMed:16088907"
FT /id="VAR_044480"
FT VARIANT 1222
FT /note="D -> N (in WD)"
FT /evidence="ECO:0000269|PubMed:10453196"
FT /id="VAR_044481"
FT VARIANT 1222
FT /note="D -> V (in WD; decreased copper transport activity;
FT loss of ATPase activity)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:22240481"
FT /id="VAR_010020"
FT VARIANT 1222
FT /note="D -> Y (in WD)"
FT /id="VAR_000779"
FT VARIANT 1228
FT /note="R -> T (in WD; yeast complementation assays show
FT that the variant fully rescue iron-uptake deficiency of
FT yeast mutant ccc2)"
FT /evidence="ECO:0000269|PubMed:18373411,
FT ECO:0000269|PubMed:20333758"
FT /id="VAR_058933"
FT VARIANT 1230
FT /note="I -> V (in WD; dbSNP:rs200911496)"
FT /evidence="ECO:0000269|PubMed:18373411"
FT /id="VAR_058934"
FT VARIANT 1232
FT /note="T -> P (in WD; dbSNP:rs568009639)"
FT /evidence="ECO:0000269|PubMed:15024742,
FT ECO:0000269|PubMed:15952988"
FT /id="VAR_023035"
FT VARIANT 1239
FT /note="V -> G (in WD; yeast complementation assays show
FT that the variant does not rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs374628199)"
FT /evidence="ECO:0000269|PubMed:20333758"
FT /id="VAR_009026"
FT VARIANT 1243
FT /note="V -> L (in dbSNP:rs1277243795)"
FT /evidence="ECO:0000269|PubMed:23333878"
FT /id="VAR_075339"
FT VARIANT 1245
FT /note="P -> S (in dbSNP:rs587783316)"
FT /evidence="ECO:0000269|PubMed:14986826"
FT /id="VAR_023036"
FT VARIANT 1245
FT /note="P -> T (in WD)"
FT /evidence="ECO:0000269|PubMed:23333878"
FT /id="VAR_075340"
FT VARIANT 1248
FT /note="K -> N (in WD)"
FT /evidence="ECO:0000269|PubMed:14986826"
FT /id="VAR_023037"
FT VARIANT 1250
FT /note="A -> G (in WD; unknown pathological significance;
FT dbSNP:rs372042739)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076707"
FT VARIANT 1252
FT /note="V -> I (in WD)"
FT /id="VAR_044482"
FT VARIANT 1255
FT /note="L -> I (in WD)"
FT /evidence="ECO:0000269|PubMed:12544487"
FT /id="VAR_023038"
FT VARIANT 1256
FT /note="Q -> R (in WD; dbSNP:rs1555283946)"
FT /evidence="ECO:0000269|PubMed:15811015"
FT /id="VAR_044483"
FT VARIANT 1262
FT /note="V -> F (in WD; dbSNP:rs769484789)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_009027"
FT VARIANT 1266
FT /note="G -> E (in WD; unknown pathological significance;
FT dbSNP:rs1566444586)"
FT /evidence="ECO:0000269|PubMed:23235335"
FT /id="VAR_076750"
FT VARIANT 1266
FT /note="G -> R (in WD; common mutation; dbSNP:rs121907992)"
FT /evidence="ECO:0000269|PubMed:11243728,
FT ECO:0000269|PubMed:23518715"
FT /id="VAR_009028"
FT VARIANT 1266
FT /note="G -> V (in WD; decreased copper transport activity;
FT loss of ATPase activity)"
FT /evidence="ECO:0000269|PubMed:22240481"
FT /id="VAR_000781"
FT VARIANT 1267
FT /note="D -> A (in WD; dbSNP:rs1555283916)"
FT /evidence="ECO:0000269|PubMed:10790207,
FT ECO:0000269|PubMed:12544487, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:9452121"
FT /id="VAR_000782"
FT VARIANT 1267
FT /note="D -> V (in WD; yeast complementation assays show
FT that the variant does not rescue iron-uptake deficiency of
FT yeast mutant ccc2)"
FT /evidence="ECO:0000269|PubMed:18373411,
FT ECO:0000269|PubMed:20333758"
FT /id="VAR_058935"
FT VARIANT 1268
FT /note="G -> R (in WD; unknown pathological significance;
FT dbSNP:rs1314712150)"
FT /evidence="ECO:0000269|PubMed:16649058"
FT /id="VAR_076751"
FT VARIANT 1270
FT /note="N -> S (in WD; loss of copper transport activity;
FT increased ATPase activity; does not affect localization to
FT late endosomes; dbSNP:rs121907990)"
FT /evidence="ECO:0000269|PubMed:10790207,
FT ECO:0000269|PubMed:11231950, ECO:0000269|PubMed:11405812,
FT ECO:0000269|PubMed:11690702, ECO:0000269|PubMed:12544487,
FT ECO:0000269|PubMed:16207219, ECO:0000269|PubMed:16649058,
FT ECO:0000269|PubMed:21645214, ECO:0000269|PubMed:22240481,
FT ECO:0000269|PubMed:23235335, ECO:0000269|PubMed:23333878,
FT ECO:0000269|PubMed:23518715, ECO:0000269|PubMed:25982861,
FT ECO:0000269|PubMed:8298641, ECO:0000269|PubMed:8533760,
FT ECO:0000269|PubMed:9452121"
FT /id="VAR_000783"
FT VARIANT 1271
FT /note="D -> N (in WD)"
FT /evidence="ECO:0000269|PubMed:15967699"
FT /id="VAR_023039"
FT VARIANT 1273
FT /note="P -> L (in WD; decreased copper transport activity;
FT increased ATPase activity; dbSNP:rs758355520)"
FT /evidence="ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:16283883, ECO:0000269|PubMed:21645214,
FT ECO:0000269|PubMed:21682854, ECO:0000269|PubMed:22240481,
FT ECO:0000269|PubMed:23235335"
FT /id="VAR_000784"
FT VARIANT 1278
FT /note="A -> V (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:9222767"
FT /id="VAR_000785"
FT VARIANT 1279
FT /note="D -> G (in WD; dbSNP:rs778914828)"
FT /evidence="ECO:0000269|PubMed:11043508"
FT /id="VAR_023040"
FT VARIANT 1279
FT /note="D -> Y (in WD)"
FT /evidence="ECO:0000269|PubMed:16207219"
FT /id="VAR_044484"
FT VARIANT 1281
FT /note="G -> D (in WD; unknown pathological significance;
FT dbSNP:rs755202606)"
FT /evidence="ECO:0000269|PubMed:22484412"
FT /id="VAR_076818"
FT VARIANT 1285..1292
FT /note="Missing (in WD)"
FT /evidence="ECO:0000269|PubMed:9222767"
FT /id="VAR_000786"
FT VARIANT 1287
FT /note="G -> S (in WD; yeast complementation assays show
FT that the variant mildly rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs762866453)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:20333758"
FT /id="VAR_044485"
FT VARIANT 1288
FT /note="T -> M (in WD; unknown pathological significance;
FT dbSNP:rs373748155)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076772"
FT VARIANT 1293
FT /note="E -> K (in WD; unknown pathological significance;
FT dbSNP:rs776300396)"
FT /evidence="ECO:0000269|PubMed:22484412,
FT ECO:0000269|PubMed:25982861"
FT /id="VAR_076819"
FT VARIANT 1295
FT /note="A -> D (in WD; yeast complementation assays show
FT that the variant does not rescue iron-uptake deficiency of
FT yeast mutant ccc2; dbSNP:rs1340942427)"
FT /evidence="ECO:0000269|PubMed:21645214"
FT /id="VAR_076752"
FT VARIANT 1296
FT /note="D -> N (in WD; dbSNP:rs199821556)"
FT /evidence="ECO:0000269|PubMed:11954751"
FT /id="VAR_044486"
FT VARIANT 1297
FT /note="V -> I (in dbSNP:rs148399850)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_009029"
FT VARIANT 1297
FT /note="Missing (in WD)"
FT /evidence="ECO:0000269|PubMed:10721669"
FT /id="VAR_044487"
FT VARIANT 1298
FT /note="V -> I (in WD; unknown pathological significance;
FT dbSNP:rs753044473)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076708"
FT VARIANT 1298
FT /note="V -> L (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076709"
FT VARIANT 1305
FT /note="L -> P (in WD; dbSNP:rs377144951)"
FT /evidence="ECO:0000269|PubMed:11180609,
FT ECO:0000269|PubMed:15967699"
FT /id="VAR_023041"
FT VARIANT 1310
FT /note="S -> R (in WD; dbSNP:rs749380700)"
FT /id="VAR_000787"
FT VARIANT 1322
FT /note="R -> P (in WD; dbSNP:rs753330854)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_000788"
FT VARIANT 1327
FT /note="L -> V (in WD)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_009030"
FT VARIANT 1328
FT /note="A -> T (in WD; dbSNP:rs1333619338)"
FT /evidence="ECO:0000269|PubMed:18373411"
FT /id="VAR_058936"
FT VARIANT 1331..1465
FT /note="Missing (in WD)"
FT /evidence="ECO:0000269|PubMed:28856630"
FT /id="VAR_079551"
FT VARIANT 1331
FT /note="Y -> S (in WD; dbSNP:rs1131691741)"
FT /evidence="ECO:0000269|PubMed:16088907"
FT /id="VAR_044488"
FT VARIANT 1332
FT /note="N -> D (in WD)"
FT /evidence="ECO:0000269|PubMed:21682854"
FT /id="VAR_067337"
FT VARIANT 1332
FT /note="N -> K (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076773"
FT VARIANT 1336
FT /note="I -> T (in WD)"
FT /evidence="ECO:0000269|PubMed:10790207"
FT /id="VAR_023042"
FT VARIANT 1341
FT /note="G -> D (in WD; dbSNP:rs779494870)"
FT /evidence="ECO:0000269|PubMed:15967699,
FT ECO:0000269|PubMed:16207219, ECO:0000269|PubMed:16283883,
FT ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:21682854,
FT ECO:0000269|PubMed:9671269"
FT /id="VAR_000789"
FT VARIANT 1341
FT /note="G -> R (in WD; dbSNP:rs587783317)"
FT /evidence="ECO:0000269|PubMed:21682854"
FT /id="VAR_067338"
FT VARIANT 1341
FT /note="G -> S (in WD; dbSNP:rs587783317)"
FT /evidence="ECO:0000269|PubMed:14639035"
FT /id="VAR_044489"
FT VARIANT 1341
FT /note="G -> V (in WD)"
FT /evidence="ECO:0000269|PubMed:16088907"
FT /id="VAR_044490"
FT VARIANT 1347
FT /note="G -> S (in WD; unknown pathological significance;
FT dbSNP:rs587783318)"
FT /evidence="ECO:0000269|PubMed:24555712"
FT /id="VAR_076973"
FT VARIANT 1352
FT /note="P -> S (in WD; dbSNP:rs1388795855)"
FT /evidence="ECO:0000269|PubMed:16207219"
FT /id="VAR_044491"
FT VARIANT 1353
FT /note="W -> R (in WD; dbSNP:rs1160679283)"
FT /id="VAR_000790"
FT VARIANT 1355
FT /note="G -> C (in WD)"
FT /evidence="ECO:0000269|PubMed:15967699"
FT /id="VAR_023043"
FT VARIANT 1355
FT /note="G -> S (in WD; dbSNP:rs1555282751)"
FT /evidence="ECO:0000269|PubMed:8938442"
FT /id="VAR_010021"
FT VARIANT 1358
FT /note="A -> S (in WD)"
FT /evidence="ECO:0000269|PubMed:9671269"
FT /id="VAR_000791"
FT VARIANT 1359
FT /note="M -> I (in WD; dbSNP:rs759551693)"
FT /evidence="ECO:0000269|PubMed:18373411"
FT /id="VAR_058937"
FT VARIANT 1363
FT /note="S -> F (in WD; dbSNP:rs776848753)"
FT /evidence="ECO:0000269|PubMed:10544227"
FT /id="VAR_009031"
FT VARIANT 1368
FT /note="L -> P (in WD; dbSNP:rs749171049)"
FT /evidence="ECO:0000269|PubMed:16207219"
FT /id="VAR_044492"
FT VARIANT 1369
FT /note="S -> L (in WD; unknown pathological significance;
FT dbSNP:rs1555282678)"
FT /evidence="ECO:0000269|PubMed:17949296"
FT /id="VAR_076774"
FT VARIANT 1373
FT /note="L -> P (in WD; increased protein degradation; the
FT mutant has a diffuse cytoplasmic localization pattern and
FT is absent from TGN under conditions of low-copper levels;
FT dbSNP:rs780811477)"
FT /evidence="ECO:0000269|PubMed:10790207,
FT ECO:0000269|PubMed:21454443"
FT /id="VAR_023044"
FT VARIANT 1373
FT /note="L -> R (in WD; increased protein degradation; the
FT mutant has a diffuse cytoplasmic localization pattern and
FT is absent from TGN under conditions of low-copper levels;
FT dbSNP:rs780811477)"
FT /evidence="ECO:0000269|PubMed:15024742,
FT ECO:0000269|PubMed:21454443"
FT /id="VAR_023045"
FT VARIANT 1375
FT /note="C -> S (in WD; unknown pathological significance;
FT localized at the TGN as the wild-type under conditions of
FT low-copper levels; dbSNP:rs1365425480)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:21454443"
FT /id="VAR_044493"
FT VARIANT 1379
FT /note="P -> S (in WD; unknown pathological significance;
FT localized at the TGN as the wild-type under conditions of
FT low-copper levels; dbSNP:rs181250704)"
FT /evidence="ECO:0000269|PubMed:16088907,
FT ECO:0000269|PubMed:21454443"
FT /id="VAR_044494"
FT VARIANT 1407
FT /note="D -> E (in dbSNP:rs587783320)"
FT /evidence="ECO:0000269|PubMed:10721669"
FT /id="VAR_044495"
FT VARIANT 1431
FT /note="S -> Y (in WD; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076710"
FT VARIANT 1432
FT /note="S -> F (in WD; unknown pathological significance;
FT dbSNP:rs375692175)"
FT /evidence="ECO:0000269|PubMed:23518715"
FT /id="VAR_076711"
FT VARIANT 1434
FT /note="T -> M (in WD; unknown pathological significance;
FT localized at the TGN as the wild-type under conditions of
FT low-copper levels; dbSNP:rs60986317)"
FT /evidence="ECO:0000269|PubMed:10544227,
FT ECO:0000269|PubMed:21454443"
FT /id="VAR_009032"
FT MUTAGEN 32
FT /note="Missing: Does not affect copper-induced
FT relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 37
FT /note="F->A: Altered copper-induced relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 39
FT /note="F->W,A: Altered copper-induced relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 39
FT /note="F->Y: Does not affect copper-induced
FT relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 40
FT /note="D->A: Altered copper-induced relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 41
FT /note="N->A: Altered copper-induced relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 42
FT /note="V->A: Altered copper-induced relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 42
FT /note="V->I: Does not affect copper-induced
FT relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 43
FT /note="G->A: Altered copper-induced relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 44
FT /note="Y->F: Does not affect copper-induced
FT relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 44
FT /note="Y->W,A: Altered copper-induced relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 45
FT /note="E->A: Altered copper-induced relocalization."
FT /evidence="ECO:0000269|PubMed:19033537"
FT MUTAGEN 653
FT /note="S->F,D,E: Altered copper-induced relocalization."
FT /evidence="ECO:0000269|PubMed:24706876"
FT MUTAGEN 1027
FT /note="D->A: Loss of copper transport activity."
FT /evidence="ECO:0000269|PubMed:22240481"
FT MUTAGEN 1031
FT /note="T->S: Decreased copper transport activity with no
FT effect on ATPase activity."
FT /evidence="ECO:0000269|PubMed:22240481"
FT MUTAGEN 1069
FT /note="H->A,C: Loss of ATPase activity. Cannot form an
FT acylphosphate intermediate during catalysis. Does not alter
FT folding of the nucleotide-binding domain."
FT /evidence="ECO:0000269|PubMed:12551905"
FT CONFLICT 488
FT /note="Q -> G (in Ref. 8; AAA16173)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="N -> T (in Ref. 8; AAA16173)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="P -> L (in Ref. 8; AAA16173)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="G -> A (in Ref. 8; AAA16173)"
FT /evidence="ECO:0000305"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:2N7Y"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:2N7Y"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2N7Y"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:2N7Y"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2N7Y"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2N7Y"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:2N7Y"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2N7Y"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:2LQB"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:2LQB"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2LQB"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:2LQB"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:2LQB"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:2LQB"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2LQB"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:2LQB"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2LQB"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:2ROP"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2ROP"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:2ROP"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:2ROP"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:2ROP"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:2ROP"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2ROP"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:2ROP"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:2ROP"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:2ROP"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:6A71"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:6A71"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:6A71"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:6A71"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:6A71"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:6A71"
FT HELIX 410..419
FT /evidence="ECO:0007829|PDB:6A71"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:6A71"
FT STRAND 488..495
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:2EW9"
FT HELIX 502..511
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:2EW9"
FT TURN 523..526
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 527..532
FT /evidence="ECO:0007829|PDB:2EW9"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:2EW9"
FT HELIX 539..549
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 552..555
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 562..572
FT /evidence="ECO:0007829|PDB:2EW9"
FT HELIX 576..588
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 594..598
FT /evidence="ECO:0007829|PDB:2EW9"
FT TURN 599..602
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:2EW9"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:2EW9"
FT HELIX 615..625
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:2EW9"
FT STRAND 1039..1044
FT /evidence="ECO:0007829|PDB:2ARF"
FT TURN 1048..1050
FT /evidence="ECO:0007829|PDB:2ARF"
FT HELIX 1053..1064
FT /evidence="ECO:0007829|PDB:2ARF"
FT HELIX 1072..1083
FT /evidence="ECO:0007829|PDB:2ARF"
FT STRAND 1091..1097
FT /evidence="ECO:0007829|PDB:2ARF"
FT TURN 1098..1100
FT /evidence="ECO:0007829|PDB:2ARF"
FT STRAND 1101..1107
FT /evidence="ECO:0007829|PDB:2ARF"
FT HELIX 1109..1113
FT /evidence="ECO:0007829|PDB:2ARF"
FT STRAND 1127..1130
FT /evidence="ECO:0007829|PDB:2ARF"
FT STRAND 1143..1149
FT /evidence="ECO:0007829|PDB:2ARF"
FT HELIX 1151..1158
FT /evidence="ECO:0007829|PDB:2ARF"
FT HELIX 1163..1173
FT /evidence="ECO:0007829|PDB:2ARF"
FT TURN 1174..1176
FT /evidence="ECO:0007829|PDB:2ARF"
FT STRAND 1177..1184
FT /evidence="ECO:0007829|PDB:2ARF"
FT STRAND 1187..1194
FT /evidence="ECO:0007829|PDB:2ARF"
SQ SEQUENCE 1465 AA; 157263 MW; 419145448F9E959A CRC64;
MPEQERQITA REGASRKILS KLSLPTRAWE PAMKKSFAFD NVGYEGGLDG LGPSSQVATS
TVRILGMTCQ SCVKSIEDRI SNLKGIISMK VSLEQGSATV KYVPSVVCLQ QVCHQIGDMG
FEASIAEGKA ASWPSRSLPA QEAVVKLRVE GMTCQSCVSS IEGKVRKLQG VVRVKVSLSN
QEAVITYQPY LIQPEDLRDH VNDMGFEAAI KSKVAPLSLG PIDIERLQST NPKRPLSSAN
QNFNNSETLG HQGSHVVTLQ LRIDGMHCKS CVLNIEENIG QLLGVQSIQV SLENKTAQVK
YDPSCTSPVA LQRAIEALPP GNFKVSLPDG AEGSGTDHRS SSSHSPGSPP RNQVQGTCST
TLIAIAGMTC ASCVHSIEGM ISQLEGVQQI SVSLAEGTAT VLYNPSVISP EELRAAIEDM
GFEASVVSES CSTNPLGNHS AGNSMVQTTD GTPTSVQEVA PHTGRLPANH APDILAKSPQ
STRAVAPQKC FLQIKGMTCA SCVSNIERNL QKEAGVLSVL VALMAGKAEI KYDPEVIQPL
EIAQFIQDLG FEAAVMEDYA GSDGNIELTI TGMTCASCVH NIESKLTRTN GITYASVALA
TSKALVKFDP EIIGPRDIIK IIEEIGFHAS LAQRNPNAHH LDHKMEIKQW KKSFLCSLVF
GIPVMALMIY MLIPSNEPHQ SMVLDHNIIP GLSILNLIFF ILCTFVQLLG GWYFYVQAYK
SLRHRSANMD VLIVLATSIA YVYSLVILVV AVAEKAERSP VTFFDTPPML FVFIALGRWL
EHLAKSKTSE ALAKLMSLQA TEATVVTLGE DNLIIREEQV PMELVQRGDI VKVVPGGKFP
VDGKVLEGNT MADESLITGE AMPVTKKPGS TVIAGSINAH GSVLIKATHV GNDTTLAQIV
KLVEEAQMSK APIQQLADRF SGYFVPFIII MSTLTLVVWI VIGFIDFGVV QRYFPNPNKH
ISQTEVIIRF AFQTSITVLC IACPCSLGLA TPTAVMVGTG VAAQNGILIK GGKPLEMAHK
IKTVMFDKTG TITHGVPRVM RVLLLGDVAT LPLRKVLAVV GTAEASSEHP LGVAVTKYCK
EELGTETLGY CTDFQAVPGC GIGCKVSNVE GILAHSERPL SAPASHLNEA GSLPAEKDAV
PQTFSVLIGN REWLRRNGLT ISSDVSDAMT DHEMKGQTAI LVAIDGVLCG MIAIADAVKQ
EAALAVHTLQ SMGVDVVLIT GDNRKTARAI ATQVGINKVF AEVLPSHKVA KVQELQNKGK
KVAMVGDGVN DSPALAQADM GVAIGTGTDV AIEAADVVLI RNDLLDVVAS IHLSKRTVRR
IRINLVLALI YNLVGIPIAA GVFMPIGIVL QPWMGSAAMA ASSVSVVLSS LQLKCYKKPD
LERYEAQAHG HMKPLTASQV SVHIGMDDRW RDSPRATPWD QVSYVSQVSL SSLTSDKPSR
HSAAADDDGD KWSLLLNGRD EEQYI
