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Copper-transporting ATPase 2 (EC 3.6.3.54) (Copper pump 2) (Wilson disease-associated protein) [Cleaved into: WND/140 kDa]

 ATP7B_HUMAN             Reviewed;        1465 AA.
P35670; Q16318; Q16319; Q4U3V3; Q59FJ9; Q5T7X7;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 4.
25-OCT-2017, entry version 200.
RecName: Full=Copper-transporting ATPase 2;
EC=3.6.3.54 {ECO:0000269|PubMed:22240481};
AltName: Full=Copper pump 2;
AltName: Full=Wilson disease-associated protein;
Contains:
RecName: Full=WND/140 kDa {ECO:0000303|PubMed:9600907};
Name=ATP7B; Synonyms=PWD, WC1, WND;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ASP-96; ARG-875
AND LYS-952.
PubMed=7833924; DOI=10.1093/hmg/3.9.1647;
Petrukhin K., Lutsenko S., Chernov I., Ross B.M., Kaplan J.H.,
Gilliam T.C.;
"Characterization of the Wilson disease gene encoding a P-type copper
transporting ATPase: genomic organization, alternative splicing, and
structure/function predictions.";
Hum. Mol. Genet. 3:1647-1656(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANTS ALA-406; LEU-456;
LYS-952 AND ALA-1140.
Carlini E.J., Booth-Genthe C.L.;
"Molecular cloning of mutant ATP7B.";
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
PubMed=10334941; DOI=10.1006/bbrc.1999.0732;
Oh W.J., Kim E.K., Park K.D., Hahn S.H., Yoo O.J.;
"Cloning and characterization of the promoter region of the Wilson
disease gene.";
Biochem. Biophys. Res. Commun. 259:206-211(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 33-1465 (ISOFORM 1), AND VARIANT
LYS-952.
PubMed=8298639; DOI=10.1038/ng1293-327;
Bull P.C., Thomas G.R., Rommens J.M., Forbes J.R., Cox D.W.;
"The Wilson disease gene is a putative copper transporting P-type
ATPase similar to the Menkes gene.";
Nat. Genet. 5:327-337(1993).
[6]
SEQUENCE REVISION.
Cox D.W.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 149-1465 (ISOFORM 2), VARIANTS WD
GLN-1069 AND SER-1270, AND VARIANT ARG-875.
PubMed=8298641; DOI=10.1038/ng1293-344;
Tanzi R.E., Petrukhin K., Chernov I., Pellequer J.L., Wasco W.,
Ross B., Romano D.M., Parano E., Pavone L., Brzustowicz L.M.,
Devoto M., Peppercorn J., Bush A.I., Sternlieb I., Pirastu M.,
Gusella J.F., Evgrafov O., Penchaszadeh G.K., Honig B., Edelman I.S.,
Soares M.B., Scheinberg I.H., Gilliam T.C.;
"The Wilson disease gene is a copper transporting ATPase with homology
to the Menkes disease gene.";
Nat. Genet. 5:344-350(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 488-837 (ISOFORM 4), AND VARIANT
ARG-832.
TISSUE=Liver;
PubMed=8250934; DOI=10.1006/bbrc.1993.2471;
Yamaguchi Y., Heiny M.E., Gitlin J.D.;
"Isolation and characterization of a human liver cDNA as a candidate
gene for Wilson disease.";
Biochem. Biophys. Res. Commun. 197:271-277(1993).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 786-1465, AND VARIANTS
ARG-832 AND ALA-1140.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS WD, AND VARIANTS.
PubMed=7626145; DOI=10.1038/ng0295-210;
Thomas G.R., Forbes J.R., Roberts E.A., Walshe J.M., Cox D.W.;
"The Wilson disease gene: spectrum of mutations and their
consequences.";
Nat. Genet. 9:210-216(1995).
[11]
ERRATUM.
Thomas G.R., Forbes J.R., Roberts E.A., Walshe J.M., Cox D.W.;
Nat. Genet. 9:451-451(1995).
[12]
ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
PubMed=9307043; DOI=10.1042/bj3260897;
Yang X.-L., Miura N., Kawarada Y., Terada K., Petrukhin K.,
Gilliam T.C., Sugiyama T.;
"Two forms of Wilson disease protein produced by alternative splicing
are localized in distinct cellular compartments.";
Biochem. J. 326:897-902(1997).
[13]
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS WD ASN-765;
VAL-776; LEU-778 AND SER-943.
PubMed=10942420; DOI=10.1093/hmg/9.13.1927;
Forbes J.R., Cox D.W.;
"Copper-dependent trafficking of Wilson disease mutant ATP7B
proteins.";
Hum. Mol. Genet. 9:1927-1935(2000).
[14]
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS WD GLN-1069 AND
SER-1270.
PubMed=11231950; DOI=10.1053/gast.2001.22543;
Harada M., Sakisaka S., Terada K., Kimura R., Kawaguchi T., Koga H.,
Kim M., Taniguchi E., Hanada S., Suganuma T., Furuta K., Sugiyama T.,
Sata M.;
"A mutation of the Wilson disease protein, ATP7B, is degraded in the
proteasomes and forms protein aggregates.";
Gastroenterology 120:967-974(2001).
[15]
MUTAGENESIS OF HIS-1069, AND CHARACTERIZATION OF VARIANT GLN-1069.
PubMed=12551905; DOI=10.1074/jbc.M300034200;
Tsivkovskii R., Efremov R.G., Lutsenko S.;
"The role of the invariant His-1069 in folding and function of the
Wilson's disease protein, the human copper-transporting ATPase
ATP7B.";
J. Biol. Chem. 278:13302-13308(2003).
[16]
SUBCELLULAR LOCATION.
PubMed=15681833; DOI=10.1016/S0002-9440(10)62272-9;
Harada M., Kawaguchi T., Kumemura H., Terada K., Ninomiya H.,
Taniguchi E., Hanada S., Baba S., Maeyama M., Koga H., Ueno T.,
Furuta K., Suganuma T., Sugiyama T., Sata M.;
"The Wilson disease protein ATP7B resides in the late endosomes with
Rab7 and the Niemann-Pick C1 protein.";
Am. J. Pathol. 166:499-510(2005).
[17]
INTERACTION WITH ZBTB16.
PubMed=16676348; DOI=10.1002/jcb.20980;
Ko J.H., Son W., Bae G.Y., Kang J.H., Oh W., Yoo O.J.;
"A new hepatocytic isoform of PLZF lacking the BTB domain interacts
with ATP7B, the Wilson disease protein, and positively regulates ERK
signal transduction.";
J. Cell. Biochem. 99:719-734(2006).
[18]
SUBCELLULAR LOCATION, INTERACTION WITH COMMD1, AND CHARACTERIZATION OF
VARIANTS WD SER-41; VAL-85; SER-486; SER-492; HIS-532; LYS-541;
ASP-591; PRO-604; GLN-616; TRP-616; ALA-626; SER-641; HIS-642 AND
ARG-645.
PubMed=17919502; DOI=10.1053/j.gastro.2007.07.020;
de Bie P., van de Sluis B., Burstein E., van de Berghe P.V.,
Muller P., Berger R., Gitlin J.D., Wijmenga C., Klomp L.W.;
"Distinct Wilson's disease mutations in ATP7B are associated with
enhanced binding to COMMD1 and reduced stability of ATP7B.";
Gastroenterology 133:1316-1326(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-478, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
CHARACTERIZATION OF VARIANTS WD ASN-765; VAL-769; VAL-776; LEU-778;
GLN-778; SER-943; MET-977 AND LEU-992, AND CHARACTERIZATION OF VARIANT
ALA-995.
PubMed=9837819; DOI=10.1086/302163;
Forbes J.R., Cox D.W.;
"Functional characterization of missense mutations in ATP7B: Wilson
disease mutation or normal variant?";
Am. J. Hum. Genet. 63:1663-1674(1998).
[21]
POSSIBLE PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
PubMed=9600907; DOI=10.1073/pnas.95.11.6004;
Lutsenko S., Cooper M.J.;
"Localization of the Wilson's disease protein product to
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 95:6004-6009(1998).
[22]
INTERACTION WITH COMMD1.
PubMed=12968035; DOI=10.1074/jbc.C300391200;
Tao T.Y., Liu F., Klomp L., Wijmenga C., Gitlin J.D.;
"The copper toxicosis gene product Murr1 directly interacts with the
Wilson disease protein.";
J. Biol. Chem. 278:41593-41596(2003).
[23]
INTERACTION WITH DCTN4.
PubMed=16554302; DOI=10.1074/jbc.M512745200;
Lim C.M., Cater M.A., Mercer J.F., La Fontaine S.;
"Copper-dependent interaction of dynactin subunit p62 with the N
terminus of ATP7B but not ATP7A.";
J. Biol. Chem. 281:14006-14014(2006).
[24]
COPPER-BINDING SITES, AND DOMAINS HMA.
PubMed=20032459; DOI=10.1074/jbc.M109.074633;
LeShane E.S., Shinde U., Walker J.M., Barry A.N., Blackburn N.J.,
Ralle M., Lutsenko S.;
"Interactions between copper-binding sites determine the redox status
and conformation of the regulatory N-terminal domain of ATP7B.";
J. Biol. Chem. 285:6327-6336(2010).
[25]
VARIANTS VAL-390; ALA-406; LEU-456; GLY-723; ARG-832; ARG-875;
VAL-929; LYS-952 AND ALA-1140, AND VARIANTS WD VAL-769; GLN-778;
LEU-778; VAL-874; GLY-919; MET-935; ASP-943; PRO-1041; ILE-1106;
HIS-1142; LYS-1173 AND SER-1270.
PubMed=11405812; DOI=10.1001/archneur.58.6.971;
Wu Z.Y., Wang N., Lin M.T., Fang L., Murong S.X., Yu L.;
"Mutation analysis and the correlation between genotype and phenotype
of Arg778Leu mutation in chinese patients with Wilson disease.";
Arch. Neurol. 58:971-976(2001).
[26]
VARIANTS WD LEU-778; MET-935; LEU-992; ARG-1268 AND SER-1270.
PubMed=16649058; DOI=10.1007/s00109-005-0036-y;
Wu Z.Y., Zhao G.X., Chen W.J., Wang N., Wan B., Lin M.T., Murong S.X.,
Yu L.;
"Mutation analysis of 218 Chinese patients with Wilson disease
revealed no correlation between the canine copper toxicosis gene MURR1
and Wilson disease.";
J. Mol. Med. 84:438-442(2006).
[27]
VARIANTS LEU-149; LEU-456; LEU-825; ALA-1140 AND ARG-1207, AND
VARIANTS WD SER-591; ALA-1031 AND ALA-1178.
PubMed=17823867; DOI=10.1007/s10571-007-9192-7;
Gupta A., Chattopadhyay I., Dey S., Nasipuri P., Das S.K.,
Gangopadhyay P.K., Ray K.;
"Molecular pathogenesis of Wilson disease among Indians: a perspective
on mutation spectrum in ATP7B gene, prevalent defects, clinical
heterogeneity and implication towards diagnosis.";
Cell. Mol. Neurobiol. 27:1023-1033(2007).
[28]
VARIANTS WD ARG-645; VAL-769; GLN-778; TRP-778; PRO-827; ALA-858;
VAL-874; PHE-899; TRP-919; MET-935; TRP-969; MET-977; VAL-982;
MET-991; ARG-1012; VAL-1012; VAL-1018; LYS-1064; SER-1099; CYS-1151;
MET-1220; MET-1288; PRO-1322; LYS-1332; ASP-1341 AND LEU-1369.
PubMed=17949296; DOI=10.1089/gte.2007.0015;
Lepori M.B., Lovicu M., Dessi V., Zappu A., Incollu S., Zancan L.,
Giacchino R., Iorio R., Vajro P., Maggiore G., Marcellini M.,
Barbera C., Pellecchia M.T., Simonetti R., Kostic V., Farci A.M.,
Solinas A., De Virgiliis S., Cao A., Loudianos G.;
"Twenty-four novel mutations in Wilson disease patients of
predominantly Italian origin.";
Genet. Test. 11:328-332(2007).
[29]
CHARACTERIZATION OF VARIANTS WD ARG-1373; PRO-1373; SER-1375; SER-1379
AND MET-1434.
PubMed=21454443; DOI=10.1152/ajpgi.00038.2011;
Braiterman L., Nyasae L., Leves F., Hubbard A.L.;
"Critical roles for the COOH terminus of the Cu-ATPase ATP7B in
protein stability, trans-Golgi network retention, copper sensing, and
retrograde trafficking.";
Am. J. Physiol. 301:G69-G81(2011).
[30]
CHARACTERIZATION OF VARIANTS WD ALA-1064 AND GLN-1069.
PubMed=21398519; DOI=10.1074/jbc.M110.198101;
Dmitriev O.Y., Bhattacharjee A., Nokhrin S., Uhlemann E.M.,
Lutsenko S.;
"Difference in stability of the N-domain underlies distinct
intracellular properties of the E1064A and H1069Q mutants of copper-
transporting ATPase ATP7B.";
J. Biol. Chem. 286:16355-16362(2011).
[31]
VARIANTS WD ARG-108; VAL-729; GLN-778; LEU-778; TRP-827; VAL-874;
ASP-891; 899-ILE--GLN-907 DEL; GLY-919; ASP-943; SER-943; GLN-969;
MET-977; LEU-992; THR-1010; ALA-1024; ILE-1029; ALA-1031; VAL-1035;
PHE-1083; TYR-1091; ILE-1106; THR-1148; CYS-1151; SER-1168; SER-1186;
MET-1216; ALA-1267; SER-1270; LEU-1273 AND ASP-1295, AND
CHARACTERIZATION OF VARIANTS WD TRP-827; THR-1010; CYS-1151 AND
ASP-1295.
PubMed=21645214; DOI=10.1111/j.1478-3231.2011.02503.x;
Lee B.H., Kim J.H., Lee S.Y., Jin H.Y., Kim K.J., Lee J.J., Park J.Y.,
Kim G.H., Choi J.H., Kim K.M., Yoo H.W.;
"Distinct clinical courses according to presenting phenotypes and
their correlations to ATP7B mutations in a large Wilson's disease
cohort.";
Liver Int. 31:831-839(2011).
[32]
CHARACTERIZATION OF VARIANT ARG-875.
PubMed=21406592; DOI=10.1073/pnas.1014959108;
Gupta A., Bhattacharjee A., Dmitriev O.Y., Nokhrin S., Braiterman L.,
Hubbard A.L., Lutsenko S.;
"Cellular copper levels determine the phenotype of the Arg875 variant
of ATP7B/Wilson disease protein.";
Proc. Natl. Acad. Sci. U.S.A. 108:5390-5395(2011).
[33]
CHARACTERIZATION OF VARIANTS WD VAL-85; SER-492; TRP-616; ALA-626;
ARG-645; SER-710; LEU-760; ASN-765; VAL-769; LEU-840; THR-857;
VAL-874; GLN-969; LEU-992; LEU-1052; LYS-1064; GLN-1069; PHE-1083;
VAL-1213; VAL-1222; ARG-1266; SER-1270 AND LEU-1273, CHARACTERIZATION
OF VARIANTS ALA-406; LEU-456 AND ARG-832, MUTAGENESIS OF ASP-1027 AND
THR-1031, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=22240481; DOI=10.1053/j.gastro.2011.12.048;
Huster D., Kuehne A., Bhattacharjee A., Raines L., Jantsch V., Noe J.,
Schirrmeister W., Sommerer I., Sabri O., Berr F., Moessner J.,
Stieger B., Caca K., Lutsenko S.;
"Diverse functional properties of Wilson disease ATP7B variants.";
Gastroenterology 142:947-956(2012).
[34]
VARIANTS WD LEU-539; SER-710; GLY-779; SER-816; GLN-1069 AND MET-1220.
PubMed=22763723; DOI=10.1038/jhg.2012.65;
Hofer H., Willheim-Polli C., Knoflach P., Gabriel C., Vogel W.,
Trauner M., Mueller T., Ferenci P.;
"Identification of a novel Wilson disease gene mutation frequent in
Upper Austria: a genetic and clinical study.";
J. Hum. Genet. 57:564-567(2012).
[35]
VARIANT WD 899-ILE--GLN-907 DEL.
PubMed=22075048; DOI=10.1016/j.jns.2011.09.007;
Lee J.Y., Kim Y.H., Kim T.W., Oh S.Y., Kim D.S., Shin B.S.;
"New novel mutation of the ATP7B gene in a family with Wilson
disease.";
J. Neurol. Sci. 313:129-131(2012).
[36]
VARIANTS WD VAL-170; HIS-765; GLU-836; CYS-939; ASP-1281 AND LYS-1293.
PubMed=22484412; DOI=10.1016/j.mcp.2012.03.007;
Lepori M.B., Zappu A., Incollu S., Dessi V., Mameli E., Demelia L.,
Nurchi A.M., Gheorghe L., Maggiore G., Sciveres M., Leuzzi V.,
Indolfi G., Bonafe L., Casali C., Angeli P., Barone P., Cao A.,
Loudianos G.;
"Mutation analysis of the ATP7B gene in a new group of Wilson's
disease patients: contribution to diagnosis.";
Mol. Cell. Probes 26:147-150(2012).
[37]
VARIANTS WD TRP-136; TRP-148; CYS-382; ALA-536; LYS-541; ILE-597;
CYS-614; SER-641; ARG-645; ILE-665; ALA-731; PRO-745; VAL-769;
TRP-778; ARG-869; TRP-919; VAL-936; MET-977; MET-991; ALA-995;
ILE-1017; VAL-1021; TRP-1041; VAL-1058; GLN-1069; SER-1070; VAL-1074;
GLY-1250; ARG-1266; SER-1270; ILE-1298; LEU-1298; TYR-1431 AND
PHE-1432.
PubMed=23518715; DOI=10.1093/brain/awt035;
Coffey A.J., Durkie M., Hague S., McLay K., Emmerson J., Lo C.,
Klaffke S., Joyce C.J., Dhawan A., Hadzic N., Mieli-Vergani G.,
Kirk R., Elizabeth Allen K., Nicholl D., Wong S., Griffiths W.,
Smithson S., Giffin N., Taha A., Connolly S., Gillett G.T., Tanner S.,
Bonham J., Sharrack B., Palotie A., Rattray M., Dalton A.,
Bandmann O.;
"A genetic study of Wilson's disease in the United Kingdom.";
Brain 136:1476-1487(2013).
[38]
VARIANT WD GLY-779.
PubMed=23159873; DOI=10.1016/j.gene.2012.10.085;
Dastsooz H., Dehghani S.M., Imanieh M.H., Haghighat M., Moini M.,
Fardaei M.;
"A new ATP7B gene mutation with severe condition in two unrelated
Iranian families with Wilson disease.";
Gene 514:48-53(2013).
[39]
VARIANTS WD ASN-44; PHE-157; GLY-606; HIS-732; PRO-732; GLY-756;
GLN-778; LEU-778; PHE-795; PRO-874; VAL-874; MET-890; GLY-919;
ARG-921; ASP-943; TYR-975; TYR-980; PRO-987; LEU-992; CYS-1151;
ALA-1178; GLU-1266; SER-1270 AND LEU-1273, AND VARIANT VAL-929.
PubMed=23235335; DOI=10.1038/jhg.2012.134;
Li K., Zhang W.M., Lin S., Wen L., Wang Z.F., Xie D., Wei M.,
Qiu Z.Q., Dai Y., Lin M.C., Kung H.F., Yao F.X.;
"Mutational analysis of ATP7B in north Chinese patients with Wilson
disease.";
J. Hum. Genet. 58:67-72(2013).
[40]
VARIANT WD GLY-1202.
PubMed=23275100; DOI=10.1007/s12519-012-0388-7;
Geng J., Wang J., Yao R.E., Liu X.Q., Fu Q.H.;
"Identification of one novel and nine recurrent mutations of the ATP7B
gene in 11 children with Wilson disease.";
World J. Pediatr. 9:158-162(2013).
[41]
VARIANT WD SER-1347.
PubMed=24555712; DOI=10.1186/1471-2350-15-22;
Forbes N., Goodwin S., Woodward K., Morgan D.G., Brady L.,
Coulthart M.B., Tarnopolsky M.A.;
"Evidence for synergistic effects of PRNP and ATP7B mutations in
severe neuropsychiatric deterioration.";
BMC Med. Genet. 15:22-22(2014).
[42]
CHARACTERIZATION OF VARIANTS WD ALA-626; TYR-639; SER-641; HIS-642;
ARG-645 AND TYR-653, MUTAGENESIS OF SER-653, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=24706876; DOI=10.1073/pnas.1314161111;
Braiterman L.T., Murthy A., Jayakanthan S., Nyasae L., Tzeng E.,
Gromadzka G., Woolf T.B., Lutsenko S., Hubbard A.L.;
"Distinct phenotype of a Wilson disease mutation reveals a novel
trafficking determinant in the copper transporter ATP7B.";
Proc. Natl. Acad. Sci. U.S.A. 111:E1364-E1373(2014).
[43]
STRUCTURE BY NMR OF 238-439, COPPER-BINDING SITES, AND INTERACTION
WITH ATOX1.
PubMed=18558714; DOI=10.1021/bi8004736;
Banci L., Bertini I., Cantini F., Rosenzweig A.C., Yatsunyk L.A.;
"Metal binding domains 3 and 4 of the Wilson disease protein: solution
structure and interaction with the copper(I) chaperone HAH1.";
Biochemistry 47:7423-7429(2008).
[44]
VARIANTS WD ALA-626; ASN-765; GLY-778; THR-857; GLN-969; LYS-1064 AND
SER-1270.
PubMed=8533760;
Figus A., Angius A., Loudianos G., Bertini C., Dessi V., Loi A.,
Deiana M., Lovicu M., Olla N., Sole G., de Virgiliis S., Lilliu F.,
Farci A.M.G., Nurchi A., Giacchino R., Barabino A., Marazzi M.,
Zancan L., Greggio N.A., Macellini M., Solinas A., Deplano A.,
Barbera C., Devoto M., Ozsoylu S., Kocak N., Akar N., Karayalcin S.,
Mokini V., Cullufi P., Balestrieri A., Cao A., Pirastu M.;
"Molecular pathology and haplotype analysis of Wilson disease in
Mediterranean populations.";
Am. J. Hum. Genet. 57:1318-1324(1995).
[45]
VARIANTS WD PHE-967; MET-977; ASP-1106; ARG-1153 AND SER-1355.
PubMed=8938442; DOI=10.1006/geno.1996.0564;
Waldenstroem E., Lagerkvist A., Dahlman T., Westermark K.,
Landegren U.;
"Efficient detection of mutations in Wilson disease by manifold
sequencing.";
Genomics 37:303-309(1996).
[46]
VARIANTS WD.
PubMed=8931691; DOI=10.1007/s004390050275;
Loudianos G., Dessi V., Angius A., Lovicu M., Loi A., Deiana M.,
Akar N., Vajro P., Figus A., Cao A., Pirastu M.;
"Wilson disease mutations associated with uncommon haplotypes in
Mediterranean patients.";
Hum. Genet. 98:640-642(1996).
[47]
VARIANTS WD GLN-778 AND LEU-778.
PubMed=8782057; DOI=10.1136/jmg.33.6.521;
Chuang L.-M., Wu H.-P., Jang M.-H., Wang T.-R., Sue W.-C., Lin B.J.,
Cox D.W., Tai T.-Y.;
"High frequency of two mutations in codon 778 in exon 8 of the ATP7B
gene in Taiwanese families with Wilson disease.";
J. Med. Genet. 33:521-523(1996).
[48]
VARIANTS WD.
PubMed=9311736; DOI=10.1086/514864;
Shah A.B., Chernov I., Zhang H.T., Ross B.M., Das K., Lutsenko S.,
Parano E., Pavone L., Evgrafov O., Ivanova-Smolenskaya I.A.,
Anneren G., Westermark K., Urrutia F.H., Penchaszadeh G.K.,
Sternlieb I., Scheinberg I.H., Gilliam T.C., Petrukhin K.;
"Identification and analysis of mutations in the Wilson disease gene
(ATP7B): population frequencies, genotype-phenotype correlation, and
functional analyses.";
Am. J. Hum. Genet. 61:317-328(1997).
[49]
VARIANT WD CYS-693.
PubMed=9772425;
Fan Y., Yang R., Yu L., Wu M., Shi S., Ren M., Han Y., Hu J., Zhao S.;
"Identification of a novel missense mutation in Wilson's disease
gene.";
Chin. Med. J. 110:887-890(1997).
[50]
VARIANTS WD VAL-1278 AND 1285-GLY--ILE-1292 DEL.
PubMed=9222767;
DOI=10.1002/(SICI)1098-1004(1997)10:1<84::AID-HUMU14>3.3.CO;2-X;
Orru S., Thomas G., Loizedda A., Cox D.W., Contu L.;
"24 bp deletion and Ala1278 to Val mutation of the ATP7B gene in a
Sardinian family with Wilson disease.";
Hum. Mutat. 10:84-85(1997).
[51]
VARIANT WD LYS-1038.
PubMed=8980283; DOI=10.1111/1523-1747.ep12285622;
Kemppainen R., Palatsi R., Kallioinen M., Oikarinen A.;
"A homozygous nonsense mutation and a combination of two mutations of
the Wilson disease gene in patients with different lysyl oxidase
activities in cultured fibroblasts.";
J. Invest. Dermatol. 108:35-39(1997).
[52]
VARIANTS WD ALA-710; CYS-741; ILE-1031; GLN-1069 AND ARG-1176, AND
VARIANTS LEU-456; GLY-949 AND ALA-1140.
PubMed=9887381;
Ha-Hao D., Hefter H., Stremmel W., Castaneda-Guillot C.,
Hernandez Hernandez A., Cox D.W., Auburger G.;
"His1069Gln and six novel Wilson disease mutations: analysis of
relevance for early diagnosis and phenotype.";
Eur. J. Hum. Genet. 6:616-623(1998).
[53]
VARIANTS WD ARG-645; ASN-765; GLN-969; ALA-1064; GLN-1069; VAL-1213
AND 1216-VAL-VAL-1217 DEL, AND VARIANTS SER-565; GLY-723; ARG-832 AND
ALA-1140.
PubMed=9482578;
DOI=10.1002/(SICI)1098-1004(1998)11:2<145::AID-HUMU7>3.0.CO;2-I;
Kalinsky H., Funes A., Zeldin A., Pel-Or Y., Korostishevsky M.,
Gershoni-Baruch R., Farrer L.A., Bonne-Tamir B.;
"Novel ATP7B mutations causing Wilson disease in several Israeli
ethnic groups.";
Hum. Mutat. 11:145-151(1998).
[54]
VARIANTS WD LEU-778; VAL-874 AND PHE-1083, AND VARIANTS ARG-832;
ILE-864; MET-1109 AND ALA-1140.
PubMed=9554743;
DOI=10.1002/(SICI)1098-1004(1998)11:4<275::AID-HUMU4>3.0.CO;2-L;
Kim E.K., Yoo O.J., Song K.Y., Yoo H.W., Choi S.Y., Cho S.W.,
Hahn S.H.;
"Identification of three novel mutations and a high frequency of the
Arg778Leu mutation in Korean patients with Wilson disease.";
Hum. Mutat. 11:275-278(1998).
[55]
VARIANTS WD LEU-778; VAL-874; GLY-919; SER-1186; ALA-1267 AND
SER-1270.
PubMed=9452121;
Yamaguchi A., Matsuura A., Arashima S., Kikuchi Y., Kikuchi K.;
"Mutations of ATP7B gene in Wilson disease in Japan: identification of
nine mutations and lack of clear founder effect in a Japanese
population.";
Hum. Mutat. Suppl. 1:S320-S322(1998).
[56]
VARIANTS WD VAL-85; SER-492; 608-PHE-ASP-609 DELINS TYR; HIS-642;
ARG-645; ILE-665; ARG-691; PHE-747; TRP-778; LEU-840; ASN-918;
TRP-919; ASN-921; PRO-933; LEU-992; THR-1003; VAL-1018; TRP-1041;
VAL-1089; MET-1146; GLY-1183; THR-1183; MET-1216; ASP-1341 AND
SER-1358.
PubMed=9671269;
DOI=10.1002/(SICI)1098-1004(1998)12:2<89::AID-HUMU3>3.0.CO;2-G;
Loudianos G., Dessi V., Lovicu M., Angius A., Nurchi A.,
Sturniolo G.C., Marcellini M., Zancan L., Bragetti P., Akar N.,
Yagci R., Vegnente A., Cao A., Pirastu M.;
"Further delineation of the molecular pathology of Wilson disease in
the Mediterranean population.";
Hum. Mutat. 12:89-94(1998).
[57]
VARIANTS WD.
PubMed=9829905;
DOI=10.1002/(SICI)1098-1004(1998)12:6<370::AID-HUMU2>3.0.CO;2-S;
Tsai C.-H., Tsai F.-J., Wu J.-Y., Chang J.-G., Lee C.-C., Lin S.-P.,
Yang C.-F., Jong Y.-J., Lo M.-C.;
"Mutation analysis of Wilson disease in Taiwan and description of six
new mutations.";
Hum. Mutat. 12:370-376(1998).
[58]
VARIANT WD PRO-1041.
PubMed=10194254;
Wu Z., Wang N., Murong S., Lin M.;
"Missense mutations of exons 14 and 18 of Wilson's disease gene in
Chinese patients.";
Zhonghua Yi Xue Yi Chuan Xue Za Zhi 16:91-93(1999).
[59]
VARIANTS WD 670-TYR-MET-671 DEL; TYR-985 AND THR-1148.
PubMed=10447265;
DOI=10.1002/(SICI)1098-1004(1999)14:1<88::AID-HUMU15>3.0.CO;2-H;
Haas R., Gutierrez-Rivero B., Knoche J., Boeker K., Manns M.P.,
Schmidt H.H.-J.;
"Mutation analysis in patients with Wilson disease: identification of
4 novel mutations.";
Hum. Mutat. 14:88-88(1999).
[60]
VARIANTS WD.
PubMed=10502776;
DOI=10.1002/(SICI)1098-1004(199910)14:4<294::AID-HUMU4>3.0.CO;2-9;
Loudianos G., Dessi V., Lovicu M., Angius A., Figus A., Lilliu F.,
De Virgiliis S., Nurchi A.M., Deplano A., Moi P., Pirastu M., Cao A.;
"Molecular characterization of Wilson disease in the Sardinian
population -- evidence of a founder effect.";
Hum. Mutat. 14:294-303(1999).
[61]
VARIANTS WD.
PubMed=10502777;
DOI=10.1002/(SICI)1098-1004(199910)14:4<304::AID-HUMU5>3.0.CO;2-W;
Curtis D., Durkie M., Balac P., Sheard D., Goodeve A., Peake I.,
Quarrell O., Tanner S.;
"A study of Wilson disease mutations in Britain.";
Hum. Mutat. 14:304-311(1999).
[62]
VARIANT WD GLN-1069.
PubMed=10051024;
Ivanova-Smolenskaya I.A., Ovchinnikov I.V., Karabanov A.V.,
Deineko N.L., Poleshchuk V.V., Markova E.D., Illarioshkin S.N.;
"The His1069Gln mutation in the ATP7B gene in Russian patients with
Wilson disease.";
J. Med. Genet. 36:174-174(1999).
[63]
VARIANTS WD SER-710; ARG-711; LEU-840; VAL-874; GLN-969; VAL-1003;
TRP-1041; PRO-1041; GLU-1061; VAL-1063; GLY-1068; GLN-1069; GLU-1089;
PHE-1104; HIS-1151; THR-1169; LYS-1173; VAL-1222; PHE-1262; VAL-1327;
PHE-1363 AND MET-1434, AND VARIANTS ARG-1207 AND ILE-1297.
PubMed=10544227;
Loudianos G., Dessi V., Lovicu M., Angius A., Altuntas B.,
Giacchino R., Marazzi M., Marcellini M., Sartorelli M.R.,
Sturniolo G.C., Kocak N., Yuce A., Akar N., Pirastu M., Cao A.;
"Mutation analysis in patients of Mediterranean descent with Wilson
disease: identification of 19 novel mutations.";
J. Med. Genet. 36:833-836(1999).
[64]
VARIANTS WD LEU-778; VAL-874; GLY-919; ILE-1029; VAL-1035; SER-1186
AND ASN-1222.
PubMed=10453196; DOI=10.1046/j.1442-200X.1999.01092.x;
Shimizu N., Nakazono H., Takeshita Y., Ikeda C., Fujii H.,
Watanabe A., Yamaguchi Y., Hemmi H., Shimatake H., Aoki T.;
"Molecular analysis and diagnosis in Japanese patients with Wilson's
disease.";
Pediatr. Int. 41:409-413(1999).
[65]
VARIANTS WD SER-486; GLY-778; MET-890; GLN-969; GLU-1061; GLN-1069;
SER-1099 AND THR-1148.
PubMed=11216666; DOI=10.1089/109065700750065162;
Loudianos G., Lovicu M., Solinas P., Kanavakis E., Tzetis M.,
Manolaki N., Panagiotakaki E., Karpathios T., Cao A.;
"Delineation of the spectrum of Wilson disease mutations in the Greek
population and the identification of six novel mutations.";
Genet. Test. 4:399-402(2000).
[66]
VARIANT WD PRO-708.
PubMed=11093740; DOI=10.1053/jhep.2000.20152;
Garcia-Villarreal L., Daniels S., Shaw S.H., Cotton D., Galvin M.,
Geskes J., Bauer P., Sierra-Hernandez A., Buckler A., Tugores A.;
"High prevalence of the very rare Wilson disease gene mutation
Leu708Pro in the Island of Gran Canaria (Canary Islands, Spain): a
genetic and clinical study.";
Hepatology 32:1329-1336(2000).
[67]
VARIANTS WD ILE-769; LEU-778; TRP-778; VAL-874; GLY-919; THR-1003;
PHE-1083; SER-1186; ALA-1267; SER-1270; THR-1336 AND PRO-1373, AND
VARIANTS ALA-406; LEU-456 AND ALA-1140.
PubMed=10790207;
DOI=10.1002/(SICI)1098-1004(200005)15:5<454::AID-HUMU7>3.3.CO;2-A;
Okada T., Shiono Y., Hayashi H., Satoh H., Sawada T., Suzuki A.,
Takeda Y., Yano M., Michitaka K., Onji M., Mabuchi H.;
"Mutational analysis of ATP7B and genotype-phenotype correlation in
Japanese with Wilson's disease.";
Hum. Mutat. 15:454-462(2000).
[68]
VARIANTS WD LEU-778; VAL-874 AND VAL-1297 DEL, AND VARIANTS LEU-290;
ALA-406; LEU-456; ARG-832; ALA-1140 AND GLU-1407.
PubMed=10721669; DOI=10.1007/s100380050017;
Kusuda Y., Hamaguchi K., Mori T., Shin R., Seike M., Sakata T.;
"Novel mutations of the ATP7B gene in Japanese patients with Wilson
disease.";
J. Hum. Genet. 45:86-91(2000).
[69]
VARIANT WD GLY-1279.
PubMed=11043508; DOI=10.1007/s100380070015;
Lee C.C., Wu J.Y., Tsai F.J., Kodama H., Abe T., Yang C.F., Tsai C.H.;
"Molecular analysis of Wilson disease in Taiwan: identification of one
novel mutation and evidence of haplotype-mutation association.";
J. Hum. Genet. 45:275-279(2000).
[70]
VARIANTS WD LEU-760 AND PRO-1305.
PubMed=11180609;
DOI=10.1002/1098-1004(200102)17:2<156::AID-HUMU18>3.0.CO;2-0;
Genschel J., Czlonkowska A., Sommer G., Buettner C., Bochow B.,
Lochs H., Schmidt H.;
"Three novel mutations (P760L, L1305P, Q1351Stop) causing Wilson
disease.";
Hum. Mutat. 17:156-156(2001).
[71]
VARIANTS WD TRP-616; ALA-710; SER-710; LEU-760; ASN-765; VAL-769;
GLN-969; LEU-992; GLN-1069 AND SER-1270, AND VARIANTS ALA-406; LEU-456
AND ARG-832.
PubMed=11690702; DOI=10.1016/S0168-8278(01)00219-7;
Caca K., Ferenci P., Kuehn H.-J., Polli C., Willgerodt H., Kunath B.,
Hermann W., Moessner J., Berr F.;
"High prevalence of the H1069Q mutation in East German patients with
Wilson disease: rapid detection of mutations by limited sequencing and
phenotype-genotype analysis.";
J. Hepatol. 35:575-581(2001).
[72]
VARIANTS WD TRP-778; ARG-898; GLN-1069; THR-1102 AND ARG-1266.
PubMed=11243728; DOI=10.1006/mgme.2000.3143;
Butler P., McIntyre N., Mistry P.K.;
"Molecular diagnosis of Wilson disease.";
Mol. Genet. Metab. 72:223-230(2001).
[73]
VARIANTS WD PHE-1083 AND ASN-1296.
PubMed=11954751; DOI=10.1007/s00431-001-0865-9;
Ohya K., Abo W., Tamaki H., Sugawara C., Endo T., Nomachi S.,
Fukushi M., Kinebuchi M., Matsuura A.;
"Presymptomatic diagnosis of Wilson disease associated with a novel
mutation of the ATP7B gene.";
Eur. J. Pediatr. 161:124-126(2002).
[74]
VARIANTS WD HIS-768; LEU-778; VAL-874; PHE-1083; SER-1168; ILE-1255;
ALA-1267 AND SER-1270.
PubMed=12544487; DOI=10.1097/00125817-200211001-00009;
Yoo H.-W.;
"Identification of novel mutations and the three most common mutations
in the human ATP7B gene of Korean patients with Wilson disease.";
Genet. Med. 4:43S-48S(2002).
[75]
VARIANTS WD PRO-721 AND GLY-1183.
PubMed=12325021; DOI=10.1002/humu.10121;
Loudianos G., Lovicu M., Dessi V., Tzetis M., Kanavakis E., Zancan L.,
Zelante L., Galvez-Galvez C., Cao A.;
"Abnormal mRNA splicing resulting from consensus sequence splicing
mutations of ATP7B.";
Hum. Mutat. 20:260-266(2002).
[76]
VARIANTS WD LEU-778; VAL-874 AND GLY-919.
PubMed=12376745; DOI=10.1007/s100380200082;
Takeshita Y., Shimizu N., Yamaguchi Y., Nakazono H., Saitou M.,
Fujikawa Y., Aoki T.;
"Two families with Wilson disease in which siblings showed different
phenotypes.";
J. Hum. Genet. 47:543-547(2002).
[77]
VARIANTS WD VAL-85; GLY-765; LEU-778; MET-890; GLY-919; MET-935;
TYR-975; LEU-992; ARG-1098; THR-1148; LYS-1173 AND ASN-1248, AND
VARIANTS ASP-14; ALA-406; LEU-456; ARG-832; ALA-1140; ASN-1143 AND
SER-1245.
PubMed=14986826; DOI=10.1046/j.1399-0004.2003.00179.x;
Gu Y.-H., Kodama H., Du S.-L., Gu Q.-J., Sun H.-J., Ushijima H.;
"Mutation spectrum and polymorphisms in ATP7B identified on direct
sequencing of all exons in Chinese Han and Hui ethnic patients with
Wilson's disease.";
Clin. Genet. 64:479-484(2003).
[78]
VARIANT WD SER-1341.
PubMed=14639035; DOI=10.1159/000075092;
Majumdar R., Al Jumah M., Zaidan R.;
"A rare homozygous missense mutation in ATP7B exon 19 in a case of
Wilson disease.";
Eur. Neurol. 51:52-54(2004).
[79]
VARIANTS WD SER-41; GLY-949; LEU-1094; PRO-1232 AND ARG-1373.
PubMed=15024742; DOI=10.1002/humu.9227;
Deguti M.M., Genschel J., Cancado E.L.R., Barbosa E.R., Bochow B.,
Mucenic M., Porta G., Lochs H., Carrilho F.J., Schmidt H.H.-J.;
"Wilson disease: novel mutations in the ATP7B gene and clinical
correlation in Brazilian patients.";
Hum. Mutat. 23:398-398(2004).
[80]
VARIANT WD ARG-766.
PubMed=15557537; DOI=10.1212/01.WNL.0000144192.30426.38;
Pendlebury S.T., Rothwell P.M., Dalton A., Burton E.A.;
"Strokelike presentation of Wilson disease with homozygosity for a
novel T766R mutation.";
Neurology 63:1982-1983(2004).
[81]
VARIANTS WD LEU-778; ASP-943; ILE-1106 AND MET-1216, AND VARIANT
ALA-1140.
PubMed=14966923; DOI=10.3748/wjg.v10.i4.590;
Liu X.-Q., Zhang Y.-F., Liu T.-T., Hsiao K.-J., Zhang J.-M., Gu X.-F.,
Bao K.-R., Yu L.-H., Wang M.-X.;
"Correlation of ATP7B genotype with phenotype in Chinese patients with
Wilson disease.";
World J. Gastroenterol. 10:590-593(2004).
[82]
VARIANTS WD THR-1148 AND ARG-1176.
PubMed=15845031; DOI=10.1046/j.1529-8817.2005.00171.x;
Dedoussis G.V.Z., Genschel J., Sialvera T.-E., Bochow B., Manolaki N.,
Manios Y., Tsafantakis E., Schmidt H.;
"Wilson disease: high prevalence in a mountainous area of Crete.";
Ann. Hum. Genet. 69:268-274(2005).
[83]
VARIANTS WD HIS-992; THR-1003; THR-1102; TYR-1104 AND ARG-1256.
PubMed=15811015; DOI=10.1111/j.1399-0004.2005.00440.x;
Kumar S., Thapa B.R., Kaur G., Prasad R.;
"Identification and molecular characterization of 18 novel mutations
in the ATP7B gene from Indian Wilson disease patients: genotype.";
Clin. Genet. 67:443-445(2005).
[84]
VARIANTS WD ARG-645; LEU-690; ARG-869; SER-943; MET-977; GLU-1061;
GLN-1069; SER-1099; MET-1216 AND PRO-1232, AND VARIANTS ALA-406;
LEU-456; ARG-832 AND ALA-1140.
PubMed=15952988; DOI=10.1111/j.1399-0004.2005.00439.x;
Margarit E., Bach V., Gomez D., Bruguera M., Jara P., Queralt R.,
Ballesta F.;
"Mutation analysis of Wilson disease in the Spanish population
-identification of a prevalent substitution and eight novel mutations
in the ATP7B gene.";
Clin. Genet. 68:61-68(2005).
[85]
VARIANTS WD GLN-616; ALA-626; TRP-778; GLY-778; VAL-874; GLN-969;
THR-1003; GLN-1069; 1217-VAL-LEU-1218 DEL; SER-1270; TYR-1279;
ASP-1341; SER-1352 AND PRO-1368.
PubMed=16207219; DOI=10.1111/j.1399-0004.2005.00516.x;
Todorov T., Savov A., Jelev H., Panteleeva E., Konstantinova D.,
Krustev Z., Mihaylova V., Tournev I., Tankova L., Tzolova N.,
Kremensky I.;
"Spectrum of mutations in the Wilson disease gene (ATP7B) in the
Bulgarian population.";
Clin. Genet. 68:474-476(2005).
[86]
VARIANTS WD GLN-616; TYR-639; TYR-653; PRO-776; GLY-778; MET-977;
ARG-988; LEU-992; GLN-1069; PRO-1095; MET-1220; LEU-1273 AND ASP-1341.
PubMed=16283883; DOI=10.1111/j.1399-0004.2005.00528.x;
Gromadzka G., Schmidt H.H.-J., Genschel J., Bochow B., Rodo M.,
Tarnacka B., Litwin T., Chabik G., Czlonkowska A.;
"Frameshift and nonsense mutations in the gene for ATPase7B are
associated with severe impairment of copper metabolism and with an
early clinical manifestation of Wilson's disease.";
Clin. Genet. 68:524-532(2005).
[87]
VARIANTS WD HIS-532; ASP-591; PRO-604; SER-641; TYR-703; VAL-710;
GLY-756; MET-766; THR-861; CYS-943; MET-991; THR-996; ARG-1000;
GLU-1176; GLU-1221; SER-1287; SER-1331; VAL-1341; SER-1375 AND
SER-1379.
PubMed=16088907; DOI=10.1002/humu.9358;
Cox D.W., Prat L., Walshe J.M., Heathcote J., Gaffney D.;
"Twenty-four novel mutations in Wilson disease patients of
predominantly European ancestry.";
Hum. Mutat. 26:280-280(2005).
[88]
VARIANTS WD SER-641; SER-710; ARG-737; GLY-778; GLU-918; GLN-969;
MET-977; VAL-1018; SER-1033; TRP-1041; VAL-1063; LYS-1064; GLN-1069;
THR-1102; ASP-1111; THR-1148; ARG-1176; SER-1186; ASN-1271; LEU-1273;
PRO-1305; ASP-1341 AND CYS-1355, AND VARIANTS LEU-456; ARG-832 AND
ALA-1140.
PubMed=15967699; DOI=10.1016/j.ymgme.2005.05.004;
Vrabelova S., Letocha O., Borsky M., Kozak L.;
"Mutation analysis of the ATP7B gene and genotype/phenotype
correlation in 227 patients with Wilson disease.";
Mol. Genet. Metab. 86:277-285(2005).
[89]
VARIANT WD ARG-691.
PubMed=17718866; DOI=10.1111/j.1399-0004.2007.00853.x;
Barada K., Nemer G., ElHajj I.I., Touma J., Cortas N., Boustany R.-M.,
Usta J.;
"Early and severe liver disease associated with homozygosity for an
exon 7 mutation, G691R, in Wilson's disease.";
Clin. Genet. 72:264-267(2007).
[90]
VARIANTS WD ALA-536; ARG-657; VAL-971; MET-974; PRO-1004; ALA-1149;
ASN-1164; GLY-1173; THR-1228; VAL-1230; VAL-1267; THR-1328 AND
ILE-1359, AND VARIANTS ALA-406; LEU-456; ARG-832; LYS-952 AND
ALA-1140.
PubMed=18373411; DOI=10.1089/gte.2007.0072;
Davies L.P., Macintyre G., Cox D.W.;
"New mutations in the Wilson disease gene, ATP7B: implications for
molecular testing.";
Genet. Test. 12:139-145(2008).
[91]
CHARACTERIZATION OF VARIANTS WD HIS-532; ALA-626; HIS-642; TRP-1041;
LYS-1064; PHE-1083; ASP-1106; VAL-1169; THR-1183 AND SER-1186,
CHARACTERIZATION OF VARIANT ALA-1140, AND FUNCTION.
PubMed=18203200; DOI=10.1002/humu.20674;
Hsi G., Cullen L.M., Macintyre G., Chen M.M., Glerum D.M., Cox D.W.;
"Sequence variation in the ATP-binding domain of the Wilson disease
transporter, ATP7B, affects copper transport in a yeast model
system.";
Hum. Mutat. 29:491-501(2008).
[92]
VARIANTS WD MET-991; ARG-1000; PRO-1043; ARG-1101; THR-1102; THR-1148;
GLY-1173; GLU-1176; THR-1228; GLY-1239; VAL-1267 AND SER-1287, AND
CHARACTERIZATION OF VARIANTS WD MET-991; ARG-1000; PRO-1043; ARG-1101;
THR-1102; THR-1148; GLY-1173; GLU-1176; THR-1228; GLY-1239; VAL-1267
AND SER-1287.
PubMed=20333758; DOI=10.1002/humu.21228;
Luoma L.M., Deeb T.M., Macintyre G., Cox D.W.;
"Functional analysis of mutations in the ATP loop of the Wilson
disease copper transporter, ATP7B.";
Hum. Mutat. 31:569-577(2010).
[93]
VARIANTS WD PRO-549; HIS-642; TYR-703; PRO-744; ASN-765; GLY-778;
MET-977; ASP-998; VAL-1063; GLN-1069; ARG-1207; LEU-1273; ASP-1332;
ARG-1341 AND ASP-1341.
PubMed=21682854; DOI=10.1186/1471-2431-11-56;
Abdel Ghaffar T.Y., Elsayed S.M., Elnaghy S., Shadeed A.,
Elsobky E.S., Schmidt H.;
"Phenotypic and genetic characterization of a cohort of pediatric
Wilson disease patients.";
BMC Pediatr. 11:56-56(2011).
[94]
VARIANTS WD SER-710; ASN-765; GLY-778; TRP-778; ILE-788; VAL-874;
TRP-919; SER-943; GLN-969; THR-1003; VAL-1003; ILE-1036; TRP-1041;
GLN-1069; CYS-1151; THR-1245 AND SER-1270, AND VARIANTS ALA-406;
LEU-456; ARG-832; LYS-952; ALA-1140; ARG-1207 AND LEU-1243.
PubMed=23333878; DOI=10.1016/j.ejmg.2013.01.003;
Simsek Papur O., Akman S.A., Cakmur R., Terzioglu O.;
"Mutation analysis of ATP7B gene in Turkish Wilson disease patients:
identification of five novel mutations.";
Eur. J. Med. Genet. 56:175-179(2013).
[95]
VARIANT ALA-1140.
PubMed=24303094; DOI=10.4254/wjh.v5.i11.649;
Nussinson E., Shahbari A., Shibli F., Chervinsky E., Trougouboff P.,
Markel A.;
"Diagnostic challenges of Wilson's disease presenting as acute
pancreatitis, cholangitis, and jaundice.";
World J. Hepatol. 5:649-653(2013).
[96]
VARIANTS WD MET-935 AND THR-982.
PubMed=24476933; DOI=10.1016/j.gene.2013.10.044;
Chen L., Li X., Zheng Z., Lu X., Lin M., Pan C., Liu J.;
"A novel ATP7B gene mutation in a liver failure patient with normal
ceruloplasmin and low serum alkaline phosphatase.";
Gene 538:204-206(2014).
[97]
VARIANTS WD LEU-778; GLY-919; LEU-992; LYS-1136 AND GLU-1149, AND
VARIANT LEU-456.
PubMed=25704634; DOI=10.1016/j.arcmed.2015.02.001;
Liu Y., Zhou H., Guo H., Bai Y.;
"Genetic and clinical analysis in a cohort of patients with Wilson's
disease in southwestern China.";
Arch. Med. Res. 46:164-169(2015).
[98]
VARIANTS WD PRO-990; VAL-1003; ARG-1010; TRP-1041; PRO-1043; GLU-1061;
ARG-1101; SER-1104; MET-1113; SER-1270 AND LYS-1293.
PubMed=25982861; DOI=10.1016/j.gene.2015.05.031;
Guggilla S.R., Senagari J.R., Rao P.N., Madireddi S.;
"Spectrum of mutations in the ATP binding domain of ATP7B gene of
Wilson Disease in a regional Indian cohort.";
Gene 569:83-87(2015).
[99]
VARIANTS WD ILE-788 AND ILE-1036, CHARACTERIZATION OF VARIANTS WD
ILE-788 AND ILE-1036, AND FUNCTION.
PubMed=26004889; DOI=10.1016/j.jtemb.2015.02.006;
Papur O.S., Terzioglu O., Koc A.;
"Functional characterization of new mutations in Wilson disease gene
(ATP7B) using the yeast model.";
J. Trace Elem. Med. Biol. 31:33-36(2015).
[100]
POSSIBLE RIBOSOMAL FRAMESHIFT TO TRANSLATE ISOFORM COPZ(A).
PubMed=28107647; DOI=10.1016/j.molcel.2016.12.008;
Meydan S., Klepacki D., Karthikeyan S., Margus T., Thomas P.,
Jones J.E., Khan Y., Briggs J., Dinman J.D., Vazquez-Laslop N.,
Mankin A.S.;
"Programmed ribosomal frameshifting generates a copper transporter and
a copper chaperone from the same gene.";
Mol. Cell 65:207-219(2017).
-!- FUNCTION: Copper ion transmembrane transporter involved in the
export of copper out of the cells, such as the efflux of hepatic
copper into the bile. {ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:24706876,
ECO:0000269|PubMed:26004889}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate
+ Cu(+)(Side 2). {ECO:0000269|PubMed:22240481}.
-!- SUBUNIT: Monomer. Interacts with COMMD1/MURR1 (PubMed:12968035,
PubMed:17919502). Interacts with DCTN4, in a copper-dependent
manner (PubMed:16554302). Interacts with ATOX1 (PubMed:18558714).
Interacts (via C-terminus) with ZBTB16/PLZF (PubMed:16676348).
{ECO:0000269|PubMed:12968035, ECO:0000269|PubMed:16554302,
ECO:0000269|PubMed:16676348, ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:18558714}.
-!- INTERACTION:
O00244:ATOX1; NbExp=3; IntAct=EBI-11668501, EBI-10179267;
Q8N668:COMMD1; NbExp=6; IntAct=EBI-11668501, EBI-1550112;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:24706876}; Multi-
pass membrane protein {ECO:0000255}. Late endosome
{ECO:0000269|PubMed:11231950, ECO:0000269|PubMed:15681833}.
Note=Predominantly found in the trans-Golgi network (TGN).
Localized in the trans-Golgi network under low copper conditions,
redistributes to cytoplasmic vesicles when cells are exposed to
elevated copper levels, and then recycles back to the trans-Golgi
network when copper is removed (PubMed:10942420). Not
redistributed to the plasma membrane in response to elevated
copper levels. {ECO:0000269|PubMed:10942420,
ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:24706876,
ECO:0000269|PubMed:9307043}.
-!- SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus membrane
{ECO:0000269|PubMed:9307043}; Multi-pass membrane protein
{ECO:0000269|PubMed:9307043}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:9307043}.
-!- SUBCELLULAR LOCATION: WND/140 kDa: Mitochondrion
{ECO:0000269|PubMed:9600907}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Ribosomal frameshifting; Named isoforms=5;
Name=1; Synonyms=A;
IsoId=P35670-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=P35670-2; Sequence=VSP_000426, VSP_000427;
Name=3;
IsoId=P35670-3; Sequence=VSP_016559;
Name=4;
IsoId=P35670-4; Sequence=VSP_016560;
Note=No experimental confirmation available.;
Name=5;
IsoId=P35670-5; Sequence=VSP_059175;
Note=May arise by a -1 programmed ribosomal frameshift at codon
233. A nucleotide 'slippery sequence' followed by an mRNA
pseudoknot are found downstream of the frameshift site and
direct frameshifting of a gene fragment with about 10%
efficiency. {ECO:0000305|PubMed:28107647};
-!- TISSUE SPECIFICITY: Most abundant in liver and kidney and also
found in brain. Isoform 2 is expressed in brain but not in liver.
The cleaved form WND/140 kDa is found in liver cell lines and
other tissues.
-!- DOMAIN: Each HMA domain can bind a copper ion, they are tightly
packed and closely interact with each other. Wild-type ATP7B can
usually be loaded with an average 5.5 copper atoms per molecule.
{ECO:0000269|PubMed:20032459}.
-!- PTM: Isoform 1 may be proteolytically cleaved at the N-terminus to
produce the WND/140 kDa form.
-!- DISEASE: Wilson disease (WD) [MIM:277900]: An autosomal recessive
disorder of copper metabolism in which copper cannot be
incorporated into ceruloplasmin in liver, and cannot be excreted
from the liver into the bile. Copper accumulates in the liver and
subsequently in the brain and kidney. The disease is characterized
by neurologic manifestations and signs of cirrhosis.
{ECO:0000269|PubMed:10051024, ECO:0000269|PubMed:10194254,
ECO:0000269|PubMed:10447265, ECO:0000269|PubMed:10453196,
ECO:0000269|PubMed:10502776, ECO:0000269|PubMed:10502777,
ECO:0000269|PubMed:10544227, ECO:0000269|PubMed:10721669,
ECO:0000269|PubMed:10790207, ECO:0000269|PubMed:10942420,
ECO:0000269|PubMed:11043508, ECO:0000269|PubMed:11093740,
ECO:0000269|PubMed:11180609, ECO:0000269|PubMed:11216666,
ECO:0000269|PubMed:11231950, ECO:0000269|PubMed:11243728,
ECO:0000269|PubMed:11405812, ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:11954751, ECO:0000269|PubMed:12325021,
ECO:0000269|PubMed:12376745, ECO:0000269|PubMed:12544487,
ECO:0000269|PubMed:14639035, ECO:0000269|PubMed:14966923,
ECO:0000269|PubMed:14986826, ECO:0000269|PubMed:15024742,
ECO:0000269|PubMed:15557537, ECO:0000269|PubMed:15811015,
ECO:0000269|PubMed:15845031, ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:15967699, ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:16207219, ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:16649058, ECO:0000269|PubMed:17718866,
ECO:0000269|PubMed:17823867, ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:17949296, ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:18373411, ECO:0000269|PubMed:20333758,
ECO:0000269|PubMed:21398519, ECO:0000269|PubMed:21454443,
ECO:0000269|PubMed:21645214, ECO:0000269|PubMed:21682854,
ECO:0000269|PubMed:22075048, ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:22484412, ECO:0000269|PubMed:22763723,
ECO:0000269|PubMed:23159873, ECO:0000269|PubMed:23235335,
ECO:0000269|PubMed:23275100, ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:23518715, ECO:0000269|PubMed:24476933,
ECO:0000269|PubMed:24555712, ECO:0000269|PubMed:24706876,
ECO:0000269|PubMed:25704634, ECO:0000269|PubMed:25982861,
ECO:0000269|PubMed:26004889, ECO:0000269|PubMed:7626145,
ECO:0000269|PubMed:8298641, ECO:0000269|PubMed:8533760,
ECO:0000269|PubMed:8782057, ECO:0000269|PubMed:8931691,
ECO:0000269|PubMed:8938442, ECO:0000269|PubMed:8980283,
ECO:0000269|PubMed:9222767, ECO:0000269|PubMed:9311736,
ECO:0000269|PubMed:9452121, ECO:0000269|PubMed:9482578,
ECO:0000269|PubMed:9554743, ECO:0000269|PubMed:9671269,
ECO:0000269|PubMed:9772425, ECO:0000269|PubMed:9829905,
ECO:0000269|PubMed:9837819, ECO:0000269|PubMed:9887381}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA16173.1; Type=Frameshift; Positions=830; Evidence={ECO:0000305};
Sequence=AAA79211.1; Type=Frameshift; Positions=456; Evidence={ECO:0000305};
Sequence=AAA79212.1; Type=Frameshift; Positions=456; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wilson Disease Mutation Database;
URL="http://www.medicalgenetics.med.ualberta.ca/wilson/index.php";
-----------------------------------------------------------------------
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EMBL; U11700; AAA92667.1; -; mRNA.
EMBL; DQ015922; AAY41166.1; -; mRNA.
EMBL; AL139082; CAI12888.1; -; Genomic_DNA.
EMBL; AL138821; CAI12888.1; JOINED; Genomic_DNA.
EMBL; AL162377; CAI12888.1; JOINED; Genomic_DNA.
EMBL; AL162377; CAI13428.1; -; Genomic_DNA.
EMBL; AL138821; CAI13428.1; JOINED; Genomic_DNA.
EMBL; AL139082; CAI13428.1; JOINED; Genomic_DNA.
EMBL; AL138821; CAI13743.1; -; Genomic_DNA.
EMBL; AL139082; CAI13743.1; JOINED; Genomic_DNA.
EMBL; AL162377; CAI13743.1; JOINED; Genomic_DNA.
EMBL; AF034838; AAD01998.1; -; Genomic_DNA.
EMBL; U03464; AAB52902.1; -; mRNA.
EMBL; L25591; AAA79211.1; ALT_FRAME; mRNA.
EMBL; L25591; AAA79212.1; ALT_FRAME; mRNA.
EMBL; L25442; AAA16173.1; ALT_FRAME; mRNA.
EMBL; AB209461; BAD92698.1; -; mRNA.
EMBL; S77446; AAD14987.1; -; Genomic_DNA.
EMBL; S77447; AAB34086.1; -; Genomic_DNA.
EMBL; S77450; AAB34087.1; -; Genomic_DNA.
CCDS; CCDS41892.1; -. [P35670-1]
CCDS; CCDS45049.1; -. [P35670-2]
CCDS; CCDS58293.1; -. [P35670-3]
PIR; I78536; I78536.
PIR; I78537; I78537.
PIR; S78555; S78555.
RefSeq; NP_000044.2; NM_000053.3. [P35670-1]
RefSeq; NP_001230111.1; NM_001243182.1. [P35670-3]
RefSeq; NP_001317507.1; NM_001330578.1.
RefSeq; NP_001317508.1; NM_001330579.1.
RefSeq; XP_005266487.1; XM_005266430.4. [P35670-1]
UniGene; Hs.492280; -.
PDB; 2ARF; NMR; -; A=1032-1196.
PDB; 2EW9; NMR; -; A=486-633.
PDB; 2KOY; NMR; -; A=1036-1196.
PDB; 2LQB; NMR; -; A=141-212.
PDB; 2N7Y; NMR; -; A=56-127.
PDB; 2ROP; NMR; -; A=238-439.
PDBsum; 2ARF; -.
PDBsum; 2EW9; -.
PDBsum; 2KOY; -.
PDBsum; 2LQB; -.
PDBsum; 2N7Y; -.
PDBsum; 2ROP; -.
ProteinModelPortal; P35670; -.
SMR; P35670; -.
BioGrid; 107022; 19.
IntAct; P35670; 2.
MINT; MINT-105941; -.
STRING; 9606.ENSP00000242839; -.
DrugBank; DB00958; Carboplatin.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00526; Oxaliplatin.
TCDB; 3.A.3.5.3; the p-type atpase (p-atpase) superfamily.
iPTMnet; P35670; -.
PhosphoSitePlus; P35670; -.
BioMuta; ATP7B; -.
DMDM; 239938919; -.
MaxQB; P35670; -.
PaxDb; P35670; -.
PeptideAtlas; P35670; -.
PRIDE; P35670; -.
Ensembl; ENST00000242839; ENSP00000242839; ENSG00000123191. [P35670-1]
Ensembl; ENST00000344297; ENSP00000342559; ENSG00000123191. [P35670-2]
Ensembl; ENST00000400366; ENSP00000383217; ENSG00000123191. [P35670-3]
GeneID; 540; -.
KEGG; hsa:540; -.
UCSC; uc001vfw.4; human. [P35670-1]
CTD; 540; -.
DisGeNET; 540; -.
EuPathDB; HostDB:ENSG00000123191.14; -.
GeneCards; ATP7B; -.
GeneReviews; ATP7B; -.
HGNC; HGNC:870; ATP7B.
HPA; HPA009137; -.
HPA; HPA013187; -.
MalaCards; ATP7B; -.
MIM; 277900; phenotype.
MIM; 606882; gene.
neXtProt; NX_P35670; -.
OpenTargets; ENSG00000123191; -.
Orphanet; 905; Wilson disease.
PharmGKB; PA73; -.
eggNOG; KOG0207; Eukaryota.
eggNOG; COG2217; LUCA.
GeneTree; ENSGT00530000063773; -.
HOGENOM; HOG000250397; -.
HOVERGEN; HBG050616; -.
InParanoid; P35670; -.
KO; K17686; -.
OMA; HKIKTVM; -.
OrthoDB; EOG091G022E; -.
PhylomeDB; P35670; -.
TreeFam; TF300460; -.
BRENDA; 3.6.3.4; 2681.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
EvolutionaryTrace; P35670; -.
GeneWiki; Wilson_disease_protein; -.
GenomeRNAi; 540; -.
PRO; PR:P35670; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000123191; -.
CleanEx; HS_ATP7B; -.
ExpressionAtlas; P35670; baseline and differential.
Genevisible; P35670; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0005375; F:copper ion transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0004008; F:copper-exporting ATPase activity; TAS:UniProtKB.
GO; GO:0043682; F:copper-transporting ATPase activity; IMP:UniProtKB.
GO; GO:0006878; P:cellular copper ion homeostasis; TAS:UniProtKB.
GO; GO:0006882; P:cellular zinc ion homeostasis; IEA:Ensembl.
GO; GO:0015677; P:copper ion import; IDA:UniProtKB.
GO; GO:0006825; P:copper ion transport; IDA:UniProtKB.
GO; GO:0015680; P:intracellular copper ion transport; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0046688; P:response to copper ion; IDA:UniProtKB.
GO; GO:0051208; P:sequestering of calcium ion; IDA:UniProtKB.
CDD; cd00371; HMA; 6.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_domN.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR017969; Heavy-metal-associated_CS.
InterPro; IPR006122; HMA_Cu_ion-bd.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
InterPro; IPR027256; P-typ_ATPase_IB.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00403; HMA; 6.
SUPFAM; SSF55008; SSF55008; 6.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 2.
TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
TIGRFAMs; TIGR00003; TIGR00003; 6.
PROSITE; PS00154; ATPASE_E1_E2; 1.
PROSITE; PS01047; HMA_1; 6.
PROSITE; PS50846; HMA_2; 6.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Copper; Copper transport; Cytoplasm; Disease mutation; Endosome;
Golgi apparatus; Hydrolase; Ion transport; Magnesium; Membrane;
Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Ribosomal frameshifting;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1465 Copper-transporting ATPase 2.
/FTId=PRO_0000046314.
CHAIN ? 1465 WND/140 kDa.
{ECO:0000305|PubMed:9600907}.
/FTId=PRO_0000296199.
TOPO_DOM 1 653 Cytoplasmic. {ECO:0000255}.
TRANSMEM 654 675 Helical. {ECO:0000255}.
TOPO_DOM 676 697 Extracellular. {ECO:0000255}.
TRANSMEM 698 717 Helical. {ECO:0000255}.
TOPO_DOM 718 724 Cytoplasmic. {ECO:0000255}.
TRANSMEM 725 745 Helical. {ECO:0000255}.
TOPO_DOM 746 764 Extracellular. {ECO:0000255}.
TRANSMEM 765 785 Helical. {ECO:0000255}.
TOPO_DOM 786 919 Cytoplasmic. {ECO:0000255}.
TRANSMEM 920 942 Helical. {ECO:0000255}.
TOPO_DOM 943 972 Extracellular. {ECO:0000255}.
TRANSMEM 973 994 Helical. {ECO:0000255}.
TOPO_DOM 995 1322 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1323 1340 Helical. {ECO:0000255}.
TOPO_DOM 1341 1351 Extracellular. {ECO:0000255}.
TRANSMEM 1352 1371 Helical. {ECO:0000255}.
TOPO_DOM 1372 1465 Cytoplasmic. {ECO:0000255}.
DOMAIN 59 125 HMA 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 144 210 HMA 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 258 327 HMA 3. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 360 426 HMA 4. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 489 555 HMA 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 565 631 HMA 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
COMPBIAS 340 345 Poly-Ser.
ACT_SITE 1027 1027 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 69 69 Copper 1. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 72 72 Copper 1. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 154 154 Copper 2. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 157 157 Copper 2. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 268 268 Copper 3. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 271 271 Copper 3. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 370 370 Copper 4. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 373 373 Copper 4. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 499 499 Copper 5. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 502 502 Copper 5. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 575 575 Copper 6. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 578 578 Copper 6. {ECO:0000269|PubMed:18558714,
ECO:0000269|PubMed:20032459}.
METAL 1267 1267 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1271 1271 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000250|UniProtKB:Q64535}.
MOD_RES 1398 1398 Phosphoserine.
{ECO:0000250|UniProtKB:Q64535}.
VAR_SEQ 234 1465 RPLSSANQNFNNSETLGHQGSHVVTLQLRIDGMHCKSCVLN
IEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAI
EALPPGNFKVSLPDGAEGSGTDHRSSSSHSPGSPPRNQVQG
TCSTTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEG
TATVLYNPSVISPEELRAAIEDMGFEASVVSESCSTNPLGN
HSAGNSMVQTTDGTPTSVQEVAPHTGRLPANHAPDILAKSP
QSTRAVAPQKCFLQIKGMTCASCVSNIERNLQKEAGVLSVL
VALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVMEDYAG
SDGNIELTITGMTCASCVHNIESKLTRTNGITYASVALATS
KALVKFDPEIIGPRDIIKIIEEIGFHASLAQRNPNAHHLDH
KMEIKQWKKSFLCSLVFGIPVMALMIYMLIPSNEPHQSMVL
DHNIIPGLSILNLIFFILCTFVQLLGGWYFYVQAYKSLRHR
SANMDVLIVLATSIAYVYSLVILVVAVAEKAERSPVTFFDT
PPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVT
LGEDNLIIREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEG
NTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATH
VGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIII
MSTLTLVVWIVIGFIDFGVVQRYFPNPNKHISQTEVIIRFA
FQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGG
KPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATLPL
RKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLGYCTDF
QAVPGCGIGCKVSNVEGILAHSERPLSAPASHLNEAGSLPA
EKDAVPQTFSVLIGNREWLRRNGLTISSDVSDAMTDHEMKG
QTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVV
LITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNK
GKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVL
IRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAA
GVFMPIGIVLQPWMGSAAMAASSVSVVLSSLQLKCYKKPDL
ERYEAQAHGHMKPLTASQVSVHIGMDDRWRDSPRATPWDQV
SYVSQVSLSSLTSDKPSRHSAAADDDGDKWSLLLNGRDEEQ
YI -> ETFIFC (in isoform 5).
{ECO:0000305|PubMed:28107647}.
/FTId=VSP_059175.
VAR_SEQ 269 379 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_016559.
VAR_SEQ 624 785 Missing (in isoform 2).
{ECO:0000303|PubMed:8298641}.
/FTId=VSP_000426.
VAR_SEQ 911 955 Missing (in isoform 2).
{ECO:0000303|PubMed:8298641}.
/FTId=VSP_000427.
VAR_SEQ 938 955 Missing (in isoform 4).
{ECO:0000303|PubMed:8250934}.
/FTId=VSP_016560.
VARIANT 14 14 A -> D (in dbSNP:rs587783319).
{ECO:0000269|PubMed:14986826}.
/FTId=VAR_023010.
VARIANT 41 41 N -> S (in WD; does not affect
interaction with COMMD1;
dbSNP:rs201738967).
{ECO:0000269|PubMed:15024742,
ECO:0000269|PubMed:17919502}.
/FTId=VAR_023011.
VARIANT 44 44 Y -> N (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076729.
VARIANT 85 85 G -> V (in WD; decreased copper transport
activity; decreased ATPase activity;
increased interaction with COMMD1;
decreased localization to trans-Golgi
network; increased degradation;
dbSNP:rs786204643).
{ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000703.
VARIANT 96 96 G -> D. {ECO:0000269|PubMed:7833924}.
/FTId=VAR_000704.
VARIANT 108 108 C -> R (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:21645214}.
/FTId=VAR_076730.
VARIANT 136 136 R -> W (in WD; unknown pathological
significance; dbSNP:rs557577836).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076693.
VARIANT 148 148 R -> W (in WD; unknown pathological
significance; dbSNP:rs373762572).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076694.
VARIANT 149 149 V -> L. {ECO:0000269|PubMed:17823867}.
/FTId=VAR_076793.
VARIANT 157 157 C -> F (in WD; dbSNP:rs551275663).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076731.
VARIANT 170 170 G -> V (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:22484412}.
/FTId=VAR_076810.
VARIANT 290 290 V -> L. {ECO:0000269|PubMed:10721669}.
/FTId=VAR_044453.
VARIANT 382 382 S -> C (in WD; unknown pathological
significance; dbSNP:rs774102085).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076695.
VARIANT 390 390 I -> V (in dbSNP:rs770903362).
{ECO:0000269|PubMed:11405812}.
/FTId=VAR_000705.
VARIANT 406 406 S -> A (no effect on copper transport
activity; dbSNP:rs1801243).
{ECO:0000269|PubMed:10721669,
ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:18373411,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23333878,
ECO:0000269|Ref.2}.
/FTId=VAR_000706.
VARIANT 446 446 V -> L (in dbSNP:rs587783298).
/FTId=VAR_000707.
VARIANT 456 456 V -> L (polymorphism; decreased copper
transport activity; no effect on ATPase
activity; dbSNP:rs1801244).
{ECO:0000269|PubMed:10721669,
ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:17823867,
ECO:0000269|PubMed:18373411,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:25704634,
ECO:0000269|PubMed:9887381,
ECO:0000269|Ref.2}.
/FTId=VAR_000708.
VARIANT 466 466 L -> V.
/FTId=VAR_000709.
VARIANT 486 486 A -> S (in WD; does not affect
interaction with COMMD1).
{ECO:0000269|PubMed:11216666,
ECO:0000269|PubMed:17919502}.
/FTId=VAR_044454.
VARIANT 492 492 L -> S (in WD; decreased copper transport
activity; decreased ATPase activity; does
not affect interaction with COMMD1).
{ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000710.
VARIANT 532 532 Y -> H (in WD; no effect on copper
transport activity; does not affect
interaction with COMMD1).
{ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:18203200}.
/FTId=VAR_044455.
VARIANT 536 536 V -> A (in WD; unknown pathological
significance; dbSNP:rs138427376).
{ECO:0000269|PubMed:18373411,
ECO:0000269|PubMed:23518715}.
/FTId=VAR_058925.
VARIANT 539 539 P -> L (in WD; dbSNP:rs572122562).
{ECO:0000269|PubMed:22763723}.
/FTId=VAR_076970.
VARIANT 541 541 E -> K (in WD; unknown pathological
significance; does not affect interaction
with COMMD1; dbSNP:rs187046823).
{ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:23518715}.
/FTId=VAR_076696.
VARIANT 549 549 L -> P (in WD).
{ECO:0000269|PubMed:21682854}.
/FTId=VAR_067335.
VARIANT 565 565 N -> S (in dbSNP:rs778475094).
{ECO:0000269|PubMed:9482578}.
/FTId=VAR_000711.
VARIANT 591 591 G -> D (in WD; increased interaction with
COMMD1; decreased localization to trans-
Glogi network; dbSNP:rs797045402).
{ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:17919502}.
/FTId=VAR_044456.
VARIANT 591 591 G -> S (in WD).
{ECO:0000269|PubMed:17823867}.
/FTId=VAR_076794.
VARIANT 597 597 V -> I (in WD; unknown pathological
significance; dbSNP:rs760501309).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076697.
VARIANT 604 604 A -> P (in WD; increased interaction with
COMMD1). {ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:17919502}.
/FTId=VAR_044457.
VARIANT 606 606 V -> G (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076732.
VARIANT 608 609 FD -> Y (in WD).
{ECO:0000269|PubMed:9671269}.
/FTId=VAR_010009.
VARIANT 614 614 G -> C (in WD; unknown pathological
significance; dbSNP:rs376565432).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076698.
VARIANT 616 616 R -> Q (in WD; does not affect
interaction with COMMD1;
dbSNP:rs752850609).
{ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:17919502}.
/FTId=VAR_009004.
VARIANT 616 616 R -> W (in WD; decreased copper transport
activity; increased ATPase activity; does
not affect interaction with COMMD1;
dbSNP:rs374172791).
{ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:22240481}.
/FTId=VAR_023012.
VARIANT 626 626 G -> A (in WD; no effect on protein
abundance; no effect on protein
localization; may have an effect on
copper transport activity; no effect on
ATPase activity; does not affect
interaction with COMMD1;
dbSNP:rs587783299).
{ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:24706876,
ECO:0000269|PubMed:8533760}.
/FTId=VAR_000712.
VARIANT 639 639 H -> Y (in WD; unknown pathological
significance; no effect on protein
abundance; no effect on protein
localization; no effect on copper
transport activity; dbSNP:rs200728096).
{ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:24706876}.
/FTId=VAR_044458.
VARIANT 641 641 L -> S (in WD; unknown pathological
significance; no effect on protein
abundance; no effect on protein
localization; no effect on copper
transport activity; does not affect
interaction with COMMD1;
dbSNP:rs186924074).
{ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:24706876}.
/FTId=VAR_023013.
VARIANT 642 642 D -> H (in WD; no effect on protein
abundance; no effect on protein
localization; no effect on copper
transport activity; does not affect
interaction with COMMD1;
dbSNP:rs72552285).
{ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:21682854,
ECO:0000269|PubMed:24706876,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000713.
VARIANT 645 645 M -> R (in WD; no effect on protein
abundance; no effect on protein
localization; no effect on copper
transport activity; increased ATPase
activity; does not affect interaction
with COMMD1; dbSNP:rs121907998).
{ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:17919502,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:24706876,
ECO:0000269|PubMed:9482578,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000714.
VARIANT 653 653 S -> Y (in WD; no effect on protein
abundance; altered copper-induced
relocalization; no effect on copper
transport activity).
{ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:24706876}.
/FTId=VAR_044459.
VARIANT 657 657 S -> R (in WD; dbSNP:rs372436901).
{ECO:0000269|PubMed:18373411}.
/FTId=VAR_058926.
VARIANT 665 665 M -> I (in WD; unknown pathological
significance; dbSNP:rs72552259).
{ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000715.
VARIANT 670 671 Missing (in WD).
{ECO:0000269|PubMed:10447265}.
/FTId=VAR_009005.
VARIANT 690 690 P -> L (in WD).
{ECO:0000269|PubMed:15952988}.
/FTId=VAR_023014.
VARIANT 691 691 G -> R (in WD; dbSNP:rs121908001).
{ECO:0000269|PubMed:17718866,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000716.
VARIANT 693 693 S -> C (in WD).
{ECO:0000269|PubMed:9772425}.
/FTId=VAR_023015.
VARIANT 703 703 C -> Y (in WD; dbSNP:rs767218895).
{ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:21682854}.
/FTId=VAR_044460.
VARIANT 708 708 L -> P (in WD; dbSNP:rs121908000).
{ECO:0000269|PubMed:11093740}.
/FTId=VAR_000717.
VARIANT 710 710 G -> A (in WD).
{ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:9887381}.
/FTId=VAR_010010.
VARIANT 710 710 G -> R (in WD).
/FTId=VAR_000718.
VARIANT 710 710 G -> S (in WD; decreased copper transport
activity; no effect on ATPase activity;
dbSNP:rs137853285).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:22763723,
ECO:0000269|PubMed:23333878}.
/FTId=VAR_000719.
VARIANT 710 710 G -> V (in WD).
{ECO:0000269|PubMed:16088907}.
/FTId=VAR_044461.
VARIANT 711 711 G -> E (in WD).
/FTId=VAR_000720.
VARIANT 711 711 G -> R (in WD).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_009006.
VARIANT 711 711 G -> W (in WD).
/FTId=VAR_009007.
VARIANT 713 713 Y -> C (in WD; dbSNP:rs756883878).
/FTId=VAR_000721.
VARIANT 721 721 S -> P (in WD; dbSNP:rs765667658).
{ECO:0000269|PubMed:12325021}.
/FTId=VAR_023016.
VARIANT 723 723 R -> G. {ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:9482578}.
/FTId=VAR_000722.
VARIANT 729 729 M -> V (in WD; unknown pathological
significance; dbSNP:rs773447981).
{ECO:0000269|PubMed:21645214}.
/FTId=VAR_076733.
VARIANT 731 731 V -> A (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076699.
VARIANT 732 732 L -> H (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076734.
VARIANT 732 732 L -> P (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076735.
VARIANT 737 737 T -> R (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:15967699}.
/FTId=VAR_023017.
VARIANT 741 741 Y -> C (in WD; dbSNP:rs770533110).
{ECO:0000269|PubMed:9887381}.
/FTId=VAR_010011.
VARIANT 744 744 S -> P (in WD).
{ECO:0000269|PubMed:21682854}.
/FTId=VAR_009008.
VARIANT 745 745 L -> P (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076700.
VARIANT 747 747 I -> F (in WD).
{ECO:0000269|PubMed:9671269}.
/FTId=VAR_000723.
VARIANT 756 756 A -> G (in WD).
{ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:23235335}.
/FTId=VAR_044462.
VARIANT 760 760 P -> L (in WD; decreased copper transport
activity; increased ATPase activity;
dbSNP:rs766907687).
{ECO:0000269|PubMed:11180609,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:22240481}.
/FTId=VAR_023018.
VARIANT 765 765 D -> G (in WD).
{ECO:0000269|PubMed:14986826}.
/FTId=VAR_023019.
VARIANT 765 765 D -> H (in WD; unknown pathological
significance; dbSNP:rs28942075).
{ECO:0000269|PubMed:22484412}.
/FTId=VAR_076811.
VARIANT 765 765 D -> N (in WD; decreased copper transport
activity; increased ATPase activity;
decreased localization to TGN and reduced
capacity to redistribute to cytoplasmic
vesicles under high-copper levels;
dbSNP:rs28942075).
{ECO:0000269|PubMed:10942420,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:21682854,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:8533760,
ECO:0000269|PubMed:9482578,
ECO:0000269|PubMed:9837819}.
/FTId=VAR_000724.
VARIANT 766 766 T -> M (in WD; dbSNP:rs121907997).
{ECO:0000269|PubMed:16088907}.
/FTId=VAR_044463.
VARIANT 766 766 T -> R (in WD; dbSNP:rs121907997).
{ECO:0000269|PubMed:15557537}.
/FTId=VAR_044464.
VARIANT 768 768 P -> H (in WD).
{ECO:0000269|PubMed:12544487}.
/FTId=VAR_023020.
VARIANT 769 769 M -> I (in WD).
{ECO:0000269|PubMed:10790207}.
/FTId=VAR_023021.
VARIANT 769 769 M -> R (in WD; dbSNP:rs772595172).
/FTId=VAR_009009.
VARIANT 769 769 M -> V (in WD; possible decreased copper
transport activity; increased ATPase
activity; dbSNP:rs193922103).
{ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:9837819}.
/FTId=VAR_000725.
VARIANT 776 776 L -> P (in WD).
{ECO:0000269|PubMed:16283883}.
/FTId=VAR_044465.
VARIANT 776 776 L -> V (in WD; unknown pathological
significance; no effect on copper
transport activity; decreased
localization to TGN and reduced capacity
to redistribute to cytoplasmic vesicles
under high-copper levels).
{ECO:0000269|PubMed:10942420,
ECO:0000269|PubMed:9837819}.
/FTId=VAR_000726.
VARIANT 778 778 R -> G (in WD; dbSNP:rs137853284).
{ECO:0000269|PubMed:11216666,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:21682854,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:8533760}.
/FTId=VAR_000727.
VARIANT 778 778 R -> L (in WD; most common mutation;
decreased copper transport activity;
extensively localized throughout the cell
in the distribution pattern of the
endoplasmic reticulum; dbSNP:rs28942074).
{ECO:0000269|PubMed:10453196,
ECO:0000269|PubMed:10721669,
ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:10942420,
ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:12376745,
ECO:0000269|PubMed:12544487,
ECO:0000269|PubMed:14966923,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:16649058,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:23235335,
ECO:0000269|PubMed:25704634,
ECO:0000269|PubMed:8782057,
ECO:0000269|PubMed:9452121,
ECO:0000269|PubMed:9554743,
ECO:0000269|PubMed:9837819}.
/FTId=VAR_000728.
VARIANT 778 778 R -> Q (in WD; decreased copper transport
activity; dbSNP:rs28942074).
{ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:23235335,
ECO:0000269|PubMed:8782057,
ECO:0000269|PubMed:9837819}.
/FTId=VAR_000729.
VARIANT 778 778 R -> W (in WD; dbSNP:rs137853284).
{ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:11243728,
ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000730.
VARIANT 779 779 W -> G (in WD; dbSNP:rs751798708).
{ECO:0000269|PubMed:22763723,
ECO:0000269|PubMed:23159873}.
/FTId=VAR_076971.
VARIANT 788 788 T -> I (in WD; decreased copper ion
transmembrane transporter activity;
dbSNP:rs541408630).
{ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:26004889}.
/FTId=VAR_075336.
VARIANT 795 795 L -> F (in WD; unknown pathological
significance; dbSNP:rs751710854).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_000731.
VARIANT 795 795 L -> R (in WD).
/FTId=VAR_009010.
VARIANT 816 816 R -> S (in WD).
{ECO:0000269|PubMed:22763723}.
/FTId=VAR_076972.
VARIANT 825 825 V -> L. {ECO:0000269|PubMed:17823867}.
/FTId=VAR_076795.
VARIANT 827 827 R -> P (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076765.
VARIANT 827 827 R -> W (in WD; yeast complementation
assays show that the variant does not
rescue iron-uptake deficiency of yeast
mutant ccc2; dbSNP:rs539585071).
{ECO:0000269|PubMed:21645214}.
/FTId=VAR_076736.
VARIANT 832 832 K -> R (decreased copper transport
activity; no effect on ATPase activity;
dbSNP:rs1061472).
{ECO:0000269|PubMed:10721669,
ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:18373411,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:8250934,
ECO:0000269|PubMed:9482578,
ECO:0000269|PubMed:9554743,
ECO:0000269|Ref.9}.
/FTId=VAR_000732.
VARIANT 836 836 G -> E (in WD; unknown pathological
significance; dbSNP:rs773809011).
{ECO:0000269|PubMed:22484412}.
/FTId=VAR_076812.
VARIANT 840 840 P -> L (in WD; decreased copper transport
activity; increased ATPase activity;
dbSNP:rs768671894).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000733.
VARIANT 857 857 I -> T (in WD; decreased copper transport
activity; increased ATPase activity).
{ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:8533760}.
/FTId=VAR_000734.
VARIANT 858 858 T -> A (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076766.
VARIANT 861 861 A -> T (in WD).
{ECO:0000269|PubMed:16088907}.
/FTId=VAR_044466.
VARIANT 864 864 V -> I. {ECO:0000269|PubMed:9554743}.
/FTId=VAR_000735.
VARIANT 869 869 G -> R (in WD; dbSNP:rs191312027).
{ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:23518715}.
/FTId=VAR_000736.
VARIANT 869 869 G -> V (in WD).
/FTId=VAR_009011.
VARIANT 874 874 A -> P (in WD; unknown pathological
significance; dbSNP:rs376355660).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076737.
VARIANT 874 874 A -> V (in WD; decreased copper transport
activity; increased ATPase activity;
decreased localization to the TGN;
dbSNP:rs121907994).
{ECO:0000269|PubMed:10453196,
ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:10721669,
ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:12376745,
ECO:0000269|PubMed:12544487,
ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23235335,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:9452121,
ECO:0000269|PubMed:9554743}.
/FTId=VAR_000737.
VARIANT 875 875 G -> R (polymorphism; individuals
heterozygous for Wilson disease mutations
on the R-875 background may manifest the
disease phenotype under conditions of
copper deficiency; affects protein
folding; localized to the ER and absent
from TGN under low copper conditions; in
response to high copper levels it
relocalizes to vesicles and properly
cycle back to TGN; dbSNP:rs587783304).
{ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:21406592,
ECO:0000269|PubMed:7833924,
ECO:0000269|PubMed:8298641}.
/FTId=VAR_023022.
VARIANT 875 875 G -> V (in WD; requires 2 nucleotide
substitutions).
/FTId=VAR_044467.
VARIANT 890 890 V -> M (in WD; dbSNP:rs786204718).
{ECO:0000269|PubMed:11216666,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:23235335}.
/FTId=VAR_023023.
VARIANT 891 891 G -> D (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:21645214}.
/FTId=VAR_076738.
VARIANT 891 891 G -> V (in WD).
/FTId=VAR_010012.
VARIANT 898 898 Q -> R (in WD).
{ECO:0000269|PubMed:11243728}.
/FTId=VAR_023024.
VARIANT 899 907 Missing (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:22075048}.
/FTId=VAR_076739.
VARIANT 899 899 I -> F (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076767.
VARIANT 918 918 D -> E (in WD).
{ECO:0000269|PubMed:15967699}.
/FTId=VAR_023025.
VARIANT 918 918 D -> N (in WD; dbSNP:rs540935874).
{ECO:0000269|PubMed:9671269}.
/FTId=VAR_000738.
VARIANT 919 919 R -> G (in WD; dbSNP:rs121907993).
{ECO:0000269|PubMed:10453196,
ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:12376745,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:23235335,
ECO:0000269|PubMed:25704634,
ECO:0000269|PubMed:9452121}.
/FTId=VAR_000739.
VARIANT 919 919 R -> W (in WD; dbSNP:rs121907993).
{ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000740.
VARIANT 921 921 S -> N (in WD).
{ECO:0000269|PubMed:9671269}.
/FTId=VAR_000741.
VARIANT 921 921 S -> R (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076740.
VARIANT 929 929 I -> V (in dbSNP:rs534960245).
{ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:23235335}.
/FTId=VAR_076741.
VARIANT 933 933 T -> P (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:9671269}.
/FTId=VAR_000742.
VARIANT 935 935 T -> M (in WD; dbSNP:rs750019452).
{ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:16649058,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:24476933}.
/FTId=VAR_000743.
VARIANT 936 936 L -> V (in WD; unknown pathological
significance; dbSNP:rs367855110).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076701.
VARIANT 939 939 W -> C (in WD).
{ECO:0000269|PubMed:22484412}.
/FTId=VAR_076813.
VARIANT 943 943 G -> C (in WD).
{ECO:0000269|PubMed:16088907}.
/FTId=VAR_044468.
VARIANT 943 943 G -> D (in WD; dbSNP:rs779323689).
{ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:14966923,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:23235335}.
/FTId=VAR_000744.
VARIANT 943 943 G -> S (in WD; no effect on copper
transport activity; normally localized to
TGN network but unable to redistribute to
cytoplasmic vesicles in response to
copper; dbSNP:rs28942076).
{ECO:0000269|PubMed:10942420,
ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:9837819}.
/FTId=VAR_000745.
VARIANT 949 949 V -> G (in WD).
{ECO:0000269|PubMed:15024742,
ECO:0000269|PubMed:9887381}.
/FTId=VAR_023026.
VARIANT 952 952 R -> K (in dbSNP:rs732774).
{ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:18373411,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:7833924,
ECO:0000269|PubMed:8298639,
ECO:0000269|Ref.2}.
/FTId=VAR_000746.
VARIANT 967 967 I -> F (in WD; dbSNP:rs60003608).
{ECO:0000269|PubMed:8938442}.
/FTId=VAR_010013.
VARIANT 969 969 R -> Q (in WD; decreased copper transport
activity; increased ATPase activity; no
effect on localization;
dbSNP:rs121907996).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:11216666,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:8533760,
ECO:0000269|PubMed:9482578}.
/FTId=VAR_000747.
VARIANT 969 969 R -> W (in WD; unknown pathological
significance; dbSNP:rs774028495).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076768.
VARIANT 971 971 A -> V (in WD; dbSNP:rs770340441).
{ECO:0000269|PubMed:18373411}.
/FTId=VAR_058927.
VARIANT 974 974 T -> M (in WD; dbSNP:rs201061621).
{ECO:0000269|PubMed:18373411}.
/FTId=VAR_058928.
VARIANT 975 975 S -> Y (in WD; dbSNP:rs778163447).
{ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:23235335}.
/FTId=VAR_023027.
VARIANT 977 977 T -> M (in WD; loss of copper transport
activity; dbSNP:rs72552255).
{ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:21682854,
ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:8938442,
ECO:0000269|PubMed:9837819}.
/FTId=VAR_000748.
VARIANT 980 980 C -> Y (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076742.
VARIANT 982 982 A -> T (in WD; unknown pathological
significance; dbSNP:rs750407121).
{ECO:0000269|PubMed:24476933}.
/FTId=VAR_077616.
VARIANT 982 982 A -> V (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076769.
VARIANT 985 985 C -> Y (in WD).
{ECO:0000269|PubMed:10447265}.
/FTId=VAR_009012.
VARIANT 987 987 L -> P (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076743.
VARIANT 988 988 G -> R (in WD; dbSNP:rs199623434).
{ECO:0000269|PubMed:16283883}.
/FTId=VAR_044469.
VARIANT 990 990 A -> P (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:25982861}.
/FTId=VAR_076814.
VARIANT 991 991 T -> M (in WD; yeast complementation
assays show that the variant mildly
rescue iron-uptake deficiency of yeast
mutant ccc2; dbSNP:rs41292782).
{ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:20333758,
ECO:0000269|PubMed:23518715}.
/FTId=VAR_044470.
VARIANT 992 992 P -> H (in WD).
{ECO:0000269|PubMed:15811015}.
/FTId=VAR_044471.
VARIANT 992 992 P -> L (in WD; common mutation; decreased
copper transport activity; no effect on
ATPase activity; dbSNP:rs201038679).
{ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:16649058,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23235335,
ECO:0000269|PubMed:25704634,
ECO:0000269|PubMed:9671269,
ECO:0000269|PubMed:9837819}.
/FTId=VAR_000749.
VARIANT 995 995 V -> A (in WD; unknown pathological
significance; no effect on copper
transport activity; dbSNP:rs777791532).
{ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:9837819}.
/FTId=VAR_000750.
VARIANT 996 996 M -> T (in WD; dbSNP:rs770782111).
{ECO:0000269|PubMed:16088907}.
/FTId=VAR_044472.
VARIANT 998 998 G -> D (in WD).
{ECO:0000269|PubMed:21682854}.
/FTId=VAR_067336.
VARIANT 1000 1000 G -> R (in WD; yeast complementation
assays show that the variant does not
rescue iron-uptake deficiency of yeast
mutant ccc2; dbSNP:rs751078884).
{ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:20333758}.
/FTId=VAR_044473.
VARIANT 1003 1003 A -> T (in WD; dbSNP:rs201497300).
{ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:15811015,
ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000751.
VARIANT 1003 1003 A -> V (in WD; dbSNP:rs775055397).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:25982861}.
/FTId=VAR_009013.
VARIANT 1004 1004 Q -> P (in WD; dbSNP:rs587783307).
{ECO:0000269|PubMed:18373411}.
/FTId=VAR_058929.
VARIANT 1010 1010 K -> R (in WD; unknown pathological
significance; dbSNP:rs747584649).
{ECO:0000269|PubMed:25982861}.
/FTId=VAR_076815.
VARIANT 1010 1010 K -> T (in WD; yeast complementation
assays show that the variant does not
rescue iron-uptake deficiency of yeast
mutant ccc2).
{ECO:0000269|PubMed:21645214}.
/FTId=VAR_076744.
VARIANT 1012 1012 G -> R (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076770.
VARIANT 1012 1012 G -> V (in WD; unknown pathological
significance; dbSNP:rs772089544).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076771.
VARIANT 1017 1017 M -> I (in WD; unknown pathological
significance; dbSNP:rs755851188).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076702.
VARIANT 1018 1018 A -> V (in WD; dbSNP:rs371840514).
{ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000752.
VARIANT 1021 1021 I -> V (in WD; unknown pathological
significance; dbSNP:rs776490710).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076703.
VARIANT 1024 1024 V -> A (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:21645214}.
/FTId=VAR_076745.
VARIANT 1029 1029 T -> I (in WD).
{ECO:0000269|PubMed:10453196,
ECO:0000269|PubMed:21645214}.
/FTId=VAR_044474.
VARIANT 1031 1031 T -> A (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:17823867,
ECO:0000269|PubMed:21645214}.
/FTId=VAR_076746.
VARIANT 1031 1031 T -> I (in WD).
{ECO:0000269|PubMed:9887381}.
/FTId=VAR_010014.
VARIANT 1033 1033 T -> A (in WD).
/FTId=VAR_009014.
VARIANT 1033 1033 T -> S (in WD).
{ECO:0000269|PubMed:15967699}.
/FTId=VAR_023028.
VARIANT 1035 1035 G -> V (in WD).
{ECO:0000269|PubMed:10453196,
ECO:0000269|PubMed:21645214}.
/FTId=VAR_000753.
VARIANT 1036 1036 V -> I (in WD; copper ion transmembrane
transporter activity; dbSNP:rs761147984).
{ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:26004889}.
/FTId=VAR_075337.
VARIANT 1038 1038 R -> K (in WD; dbSNP:rs59959366).
{ECO:0000269|PubMed:8980283}.
/FTId=VAR_010015.
VARIANT 1041 1041 R -> P (in WD).
{ECO:0000269|PubMed:10194254,
ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:11405812}.
/FTId=VAR_009015.
VARIANT 1041 1041 R -> W (in WD; unknown pathological
significance; no effect on copper
transport activity; dbSNP:rs746485916).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:25982861,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000754.
VARIANT 1043 1043 L -> P (in WD; yeast complementation
assays show that the variant does not
rescue iron-uptake deficiency of yeast
mutant ccc2).
{ECO:0000269|PubMed:20333758,
ECO:0000269|PubMed:25982861}.
/FTId=VAR_000755.
VARIANT 1052 1052 P -> L (in WD; loss of copper transport
activity; no effect on ATPase activity;
dbSNP:rs778543794).
{ECO:0000269|PubMed:22240481}.
/FTId=VAR_009016.
VARIANT 1058 1058 A -> V (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076704.
VARIANT 1061 1061 G -> E (in WD; dbSNP:rs764131178).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:11216666,
ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:25982861}.
/FTId=VAR_009017.
VARIANT 1063 1063 A -> V (in WD; dbSNP:rs587783309).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:21682854}.
/FTId=VAR_009018.
VARIANT 1064 1064 E -> A (in WD; does not bind ATP; the
mutant is stable and is properly targeted
to the TGN; dbSNP:rs374094065).
{ECO:0000269|PubMed:21398519,
ECO:0000269|PubMed:9482578}.
/FTId=VAR_000756.
VARIANT 1064 1064 E -> K (in WD; loss of copper transport
activity; loss of ATPase activity;
dbSNP:rs376910645).
{ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:8533760}.
/FTId=VAR_000757.
VARIANT 1065 1065 A -> P (in WD).
/FTId=VAR_044475.
VARIANT 1068 1068 E -> G (in WD; common mutation).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_009019.
VARIANT 1069 1069 H -> Q (in WD; common mutation; decreased
copper transport activity; loss of ATPase
activity; cannot form an acylphosphate
intermediate during catalysis; does not
alter the folding of the nucleotide-
binding domain; decreased stability; does
not localizes to late endosomes;
dbSNP:rs76151636).
{ECO:0000269|PubMed:10051024,
ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:11216666,
ECO:0000269|PubMed:11231950,
ECO:0000269|PubMed:11243728,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:12551905,
ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:21398519,
ECO:0000269|PubMed:21682854,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:22763723,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:8298641,
ECO:0000269|PubMed:9482578,
ECO:0000269|PubMed:9887381}.
/FTId=VAR_000758.
VARIANT 1070 1070 P -> S (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076705.
VARIANT 1074 1074 A -> V (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076706.
VARIANT 1083 1083 L -> F (in WD; decreased copper transport
activity; no effect on ATPase activity;
decreased localization to the TGN).
{ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:11954751,
ECO:0000269|PubMed:12544487,
ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:9554743}.
/FTId=VAR_000759.
VARIANT 1089 1089 G -> E (in WD).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_000760.
VARIANT 1089 1089 G -> V (in WD).
{ECO:0000269|PubMed:9671269}.
/FTId=VAR_000761.
VARIANT 1091 1091 C -> Y (in WD; unknown pathological
significance; dbSNP:rs778825095).
{ECO:0000269|PubMed:21645214}.
/FTId=VAR_076747.
VARIANT 1094 1094 F -> L (in WD).
{ECO:0000269|PubMed:15024742}.
/FTId=VAR_023029.
VARIANT 1095 1095 Q -> P (in WD).
{ECO:0000269|PubMed:16283883}.
/FTId=VAR_009020.
VARIANT 1098 1098 P -> R (in WD).
{ECO:0000269|PubMed:14986826}.
/FTId=VAR_023030.
VARIANT 1099 1099 G -> S (in WD; dbSNP:rs761632029).
{ECO:0000269|PubMed:11216666,
ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:17949296}.
/FTId=VAR_023031.
VARIANT 1101 1101 G -> R (in WD; yeast complementation
assays show that the variant does not
rescue iron-uptake deficiency of yeast
mutant ccc2; dbSNP:rs786204483).
{ECO:0000269|PubMed:20333758,
ECO:0000269|PubMed:25982861}.
/FTId=VAR_000762.
VARIANT 1102 1102 I -> T (in WD; yeast complementation
assays show that the variant
intermediately rescue iron-uptake
deficiency of yeast mutant ccc2;
dbSNP:rs560952220).
{ECO:0000269|PubMed:11243728,
ECO:0000269|PubMed:15811015,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:20333758}.
/FTId=VAR_000763.
VARIANT 1104 1104 C -> F (in WD).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_009021.
VARIANT 1104 1104 C -> S (in WD).
{ECO:0000269|PubMed:25982861}.
/FTId=VAR_076816.
VARIANT 1104 1104 C -> Y (in WD; dbSNP:rs764041557).
{ECO:0000269|PubMed:15811015}.
/FTId=VAR_044476.
VARIANT 1106 1106 V -> D (in WD; marked impairment in
copper transport; dbSNP:rs775541743).
{ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:8938442}.
/FTId=VAR_010017.
VARIANT 1106 1106 V -> I (in WD; unknown pathological
significance; dbSNP:rs541208827).
{ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:14966923,
ECO:0000269|PubMed:21645214}.
/FTId=VAR_044477.
VARIANT 1109 1109 V -> M (in dbSNP:rs759109027).
{ECO:0000269|PubMed:9554743}.
/FTId=VAR_000764.
VARIANT 1111 1111 G -> D (in WD; dbSNP:rs182659444).
{ECO:0000269|PubMed:15967699}.
/FTId=VAR_023032.
VARIANT 1113 1113 L -> M (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:25982861}.
/FTId=VAR_076817.
VARIANT 1136 1136 E -> K (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:25704634}.
/FTId=VAR_077617.
VARIANT 1140 1140 V -> A (polymorphism; no effect on copper
transport activity; dbSNP:rs1801249).
{ECO:0000269|PubMed:10721669,
ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:14966923,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:17823867,
ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:18373411,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:24303094,
ECO:0000269|PubMed:9482578,
ECO:0000269|PubMed:9554743,
ECO:0000269|PubMed:9887381,
ECO:0000269|Ref.2, ECO:0000269|Ref.9}.
/FTId=VAR_000765.
VARIANT 1142 1142 Q -> H (in WD; dbSNP:rs778749563).
{ECO:0000269|PubMed:11405812}.
/FTId=VAR_000766.
VARIANT 1143 1143 T -> N (in dbSNP:rs587783313).
{ECO:0000269|PubMed:14986826}.
/FTId=VAR_023033.
VARIANT 1146 1146 V -> M (in WD).
{ECO:0000269|PubMed:9671269}.
/FTId=VAR_000767.
VARIANT 1148 1148 I -> T (in WD; yeast complementation
assays show that the variant mildly
rescue iron-uptake deficiency of yeast
mutant ccc2; dbSNP:rs60431989).
{ECO:0000269|PubMed:10447265,
ECO:0000269|PubMed:11216666,
ECO:0000269|PubMed:14986826,
ECO:0000269|PubMed:15845031,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:20333758,
ECO:0000269|PubMed:21645214}.
/FTId=VAR_000768.
VARIANT 1149 1149 G -> A (in WD).
{ECO:0000269|PubMed:18373411}.
/FTId=VAR_058930.
VARIANT 1149 1149 G -> E (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:25704634}.
/FTId=VAR_077618.
VARIANT 1151 1151 R -> C (in WD; yeast complementation
assays show that the variant does not
rescue iron-uptake deficiency of yeast
mutant ccc2; dbSNP:rs755554442).
{ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:23235335,
ECO:0000269|PubMed:23333878}.
/FTId=VAR_075338.
VARIANT 1151 1151 R -> H (in WD; dbSNP:rs377297166).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_009022.
VARIANT 1153 1153 W -> C (in WD).
/FTId=VAR_000769.
VARIANT 1153 1153 W -> R (in WD).
{ECO:0000269|PubMed:8938442}.
/FTId=VAR_010018.
VARIANT 1164 1164 D -> N (in WD; dbSNP:rs867107727).
{ECO:0000269|PubMed:18373411}.
/FTId=VAR_058931.
VARIANT 1168 1168 A -> S (in WD; dbSNP:rs777879359).
{ECO:0000269|PubMed:12544487,
ECO:0000269|PubMed:21645214}.
/FTId=VAR_023034.
VARIANT 1169 1169 M -> T (in WD).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_009023.
VARIANT 1169 1169 M -> V (in WD; moderate impairment in
copper transport; dbSNP:rs749085322).
{ECO:0000269|PubMed:18203200}.
/FTId=VAR_000770.
VARIANT 1173 1173 E -> G (in WD; yeast complementation
assays show that the variant fully rescue
iron-uptake deficiency of yeast mutant
ccc2). {ECO:0000269|PubMed:18373411,
ECO:0000269|PubMed:20333758}.
/FTId=VAR_058932.
VARIANT 1173 1173 E -> K (in WD; dbSNP:rs756029120).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:14986826}.
/FTId=VAR_009024.
VARIANT 1176 1176 G -> E (in WD; yeast complementation
assays show that the variant mildly
rescue iron-uptake deficiency of yeast
mutant ccc2).
{ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:20333758}.
/FTId=VAR_044478.
VARIANT 1176 1176 G -> R (in WD; dbSNP:rs137853279).
{ECO:0000269|PubMed:15845031,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:9887381}.
/FTId=VAR_010019.
VARIANT 1178 1178 T -> A (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:17823867,
ECO:0000269|PubMed:23235335}.
/FTId=VAR_076748.
VARIANT 1183 1183 A -> G (in WD; dbSNP:rs587783315).
{ECO:0000269|PubMed:12325021,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000771.
VARIANT 1183 1183 A -> T (in WD; unknown pathological
significance; no effect on copper
transport activity).
{ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000772.
VARIANT 1186 1186 G -> C (in WD).
/FTId=VAR_000773.
VARIANT 1186 1186 G -> S (in WD; unknown pathological
significance; no effect on copper
transport activity; dbSNP:rs786204547).
{ECO:0000269|PubMed:10453196,
ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:18203200,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:9452121}.
/FTId=VAR_000774.
VARIANT 1202 1202 A -> G (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23275100}.
/FTId=VAR_076749.
VARIANT 1207 1207 H -> R (in dbSNP:rs7334118).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:17823867,
ECO:0000269|PubMed:21682854,
ECO:0000269|PubMed:23333878}.
/FTId=VAR_009025.
VARIANT 1213 1213 G -> V (in WD; loss of copper transport
activity; no effect on ATPase activity).
{ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:9482578}.
/FTId=VAR_000775.
VARIANT 1216 1217 Missing (in WD).
{ECO:0000269|PubMed:9482578}.
/FTId=VAR_000777.
VARIANT 1216 1216 V -> M (in WD; dbSNP:rs776280797).
{ECO:0000269|PubMed:14966923,
ECO:0000269|PubMed:15952988,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000776.
VARIANT 1217 1218 Missing (in WD).
{ECO:0000269|PubMed:16207219}.
/FTId=VAR_044479.
VARIANT 1220 1220 T -> M (in WD; dbSNP:rs193922107).
{ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:22763723}.
/FTId=VAR_000778.
VARIANT 1221 1221 G -> E (in WD).
{ECO:0000269|PubMed:16088907}.
/FTId=VAR_044480.
VARIANT 1222 1222 D -> N (in WD).
{ECO:0000269|PubMed:10453196}.
/FTId=VAR_044481.
VARIANT 1222 1222 D -> V (in WD; decreased copper transport
activity; loss of ATPase activity).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:22240481}.
/FTId=VAR_010020.
VARIANT 1222 1222 D -> Y (in WD).
/FTId=VAR_000779.
VARIANT 1228 1228 R -> T (in WD; yeast complementation
assays show that the variant fully rescue
iron-uptake deficiency of yeast mutant
ccc2). {ECO:0000269|PubMed:18373411,
ECO:0000269|PubMed:20333758}.
/FTId=VAR_058933.
VARIANT 1230 1230 I -> V (in WD; dbSNP:rs200911496).
{ECO:0000269|PubMed:18373411}.
/FTId=VAR_058934.
VARIANT 1232 1232 T -> P (in WD; dbSNP:rs568009639).
{ECO:0000269|PubMed:15024742,
ECO:0000269|PubMed:15952988}.
/FTId=VAR_023035.
VARIANT 1239 1239 V -> G (in WD; yeast complementation
assays show that the variant does not
rescue iron-uptake deficiency of yeast
mutant ccc2; dbSNP:rs374628199).
{ECO:0000269|PubMed:20333758}.
/FTId=VAR_009026.
VARIANT 1243 1243 V -> L. {ECO:0000269|PubMed:23333878}.
/FTId=VAR_075339.
VARIANT 1245 1245 P -> S (in dbSNP:rs587783316).
{ECO:0000269|PubMed:14986826}.
/FTId=VAR_023036.
VARIANT 1245 1245 P -> T (in WD).
{ECO:0000269|PubMed:23333878}.
/FTId=VAR_075340.
VARIANT 1248 1248 K -> N (in WD).
{ECO:0000269|PubMed:14986826}.
/FTId=VAR_023037.
VARIANT 1250 1250 A -> G (in WD; unknown pathological
significance; dbSNP:rs372042739).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076707.
VARIANT 1252 1252 V -> I (in WD).
/FTId=VAR_044482.
VARIANT 1255 1255 L -> I (in WD).
{ECO:0000269|PubMed:12544487}.
/FTId=VAR_023038.
VARIANT 1256 1256 Q -> R (in WD).
{ECO:0000269|PubMed:15811015}.
/FTId=VAR_044483.
VARIANT 1262 1262 V -> F (in WD; dbSNP:rs769484789).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_009027.
VARIANT 1266 1266 G -> E (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23235335}.
/FTId=VAR_076750.
VARIANT 1266 1266 G -> R (in WD; common mutation;
dbSNP:rs121907992).
{ECO:0000269|PubMed:11243728,
ECO:0000269|PubMed:23518715}.
/FTId=VAR_009028.
VARIANT 1266 1266 G -> V (in WD; decreased copper transport
activity; loss of ATPase activity).
{ECO:0000269|PubMed:22240481}.
/FTId=VAR_000781.
VARIANT 1267 1267 D -> A (in WD).
{ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:12544487,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:9452121}.
/FTId=VAR_000782.
VARIANT 1267 1267 D -> V (in WD; yeast complementation
assays show that the variant does not
rescue iron-uptake deficiency of yeast
mutant ccc2).
{ECO:0000269|PubMed:18373411,
ECO:0000269|PubMed:20333758}.
/FTId=VAR_058935.
VARIANT 1268 1268 G -> R (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:16649058}.
/FTId=VAR_076751.
VARIANT 1270 1270 N -> S (in WD; loss of copper transport
activity; increased ATPase activity; does
not affect localization to late
endosomes; dbSNP:rs121907990).
{ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:11231950,
ECO:0000269|PubMed:11405812,
ECO:0000269|PubMed:11690702,
ECO:0000269|PubMed:12544487,
ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:16649058,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23235335,
ECO:0000269|PubMed:23333878,
ECO:0000269|PubMed:23518715,
ECO:0000269|PubMed:25982861,
ECO:0000269|PubMed:8298641,
ECO:0000269|PubMed:8533760,
ECO:0000269|PubMed:9452121}.
/FTId=VAR_000783.
VARIANT 1271 1271 D -> N (in WD).
{ECO:0000269|PubMed:15967699}.
/FTId=VAR_023039.
VARIANT 1273 1273 P -> L (in WD; decreased copper transport
activity; increased ATPase activity;
dbSNP:rs758355520).
{ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:21645214,
ECO:0000269|PubMed:21682854,
ECO:0000269|PubMed:22240481,
ECO:0000269|PubMed:23235335}.
/FTId=VAR_000784.
VARIANT 1278 1278 A -> V (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:9222767}.
/FTId=VAR_000785.
VARIANT 1279 1279 D -> G (in WD; dbSNP:rs778914828).
{ECO:0000269|PubMed:11043508}.
/FTId=VAR_023040.
VARIANT 1279 1279 D -> Y (in WD).
{ECO:0000269|PubMed:16207219}.
/FTId=VAR_044484.
VARIANT 1281 1281 G -> D (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:22484412}.
/FTId=VAR_076818.
VARIANT 1285 1292 Missing (in WD).
{ECO:0000269|PubMed:9222767}.
/FTId=VAR_000786.
VARIANT 1287 1287 G -> S (in WD; yeast complementation
assays show that the variant mildly
rescue iron-uptake deficiency of yeast
mutant ccc2; dbSNP:rs762866453).
{ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:20333758}.
/FTId=VAR_044485.
VARIANT 1288 1288 T -> M (in WD; unknown pathological
significance; dbSNP:rs373748155).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076772.
VARIANT 1293 1293 E -> K (in WD; unknown pathological
significance; dbSNP:rs776300396).
{ECO:0000269|PubMed:22484412,
ECO:0000269|PubMed:25982861}.
/FTId=VAR_076819.
VARIANT 1295 1295 A -> D (in WD; yeast complementation
assays show that the variant does not
rescue iron-uptake deficiency of yeast
mutant ccc2).
{ECO:0000269|PubMed:21645214}.
/FTId=VAR_076752.
VARIANT 1296 1296 D -> N (in WD; dbSNP:rs199821556).
{ECO:0000269|PubMed:11954751}.
/FTId=VAR_044486.
VARIANT 1297 1297 V -> I (in dbSNP:rs148399850).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_009029.
VARIANT 1297 1297 Missing (in WD).
{ECO:0000269|PubMed:10721669}.
/FTId=VAR_044487.
VARIANT 1298 1298 V -> I (in WD; unknown pathological
significance; dbSNP:rs753044473).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076708.
VARIANT 1298 1298 V -> L (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076709.
VARIANT 1305 1305 L -> P (in WD; dbSNP:rs377144951).
{ECO:0000269|PubMed:11180609,
ECO:0000269|PubMed:15967699}.
/FTId=VAR_023041.
VARIANT 1310 1310 S -> R (in WD; dbSNP:rs749380700).
/FTId=VAR_000787.
VARIANT 1322 1322 R -> P (in WD).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_000788.
VARIANT 1327 1327 L -> V (in WD).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_009030.
VARIANT 1328 1328 A -> T (in WD).
{ECO:0000269|PubMed:18373411}.
/FTId=VAR_058936.
VARIANT 1331 1331 Y -> S (in WD).
{ECO:0000269|PubMed:16088907}.
/FTId=VAR_044488.
VARIANT 1332 1332 N -> D (in WD).
{ECO:0000269|PubMed:21682854}.
/FTId=VAR_067337.
VARIANT 1332 1332 N -> K (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076773.
VARIANT 1336 1336 I -> T (in WD).
{ECO:0000269|PubMed:10790207}.
/FTId=VAR_023042.
VARIANT 1341 1341 G -> D (in WD; dbSNP:rs779494870).
{ECO:0000269|PubMed:15967699,
ECO:0000269|PubMed:16207219,
ECO:0000269|PubMed:16283883,
ECO:0000269|PubMed:17949296,
ECO:0000269|PubMed:21682854,
ECO:0000269|PubMed:9671269}.
/FTId=VAR_000789.
VARIANT 1341 1341 G -> R (in WD).
{ECO:0000269|PubMed:21682854}.
/FTId=VAR_067338.
VARIANT 1341 1341 G -> S (in WD; dbSNP:rs587783317).
{ECO:0000269|PubMed:14639035}.
/FTId=VAR_044489.
VARIANT 1341 1341 G -> V (in WD).
{ECO:0000269|PubMed:16088907}.
/FTId=VAR_044490.
VARIANT 1347 1347 G -> S (in WD; unknown pathological
significance; dbSNP:rs587783318).
{ECO:0000269|PubMed:24555712}.
/FTId=VAR_076973.
VARIANT 1352 1352 P -> S (in WD).
{ECO:0000269|PubMed:16207219}.
/FTId=VAR_044491.
VARIANT 1353 1353 W -> R (in WD).
/FTId=VAR_000790.
VARIANT 1355 1355 G -> C (in WD).
{ECO:0000269|PubMed:15967699}.
/FTId=VAR_023043.
VARIANT 1355 1355 G -> S (in WD).
{ECO:0000269|PubMed:8938442}.
/FTId=VAR_010021.
VARIANT 1358 1358 A -> S (in WD).
{ECO:0000269|PubMed:9671269}.
/FTId=VAR_000791.
VARIANT 1359 1359 M -> I (in WD; dbSNP:rs759551693).
{ECO:0000269|PubMed:18373411}.
/FTId=VAR_058937.
VARIANT 1363 1363 S -> F (in WD; dbSNP:rs776848753).
{ECO:0000269|PubMed:10544227}.
/FTId=VAR_009031.
VARIANT 1368 1368 L -> P (in WD; dbSNP:rs749171049).
{ECO:0000269|PubMed:16207219}.
/FTId=VAR_044492.
VARIANT 1369 1369 S -> L (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:17949296}.
/FTId=VAR_076774.
VARIANT 1373 1373 L -> P (in WD; increased protein
degradation; the mutant has a diffuse
cytoplasmic localization pattern and is
absent from TGN under conditions of low-
copper levels).
{ECO:0000269|PubMed:10790207,
ECO:0000269|PubMed:21454443}.
/FTId=VAR_023044.
VARIANT 1373 1373 L -> R (in WD; increased protein
degradation; the mutant has a diffuse
cytoplasmic localization pattern and is
absent from TGN under conditions of low-
copper levels; dbSNP:rs780811477).
{ECO:0000269|PubMed:15024742,
ECO:0000269|PubMed:21454443}.
/FTId=VAR_023045.
VARIANT 1375 1375 C -> S (in WD; unknown pathological
significance; localized at the TGN as the
wild-type under conditions of low-copper
levels). {ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:21454443}.
/FTId=VAR_044493.
VARIANT 1379 1379 P -> S (in WD; unknown pathological
significance; localized at the TGN as the
wild-type under conditions of low-copper
levels; dbSNP:rs181250704).
{ECO:0000269|PubMed:16088907,
ECO:0000269|PubMed:21454443}.
/FTId=VAR_044494.
VARIANT 1407 1407 D -> E (in dbSNP:rs587783320).
{ECO:0000269|PubMed:10721669}.
/FTId=VAR_044495.
VARIANT 1431 1431 S -> Y (in WD; unknown pathological
significance).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076710.
VARIANT 1432 1432 S -> F (in WD; unknown pathological
significance; dbSNP:rs375692175).
{ECO:0000269|PubMed:23518715}.
/FTId=VAR_076711.
VARIANT 1434 1434 T -> M (in WD; unknown pathological
significance; localized at the TGN as the
wild-type under conditions of low-copper
levels; dbSNP:rs60986317).
{ECO:0000269|PubMed:10544227,
ECO:0000269|PubMed:21454443}.
/FTId=VAR_009032.
MUTAGEN 653 653 S->F,D,E: Altered copper-induced
relocalization.
{ECO:0000269|PubMed:24706876}.
MUTAGEN 1027 1027 D->A: Loss of copper transport activity.
{ECO:0000269|PubMed:22240481}.
MUTAGEN 1031 1031 T->S: Decreased copper transport activity
with no effect on ATPase activity.
{ECO:0000269|PubMed:22240481}.
MUTAGEN 1069 1069 H->A,C: Loss of ATPase activity. Cannot
form an acylphosphate intermediate during
catalysis. Does not alter folding of the
nucleotide-binding domain.
{ECO:0000269|PubMed:12551905}.
CONFLICT 488 488 Q -> G (in Ref. 8; AAA16173).
{ECO:0000305}.
CONFLICT 635 635 N -> T (in Ref. 8; AAA16173).
{ECO:0000305}.
CONFLICT 767 767 P -> L (in Ref. 8; AAA16173).
{ECO:0000305}.
CONFLICT 837 837 G -> A (in Ref. 8; AAA16173).
{ECO:0000305}.
STRAND 58 65 {ECO:0000244|PDB:2N7Y}.
HELIX 69 82 {ECO:0000244|PDB:2N7Y}.
STRAND 88 92 {ECO:0000244|PDB:2N7Y}.
TURN 93 96 {ECO:0000244|PDB:2N7Y}.
STRAND 97 102 {ECO:0000244|PDB:2N7Y}.
TURN 104 106 {ECO:0000244|PDB:2N7Y}.
HELIX 109 119 {ECO:0000244|PDB:2N7Y}.
STRAND 122 124 {ECO:0000244|PDB:2N7Y}.
STRAND 143 151 {ECO:0000244|PDB:2LQB}.
HELIX 157 164 {ECO:0000244|PDB:2LQB}.
HELIX 165 167 {ECO:0000244|PDB:2LQB}.
STRAND 173 177 {ECO:0000244|PDB:2LQB}.
TURN 178 181 {ECO:0000244|PDB:2LQB}.
STRAND 182 187 {ECO:0000244|PDB:2LQB}.
TURN 189 191 {ECO:0000244|PDB:2LQB}.
HELIX 194 202 {ECO:0000244|PDB:2LQB}.
STRAND 208 210 {ECO:0000244|PDB:2LQB}.
STRAND 258 265 {ECO:0000244|PDB:2ROP}.
HELIX 266 268 {ECO:0000244|PDB:2ROP}.
HELIX 271 278 {ECO:0000244|PDB:2ROP}.
STRAND 285 291 {ECO:0000244|PDB:2ROP}.
TURN 292 295 {ECO:0000244|PDB:2ROP}.
STRAND 296 301 {ECO:0000244|PDB:2ROP}.
TURN 303 305 {ECO:0000244|PDB:2ROP}.
HELIX 308 315 {ECO:0000244|PDB:2ROP}.
STRAND 318 321 {ECO:0000244|PDB:2ROP}.
STRAND 323 326 {ECO:0000244|PDB:2ROP}.
STRAND 359 366 {ECO:0000244|PDB:2ROP}.
HELIX 372 380 {ECO:0000244|PDB:2ROP}.
HELIX 381 383 {ECO:0000244|PDB:2ROP}.
STRAND 384 393 {ECO:0000244|PDB:2ROP}.
TURN 394 397 {ECO:0000244|PDB:2ROP}.
STRAND 398 403 {ECO:0000244|PDB:2ROP}.
TURN 405 407 {ECO:0000244|PDB:2ROP}.
HELIX 410 420 {ECO:0000244|PDB:2ROP}.
STRAND 424 426 {ECO:0000244|PDB:2ROP}.
STRAND 488 495 {ECO:0000244|PDB:2EW9}.
STRAND 499 501 {ECO:0000244|PDB:2EW9}.
HELIX 502 511 {ECO:0000244|PDB:2EW9}.
STRAND 519 522 {ECO:0000244|PDB:2EW9}.
TURN 523 526 {ECO:0000244|PDB:2EW9}.
STRAND 527 532 {ECO:0000244|PDB:2EW9}.
TURN 534 536 {ECO:0000244|PDB:2EW9}.
HELIX 539 549 {ECO:0000244|PDB:2EW9}.
STRAND 552 555 {ECO:0000244|PDB:2EW9}.
STRAND 562 572 {ECO:0000244|PDB:2EW9}.
HELIX 576 588 {ECO:0000244|PDB:2EW9}.
STRAND 589 591 {ECO:0000244|PDB:2EW9}.
STRAND 594 598 {ECO:0000244|PDB:2EW9}.
TURN 599 602 {ECO:0000244|PDB:2EW9}.
STRAND 603 607 {ECO:0000244|PDB:2EW9}.
TURN 610 612 {ECO:0000244|PDB:2EW9}.
HELIX 615 625 {ECO:0000244|PDB:2EW9}.
STRAND 628 630 {ECO:0000244|PDB:2EW9}.
STRAND 1039 1044 {ECO:0000244|PDB:2ARF}.
TURN 1048 1050 {ECO:0000244|PDB:2ARF}.
HELIX 1053 1064 {ECO:0000244|PDB:2ARF}.
HELIX 1072 1083 {ECO:0000244|PDB:2ARF}.
STRAND 1091 1097 {ECO:0000244|PDB:2ARF}.
TURN 1098 1100 {ECO:0000244|PDB:2ARF}.
STRAND 1101 1107 {ECO:0000244|PDB:2ARF}.
HELIX 1109 1113 {ECO:0000244|PDB:2ARF}.
STRAND 1127 1130 {ECO:0000244|PDB:2ARF}.
STRAND 1143 1149 {ECO:0000244|PDB:2ARF}.
HELIX 1151 1158 {ECO:0000244|PDB:2ARF}.
HELIX 1163 1173 {ECO:0000244|PDB:2ARF}.
TURN 1174 1176 {ECO:0000244|PDB:2ARF}.
STRAND 1177 1184 {ECO:0000244|PDB:2ARF}.
STRAND 1187 1194 {ECO:0000244|PDB:2ARF}.
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


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